{
"uniprot_canonical_ac": "O60674-1",
"uniprot_ac": "O60674",
"uniprot_id": "JAK2_HUMAN",
"mass": {
"chemical_mass": 130674.0,
"monoisotopic_mass": 130674.0
},
"refseq": {
"ac": "NP_001309123",
"name": "tyrosine-protein kinase JAK2 isoform a",
"summary": "This gene encodes a non-receptor tyrosine kinase that plays a central role in cytokine and growth factor signalling. The primary isoform of this protein has an N-terminal FERM domain that is required for erythropoietin receptor association, an SH2 domain that binds STAT transcription factors, a pseudokinase domain and a C-terminal tyrosine kinase domain. Cytokine binding induces autophosphorylation and activation of this kinase. This kinase then recruits and phosphorylates signal transducer and activator of transcription (STAT) proteins. Growth factors like TGF-beta 1 also induce phosphorylation and activation of this kinase and translocation of downstream STAT proteins to the nucleus where they influence gene transcription. Mutations in this gene are associated with numerous inflammatory diseases and malignancies. This gene is a downstream target of the pleiotropic cytokine IL6 that is produced by B cells, T cells, dendritic cells and macrophages to produce an immune response or inflammation. Disregulation of the IL6/JAK2/STAT3 signalling pathways produces increased cellular proliferation and myeloproliferative neoplasms of hematopoietic stem cells. A nonsynonymous mutation in the pseudokinase domain of this gene disrupts the domains inhibitory effect and results in constitutive tyrosine phosphorylation activity and hypersensitivity to cytokine signalling. This gene and the IL6/JAK2/STAT3 signalling pathway is a therapeutic target for the treatment of excessive inflammatory responses to viral infections. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Jul 2020].",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001309123"
},
"gene_names": [
{
"name": "JAK2",
"resource": "UniProtKB",
"type": "recommended",
"url": "https://www.uniprot.org/uniprot/O60674",
"id": "O60674"
},
{
"name": "JAK2",
"resource": "RefSeq",
"type": "synonym",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001309123",
"id": "NP_001309123"
},
{
"name": "JTK10",
"resource": "RefSeq",
"type": "synonym",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001309123",
"id": "NP_001309123"
}
],
"protein_names": [
{
"name": "Tyrosine-protein kinase JAK2",
"resource": "UniProtKB",
"type": "recommended",
"url": "",
"id": "O60674"
},
{
"name": "2.7.10.2",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "O60674"
},
{
"name": "JAK-2",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "O60674"
},
{
"name": "Janus kinase 2",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "O60674"
},
{
"name": "tyrosine-protein kinase JAK2 isoform a",
"resource": "RefSeq",
"type": "synonym",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001309123",
"id": "NP_001309123"
},
{
"name": "tyrosine-protein kinase JAK2; Janus kinase 2 (a protein tyrosine kinase); JAK-2",
"resource": "RefSeq",
"type": "synonym",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001309123",
"id": "NP_001309123"
}
],
"function": [
{
"annotation": "Exploiting Synthetic Lethality between Germline BRCA1 Haploinsufficiency and PARP Inhibition in JAK2V617F-Positive Myeloproliferative Neoplasms. Publication Status: Online-Only",
"evidence": [
{
"database": "RefSeq",
"id": "NP_001309123",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001309123"
},
{
"database": "PubMed",
"id": "38139386",
"url": "https://glygen.org/publication/PubMed/38139386"
}
]
},
{
"annotation": "Insights into the role of JAK2-I724T variant in myeloproliferative neoplasms from a unique cohort of New Zealand patients.",
"evidence": [
{
"database": "RefSeq",
"id": "NP_001309123",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001309123"
},
{
"database": "PubMed",
"id": "38197452",
"url": "https://glygen.org/publication/PubMed/38197452"
}
]
},
{
"annotation": "JAK2 as a surface marker for enrichment of human pluripotent stem cells-derived ventricular cardiomyocytes. Publication Status: Online-Only",
"evidence": [
{
"database": "RefSeq",
"id": "NP_001309123",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001309123"
},
{
"database": "PubMed",
"id": "38093391",
"url": "https://glygen.org/publication/PubMed/38093391"
}
]
},
{
"annotation": "JAK2, CALR, and MPL Mutation Profiles in Colombian patients with BCR-ABL Negative Myeloproliferative Neoplasms. Publication Status: Online-Only",
"evidence": [
{
"database": "RefSeq",
"id": "NP_001309123",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001309123"
},
{
"database": "PubMed",
"id": "38111518",
"url": "https://glygen.org/publication/PubMed/38111518"
}
]
},
{
"annotation": "Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins (PubMed:7615558). Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins (PubMed:9618263). Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. Part of a signaling cascade that is activated by increased cellular retinol and that leads to the activation of STAT5 (STAT5A or STAT5B) (PubMed:21368206). In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation (PubMed:20098430). Plays a role in cell cycle by phosphorylating CDKN1B (PubMed:21423214). Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin (PubMed:19783980).",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674#function"
},
{
"database": "PubMed",
"id": "20098430",
"url": "https://glygen.org/publication/PubMed/20098430"
},
{
"database": "PubMed",
"id": "19783980",
"url": "https://glygen.org/publication/PubMed/19783980"
},
{
"database": "PubMed",
"id": "12023369",
"url": "https://glygen.org/publication/PubMed/12023369"
},
{
"database": "PubMed",
"id": "9618263",
"url": "https://glygen.org/publication/PubMed/9618263"
},
{
"database": "PubMed",
"id": "21423214",
"url": "https://glygen.org/publication/PubMed/21423214"
},
{
"database": "PubMed",
"id": "7615558",
"url": "https://glygen.org/publication/PubMed/7615558"
},
{
"database": "PubMed",
"id": "21368206",
"url": "https://glygen.org/publication/PubMed/21368206"
}
]
},
{
"annotation": "This gene encodes a non-receptor tyrosine kinase that plays a central role in cytokine and growth factor signalling. The primary isoform of this protein has an N-terminal FERM domain that is required for erythropoietin receptor association, an SH2 domain that binds STAT transcription factors, a pseudokinase domain and a C-terminal tyrosine kinase domain. Cytokine binding induces autophosphorylation and activation of this kinase. This kinase then recruits and phosphorylates signal transducer and activator of transcription (STAT) proteins. Growth factors like TGF-beta 1 also induce phosphorylation and activation of this kinase and translocation of downstream STAT proteins to the nucleus where they influence gene transcription. Mutations in this gene are associated with numerous inflammatory diseases and malignancies. This gene is a downstream target of the pleiotropic cytokine IL6 that is produced by B cells, T cells, dendritic cells and macrophages to produce an immune response or inflammation. Disregulation of the IL6/JAK2/STAT3 signalling pathways produces increased cellular proliferation and myeloproliferative neoplasms of hematopoietic stem cells. A nonsynonymous mutation in the pseudokinase domain of this gene disrupts the domains inhibitory effect and results in constitutive tyrosine phosphorylation activity and hypersensitivity to cytokine signalling. This gene and the IL6/JAK2/STAT3 signalling pathway is a therapeutic target for the treatment of excessive inflammatory responses to viral infections. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Jul 2020].",
"evidence": [
{
"database": "RefSeq",
"id": "NP_001309123",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001309123"
}
]
},
{
"annotation": "[Analysis of risk factors for thromboembolism in patients with JAK2[V617F] gene mutation positive myeloproliferative neoplasms].",
"evidence": [
{
"database": "RefSeq",
"id": "NP_001309123",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001309123"
},
{
"database": "PubMed",
"id": "38018064",
"url": "https://glygen.org/publication/PubMed/38018064"
}
]
}
],
"disease": [
{
"disease_id": "DOID:11512",
"recommended_name": {
"id": "DOID:11512",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:11512",
"name": "Budd-Chiari syndrome",
"description": "A hepatic vascular disease that is characterized by a spectrum of disease states, including anatomic abnormalities and hypercoagulable disorders, resulting in hepatic venous outflow occlusion."
},
"synonyms": [
{
"id": "DOID:11512",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:11512",
"name": "hepatic vein thrombosis",
"description": ""
},
{
"id": "MONDO:0010947",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0010947",
"name": "Budd-Chiari syndrome",
"description": "Budd-Chiari syndrome (BCS) is caused by obstruction of hepatic venous outflow involving either the hepatic veins or the terminal segment of the inferior vena cava."
},
{
"id": "MONDO:0010947",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0010947",
"name": "Budd-Chiari syndrome",
"description": ""
},
{
"id": "MONDO:0010947",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0010947",
"name": "Budd-Chiari syndrome, somatic",
"description": ""
},
{
"id": "MONDO:0010947",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0010947",
"name": "BDCHS",
"description": ""
},
{
"id": "MONDO:0010947",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0010947",
"name": "membranous obstruction of Inferior vena cava",
"description": ""
},
{
"id": "MONDO:0010947",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0010947",
"name": "membranous obstruction of the inferior vena cava",
"description": ""
},
{
"id": "MIM:600880",
"resource": "MIM",
"url": "https://www.omim.org/entry/600880",
"name": "Budd-Chiari syndrome",
"description": "Budd-Chiari syndrome"
}
],
"evidence": [
{
"id": "600880",
"database": "MIM",
"url": "https://www.omim.org/entry/600880"
}
]
},
{
"disease_id": "DOID:2224",
"recommended_name": {
"id": "DOID:2224",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:2224",
"name": "essential thrombocythemia",
"description": "A myeloproliferative neoplasm that is characterized by sustained thrombocytosis in the blood, increased numbers of large, mature megakaryocytes in the bone marrow, and episodes of thrombosis and/or hemorrhage and that results_in the overproduction of platelets."
},
"synonyms": [
{
"id": "DOID:2224",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:2224",
"name": "Essential thrombocythaemia",
"description": ""
},
{
"id": "DOID:2224",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:2224",
"name": "familial thrombocytosis",
"description": ""
},
{
"id": "DOID:2224",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:2224",
"name": "hemorrhagic thrombocythemia",
"description": ""
},
{
"id": "DOID:2224",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:2224",
"name": "hereditary thrombocythemia",
"description": ""
},
{
"id": "DOID:2224",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:2224",
"name": "primary Thrombocytosis",
"description": ""
},
{
"id": "MONDO:0013794",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0013794",
"name": "thrombocythemia 3",
"description": "Familial thrombocytosis in which the cause of the disease is a mutation in the JAK2 gene."
},
{
"id": "MONDO:0013794",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0013794",
"name": "JAK2 familial thrombocytosis",
"description": ""
},
{
"id": "MONDO:0013794",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0013794",
"name": "familial thrombocytosis caused by mutation in JAK2",
"description": ""
},
{
"id": "MONDO:0013794",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0013794",
"name": "thrombocythemia 3",
"description": ""
},
{
"id": "MONDO:0013794",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0013794",
"name": "thrombocythemia 3, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0013794",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0013794",
"name": "thrombocythemia type 3",
"description": ""
},
{
"id": "MONDO:0013794",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0013794",
"name": "THCYT3",
"description": ""
},
{
"id": "MONDO:0013794",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0013794",
"name": "thrombocytosis 3",
"description": ""
},
{
"id": "MONDO:0011173",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011173",
"name": "thrombocythemia 2",
"description": "Familial thrombocytosis in which the cause of the disease is a mutation in the MPL gene."
},
{
"id": "MONDO:0011173",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011173",
"name": "MPL familial thrombocytosis",
"description": ""
},
{
"id": "MONDO:0011173",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011173",
"name": "familial thrombocytosis caused by mutation in MPL",
"description": ""
},
{
"id": "MONDO:0011173",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011173",
"name": "thrombocythemia 2",
"description": ""
},
{
"id": "MONDO:0011173",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011173",
"name": "thrombocythemia 2, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0011173",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011173",
"name": "thrombocythemia type 2",
"description": ""
},
{
"id": "MONDO:0011173",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011173",
"name": "THCYT2",
"description": ""
},
{
"id": "MONDO:0008554",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008554",
"name": "thrombocythemia 1",
"description": ""
},
{
"id": "MONDO:0008554",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008554",
"name": "thrombocythemia 1",
"description": ""
},
{
"id": "MONDO:0008554",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008554",
"name": "thrombocythemia type 1",
"description": ""
},
{
"id": "MONDO:0008554",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008554",
"name": "thrombocythemia, somatic",
"description": ""
},
{
"id": "MONDO:0008554",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008554",
"name": "THCYT1",
"description": ""
},
{
"id": "MONDO:0008554",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008554",
"name": "thrombocytosis 1",
"description": ""
},
{
"id": "MIM:614521",
"resource": "MIM",
"url": "https://www.omim.org/entry/614521",
"name": "Thrombocythemia 3",
"description": "Thrombocythemia 3"
},
{
"id": "MIM:601977",
"resource": "MIM",
"url": "https://www.omim.org/entry/601977",
"name": "Thrombocythemia 2",
"description": "Thrombocythemia 2"
},
{
"id": "MIM:187950",
"resource": "MIM",
"url": "https://www.omim.org/entry/187950",
"name": "Thrombocythemia 1",
"description": "Thrombocythemia 1"
}
],
"evidence": [
{
"id": "614521",
"database": "MIM",
"url": "https://www.omim.org/entry/614521"
}
]
},
{
"disease_id": "DOID:4971",
"recommended_name": {
"id": "DOID:4971",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:4971",
"name": "myelofibrosis",
"description": "A myeloid neoplasm that is located in the bone marrow which results in bone marrow being replaced by fibrous (scar) tissue."
},
"synonyms": [
{
"id": "DOID:4971",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:4971",
"name": "Agnogenic myeloid metaplasia",
"description": ""
},
{
"id": "DOID:4971",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:4971",
"name": "Aleukemic myelosis",
"description": ""
},
{
"id": "DOID:4971",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:4971",
"name": "Megakaryocytic myelosclerosis",
"description": ""
},
{
"id": "DOID:4971",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:4971",
"name": "bone Marrow Fibrosis",
"description": ""
},
{
"id": "DOID:4971",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:4971",
"name": "myelosclerosis",
"description": ""
},
{
"id": "DOID:4971",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:4971",
"name": "primary myelofibrosis",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "primary myelofibrosis",
"description": "Myelofibrosis with myeloid metaplasia is a myeloproliferative disease with annual incidence of approximately 1 case per 100,000 individuals and age at diagnosis around 60 (an increased prevalence is noted in Ashkenazi Jews). Clinical manifestations depend on the type of blood cell affected and may include anemia, pallor, splenomegaly, hypermetabolic state, petechiae, ecchymosis, bleeding, lymphadenopathy, hepatomegaly, portal hypertension."
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "AMM",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "Agnogenic myeloid metaplasia",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "CIMF",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "aleukemic myelosis",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "bone marrow fibrosis",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "chronic idiopathic myelofibrosis",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "idiopathic bone marrow fibrosis",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "idiopathic myelofibrosis",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "megakaryocytic myelosclerosis",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "myelofibrosis with myeloid metaplasia, somatic",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "myelofibrosis, somatic",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "myelosclerosis",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "myelosclerosis with myeloid metaplasia",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "osteomyelofibrosis",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "primary myelofibrosis",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "myelofibrosis with myeloid metaplasia",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "myelofibrosis",
"description": ""
},
{
"id": "MONDO:0009692",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009692",
"name": "myeloid metaplasia",
"description": ""
},
{
"id": "MIM:254450",
"resource": "MIM",
"url": "https://www.omim.org/entry/254450",
"name": "Myelofibrosis with myeloid metaplasia",
"description": "Myelofibrosis with myeloid metaplasia"
}
],
"evidence": [
{
"id": "254450",
"database": "MIM",
"url": "https://www.omim.org/entry/254450"
}
]
},
{
"disease_id": "DOID:8997",
"recommended_name": {
"id": "DOID:8997",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:8997",
"name": "polycythemia vera",
"description": "A myeloproliferative neoplasm characterized by erythroid hyperplasia, myeloid leukocytosis, thrombocytosis, and splenomegaly."
},
"synonyms": [
{
"id": "DOID:8997",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:8997",
"name": "chronic erythremia",
"description": ""
},
{
"id": "DOID:8997",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:8997",
"name": "Osler-Vaquez syndrome",
"description": ""
},
{
"id": "DOID:8997",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:8997",
"name": "Polycythaemia rubra vera",
"description": ""
},
{
"id": "DOID:8997",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:8997",
"name": "Proliferative polycythaemia",
"description": ""
},
{
"id": "MONDO:0009891",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009891",
"name": "acquired polycythemia vera",
"description": "Polycythemia vera (PV) is an acquired myeloproliferative disorder characterized by an elevated absolute red blood cell mass caused by uncontrolled red blood cell production, frequently associated with uncontrolled white blood cell and platelet production."
},
{
"id": "MONDO:0009891",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009891",
"name": "Osler-Vaquez disease",
"description": ""
},
{
"id": "MONDO:0009891",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009891",
"name": "Osler-Vaquez syndrome",
"description": ""
},
{
"id": "MONDO:0009891",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009891",
"name": "PV",
"description": ""
},
{
"id": "MONDO:0009891",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009891",
"name": "Vaquez disease",
"description": ""
},
{
"id": "MONDO:0009891",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009891",
"name": "acquired primary erythrocytosis",
"description": ""
},
{
"id": "MONDO:0009891",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009891",
"name": "polycythaemia rubra vera",
"description": ""
},
{
"id": "MONDO:0009891",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009891",
"name": "polycythemia rubra vera",
"description": ""
},
{
"id": "MONDO:0009891",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009891",
"name": "polycythemia vera",
"description": ""
},
{
"id": "MONDO:0009891",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009891",
"name": "polycythemia vera, somatic",
"description": ""
},
{
"id": "MONDO:0009891",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009891",
"name": "proliferative polycythaemia",
"description": ""
},
{
"id": "MONDO:0009891",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009891",
"name": "PRV",
"description": ""
},
{
"id": "MONDO:0009891",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0009891",
"name": "primary polycythemia",
"description": ""
},
{
"id": "MIM:263300",
"resource": "MIM",
"url": "https://www.omim.org/entry/263300",
"name": "Polycythemia vera",
"description": "Polycythemia vera"
}
],
"evidence": [
{
"id": "263300",
"database": "MIM",
"url": "https://www.omim.org/entry/263300"
}
]
},
{
"disease_id": "DOID:9119",
"recommended_name": {
"id": "DOID:9119",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:9119",
"name": "acute myeloid leukemia",
"description": "A myeloid leukemia that is characterized by the rapid growth of abnormal white blood cells that accumulate in the bone marrow and interfere with the production of normal blood cells."
},
"synonyms": [
{
"id": "DOID:9119",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:9119",
"name": "AML - acute Myeloid Leukemia",
"description": ""
},
{
"id": "DOID:9119",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:9119",
"name": "Leukemia, Myelocytic, acute",
"description": ""
},
{
"id": "DOID:9119",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:9119",
"name": "acute myeloblastic leukaemia",
"description": ""
},
{
"id": "DOID:9119",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:9119",
"name": "acute myeloblastic leukemia",
"description": ""
},
{
"id": "DOID:9119",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:9119",
"name": "acute myelogenous leukaemia",
"description": ""
},
{
"id": "DOID:9119",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:9119",
"name": "acute myelogenous leukemia",
"description": ""
},
{
"id": "DOID:9119",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:9119",
"name": "acute myeloid leukaemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute myeloid leukemia",
"description": "Acute myeloid leukemia (AML) is a group of neoplasms arising from precursor cells committed to the myeloid cell-line differentiation. All of them are characterized by clonal expansion of myeloid blasts. AML manifests by fever, pallor, anemia, hemorrhages and recurrent infections."
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "AML",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "AML - acute myeloid leukaemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "AML - acute myeloid leukemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "ANLL",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute Nonlymphocytic leukaemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute Nonlymphocytic leukemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute granulocytic leukaemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute granulocytic leukemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute myeloblastic leukaemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute myeloblastic leukemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute myelocytic leukaemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute myelocytic leukemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute myelogenous leukaemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute myelogenous leukemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute myelogenous leukemias",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute myeloid leukaemia (AML)",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute myeloid leukemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute myeloid leukemia (AML)",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute myeloid leukemia, somatic",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute nonlymphocytic leukaemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute nonlymphocytic leukemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "hematopoeitic - acute Myleogenous leukaemia (AML)",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "hematopoeitic - acute Myleogenous leukemia (AML)",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "leukemia, acute myeloid, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "leukemia, acute myeloid, reduced survival in, somatic",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "leukemia, acute myeloid, somatic",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "leukemia, acute myeloid, susceptibility to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "leukemia, myelocytic, acute",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "myeloid leukemia, acute",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "myeloid leukemia, acute, M4/M4Eo subtype, somatic",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute non lymphoblastic leukaemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "acute non lymphoblastic leukemia",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "leukemia, acute myelogenous",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "leukemia, acute myeloid",
"description": ""
},
{
"id": "MONDO:0018874",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0018874",
"name": "leukemia, acute myeloid, susceptibility to",
"description": ""
},
{
"id": "MIM:601626",
"resource": "MIM",
"url": "https://www.omim.org/entry/601626",
"name": "Leukemia, acute myelogenous",
"description": "Leukemia, acute myelogenous"
}
],
"evidence": [
{
"id": "601626",
"database": "MIM",
"url": "https://www.omim.org/entry/601626"
}
]
}
],
"snv": [
{
"evidence": [
{
"id": "O60674",
"database": "BioMuta",
"url": "https://hive.biochemistry.gwu.edu/biomuta/proteinview/O60674"
}
],
"glycoeffect": [],
"start_pos": 319,
"end_pos": 319,
"subjects_tested": "0",
"subjects_positive": "0",
"frequency": "0.0",
"sequence_org": "D",
"sequence_mut": "N",
"comment": "Somatic mutation passed 1 out of 6 filters: num. of cancers (3).",
"chr_id": "9",
"chr_pos": "5055687",
"ref_nt": "G",
"alt_nt": "A",
"minor_allelic_frequency": "",
"site_lbl": "D319",
"disease": [
{
"disease_id": "DOID:363",
"recommended_name": {
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "uterine cancer",
"description": "A female reproductive organ cancer that is located_in the uterus."
},
"synonyms": [
{
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "CA - cancer of uterus",
"description": ""
},
{
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "Tumour of uterus",
"description": ""
},
{
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "malignant neoplasm of uterus",
"description": ""
},
{
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "malignant uterine tumor",
"description": ""
},
{
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "neoplasm of uterus",
"description": ""
},
{
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "uterine tumor",
"description": ""
},
{
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "uterus neoplasm",
"description": ""
}
]
},
{
"disease_id": "DOID:9256",
"recommended_name": {
"id": "DOID:9256",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:9256",
"name": "colorectal cancer",
"description": "A large intestine cancer that is located_in the colon and/or located_in the rectum."
},
"synonyms": [
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colorectal cancer",
"description": "A primary or metastatic malignant neoplasm that affects the colon or rectum. Representative examples include carcinoma, lymphoma, and sarcoma."
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "cancer of colorectum",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "cancer of large bowel",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "cancer of large intestine",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "cancer of the large bowel",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colon cancer, advanced, somatic",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colon cancer, somatic",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colorectal cancer",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colorectal cancer with chromosomal instability, somatic",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colorectal cancer, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colorectal cancer, somatic",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colorectal cancer, susceptibility to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colorectum cancer",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant colorectal neoplasm",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant colorectal tumor",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant colorectal tumour",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant colorectum neoplasm",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant large bowel neoplasm",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant large bowel tumor",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant large bowel tumour",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant large intestine neoplasm",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant large intestine tumor",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant large intestine tumour",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant neoplasm of colorectum",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant neoplasm of large bowel",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant neoplasm of large intestine",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant neoplasm of the large bowel",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
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{
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{
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{
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{
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{
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{
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{
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},
{
"id": "MONDO:0005575",
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"name": "colon cancer",
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},
{
"id": "MONDO:0005575",
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},
{
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{
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{
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{
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{
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{
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{
"id": "MONDO:0012244",
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{
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{
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},
{
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{
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{
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{
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{
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{
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{
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{
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{
"id": "MONDO:0012758",
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{
"id": "MONDO:0012758",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012758",
"name": "prostate cancer, hereditary, 13",
"description": ""
},
{
"id": "MONDO:0012758",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012758",
"name": "prostate cancer, hereditary, type 13",
"description": ""
},
{
"id": "MONDO:0012758",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012758",
"name": "HPC13",
"description": ""
},
{
"id": "MONDO:0011270",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011270",
"name": "prostate cancer, hereditary, 8",
"description": ""
},
{
"id": "MONDO:0011270",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011270",
"name": "prostate cancer, hereditary, 8",
"description": ""
},
{
"id": "MONDO:0011270",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011270",
"name": "prostate cancer, hereditary, type 8",
"description": ""
},
{
"id": "MONDO:0011270",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011270",
"name": "HPC8",
"description": ""
},
{
"id": "MONDO:0011270",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011270",
"name": "predisposing for prostate cancer",
"description": ""
},
{
"id": "MONDO:0011270",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011270",
"name": "prostate cancer, susceptibility to",
"description": ""
},
{
"id": "MONDO:0012300",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012300",
"name": "prostate cancer, hereditary, 6",
"description": ""
},
{
"id": "MONDO:0012300",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012300",
"name": "prostate cancer, hereditary, 6",
"description": ""
},
{
"id": "MONDO:0012300",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012300",
"name": "prostate cancer, hereditary, type 6",
"description": ""
},
{
"id": "MONDO:0012300",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012300",
"name": "HPC6",
"description": ""
},
{
"id": "MONDO:0012300",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012300",
"name": "prostate cancer, susceptibility to",
"description": ""
},
{
"id": "MONDO:0012620",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012620",
"name": "prostate cancer, hereditary, 10",
"description": ""
},
{
"id": "MONDO:0012620",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012620",
"name": "HPC10",
"description": ""
},
{
"id": "MONDO:0012620",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012620",
"name": "prostate cancer, hereditary, 10",
"description": ""
},
{
"id": "MONDO:0023122",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0023122",
"name": "familial prostate carcinoma",
"description": "Prostate carcinoma that has developed in relatives of patients with a history of prostate carcinoma."
},
{
"id": "MONDO:0023122",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0023122",
"name": "familial prostate cancer",
"description": ""
},
{
"id": "MONDO:0023122",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0023122",
"name": "hereditary prostate cancer",
"description": ""
},
{
"id": "MONDO:0023122",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0023122",
"name": "hereditary prostate carcinoma",
"description": ""
},
{
"id": "MONDO:0023122",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0023122",
"name": "prostate cancer, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0023122",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0023122",
"name": "prostate cancer, familial, susceptibility to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0023122",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0023122",
"name": "prostate cancer, somatic",
"description": ""
},
{
"id": "MONDO:0023122",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0023122",
"name": "prostate cancer, susceptibility to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0023122",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0023122",
"name": "prostate cancer, familial",
"description": ""
},
{
"id": "MONDO:0023122",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0023122",
"name": "prostate cancer, hereditary",
"description": ""
},
{
"id": "MONDO:0012470",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012470",
"name": "prostate cancer, hereditary, 7",
"description": ""
},
{
"id": "MONDO:0012470",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012470",
"name": "HPC7",
"description": ""
},
{
"id": "MONDO:0012470",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012470",
"name": "prostate cancer, hereditary, 7",
"description": ""
},
{
"id": "MONDO:0012470",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012470",
"name": "prostate cancer aggressiveness",
"description": ""
},
{
"id": "MONDO:0011098",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011098",
"name": "prostate cancer, hereditary, 1",
"description": "Any familial prostate cancer in which the cause of the disease is a mutation in the RNASEL gene."
},
{
"id": "MONDO:0011098",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011098",
"name": "RNASEL familial prostate cancer",
"description": ""
},
{
"id": "MONDO:0011098",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011098",
"name": "familial prostate cancer caused by mutation in RNASEL",
"description": ""
},
{
"id": "MONDO:0011098",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011098",
"name": "prostate cancer 1",
"description": ""
},
{
"id": "MONDO:0011098",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011098",
"name": "prostate cancer, hereditary, 1",
"description": ""
},
{
"id": "MONDO:0011098",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011098",
"name": "prostate cancer, hereditary, type 1",
"description": ""
},
{
"id": "MONDO:0011098",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011098",
"name": "HPC1",
"description": ""
},
{
"id": "MONDO:0011098",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0011098",
"name": "Prca1",
"description": ""
},
{
"id": "MONDO:0012768",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012768",
"name": "prostate cancer, hereditary, 11",
"description": ""
},
{
"id": "MONDO:0012768",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012768",
"name": "HPC11",
"description": ""
},
{
"id": "MONDO:0012768",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012768",
"name": "prostate cancer, hereditary, 11",
"description": ""
},
{
"id": "MONDO:0012769",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012769",
"name": "prostate cancer, hereditary, 14",
"description": ""
},
{
"id": "MONDO:0012769",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012769",
"name": "HPC14",
"description": ""
},
{
"id": "MONDO:0012769",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012769",
"name": "prostate cancer, hereditary, 14",
"description": ""
},
{
"id": "MONDO:0012770",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012770",
"name": "prostate cancer, hereditary, 15",
"description": ""
},
{
"id": "MONDO:0012770",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012770",
"name": "HPC15",
"description": ""
},
{
"id": "MONDO:0012770",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012770",
"name": "prostate cancer, hereditary, 15",
"description": ""
},
{
"id": "MONDO:0010257",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0010257",
"name": "prostate cancer, hereditary, X-linked 1",
"description": ""
},
{
"id": "MONDO:0010257",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0010257",
"name": "HPCX1",
"description": ""
},
{
"id": "MONDO:0010257",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0010257",
"name": "prostate cancer, hereditary, X-linked 1",
"description": ""
},
{
"id": "MONDO:0010257",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0010257",
"name": "prostate cancer susceptibility, X-linked",
"description": ""
},
{
"id": "MONDO:0010405",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0010405",
"name": "prostate cancer, hereditary, X-linked 2",
"description": ""
},
{
"id": "MONDO:0010405",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0010405",
"name": "HPCX2",
"description": ""
},
{
"id": "MONDO:0010405",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0010405",
"name": "prostate cancer, hereditary, X-linked 2",
"description": ""
},
{
"id": "MIM:611868",
"resource": "MIM",
"url": "https://www.omim.org/entry/611868",
"name": "Prostate cancer, hereditary, 12",
"description": "Prostate cancer, hereditary, 12"
},
{
"id": "MIM:611928",
"resource": "MIM",
"url": "https://www.omim.org/entry/611928",
"name": "Prostate cancer, hereditary, 13",
"description": "Prostate cancer, hereditary, 13"
},
{
"id": "MIM:176807",
"resource": "MIM",
"url": "https://www.omim.org/entry/176807",
"name": "Prostate cancer",
"description": "Prostate cancer"
},
{
"id": "MIM:601518",
"resource": "MIM",
"url": "https://www.omim.org/entry/601518",
"name": "Prostate cancer, hereditary, 1",
"description": "Prostate cancer, hereditary, 1"
},
{
"id": "MIM:611955",
"resource": "MIM",
"url": "https://www.omim.org/entry/611955",
"name": "Prostate cancer, hereditary, 11",
"description": "Prostate cancer, hereditary, 11"
}
]
}
]
},
{
"significant": "No",
"trend": "up",
"name": "Stomach cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:10534",
"evidence": [
{
"database": "BioXpress",
"id": "O60674",
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}
],
"disease": [
{
"disease_id": "DOID:10534",
"recommended_name": {
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"resource": "Disease Ontology",
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},
"synonyms": [
{
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"name": "gastric cancer",
"description": ""
},
{
"id": "DOID:10534",
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"url": "http://disease-ontology.org/term/DOID:10534",
"name": "gastric neoplasm",
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},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "gastric cancer",
"description": "A primary or metastatic malignant neoplasm involving the stomach."
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "gastric neoplasm",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "Ca lesser curvature - stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "cancer of stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "gastric cancer",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "gastric cancer risk after h. pylori infection",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "gastric cancer, somatic",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant gastric neoplasm",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant gastric tumor",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant gastric tumour",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant neoplasm of lesser curve of stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant neoplasm of stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant neoplasm of the stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant stomach neoplasm",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant tumor of body of stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant tumor of greater curve of stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant tumor of lesser curve of stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant tumor of stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant tumor of the stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant tumour of body of stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant tumour of greater curve of stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant tumour of lesser curve of stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant tumour of stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant tumour of the stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "stomach cancer",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "Ca body - stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "ca greater curvature of stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "malignant neoplasm of body of stomach",
"description": ""
},
{
"id": "MONDO:0001056",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001056",
"name": "gastric cancer, intestinal",
"description": ""
},
{
"id": "MIM:613659",
"resource": "MIM",
"url": "https://www.omim.org/entry/613659",
"name": "Gastric cancer",
"description": "Gastric cancer"
}
]
}
]
},
{
"significant": "Yes",
"trend": "down",
"name": "Urinary bladder cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:11054",
"evidence": [
{
"database": "BioXpress",
"id": "O60674",
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}
],
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{
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},
"synonyms": [
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"url": "http://disease-ontology.org/term/DOID:11054",
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},
{
"id": "DOID:11054",
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"url": "http://disease-ontology.org/term/DOID:11054",
"name": "tumor of the bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "urinary bladder cancer",
"description": "A primary or metastatic malignant neoplasm involving the bladder."
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "tumor of the bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "tumour of the bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "bladder cancer, somatic",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "cancer of urinary bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant bladder neoplasm",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant bladder tumor",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant bladder tumour",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant neoplasm of bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant neoplasm of the bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant neoplasm of the urinary bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant neoplasm of urinary bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant neoplasm, bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant neoplasm, urinary bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant tumor of bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant tumor of the bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant tumor of the urinary bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant tumor of urinary bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant tumor, urinary bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant tumour of bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant tumour of the bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant tumour of the urinary bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant tumour of urinary bladder",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant urinary bladder neoplasm",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant urinary bladder tumor",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "malignant urinary bladder tumour",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "urinary bladder cancer",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "urinary bladder malignant neoplasm",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "urinary bladder malignant tumor",
"description": ""
},
{
"id": "MONDO:0001187",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0001187",
"name": "urinary bladder malignant tumour",
"description": ""
},
{
"id": "MIM:109800",
"resource": "MIM",
"url": "https://www.omim.org/entry/109800",
"name": "Bladder cancer",
"description": "Bladder cancer"
}
]
}
]
},
{
"significant": "No",
"trend": "down",
"name": "Head and neck cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:11934",
"evidence": [
{
"database": "BioXpress",
"id": "O60674",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/O60674"
}
],
"disease": [
{
"disease_id": "DOID:11934",
"recommended_name": {
"id": "DOID:11934",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:11934",
"name": "head and neck cancer",
"description": "An organ system cancer that arises in the head or neck region. This region includes the nasal cavity, sinuses, lips, mouth, salivary glands, throat, or larynx."
},
"synonyms": [
{
"id": "DOID:11934",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:11934",
"name": "head and neck neoplasm",
"description": ""
},
{
"id": "DOID:11934",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:11934",
"name": "head and neck tumours",
"description": ""
},
{
"id": "DOID:11934",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:11934",
"name": "head/neck neoplasm",
"description": ""
},
{
"id": "DOID:11934",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:11934",
"name": "tumor of head and neck",
"description": ""
}
]
}
]
},
{
"significant": "Yes",
"trend": "down",
"name": "Lung cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:1324",
"evidence": [
{
"database": "BioXpress",
"id": "O60674",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/O60674"
}
],
"disease": [
{
"disease_id": "DOID:1324",
"recommended_name": {
"id": "DOID:1324",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1324",
"name": "lung cancer",
"description": "A respiratory system cancer that is located_in the lung."
},
"synonyms": [
{
"id": "MONDO:0012159",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012159",
"name": "lung cancer susceptibility 1",
"description": ""
},
{
"id": "MONDO:0012159",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012159",
"name": "LNCR1",
"description": ""
},
{
"id": "MONDO:0012159",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012159",
"name": "lung cancer susceptibility",
"description": ""
},
{
"id": "MONDO:0012159",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012159",
"name": "lung cancer susceptibility 1",
"description": ""
},
{
"id": "MONDO:0012942",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012942",
"name": "lung cancer susceptibility 3",
"description": ""
},
{
"id": "MONDO:0012942",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012942",
"name": "LNCR3",
"description": ""
},
{
"id": "MONDO:0012942",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012942",
"name": "lung cancer susceptibility 3",
"description": ""
},
{
"id": "MONDO:0012942",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012942",
"name": "adenocarcinoma of lung, susceptibility to",
"description": ""
},
{
"id": "MONDO:0012955",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012955",
"name": "lung cancer susceptibility 4",
"description": ""
},
{
"id": "MONDO:0012955",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012955",
"name": "LNCR4",
"description": ""
},
{
"id": "MONDO:0012955",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012955",
"name": "lung cancer susceptibility 4",
"description": ""
},
{
"id": "MONDO:0013631",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0013631",
"name": "lung cancer susceptibility 5",
"description": ""
},
{
"id": "MONDO:0013631",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0013631",
"name": "LNCR5",
"description": ""
},
{
"id": "MONDO:0013631",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0013631",
"name": "lung cancer susceptibility 5",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "lung cancer",
"description": "A malignant neoplasm involving the lung."
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "adenocarcinoma of lung, response to tyrosine kinase inhibitor in, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "adenocarcinoma of lung, somatic",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "cancer of lung",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "lung cancer",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "lung cancer, protection against, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "lung cancer, resistance to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "lung cancer, somatic",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "lung cancer, susceptibility to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "malignant lung neoplasm",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "malignant lung tumor",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "malignant lung tumour",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "malignant neoplasm of lung",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "malignant neoplasm of the lung",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "malignant tumor of lung",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "malignant tumor of the lung",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "malignant tumour of lung",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "malignant tumour of the lung",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "nonsmall cell lung cancer, response to tyrosine kinase inhibitor in, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "nonsmall cell lung cancer, somatic",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "nonsmall cell lung cancer, susceptibility to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "Nonsmall cell lung cancer",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "alveolar cell carcinoma",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "lung cancer, protection against",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "lung neoplasm",
"description": ""
},
{
"id": "MIM:211980",
"resource": "MIM",
"url": "https://www.omim.org/entry/211980",
"name": "Lung cancer",
"description": "Lung cancer"
}
]
}
]
},
{
"significant": "Yes",
"trend": "down",
"name": "Breast cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:1612",
"evidence": [
{
"database": "BioXpress",
"id": "O60674",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/O60674"
}
],
"disease": [
{
"disease_id": "DOID:1612",
"recommended_name": {
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
"name": "breast cancer",
"description": "A thoracic cancer that originates in the mammary gland."
},
"synonyms": [
{
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
"name": "breast tumor",
"description": ""
},
{
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
"name": "malignant neoplasm of breast",
"description": ""
},
{
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
"name": "malignant tumor of the breast",
"description": ""
},
{
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
"name": "mammary cancer",
"description": ""
},
{
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
"name": "mammary tumor",
"description": ""
},
{
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
"name": "primary breast cancer",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "hereditary breast carcinoma",
"description": "Breast carcinoma that has developed in relatives of patients with history of breast carcinoma."
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer susceptibility, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, early-onset, susceptibility to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, invasive ductal, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, lobular, somatic",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, male, susceptibility to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, protection against, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, somatic",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, susceptibility to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "familial breast cancer",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "familial breast carcinoma",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "familial cancer of breast",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "familial cancer of the breast",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "hereditary breast cancer",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "hereditary breast carcinoma",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, familial",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, familial Male",
"description": ""
},
{
"id": "MIM:114480",
"resource": "MIM",
"url": "https://www.omim.org/entry/114480",
"name": "Breast cancer",
"description": "Breast cancer"
}
]
}
]
},
{
"significant": "Yes",
"trend": "down",
"name": "Thyroid cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:1781",
"evidence": [
{
"database": "BioXpress",
"id": "O60674",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/O60674"
}
],
"disease": [
{
"disease_id": "DOID:1781",
"recommended_name": {
"id": "DOID:1781",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1781",
"name": "thyroid cancer",
"description": "An endocrine gland cancer located in the thryoid gland located in the neck below the thyroid cartilage."
},
"synonyms": [
{
"id": "DOID:1781",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1781",
"name": "thyroid gland cancer",
"description": ""
},
{
"id": "DOID:1781",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1781",
"name": "Thyroid gland neoplasm",
"description": ""
},
{
"id": "DOID:1781",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1781",
"name": "malignant neoplasm of thyroid gland",
"description": ""
},
{
"id": "DOID:1781",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1781",
"name": "malignant tumour of thyroid gland",
"description": ""
},
{
"id": "DOID:1781",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1781",
"name": "neoplasm of thyroid gland",
"description": ""
},
{
"id": "DOID:1781",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1781",
"name": "thyroid neoplasm",
"description": ""
}
]
}
]
},
{
"significant": "Yes",
"trend": "down",
"name": "Kidney cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:263",
"evidence": [
{
"database": "BioXpress",
"id": "O60674",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/O60674"
}
],
"disease": [
{
"disease_id": "DOID:263",
"recommended_name": {
"id": "DOID:263",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:263",
"name": "kidney cancer",
"description": "A urinary system cancer that is located_in the kidney."
},
"synonyms": [
{
"id": "DOID:263",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:263",
"name": "malignant neoplasm of kidney except pelvis",
"description": ""
},
{
"id": "DOID:263",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:263",
"name": "malignant tumour of kidney",
"description": ""
},
{
"id": "DOID:263",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:263",
"name": "renal cancer",
"description": ""
}
]
}
]
},
{
"significant": "Yes",
"trend": "down",
"name": "Liver cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:3571",
"evidence": [
{
"database": "BioXpress",
"id": "O60674",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/O60674"
}
],
"disease": [
{
"disease_id": "DOID:3571",
"recommended_name": {
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "liver cancer",
"description": "A hepatobiliary system cancer that is located_in the liver."
},
"synonyms": [
{
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "Ca liver - primary",
"description": ""
},
{
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "Resectable malignant neoplasm of Liver",
"description": ""
},
{
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "hepatic cancer",
"description": ""
},
{
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "hepatic neoplasm",
"description": ""
},
{
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "malignant hepato-biliary neoplasm",
"description": ""
},
{
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "malignant neoplasm of liver",
"description": ""
},
{
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "malignant neoplasm of liver, primary",
"description": ""
},
{
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "malignant tumor of liver",
"description": ""
},
{
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "neoplasm of liver",
"description": ""
},
{
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "non-resectable primary hepatic malignant neoplasm",
"description": ""
},
{
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "primary liver cancer",
"description": ""
},
{
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "primary malignant neoplasm of liver",
"description": ""
},
{
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "resectable malignant neoplasm of the liver",
"description": ""
},
{
"id": "DOID:3571",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:3571",
"name": "malignant neoplasm of liver, not specified as primary or secondary",
"description": ""
}
]
}
]
},
{
"significant": "Yes",
"trend": "down",
"name": "Uterine cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:363",
"evidence": [
{
"database": "BioXpress",
"id": "O60674",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/O60674"
}
],
"disease": [
{
"disease_id": "DOID:363",
"recommended_name": {
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "uterine cancer",
"description": "A female reproductive organ cancer that is located_in the uterus."
},
"synonyms": [
{
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "CA - cancer of uterus",
"description": ""
},
{
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "Tumour of uterus",
"description": ""
},
{
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "malignant neoplasm of uterus",
"description": ""
},
{
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "malignant uterine tumor",
"description": ""
},
{
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "neoplasm of uterus",
"description": ""
},
{
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "uterine tumor",
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},
{
"id": "DOID:363",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:363",
"name": "uterus neoplasm",
"description": ""
}
]
}
]
},
{
"significant": "No",
"trend": "up",
"name": "Esophageal cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:5041",
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{
"database": "BioXpress",
"id": "O60674",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/O60674"
}
],
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{
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"id": "DOID:5041",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:5041",
"name": "esophageal cancer",
"description": "A gastrointestinal system cancer that is located_in the esophagus."
},
"synonyms": [
{
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"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:5041",
"name": "Ca lower third oesophagus",
"description": ""
},
{
"id": "DOID:5041",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:5041",
"name": "Ca middle third oesophagus",
"description": ""
},
{
"id": "DOID:5041",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:5041",
"name": "esophagus cancer",
"description": ""
},
{
"id": "DOID:5041",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:5041",
"name": "malignant neoplasm of distal third of esophagus",
"description": ""
},
{
"id": "DOID:5041",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:5041",
"name": "malignant neoplasm of lower third of oesophagus",
"description": ""
},
{
"id": "DOID:5041",
"resource": "Disease Ontology",
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"name": "malignant neoplasm of middle third of oesophagus",
"description": ""
},
{
"id": "DOID:5041",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:5041",
"name": "malignant neoplasm of proximal third of esophagus",
"description": ""
},
{
"id": "DOID:5041",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:5041",
"name": "malignant neoplasm of upper third esophagus",
"description": ""
},
{
"id": "DOID:5041",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:5041",
"name": "malignant tumor of Distal Third of esophagus",
"description": ""
},
{
"id": "DOID:5041",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:5041",
"name": "malignant tumor of Proximal Third of esophagus",
"description": ""
},
{
"id": "DOID:5041",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:5041",
"name": "malignant tumor of abdominal esophagus",
"description": ""
},
{
"id": "DOID:5041",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:5041",
"name": "malignant tumor of the middle Third of the esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "esophageal cancer",
"description": "A primary or metastatic malignant neoplasm involving the esophagus."
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "cancer of esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "cancer of oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "esophageal cancer",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "esophageal cancer, somatic",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "esophageal carcinoma, somatic",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "esophageal squamous cell carcinoma, somatic",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "esophagus cancer",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant esophageal neoplasm",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant esophageal tumor",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant esophageal tumour",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant esophagus neoplasm",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant esophagus tumor",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant neoplasm of esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant neoplasm of oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant neoplasm of the esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant neoplasm of the oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant oesophagus neoplasm",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant oesophagus tumour",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant tumor of esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant tumor of the esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant tumour of oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant tumour of the oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "oesophagus cancer",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "Ca lower third esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "Ca lower third oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "Ca middle third esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "Ca middle third oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant neoplasm of distal third of esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant neoplasm of distal third of oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant neoplasm of lower third of esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
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"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant neoplasm of lower third of oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant neoplasm of middle third of esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant neoplasm of middle third of oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant neoplasm of proximal third of esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant neoplasm of proximal third of oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant neoplasm of upper third esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant neoplasm of upper third oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant tumor of abdominal esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant tumor of distal third of esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant tumor of proximal third of esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant tumor of the middle third of the esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant tumour of abdominal oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant tumour of distal third of oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant tumour of proximal third of oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "malignant tumour of the middle third of the oesophagus",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "Aerodigestive tract cancer, susceptibility to",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "Escc, susceptibility to",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "esophageal squamous cell carcinoma, susceptibility to",
"description": ""
},
{
"id": "MONDO:0007576",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0007576",
"name": "gastric cardia adenocarcinoma, susceptibility to",
"description": ""
},
{
"id": "MIM:133239",
"resource": "MIM",
"url": "https://www.omim.org/entry/133239",
"name": "Esophageal cancer",
"description": "Esophageal cancer"
}
]
}
]
},
{
"significant": "Yes",
"trend": "down",
"name": "Colorectal cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:9256",
"evidence": [
{
"database": "BioXpress",
"id": "O60674",
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],
"disease": [
{
"disease_id": "DOID:9256",
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"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:9256",
"name": "colorectal cancer",
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},
"synonyms": [
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colorectal cancer",
"description": "A primary or metastatic malignant neoplasm that affects the colon or rectum. Representative examples include carcinoma, lymphoma, and sarcoma."
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "cancer of colorectum",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "cancer of large bowel",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "cancer of large intestine",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "cancer of the large bowel",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colon cancer, advanced, somatic",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colon cancer, somatic",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colorectal cancer",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colorectal cancer with chromosomal instability, somatic",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colorectal cancer, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "colorectal cancer, somatic",
"description": ""
},
{
"id": "MONDO:0005575",
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"name": "colorectal cancer, susceptibility to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0005575",
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"name": "colorectum cancer",
"description": ""
},
{
"id": "MONDO:0005575",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0005575",
"name": "malignant colorectal neoplasm",
"description": ""
},
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{
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"length": 1132
},
"evidence": [
{
"id": "45917234",
"url": "http://www.informatics.jax.org/homology/45917234",
"database": "MGI"
},
{
"id": "O60674",
"url": "https://omabrowser.org/oma/group/O60674/",
"database": "OMA"
}
],
"common_name": "Rat"
}
],
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"categories": [
{
"name": "Biological Process",
"total": 100,
"go_terms": [
{
"name": "positive regulation of protein import into nucleus",
"id": "GO:0042307",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042307",
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{
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}
],
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{
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{
"database": "UniProtKB",
"id": "O60674",
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}
],
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},
{
"name": "positive regulation of growth hormone receptor signaling pathway",
"id": "GO:0060399",
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{
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}
],
"pmid": ""
},
{
"name": "regulation of receptor signaling pathway via JAK-STAT",
"id": "GO:0046425",
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"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "positive regulation of interleukin-17 production",
"id": "GO:0032740",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0032740",
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{
"database": "UniProtKB",
"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "interleukin-5-mediated signaling pathway",
"id": "GO:0038043",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0038043",
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{
"database": "UniProtKB",
"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "interleukin-3-mediated signaling pathway",
"id": "GO:0038156",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0038156",
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{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "microglial cell activation",
"id": "GO:0001774",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0001774",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "protein phosphorylation",
"id": "GO:0006468",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006468",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "immune response",
"id": "GO:0006955",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006955",
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{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "signal transduction",
"id": "GO:0007165",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007165",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "G protein-coupled receptor signaling pathway",
"id": "GO:0007186",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007186",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "positive regulation of cytosolic calcium ion concentration",
"id": "GO:0007204",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007204",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
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}
],
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},
{
"name": "negative regulation of cell population proliferation",
"id": "GO:0008285",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0008285",
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"database": "UniProtKB",
"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "peptidyl-tyrosine phosphorylation",
"id": "GO:0018108",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0018108",
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"database": "UniProtKB",
"id": "O60674",
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}
],
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},
{
"name": "cell differentiation",
"id": "GO:0030154",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030154",
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"id": "O60674",
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}
],
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},
{
"name": "positive regulation of cell migration",
"id": "GO:0030335",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030335",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
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}
],
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},
{
"name": "positive regulation of insulin secretion",
"id": "GO:0032024",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0032024",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
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}
],
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},
{
"name": "response to lipopolysaccharide",
"id": "GO:0032496",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0032496",
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"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "response to tumor necrosis factor",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0034612",
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"url": "https://www.uniprot.org/uniprot/O60674"
}
],
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},
{
"name": "intracellular signal transduction",
"id": "GO:0035556",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035556",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "positive regulation of MAPK cascade",
"id": "GO:0043410",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043410",
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{
"database": "UniProtKB",
"id": "O60674",
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}
],
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},
{
"name": "post-translational protein modification",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043687",
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"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "positive regulation of nitric oxide biosynthetic process",
"id": "GO:0045429",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045429",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
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}
],
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},
{
"name": "positive regulation of transcription by RNA polymerase II",
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"database": "UniProtKB",
"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction",
"id": "GO:0051897",
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"id": "O60674",
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],
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{
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"id": "O60674",
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}
],
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},
{
"name": "positive regulation of apoptotic signaling pathway",
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"id": "O60674",
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}
],
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},
{
"name": "erythrocyte differentiation",
"id": "GO:0030218",
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"id": "O60674",
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}
],
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},
{
"name": "negative regulation of neuron apoptotic process",
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"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
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},
{
"name": "type II interferon-mediated signaling pathway",
"id": "GO:0060333",
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}
],
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},
{
"name": "cellular response to lipopolysaccharide",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0071222",
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"id": "O60674",
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}
],
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},
{
"name": "activation of cysteine-type endopeptidase activity involved in apoptotic process",
"id": "GO:0006919",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006919",
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"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "positive regulation of cell differentiation",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
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},
{
"name": "protein autophosphorylation",
"id": "GO:0046777",
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"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
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},
{
"name": "adaptive immune response",
"id": "GO:0002250",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0002250",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
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},
{
"name": "positive regulation of cell-substrate adhesion",
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{
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"id": "O60674",
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}
],
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},
{
"name": "negative regulation of cell-cell adhesion",
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"id": "O60674",
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],
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},
{
"name": "interleukin-12-mediated signaling pathway",
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"id": "O60674",
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}
],
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},
{
"name": "regulation of inflammatory response",
"id": "GO:0050727",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050727",
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"database": "UniProtKB",
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}
],
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},
{
"name": "cellular response to dexamethasone stimulus",
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}
],
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},
{
"name": "positive regulation of vascular associated smooth muscle cell proliferation",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:1904707",
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],
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},
{
"name": "positive regulation of tumor necrosis factor production",
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{
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}
],
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},
{
"name": "response to antibiotic",
"id": "GO:0046677",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0046677",
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"id": "O60674",
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}
],
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},
{
"name": "transcription by RNA polymerase II",
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}
],
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},
{
"name": "positive regulation of type II interferon production",
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"database": "UniProtKB",
"id": "O60674",
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}
],
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},
{
"name": "regulation of apoptotic process",
"id": "GO:0042981",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042981",
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}
],
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},
{
"name": "modulation of chemical synaptic transmission",
"id": "GO:0050804",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050804",
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"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "extrinsic apoptotic signaling pathway",
"id": "GO:0097191",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0097191",
"evidence": [
{
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"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "actin filament polymerization",
"id": "GO:0030041",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030041",
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"database": "UniProtKB",
"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "positive regulation of receptor signaling pathway via JAK-STAT",
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}
],
"pmid": ""
},
{
"name": "positive regulation of T cell proliferation",
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"database": "UniProtKB",
"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "tumor necrosis factor-mediated signaling pathway",
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}
],
"pmid": ""
},
{
"name": "positive regulation of interleukin-1 beta production",
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"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "negative regulation of cardiac muscle cell apoptotic process",
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{
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}
],
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},
{
"name": "cellular response to virus",
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"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "positive regulation of tyrosine phosphorylation of STAT protein",
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{
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}
],
"pmid": ""
},
{
"name": "platelet-derived growth factor receptor signaling pathway",
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"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "response to amine",
"id": "GO:0014075",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0014075",
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{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "cytokine-mediated signaling pathway",
"id": "GO:0019221",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019221",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "activation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway",
"id": "GO:0097296",
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{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "response to hydroperoxide",
"id": "GO:0033194",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0033194",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "tyrosine phosphorylation of STAT protein",
"id": "GO:0007260",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007260",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "growth hormone receptor signaling pathway",
"id": "GO:0060396",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0060396",
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"database": "UniProtKB",
"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "programmed cell death induced by symbiont",
"id": "GO:0034050",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0034050",
"evidence": [
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"database": "UniProtKB",
"id": "O60674",
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],
"pmid": ""
},
{
"name": "mesoderm development",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007498",
"evidence": [
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"database": "UniProtKB",
"id": "O60674",
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],
"pmid": ""
},
{
"name": "intrinsic apoptotic signaling pathway in response to oxidative stress",
"id": "GO:0008631",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0008631",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
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],
"pmid": ""
},
{
"name": "axon regeneration",
"id": "GO:0031103",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0031103",
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"database": "UniProtKB",
"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "positive regulation of SMAD protein signal transduction",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0060391",
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{
"database": "UniProtKB",
"id": "O60674",
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],
"pmid": ""
},
{
"name": "positive regulation of MHC class II biosynthetic process",
"id": "GO:0045348",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045348",
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{
"database": "UniProtKB",
"id": "O60674",
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],
"pmid": ""
},
{
"name": "regulation of nitric oxide biosynthetic process",
"id": "GO:0045428",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045428",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "positive regulation of platelet aggregation",
"id": "GO:1901731",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:1901731",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "receptor signaling pathway via JAK-STAT",
"id": "GO:0007259",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007259",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "positive regulation of nitric-oxide synthase biosynthetic process",
"id": "GO:0051770",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051770",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "enzyme-linked receptor protein signaling pathway",
"id": "GO:0007167",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007167",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "mineralocorticoid receptor signaling pathway",
"id": "GO:0031959",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0031959",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "mammary gland epithelium development",
"id": "GO:0061180",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0061180",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "response to interleukin-12",
"id": "GO:0070671",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070671",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "positive regulation of growth factor dependent skeletal muscle satellite cell proliferation",
"id": "GO:1902728",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:1902728",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "positive regulation of epithelial cell apoptotic process",
"id": "GO:1904037",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:1904037",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "interleukin-6-mediated signaling pathway",
"id": "GO:0070102",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070102",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "growth hormone receptor signaling pathway via JAK-STAT",
"id": "GO:0060397",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0060397",
"evidence": [
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "positive regulation of natural killer cell proliferation",
"id": "GO:0032819",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0032819",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "negative regulation of DNA binding",
"id": "GO:0043392",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043392",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "cellular response to interleukin-3",
"id": "GO:0036016",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0036016",
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"database": "UniProtKB",
"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "collagen-activated signaling pathway",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0038065",
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{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "interleukin-35-mediated signaling pathway",
"id": "GO:0070757",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070757",
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"database": "UniProtKB",
"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "positive regulation of cold-induced thermogenesis",
"id": "GO:0120162",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0120162",
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{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "post-embryonic hemopoiesis",
"id": "GO:0035166",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035166",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "activation of Janus kinase activity",
"id": "GO:0042976",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042976",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "positive regulation of T-helper 17 type immune response",
"id": "GO:2000318",
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{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "positive regulation of platelet activation",
"id": "GO:0010572",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0010572",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "positive regulation of signaling receptor activity",
"id": "GO:2000273",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:2000273",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "positive regulation of leukocyte proliferation",
"id": "GO:0070665",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070665",
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"database": "UniProtKB",
"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "regulation of postsynapse to nucleus signaling pathway",
"id": "GO:1905539",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:1905539",
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"database": "UniProtKB",
"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "granulocyte-macrophage colony-stimulating factor signaling pathway",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "positive regulation of cell population proliferation",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0008284",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "regulation of cell adhesion",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030155",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "phosphorylation",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0016310",
"evidence": [
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "chromatin organization",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006325",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
}
]
},
{
"name": "Cellular Component",
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"name": "glutamatergic synapse",
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"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "granulocyte macrophage colony-stimulating factor receptor complex",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030526",
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"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "nucleus",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005634",
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"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "nucleoplasm",
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"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
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],
"pmid": ""
},
{
"name": "cytoplasm",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005737",
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"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "cytosol",
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"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "cytoskeleton",
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"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "plasma membrane",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005886",
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"id": "O60674",
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}
],
"pmid": ""
},
{
"name": "focal adhesion",
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"id": "O60674",
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],
"pmid": ""
},
{
"name": "extrinsic component of cytoplasmic side of plasma membrane",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0031234",
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"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "endosome lumen",
"id": "GO:0031904",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0031904",
"evidence": [
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "membrane raft",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045121",
"evidence": [
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "postsynapse",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0098794",
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"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "extrinsic component of plasma membrane",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019897",
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"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "caveola",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005901",
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "euchromatin",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0000791",
"evidence": [
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"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "interleukin-12 receptor complex",
"id": "GO:0042022",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042022",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "interleukin-23 receptor complex",
"id": "GO:0072536",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0072536",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "endomembrane system",
"id": "GO:0012505",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0012505",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
}
]
},
{
"name": "Molecular Function",
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{
"name": "interleukin-12 receptor binding",
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"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "protein kinase activity",
"id": "GO:0004672",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004672",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "protein tyrosine kinase activity",
"id": "GO:0004713",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004713",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "non-membrane spanning protein tyrosine kinase activity",
"id": "GO:0004715",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004715",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "signaling receptor binding",
"id": "GO:0005102",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005102",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "ATP binding",
"id": "GO:0005524",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005524",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "protein kinase binding",
"id": "GO:0019901",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019901",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "acetylcholine receptor binding",
"id": "GO:0033130",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0033130",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "identical protein binding",
"id": "GO:0042802",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042802",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "metal ion binding",
"id": "GO:0046872",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0046872",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "SH2 domain binding",
"id": "GO:0042169",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042169",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "heme binding",
"id": "GO:0020037",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0020037",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "histone binding",
"id": "GO:0042393",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042393",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "peptide hormone receptor binding",
"id": "GO:0051428",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051428",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "type 1 angiotensin receptor binding",
"id": "GO:0031702",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0031702",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "insulin receptor substrate binding",
"id": "GO:0043560",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043560",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "phosphatidylinositol 3-kinase binding",
"id": "GO:0043548",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043548",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "growth hormone receptor binding",
"id": "GO:0005131",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005131",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
},
{
"name": "histone H3Y41 kinase activity",
"id": "GO:0035401",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035401",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
}
],
"pmid": ""
}
]
}
]
},
"pro_annotation": [],
"site_annotation": [
{
"start_pos": 337,
"end_pos": 339,
"annotation": "n_glycosylation_sequon"
},
{
"start_pos": 418,
"end_pos": 420,
"annotation": "n_glycosylation_sequon"
},
{
"start_pos": 463,
"end_pos": 465,
"annotation": "n_glycosylation_sequon"
},
{
"start_pos": 470,
"end_pos": 472,
"annotation": "n_glycosylation_sequon"
},
{
"start_pos": 548,
"end_pos": 550,
"annotation": "n_glycosylation_sequon"
},
{
"start_pos": 589,
"end_pos": 591,
"annotation": "n_glycosylation_sequon"
}
],
"ptm_annotation": [
{
"annotation": "Autophosphorylated, leading to regulate its activity. Leptin promotes phosphorylation on tyrosine residues, including phosphorylation on Tyr-813 (By similarity). Autophosphorylation on Tyr-119 in response to EPO down-regulates its kinase activity (By similarity). Autophosphorylation on Tyr-868, Tyr-966 and Tyr-972 in response to growth hormone (GH) are required for maximal kinase activity (By similarity). Also phosphorylated by TEC (By similarity). Phosphorylated on tyrosine residues in response to interferon gamma signaling (PubMed:7615558, PubMed:7673114). Phosphorylated on tyrosine residues in response to a signaling cascade that is activated by increased cellular retinol (PubMed:21368206).",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
},
{
"database": "PubMed",
"id": "7673114",
"url": "https://glygen.org/publication/PubMed/7673114"
},
{
"database": "PubMed",
"id": "7615558",
"url": "https://glygen.org/publication/PubMed/7615558"
},
{
"database": "PubMed",
"id": "21368206",
"url": "https://glygen.org/publication/PubMed/21368206"
}
]
},
{
"annotation": "Undergoes Notch-induced ubiquitination and subsequent proteasomal degradation which is mediated by ASB1 or ASB2, the substrate-recognition components of probable ECS E3 ubiquitin-protein ligase complexes.",
"evidence": [
{
"database": "UniProtKB",
"id": "O60674",
"url": "https://www.uniprot.org/uniprot/O60674"
},
{
"database": "PubMed",
"id": "21119685",
"url": "https://glygen.org/publication/PubMed/21119685"
}
]
}
],
"interactions": [],
"reactions": [
{
"id": "10596",
"name": "",
"equation": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]",
"summary": "",
"cellular_location": "",
"input_participant_list": [],
"output_participant_list": [],
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"evidence": [
{
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"database": "Rhea",
"url": "https://www.rhea-db.org/rhea/10596"
}
]
},
{
"id": "R-HSA-1067646",
"name": "JAK1,JAK2,(TYK2) bind IL6ST",
"equation": "",
"summary": "The tyrosine kinases JAK1, JAK2 and Tyk2 associate with the cytoplasmic domain of the interleukin-6 receptor beta subunit (IL6ST, GP130) (Stahl et al. 1994), via interactions with the membrane proximal Box1/Box2 region, motifs conserved amongst many cytokine receptors. This region of IL6ST is sufficient for JAK activation (Narazaki et al. 1994). The interbox region is also involved in JAK binding (Haan et al. 2000). This is a strong and stable assocation considered to be constitutive (Heinrich et al. 2003). The N-terminal region of JAK1 contains a FERM domain that is crucial for receptor association (Haan et al. 2001, Hilkens et al. 2001). Interleukin-6 (IL6) induces rapid phosphorylation and activation of JAK1, JAK2 and TYK2 in cells (Guschin et al. 1995), but experiments in JAK1 deficient cell lines (Guschin et al. 1995) and Jak1 -/- mice (Rodig et al. 1998) where IL6-induced responses (Il6st phosphorylation and actvation of Stat1 and Stat3) were greatly impaired, suggest that JAK1 is the key kinase for signal transduction. One possible model is that JAK1 associates with IL6ST and triggers downstream events, but requires either JAK2 or TYK2 for efficient activation or ligand-induced dimerization of the receptor complex.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-1067646",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1067646"
}
]
},
{
"id": "R-HSA-1067651",
"name": "IL6:IL6R-2 binds IL6ST:JAK1, JAK2, (TYK2)",
"equation": "",
"summary": "The complex of interleukin-6 (IL6) and the soluble, short form of the IL6 receptor (IL6R-2) binds to surface expressed IL6ST (gp130), a process known as trans signaling (Rose-John et al. 2006). This process is negatively regulated by the soluble form of IL6ST (IL6ST-2).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-1067651",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1067651"
}
]
},
{
"id": "R-HSA-1067659",
"name": "Assembly of hexameric IL-6 receptor",
"equation": "",
"summary": "There are three contact sites between IL-6, IL-6R and gp130, named site I, II and III. Site I and II correspond to the respective sites of the growth hormone receptor complex whereas site III is only found in receptor complexes with at least three subunits. Various models of the IL-6 receptor complex have been proposed (Scheller & Rose-John 2006), but crystallographic data suggests the assembly of a hexameric complex containing two IL-6, two IL-6RA and two gp130 subunits. It has been argued that the minimal signalling complex is one IL6:IL6R complex bound to two gp130 proteins (Grotzinger et al. 1999).; ; The quaternary structures of other IL-6/IL-12 family signaling complexes suggest they have a similar topology (Boulanger et al. 2003). IL-6 binding is achieved by the cytokine-binding and the immunglobulin-like domains (Boulanger et al. 2003). The gp130 fibronectin-like domains are thought to position the transmembrane domains of the paired gp130 receptor complexes in close proximity and thereby induce signaling (Skiniotis et al. 2005). Forced dimerization of gp130 with itself or the related Interleukin-27 receptor subunit alpha (WSX-1), Leukemia inhibitory factor receptor or Oncostatin M receptors led to constitutive, ligand-independent STAT1 and/or STAT3 activation and ERK1/2 phosphorylation, suggesting that all heterodimeric gp130-type receptor complexes are activated by a similar mechanism in which close juxtaposition of the intracellular receptor domains is sufficient for signal induction (Suthaus et al. 2010).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-1067659",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1067659"
}
]
},
{
"id": "R-HSA-1067688",
"name": "IL6:IL6R binds IL6ST:JAK1,JAK2,(TYK2)",
"equation": "",
"summary": "The complex of interleukin-6 (IL6) bound to the IL6 receptor alpha subunit (IL6R) binds the IL-6 receptor beta subunit IL6ST (gp130), which constitutively binds JAK kinases. Site II of IL6 interacts with the cytokine binding-homology region of IL6ST. Subsequently, site III of IL6 interacts with the IL6ST immunoglobulin-like activation domain.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-1067688",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1067688"
}
]
},
{
"id": "R-HSA-109857",
"name": "MAP2K1 binds MAPK3",
"equation": "",
"summary": "In the cytoplasm phosphorylated MAP2K1 (MEK1) may encounter monomeric, inactive MAPK3 (ERK1).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P27361-1",
"O60674-1",
"Q06124-2",
"P29597-1",
"Q02750-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-109857",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-109857"
}
]
},
{
"id": "R-HSA-109858",
"name": "MAP2K2 binds MAPK1",
"equation": "",
"summary": "In the cytoplasm phosphorylated MAP2K2 (MEK2) may encounter monomeric, inactive MAPK1 (ERK2). IL-6-type receptor activation leads to induction of the MAPK cascade. Experiments using gp130 identified that the gp130 SHP2 (SH2-domain-containing tyrosine phosphatase)-binding site Tyr-759 (Stahl et al. 1995) is required for this activation. Mutation of gp130 Tyr-759 impairs IL-6 induced activation of the MAPK cascade (Kim et al. 1998). While there is a consensus that SHP2 is involved in IL-6-induced activation of the MAPK pathway, the molecular details are uncertain. One proposed mechanism suggests SHP2 acts as an adaptor for Grb2-Sos recruitment (Fukada et al. 1996, Kim & Baumann 1999). IL-6 induced SHP2 recruitment to p-Tyr-759 of gp130 was demonstrated but relatively little of the SHP2 remained associated with gp130, suggesting that SHP2 dissociates from the receptor when phosphorylated. This seems inconsistent with a Grb2-Sos recruitment role for SHP2, though it is possible that only low levels or transient recruitment are required. IL-6 induced ERK activation was not inhibited in cells transfected with a phosphatase inactive mutant of SHP2, whereas an SHP2 mutant missing the Grb2 interaction region significantly suppressed ERK activation. This suggests phosphatase activity is not required for ERK activation while SHP-2 interaction with Grb2 is important. However, overexpression studies can generate artefactual interactions and this interpretation has been questioned (Dance et al. 2008). An alternative proposal suggests that SHP2 and the adaptor protein Gab1 couple gp130 signalling to Erk activation. In this proposal phosphorylated SHP2 dissociates from gp130 and becomes associated with membrane associated Gab1 in a complex with PI3-kinase (Takahashi-Tezuka et al. 1998, Eulenfeld & Schaper 2009). SHP2 interaction is suggested to induce a conformational change in Gab1 that permits Gab1-PI3-kinase activation and enhancement of IL-6-induced Erk pathway activation. However this is speculative, the role of SHP2 phosphatase activity is unclear. Other possible mechanisms are outlined by Dance et al. (2008), extrapolated from growth factor receptor mechanisms but with unknown relevance to IL-6/gp130.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"Q06124-2",
"P28482-1",
"P36507-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-109858",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-109858"
}
]
},
{
"id": "R-HSA-1112510",
"name": "IL6ST is tyrosine phosphorylated",
"equation": "",
"summary": "Activated JAKs are believed to be responsible for phosphorylating the cytoplasmic region of IL6ST (gp130) (Wang & Fuller 1994, Reich & Liu 2006) creating docking sites for adaptor and downstream signaling molecules, in particular the factors STAT1 and STAT3. Several phosphotyrosine residues of IL6ST are docking sites for STATs (Stahl et al. 1995, Gerhartz et al. 1996), Tyr-759 phosphorylation allows recruitment of the phosphatase SHP2.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-1112510",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1112510"
}
]
},
{
"id": "R-HSA-1112514",
"name": "JAK activation",
"equation": "",
"summary": "The molecular mechanism of Jak activation upon cytokine stimulation is not understood in detail (Haan et al. 2008). Cytokine-induced receptor aggregation and the resulting close proximity of Jaks bound to the beta receptor subunit is believed to trigger trans-phosphorylation of Jak tyrosines in their kinase activation loop, confering kinase activity. This active state is believed to be maintained by further autocatalytic tyrosine phosphorylations. For JAK1 the activation loop tyrosine residues are predicted by homology with models of JAK2 (Lindauer et al. 2001) to be Tyr-1034/1035. Mutation of Tyr-1034 abolishes JAK1 kinase activity (Liu et al. 1997). Evidence supporting JAK1 transphosphorylation includes JAK1 mutant cell lines, which cannot activate Tyk2 after stimulation with interferon alpha/beta (Velazquez et al. 1995) and the observation that IL-2 cannot activate JAK1 in the absence of JAK3 (Oakes et al. 1996). The receptor is not merely a docking site for JAKs as certain gp130 residues are required for JAK1 activation, but not essential for JAK1 binding (Haan et al. 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-1112514",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1112514"
}
]
},
{
"id": "R-HSA-1112565",
"name": "Tyrosine phosphorylated IL6ST binds STAT1,STAT3",
"equation": "",
"summary": "STAT1 binds to IL6ST (gp130) via phosphotyrosine residues 905 and 915 within two YXPD recognition motifs. STAT3 can be recruited to these sites and to two additional sites around Y767 and Y814 that have less restricted sequence recognition requirements (YXXQ) (Gerhartz et al. 1996). After receptor binding, STATs are phosphorylated on a single tyrosine residue by JAKs (Hemmann et al. 1996).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-1112565",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1112565"
}
]
},
{
"id": "R-HSA-1112602",
"name": "Tyrosine phosphorylation of STAT1, STAT3 by IL6 receptor",
"equation": "",
"summary": "Interleukin-6 (IL6) activates the tyrosine phosphorylation of STATs (Akira et al. 1994, Zhong et al. 1994) by receptor-associated JAKs (Hemmann et al. 1996) at a site that is essential for dimerization. For STAT1 this is tyrosine-701, for STAT3 tyrosine-705 (Kaptein et al. 1996, Shuai et al. 1994). Tyrosine phosphorylation leads to homo- or heterodimerization and translocation to the nucleus (Zhong et al. 1994), where the dimers bind to enhancers of IL6- inducible genes e.g. acute phase protein genes, resulting in transcriptional activation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-1112602",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1112602"
}
]
},
{
"id": "R-HSA-1112604",
"name": "Phosphorylated STATs are released",
"equation": "",
"summary": "Following phosphorylation, STATs are released from the receptor.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-1112604",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1112604"
}
]
},
{
"id": "R-HSA-1112690",
"name": "PTPN11 binds CBL",
"equation": "",
"summary": "SHP2 binds CBL in response to IL-6 stimulation in 293T cells and contributes to the ubiquitination of gp130 (Tanaka et al. 2008).
; IL-6 stimulation induced lysosome-dependent degradation of gp130, which correlated with an increase in its K63-linked polyubiquitination. This stimulation-dependent ubiquitination was mediated by CBL, an E3 ligase, which was recruited to gp130 in a tyrosine-phosphorylated SHP2-dependent manner. IL-6 induced a rapid translocation of gp130 from the cell surface to endosomal compartments. The vesicular sorting molecule Hrs contributed to the lysosomal degradation of gp130 by directly recognizing its ubiquitinated form. Deficiency of either Hrs or CBL suppressed gp130 degradation, leading to a prolonged and amplified IL-6 signal.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P22681-1",
"Q06124-2",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-1112690",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1112690"
}
]
},
{
"id": "R-HSA-1112703",
"name": "PTPN11 is phosphorylated",
"equation": "",
"summary": "PTPN11 (SHP2) is tyrosine-phosphorylated in a JAK1-dependent manner (Schaper et al. 1998, Lehmann et al. 2003, Fischer, 2004). Cells lacking JAK1 showed drastically reduced PTPN11 phosphorylation following Interleuikin-6 (IL6) treatment, but it is not entirely clear whether JAK1 directly phosphorylates PTPN11 or alternatively is required for IL6ST activation, which indirectly leads to PTPN11 phosphorylation (Schaper et al, 1998). PTPN11 tyrosine phosphorylation at Y546 or Y584 (usually described as Y542 or Y580 in literature references where numbering is based on a short isoform) relieves the PTP domain from the N-SH2 domain-mediated inhibition (Lu et al. 2001). Studies using catalytically-inactive PTPN11 (Symes et al. 1997) suggest that it may dephosphorylate IL6ST and/or associated signaling factors such as JAKs and STATs, limiting acute phase gene expression (Kim and Baumann, 1999). There is a consensus that SHP2 is involved in IL6-induced activation of the MAPK pathway, but the molecular details are unclear.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"Q06124-2",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-1112703",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1112703"
}
]
},
{
"id": "R-HSA-1112708",
"name": "PTPN11 binds p-Y759-IL6ST",
"equation": "",
"summary": "Following Interleukin-6 (IL6) stimulation, Tyrosine-protein phosphatase non-receptor type 11 (PTPN11, SHP2) is recruited to IL6ST (gp130) phosphotyrosine-759 and is subsequently tyrosine-phosphorylated in a JAK1-dependent manner (Schaper et al. 1998, Lehmann et al. 2003, Fischer, 2004). Mutation of Tyr-759 impairs PTPN11 recruitment and phosphorylation (Schaper et al. 1998).
There is a consensus that PTPN11 is involved in IL6-induced activation of the MAPK pathway but the molecular details are uncertain, in particular it is not clear whether the phosphatase activity of PTPN11 is required. Two pathways have been linked with activation of MAPK. One proposed mechanism is that PTPN11 acts as an adaptor for Growth factor receptor-bound protein 2-Son of sevenless homolog 1 (GRB2-SOS1) recruitment (Fukada et al. 1996, Kim & Baumann 1999). Kim & Baumann demonstrate IL6 induced PTPN11 recruitment to p-Tyr-759 of IL6ST but note that relatively little of the PTPN11 remains associated with IL6ST, suggesting that PTPN11 dissociates from the receptors when phosphorylated. This seems inconsistent with a GRB2:SOS1 recruitment role for PTPN11, though it is possible that only low levels or transient recruitment are required. Kim & Baumann demonstrated that IL6 induced ERK activation was not inhibited in cells transfected with a phosphatase inactive mutant of PTPN11, whereas a PTPN11 mutant missing the GRB2 interaction region significantly suppressed ERK activation. This suggests that phosphatase activity is not required for ERK activation while PTPN11 interaction with GRB2 is important. However, overexpression studies can generate artefactual interactions and this interpretation has been questioned (Dance et al. 2008). PTPN11 and the adaptor protein GRB2-associated-binding protein 1 (GAB1) have been reported to couple IL6ST signalling to ERK activation. In this proposal phosphorylated PTPN11 dissociates from IL6ST and becomes associated with membrane associated GAB1 in a complex with PI3-kinases (Takahashi-Tezuka et al. 1998, Eulenfeld & Schaper 2009). PTPN11 interaction is suggested to induce a conformational change in GAB1 that permits GAB1-PI3-kinase activation and enhancement of IL6-induced ERK pathway activation. However this is speculative, the role of PTPN11 phosphatase function is unclear. Other possible mechanisms are outlined by Dance et al. (2008), extrapolated from growth factor receptor mechanisms but with unknown relevance to IL6 and its interaction with IL6ST.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"Q06124-2",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-1112708",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1112708"
}
]
},
{
"id": "R-HSA-1112727",
"name": "Serine phosphorylation of STATs",
"equation": "",
"summary": "In addition to tyrosine phosphorylation, STAT1 and STAT3 are phosphorylated at serine-727, which contributes to maximal transcriptional activity (Wen & Darnell 1997, Shen et al. 2004). Though several candidates exist, including Protein kinase C delta (Jain et al. 1999), the kinase responsible for Interleukin-6 regulation of STAT serine phosphorylation is unknown (Jain et al. 1999, Abe et al. 2001, Chung et al. 1997) and the significance of serine phosphorylation is unclear (Decker & Kovarik 2000). STAT3 modifed by serine phosphorylation augments oxidative phosphorylation in mitochondria and supported cellular transformation by oncogenic Ras (Reich 2009).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-1112727",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1112727"
}
]
},
{
"id": "R-HSA-1112755",
"name": "SOCS3 binds IL6ST",
"equation": "",
"summary": "Suppressor of cytokine signaling protein 3 (SOCS3) binds to the same IL6ST (gp130) phosphotyrosine (Tyr-759) as PTPN11 (SHP2) (Schmitz et al. 2000) though they appear to suppress Interleukin-6 (IL6) signaling by independent mechanisms (Lehmann et al. 2003).; ; Members of the SOCS family (CIS and SOCS1-7) have an N-terminal SH2 domain preceded by an extended SH2 domain (ESS) and kinase inhibitory region (KIR) (Hilton et al. 1998). The related SOCS1 associates with JAKs via its KIR and SH2 domains (Narazaki et al. 1998, Yasukawa et al. 1999) leading to inhibition of JAK signaling and kinase activity. SOCS3 was unable to inhibit JAK kinase activity in vitro, suggesting that SOCS1 and SOCS3 inhibit signaling in different ways (Nicholson et al. 1999), but it is possible that SOCS3's inhibitory actions require binding to both activated receptor gp130 Tyr-759 and the associated JAK for maximal inhibition (Greenhalgh & Hilton 2001). Socs3 deficiency results in prolonged STAT1/3 activation after IL6 but not interferon-gamma (IFNG) stimulation suggesting that SOCS3 has a role in preventing IFNG-like responses in cells stimulated by IL6 (Croker et al. 2003).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-1112755",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1112755"
}
]
},
{
"id": "R-HSA-1168393",
"name": "STAT5 association with GHR",
"equation": "",
"summary": "JAK2 is required for GH-mediated phosphorylation of STATs 1,3,5A and 5B (Smit et al.1996). Some STAT activation may be mediated by direct association of JAK and STAT but maximal activation requires binding of STATs to phosphorylated tyrosines of the receptor (Smit et al. 1996, Lichanska & Waters 2006). Studies using mouse GHR truncated at K391, equivalent to human K380, suggest that STAT5 signaling is mediated by distal tyrosines, with 70% of the signaling lost if the receptor is truncated at P569, equivalent to human P558 (Rowland et al. 2005). Wang et al. (1996) using the porcine receptor found that phosphorylation at any one of the positions Y487, Y534, Y566 or Y627 (numbering identical in humans) was sufficient to allow STAT5 phosphorylation. Smit et al. (1996) identified mouse residues Y341 (human Y332) and Y346 (not conserved in human) as required for STAT1, 3, and maximal STAT5 activation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1168393",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1168393"
}
]
},
{
"id": "R-HSA-1168394",
"name": "STAT5 tyrosine phosphorylation",
"equation": "",
"summary": "Stat5 tyrosine phosphorylation was seen in response to GH in CHO cells expressing mouse GHR forms capable of binding JAK2 (Smit et al. 1996). Similar results were obtained using the porcine receptor (Wang et al. 1996). Thus Jak2 phosphorylates Stat5, the phosphorylated monomers form dimers and translocate to the nucleus (Darnell et al. 1994).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1168394",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1168394"
}
]
},
{
"id": "R-HSA-1168423",
"name": "JAK2 phosphorylation of IRS-1/2",
"equation": "",
"summary": "GH has short term effects that mimic the actions of insulin in tissues that have been deprived of GH, including increased amino acid transport, glucose transport, and lipogenesis (Davidson 1987). GH and insulin have overlapping signaling pathways (Dominici et al. 2005). GH stimulates tyrosyl phosphorylation of insulin receptor substrate-1 (IRS-1) (Souza et al. 1994, Thirone et al. 1999), and IRS-2 (Argetsinger et al. 1996, Thirone et al. 1999), although more modestly than insulin or IGF-1. Tyrosyl phosphorylation of IRS-1 and IRS-2 in response to insulin provides binding sites for specific proteins containing SH2 domains, including the 85-kDa regulatory subunit of phosphatidylinositol 3-kinase (PI3K), tyrosine phosphatase SHP2, and Grb2. This is one of several mechanisms proposed to explain the stimulatory effect of GH on the PI3-kinase/Akt pathway (Jin et al. 2008). GH promotes the binding of the 85-kDa regulatory subunit of PI3K to IRS-1 and IRS-2 in cultured cells (Ridderstrale et al. 1995, Argetsinger et al. 1995, 1996). Studies using truncated or mutated GHRs suggest that tyrosyl phosphorylation of IRS-1, IRS-2, and Shc is dependent on JAK2 activation (Argetsinger et al. 1995, 1996, VanderKuur et al. 1995). Despite a strong correlation between JAK2 activation and IRS phosphorylation it is not clear whether there is a direct association. JAK2 has been reported to interact directly with IRS in response to angiotensin II (Velloso et al. 1996) but also reported to interact indirectly via SH2B in response to leptin (Duan et al.2004).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1168423",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1168423"
}
]
},
{
"id": "R-HSA-1168445",
"name": "PTP1B binds the GH receptor complex",
"equation": "",
"summary": "PTP1B has been shown to associate with GH-dependent phosphorylated GHR and induce its dephosphorylation (Pasquali et al. 2003). It can also dephosphorylate JAK2 (Gu et al. 2003). Both have the effect of reducing JAK signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P18031-1"
],
"evidence": [
{
"id": "R-HSA-1168445",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1168445"
}
]
},
{
"id": "R-HSA-1168456",
"name": "Growth hormone receptor binds Lyn",
"equation": "",
"summary": "There is accumulating evidence that GH signalling utilises a Src family tyrosine kinase independently of JAK2, and that this is linked to activation of extracellular regulated kinases (ERKs) 1 and 2 (p44/42 MAPK). The relative strengths of these signaling pathways probably depends on cell type and may be mediated by conformational changes that are a consequence of ligand binding (Rowlinson et al. 2007). In NIH-3T3 cells GH activated c-Src, which in turn activated ERK1/2 via a pathway involving the activation of the Ras-like small GTPases RalA and RalB, leading to Elk-1 mediated transcription (Zhu et al. 2002). JAK2 and c-Src were both found to activate the Ras-like small GTPases Rap1 and Rap2 which inhibit RalA mediated activation of ERK1/2 (Ling et al. 2003). Src kinase inhibition was found to block ERK activation by GH. The major contributing kinase was identified as Lyn, which was found to co-immunoprecipitate with GHR and bind to the proximal 150 residues of the cytoplasmic domain (Rowlinson et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-1168456",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1168456"
}
]
},
{
"id": "R-HSA-1168459",
"name": "Lyn activates ERK",
"equation": "",
"summary": "The activation of Lyn by GHR is thought to indirectly activate ERK. Mutations of GHR predicted to disable a conformational change brought about by GH binding impaired ERK signaling but not JAK2/STAT5 signaling. ERK signaling was demonstrated to involve the Src family kinase Lyn (Rowlinson et al. 2008) and suggested to involve Src kinase dependent activation of Phospholipase C gamma and thereby Ras, similar to a mechanism proposed by Bivona et al. (2003). ERK activation mechanisms involving Src kinases and PLCgamma have been reported for the erythropoietin, thrombopoietin and prolactin receptors (Brooks & Waters 2010).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P27361-1",
"O60674-1",
"P07948-1",
"P28482-1"
],
"evidence": [
{
"id": "R-HSA-1168459",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1168459"
}
]
},
{
"id": "R-HSA-1168767",
"name": "JAK2 phosphorylates STAT1/STAT3",
"equation": "",
"summary": "GH stimulated tyrosyl phosphorylation of Stats 1, 3, and 5 in CHO cells expressing GHR constructs that bind JAK2 but not in CHO cells expressing GHR constructs that do not bind JAK2 (Smit et al. 1996). STAT5 phosphorylation was greatly reduced in GHR mutants with the distal region of the cytoplasmic tail removed and by mutation of distal GHR tyrosine residues to phenylalanine but this had no effect on STAT1/STAT3 phosphorylation, suggesting that the latter interact with JAK2 directly.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1168767",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1168767"
}
]
},
{
"id": "R-HSA-1168768",
"name": "JAK2 binds STAT1/3",
"equation": "",
"summary": "JAK2 is believed to bind STAT1 and STAT3 directly in response to GH, as opposed to STAT5 which binds to phosphorylated tyrosine residues in the distal portion of the GHR cytoplasmic region (Smit et al. 1996). When associated with the prolactin receptor JAK2 is able to bind STAT1, STAT3 and STAT5 (DaSilva et al. 1996).; ; Smit et al. identified mouse GHR residues Y341 (human Y332) and Y346 (not conserved in human) as required for STAT1, 3, and maximal STAT5 activation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1168768",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1168768"
}
]
},
{
"id": "R-HSA-1168809",
"name": "SOCS binding to GHR",
"equation": "",
"summary": "Suppressor of Cytokine Signaling (SOCS) proteins inhibit the GH signal; SOCS2 null mice exhibit giantism (Greenhalgh et al. 2005). Suppressor of Cytokine Signaling (SOCS)1-3, and the realted Cytokine-inducible SH2-containing protein (CIS) all bind tyrosine-phosphorylated GHR; SOCS1 can also binds GHR in the absence of tyrosine phosphorylation (Ram & Waxman 1999, Hansen et al. 1999). SOCS3 binding has been mapped to phosphorylated tyrosines Y338, Y333 (Ram & Waxman 1999), and Y487 (Hansen et al. 1999) in the membrane proximal region of the receptor while SOCS2 and CIS bind to residues Y487 and Y595 (Uyttendaele et al. 2007). SOCS2/3/CIS may compete with STAT5 for GHR binding at these sites but in the case of SOCS3 also appears to act by inhibiting JAK2 directly (Yasukawa et al. 1999).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1168809",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1168809"
}
]
},
{
"id": "R-HSA-1168813",
"name": "SOCS binding to JAK2",
"equation": "",
"summary": "SOCS1 can bind JAK2 and inhibit JAK kinase activity (Yasukawa et al. 1999). SOCS3 also inhibits JAK2 kinase activity (Sasaki et al. 1999) while all of SOCS1 -3 and CIS inhibit GHR signaling (Ram & Waxman 1999, Nicholson et al. 2000). This is not thought to be simply the outcome of binding competition between SOCS and STAT5, but a direct action of SOCS on JAK2 (Ram & Waxman 1999). Although SOCS are known to be ubiquitin ligases (Kamura et al. 2004), ubiquitin ligase activity on JAK2 or GHR has not been demonstrated and a role for SOCS in the ubiquitination of these proteins has been questioned (Flores-Morales et al. 2006). An alternative model suggested by the observation that SOCS3 strongly inhibits JAK2 only in the presence of GHR proposes that SOCS serve as an inhibitory 'bridge' by binding simultaneously to GHR and JAK2 (Ram & Waxman 1999).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1168813",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1168813"
}
]
},
{
"id": "R-HSA-1168839",
"name": "SHP1 (PTPN6) binds JAK2 in the receptor complex",
"equation": "",
"summary": "SHP1 binds GH-activated JAK2 and controls the duration of GH-dependent JAK2 phosphorylation in the liver, consequently hepatic GH signaling is prolonged in mice lacking SHP1 (Hackett et al. 1999).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29350-1"
],
"evidence": [
{
"id": "R-HSA-1168839",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1168839"
}
]
},
{
"id": "R-HSA-1168894",
"name": "p-STAT5A/B dissociates from the Growth Hormone receptor",
"equation": "",
"summary": "Deletion mutants have demonstrated that STAT dimerization can occur independently of the binding of 2 STAT molecules by a dimeric receptor. Although this does not exclude the possibility that STATs may dimerize while still associated with the receptor complex, dimerization is believed to occur following release of the phosphorylated monomers from the receptor complex and is typically represented in this manner (e.g. Turkson & Jove 2000).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1168894",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1168894"
}
]
},
{
"id": "R-HSA-1169188",
"name": "SHP1 (PTPN6) dephosphorylates JAK2",
"equation": "",
"summary": "SHP1 (PTPN6) dephosphorylates GH-activated JAK2, limiting the duration of signaling (Hackett et al. 1999).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29350-1"
],
"evidence": [
{
"id": "R-HSA-1169188",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1169188"
}
]
},
{
"id": "R-HSA-1169192",
"name": "PTP1B dephosphorylates GHR",
"equation": "",
"summary": "PTP1B induces the dephosphorylation of GHR (Pasquali et al. 2003).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P18031-1"
],
"evidence": [
{
"id": "R-HSA-1169192",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1169192"
}
]
},
{
"id": "R-HSA-1169210",
"name": "PTP1B dephosphorylates JAK2",
"equation": "",
"summary": "PTP1B dephosphorylates JAK2 (Gu et al. 2003), limiting ligand-dependent signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P18031-1"
],
"evidence": [
{
"id": "R-HSA-1169210",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1169210"
}
]
},
{
"id": "R-HSA-1170539",
"name": "Prolactin receptor is internalized",
"equation": "",
"summary": "PRLR is regulated by ubiquitination of the activated receptor, leading to lysosomal degradation (Djiane et al. 1981, 1982, Lu et al. 2002). Recruitment of the SCFbeta-TrCP ubiquitin ligase complex enables receptor ubiquitination and internalization (Li et al. 2004). This limits the duration and intensity of receptor signaling. Deregulation of this negative control lead to pathological conditions including cancer (Swaminathan et al. 2008).",
"cellular_location": "cytosol, endosome lumen, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P62877-1",
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1170539",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1170539"
}
]
},
{
"id": "R-HSA-1302698",
"name": "PRLR associates with JAK2",
"equation": "",
"summary": "PRLR has no intrinsic kinase activity but associates with Janus kinase 2 (JAK2) (Lebrun et al. 1994, 1995, Campbell et al. 1994, Rui et al. 1994). PRLR to JAK2 binding has been described as constitutive but a recent computational model suggests that roughly half of dimerized Growth Hormone receptors are bound with JAK2 (Barua et al. 2009), a model that may apply to other receptors that promote JAK2 trans-activation. The box 1 region of PRLR is a membrane proximal proline-rich region in the intracellular domain, conserved in all members of the growth hormone rereptor family. This region is critical for JAK2 association; deletion of box 1 virtually abolishes PRLR signaling (Edery et al. 1994). Alanine substitutions of individual residues within box 1 of rat PRLR have shown that the most C-terminal proline (P269 in the Uniprot canonical sequence, 250 in the mature peptide) is critical for association with and subsequent activation of JAK2 (Pezet et al. 1997). It is not known whether the interaction of JAK2 with PRLR is direct or involves an adaptor protein.
When the receptor is activated by ligand binding JAK2 (receptor pre-bound or recruited after ligand binding) becomes activated and phosphorylates the dimerized receptor preferentially at Y611 (position 587 in the mature peptide), a consensus tyrosine phosphorylation site. This is followed by the phosphorylation, dimerization and nuclear translocation of STAT5. There are nine other tyrosines in the cytoplasmic domain, some of which may undergo phosphorylation and may participate in signal transduction.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1302698",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1302698"
}
]
},
{
"id": "R-HSA-1364043",
"name": "Tyrosine phosphorylation of PRLR",
"equation": "",
"summary": "The model for PRL-induced PRLR activation suggests that JAK2 phosphorylates PRLR on specific tyrosine residues. Consistent with this, JAK2 and PRLR are phosphorylated in response to activating ligand (Lebrun et al. 1994) and PRLR tyrosine phosphorylation is required for subsequent Stat signaling (Pezet et al. 1997). Though this evidence is consistent with a role for JAK2, it has not been formally demonstrated that JAK2 is the kinase responsible for PRLR tyrosine phosphorylation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1364043",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1364043"
}
]
},
{
"id": "R-HSA-1364044",
"name": "PRLR:JAK2 dimerizes",
"equation": "",
"summary": "The prolactin receptor (PRLR) peptide is a single transmembrane domain protein that functions as a dimer. Recent reports suggest that like many other cytokine receptors, the prolactin receptor (PRLR) pre-assembles at the plasma membrane in the absence of ligand (Gadd & Clevenger 2006, Tallet et al. 2011), suggesting that ligand-induced activation involves conformational changes in the preformed receptor dimer (Broutin et al. 2010).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1364044",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1364044"
}
]
},
{
"id": "R-HSA-1369080",
"name": "PRLR binds STAT5",
"equation": "",
"summary": "PRLRs contain intracellular phosphorylated tyrosine residues that are able to bind and activate STATs, demonstrated by the co-immunoprecipitation of rat Stat5 and Prlrs mutated to have a single intracellular tyrosine (Pezet et al. 1997). Prlr mutants with a single tyrosine residue at positions 599, 498 or 492 (reported according to their position in the mature peptide as 580, 479 or 473 in Pezet et al. 1997) were all able to activate Stat5; Y599 gave a much stronger response. Short forms of PRLR lacking these tyrosines did not bind STAT5. The equivalent human tyrosine residues are Y509 and Y611; Y492 is not conserved in humans.
Activation of STAT1 and STAT3 by PRLR has been reported (Da Silva et al. 1996) but the interaction has been suggested to be indirect and possibly mediated by JAK2.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1369080",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1369080"
}
]
},
{
"id": "R-HSA-1369114",
"name": "PRLR binds SHP2 (PTPN11)",
"equation": "",
"summary": "Tyrosine-phosphorylated PRLR can bind the protein-tyrosine Phosphatase SHP2 (PTPN11) via its C-terminal SH2 Domain. This binding does not occur when the most C-terminal PRLR tyrosine residue (residue 611 in the human canonical Uniprot sequence, equivalent to 587 in the mature protein with signal peptide removed) is mutated to alanine (Ali & Ali 2000).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"Q06124-2"
],
"evidence": [
{
"id": "R-HSA-1369114",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1369114"
}
]
},
{
"id": "R-HSA-1369115",
"name": "SHP2 is phosphorylated",
"equation": "",
"summary": "Prolactin stimulation leads to tyrosine phosphorylation of the C-terminal SH2 domain of SHP2 and requires JAK2 (Ali et al. 1996). This has a positive regulatory influence on PRLR signaling. SHP2 has a number of signaling-capable interactors such as signal regulatory proteins (SIRPs, Kharitonenkov et al. 1997), SH2-containing inositol phosphatase (SHIP, Liu et al. 1997), insulin receptor substrates 1 and 2 (Myers et al. 1998), JAK2 (Jiao et al. 1996) and GRB2 associated binder 2 (GAB2) an adaptor protein that links activated receptor tyrosine kinase and cytokine receptors to downstream signaling molecules. PRL stimulation leads to SHP2-GAB2 association, GAB2 tyrosine phosphorylation, and GAB2-PI3K p85 subunit association, though it is not clear that this is the order of events, nor that SHP2 serves as a link between PRLR and GAB2 (Ali & Ali 2000).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"Q06124-2"
],
"evidence": [
{
"id": "R-HSA-1369115",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1369115"
}
]
},
{
"id": "R-HSA-1370500",
"name": "PRLR binds SCF beta-TrCP complex",
"equation": "",
"summary": "Phosphorylation of PRLR on Ser-349 by an unidentified kinase enables recruitment of the SCF beta-TrCP ubiquitin ligase complex, which catalyzes ubiquitination of the receptor (Li et al. 2004). This downregulation mechanism is impaired in some forms of breast cancer (Li et al. 2006).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P62877-1",
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1370500",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1370500"
}
]
},
{
"id": "R-HSA-1370505",
"name": "PRLR is phosphorylated at Ser-349",
"equation": "",
"summary": "The PRL responsiveness of target cells is negatively regulated by receptor internalization, ubiquitination and degradation, which limit the duration and intensity of receptor signaling (Djiane et al. 1981, 1982, Lu et al. 2002). The PRLR is phosphorylated on Ser-349 by an unidentified kinase (Li et al. 2006) enabling subsequent recruitment of the SCF beta-TrCP ubiquitin ligase complex (Li et al. 2004).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1370505",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1370505"
}
]
},
{
"id": "R-HSA-1433418",
"name": "Phosphorylation of JAK2",
"equation": "",
"summary": "SCF induces rapid and transient autophosphorylation of JAK2 bound to c-KIT. JAKs bound to activated, dimerized receptors cross-phosphorylate and thereby activate each other. Multiple phosphorylation sites have been identified in JAK2 (tyrosines 221, 570, 868, 966, 972, 1007 and 1008 ). Phosphorylation of tyrosine 1007 is essential for kinase activity (Feng et al 1997, Argetsinger et al. 2004, 2010). Tyrosine 1007 is in the activation loop and phosphorylation allows access of the catalytic loop to the ATP in the ATP binding domain. Of all the predicted phoshorylation sites only the critical tyrosine 1007 is represented in the reaction.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-1433418",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1433418"
}
]
},
{
"id": "R-HSA-1433451",
"name": "JAK2 binds to p-KIT",
"equation": "",
"summary": "Janus kinase 2 (JAK2) plays an important role in SCF-induced proliferation (Radosevic et al. 2004). JAK2 was observed to pre-associate with KIT, with increased association after SCF stimulation of KIT (Weiler et al. 1996).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-1433451",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1433451"
}
]
},
{
"id": "R-HSA-1433456",
"name": "Recruitment of STATs",
"equation": "",
"summary": "Activation of KIT mediates the recruitment of and association with STAT1alpha, STAT3, STAT5A and STAT5B (Deberry et al. 1997, Brizzi et al. 1999, R\u00f6nnstrand 2004).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-1433456",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1433456"
}
]
},
{
"id": "R-HSA-1470009",
"name": "Phosphorylation of STATs",
"equation": "",
"summary": "JAK2 activation results in the phosphorylation and activation of STAT1alpha, STAT3, STAT5A and STAT5B (Deberry et al. 1997, Brizzi et al. 1999, Ning et al. 2001, Ronnstrand 2004). STAT family members can be activated by JAK kinases, receptor tyrosine kinases or SFKs. LYN kinase has been identified to have role in SCF-induced phosphorylation of STAT3 (Shivakrupa & Linnekin 2005).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-1470009",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1470009"
}
]
},
{
"id": "R-HSA-1470010",
"name": "Dimerization of STATs",
"equation": "",
"summary": "Phosphorylation on tyrosine residues immediately distal to the SH2 domain induces STATs homo- or heterodimerization through phosphotyrosine-SH2 interactions.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-1470010",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1470010"
}
]
},
{
"id": "R-HSA-1470012",
"name": "Disassociation and translocation of STATs to the nucleus",
"equation": "",
"summary": "After dimerization STAT dimers release from the receptor complex and migrate to the nucleus for DNA binding. STAT5s/STAT1alpha heterodimeric complexes specifically recognize beta-casein promoter region (PIE) (Brizzi et al. 1999). c-Kit dependent JAK/STAT activation is associated with the growth and differentiation of fetal liver haematopoietic progenitor cells (R\u00f6nnstrand 2004, Reber et al. 2006).",
"cellular_location": "cytosol, extracellular region, nucleoplasm, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-1470012",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1470012"
}
]
},
{
"id": "R-HSA-1671687",
"name": "PRLR activation",
"equation": "",
"summary": "Ligand binding activates the PRLR, probably by causing a subtle conformational change (Broutin et al. 2010).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1671687",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1671687"
}
]
},
{
"id": "R-HSA-1671691",
"name": "PRLR-bound STAT5 is phosphorylated",
"equation": "",
"summary": "Co-immunoprecipitation of rat Stat5 and Prlrs mutated to have a single intracellular tyrosine suggests that phosphorylation of these tyrosines is required for Stat5 binding and leads to Stat5 tyrosine phosphorylation (Pezet et al. 1997). STAT1 and STAT3 have both been reported to be activated by PRLR (DaSilva et al. 1996), but the region(s) of PRLR required for activation of these Stats remains poorly documented.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1671691",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1671691"
}
]
},
{
"id": "R-HSA-1675473",
"name": "SH2B binds JAK2",
"equation": "",
"summary": "The SH2 domains of SH2B beta (Uniprot isoform Q9NRF2-2) binds JAK2 at Tyr813. SH2B beta is able to homodimerize while bound to JAK2 molecules, suggesting that SH2B binding and dimerization may help induce JAK2 transactivation (Nishi et al. 2005). Computational modeling suggests that SH2B beta can enhance Jak2 activation (Barua et al. 2009). The relevance of this for PRLR signalling has yet to be demonstrated.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-1675473",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1675473"
}
]
},
{
"id": "R-HSA-2586553",
"name": "JAK2 Phosphorylates LEPR",
"equation": "",
"summary": "Phosphorylated JAK2 phosphorylates the Leptin receptor (LEPR or OB-Rl, long isoform) at multiple tyrosine residues in the C-terminal, cytoplasmic domain (Bjorbaek et al. 1997, White et al. 1997, Ghilardi and Skoda 1997, Carpenter et al. 1998). The phosphotyrosines residues of LEPR then act as docking sites for downstream effectors STAT5, STAT3, SHP2, SH2B1, and SOCS3.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-2586553",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2586553"
}
]
},
{
"id": "R-HSA-2586555",
"name": "JAK2 Autophosphorylates in Response to Leptin",
"equation": "",
"summary": "As inferred from mouse, binding of Leptin (LEP) to the Leptin receptor (LEPR) causes a conformational change in LEPR that activates autophosphorylation of JAK2 at multiple tyrosine residues. Phosphorylated JAK2 has much higher kinase activity than unphosphorylated JAK2.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-2586555",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2586555"
}
]
},
{
"id": "R-HSA-2586559",
"name": "Leptin Binds Leptin Receptor",
"equation": "",
"summary": "Analysis of a structural model of the Leptin-LEPR complex using as a basis the complex formed by granulocyte-colony stimulator factor (GCSF) and its receptor G-CSF R (Hiroike et al., 2000) suggested that helices I and III of the human leptin structure were likely sites of interaction with the cytokine binding domain of leptin receptor (Gonzalez and Leavis, 2003). It is believed that the Leptin receptor (LEPR) is a dimer constitutively bound in a complex with JAK2 kinase (Couturier and Jockers 2003). It has been proposed that one molecule of Leptin binds each monomer of LEPR (Luoh et al. 1997, Mistrik et al. 2004), however these suggestions need further proof becasue the structure of the Leptin:LEPR complex has not yet been solved.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-2586559",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2586559"
}
]
},
{
"id": "R-HSA-2671742",
"name": "JAK2 Phosphorylates SHP2 (PTPN11) in Response to Leptin",
"equation": "",
"summary": "Phosphorylated JAK2 in the LEP:LEPR:JAK2:SHP2 complex phosphorylates SHP2 (Carpenter et al. 1998). Phosphorylated SHP2, in turn, activates the RAS-MAPK signaling pathway, possibly via GRB2:SOS.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"Q06124-2"
],
"evidence": [
{
"id": "R-HSA-2671742",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2671742"
}
]
},
{
"id": "R-HSA-2671747",
"name": "Phosphorylated LEPR Binds SHP2 (PTPN11)",
"equation": "",
"summary": "SHP2 (PTPN11) interacts with phosphotyrosine-986 of the phosphorylated Leptin receptor (LEPR) (Carpenter et al. 1998). The corresponding site in mouse is phosphotyrosine-985 and in rat phosphotyrosine-986.
SHP2 and SOCS3 compete for the same binding site on LEPR. SHP2 activates MAPK signaling, probably by recruiting GRB2:SOS which activates RAS.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"Q06124-2"
],
"evidence": [
{
"id": "R-HSA-2671747",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2671747"
}
]
},
{
"id": "R-HSA-2671829",
"name": "JAK2 Phosphorylates STAT5 in Response to Leptin",
"equation": "",
"summary": "Phosphorylated JAK2 phosphorylates STAT5 (at phosphotyrosine-694 of STAT5A and probably at the homologous residue in STAT5B) while STAT5 and JAK2 are bound to LEPR (Briscoe et al. 2001).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-2671829",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2671829"
}
]
},
{
"id": "R-HSA-2671839",
"name": "Phosphorylated STAT3 Dissociates from Leptin Receptor",
"equation": "",
"summary": "Phosphorylated STAT3 dissociates from LEPR in the LEP:LEPR:JAK2 complex, dimerizes, and translocates to the nucleus.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-2671839",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2671839"
}
]
},
{
"id": "R-HSA-2671850",
"name": "JAK2 Phosphoryates STAT3 in Response to Leptin",
"equation": "",
"summary": "Phosphorylated JAK2 in the LEP:LEPR:JAK2:STAT3 complex phosphorylates STAT3 at tyrosine-705 (Bjorbaek et al. 1997).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-2671850",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2671850"
}
]
},
{
"id": "R-HSA-2671855",
"name": "Phosphorylated LEPR Binds STAT5",
"equation": "",
"summary": "STAT5 interacts with phosphotyrosine-1079 of LEPR in the LEP:LEPR:JAK2 complex, bringing STAT5 in proximity to the JAK2 kinase (Briscoe et al. 2001).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-2671855",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2671855"
}
]
},
{
"id": "R-HSA-2671862",
"name": "JAK2 Phosphorylates IRS in Response to Leptin",
"equation": "",
"summary": "JAK2 phosphorylates IRS1/2 after IRS1/2 binds SH2B1 in the LEP:LEPR:JAK2:SH2B1 complex (Martin-Romero and Sanchez-Margalet 2001, Li et al. 2007). However, in some cells leptin may only affect phosphorylation of IRS1/2 when insulin signaling subsequently occurs (Szanto and Kahn 2000). As inferred from mouse and rat (Buettner et al. 2008, Hill et al. 2008) phosphorylated IRS1/2 then activates PI3K independently of STAT3 signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-2671862",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2671862"
}
]
},
{
"id": "R-HSA-2671868",
"name": "Phosphorylated LEPR Binds STAT3",
"equation": "",
"summary": "STAT3 binds phosphotyrosine-1141 of the C-terminal, cytoplasmic region of LEPR (Bjorbaek et al. 1997). Only the long isoform of LEPR has tyrosine-1141 and consequently only the long isoform of LEPR activates STAT3. Short isoforms of LEPR exist but their function is uncertain. Shorter LEPR isoforms bind JAK2 and can signal through IRS-1 or ERKs, including MAPKs (Bjorbaek et al. 1997).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-2671868",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2671868"
}
]
},
{
"id": "R-HSA-2671872",
"name": "Phosphorylated LEP:LEPR:JAK2 Binds SH2B1",
"equation": "",
"summary": "The SH2 domain of SH2B1 binds phosphotyrosine-813 of JAK2 (Nishi et al. 2005, Li et al. 2007). Binding of SH2B1 to JAK2 enhances leptin-induced JAK2 activity. SH2B1 also recruits IRS1 for phosphorylation by JAK2 (Li et al. 2007).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-2671872",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2671872"
}
]
},
{
"id": "R-HSA-2671873",
"name": "Phosphorylated LEP:LEPR:JAK2:SH2B1 Binds IRS1/2",
"equation": "",
"summary": "SH2B1 in the LEP:LEPR:JAK2:SH2B1 complex can bind either IRS1 or IRS2 (Duan et al. 2004, Li et al. 2007). The binding brings IRS1/2 into proximity with JAK2 for phosphorylation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-2671873",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2671873"
}
]
},
{
"id": "R-HSA-2671876",
"name": "Phosphorylated STAT5 Dissociates from Leptin Receptor",
"equation": "",
"summary": "Phosphorylated STAT5 dissociates from LEPR, dimerizes, and then translocates to the nucleus.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-2671876",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2671876"
}
]
},
{
"id": "R-HSA-2672302",
"name": "Phosphorylated LEPR Binds SOCS3",
"equation": "",
"summary": "As inferred from mouse, SOCS3 binds LEPR at phosphotyrosine-986 and phosphotyrosine-1079. SOCS3 competes with SHP2 (PTPN11) for phosphotyrosine-986 and with STAT5 for phosphotyrosine-1079. SOCS3 expression is upregulated by leptin and SOCS3 downregulates prolonged leptin signaling, providing a feedback loop to limit leptin's action.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-2672302",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2672302"
}
]
},
{
"id": "R-HSA-3215391",
"name": "PRMT5 is tyrosine phosphorylated by JAK2 V617F",
"equation": "",
"summary": "Tyrosine phosphorylation of PRMT5 can block WDR77 (MEP50) binding, which attenuates PRMT5 activity (Liu et al. 2011). The kinase JAK2 is constitutively activated by the mutation V617F, observed in most patients with non-chronic myelogenous leukemia (nCML) myeloproliferative neoplasms (MPNs) (Liu et al. 2011). JAK2 V617F can phosphorylate STAT5 in the absence of upstream signals, which confers cytokine-independent growth to Ba/F3 cells and induces a myeloproliferative disease in mouse models (Akada et al. 2010, Marty et al., 2010, Mullally et al. 2010). JAK2 V617F phosphorylates PRMT5 predominantly at tyrosines 297, 304, and 307, significantly reducing the activity-enhancing interaction between PRMT5 and WDR77 (MEP50) (Liu et al. 2011).",
"cellular_location": "nucleoplasm",
"input_participant_list": [
"R-HSA-5205609"
],
"output_participant_list": [
"R-HSA-5211300"
],
"enzyme_list": [
"O60674-1",
"O14744-1"
],
"evidence": [
{
"id": "R-HSA-3215391",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-3215391"
}
]
},
{
"id": "R-HSA-447130",
"name": "Interleukin-23 binds interleukin-23 receptor",
"equation": "",
"summary": "Interleukin-23 (IL23) is a complex of Interleukin-23 subunit alpha (IL23A) and Interleukin-12 subunit beta (IL12B, IL-12p40). IL12B is also a component of Interleukin-12 (IL12) (Oppmann et al. 2000, Lupardus & Garcia et al. 2008).
The Interleukin-23 receptor consists of Interleukin 23 receptor subunit (IL23R) and Interleukin 12 receptor subunit beta 1 (IL12RB1). IL12RB1 is shared with the Interleukin-12 receptor.
The Interleukin-23 receptor binds IL23 but does not interact with IL12. IL12RB1 is required to confer IL23 responsiveness in cells (Parham et al. 2002).
IL23 is produced by antigen presenting cells and promotes the expansion and survival of a distinct lineage of T cells called T helper 17 (Th17) (Langrish et al. 2005). Increasing evidence supports the idea that Th17 cells do not require traditional T helper 1(Th1) or T helper 2 (Th2) transcription factors or regulatory genes, and that their differentiation is inhibited by Interferon-gamma (IFNG) and Interleukin 4 (IL4) (Hoeve et al. 2006).
Naive T cells cultured in the presence of Transforming growth factor beta 1(TGFB1) and Interleukin 6 (IL6) and in the absence of IFNG or IL4 are polarized to Th17 cells and upregulate IL23R (Veldhoen et al. 2006).
Subsequently, IL23 appears to be required for the expansion and survival of Th17 cells. Like Th1 and Th2 cells, Th17 cells remain committed to their lineage, even in the presence of other Th polarizing cytokines (Harrington et al. 2005).
The Interleukin 23 receptor ligand interaction has been shown to activate Signal transducer and activator of transcription 3 (STAT3), resulting in binding to the Interleukin 17A(IL17A) and Interleukin 17F (IL17F) promoters. The T cell response activated by Interleukin 23 heterodimer is attenuated by Suppressor of cytokine signaling 3 (SOCS3), which acts as a feedback inhibitor to regulate Th17 cells (Chen et al. 2006).
Knockout mice deficient in either IL12B or IL23A, or in either subunit of the Interleukin-23 receptor (IL23R or IL12RB1) have reduced symptoms of multiple sclerosis and inflammatory bowel disease suggesting that IL23 is involved in these inflammatory diseases (Kikly et al. 2006).
As it is not clear whether the dimeric receptor can form in the absence of ligand, formation of the receptor dimer is represented here as a black box event.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [
"R-HSA-447217"
],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-447130",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-447130"
}
]
},
{
"id": "R-HSA-447226",
"name": "Interleukin-12 binds Interleukin-12 receptor",
"equation": "",
"summary": "Interleukin-12 (IL12) is a heterodimer of interleukin 12 alpha subunit (IL12A, IL-12p35) and interleukin 12 beta subunit (IL12B, IL-12p40) that binds the Interleukin 12 receptor, which is a heterodimer of Interleukin 12 receptor alpha subunit (IL12RB1) and Interleukin 12 beta subunit (IL12RB2) (Chua et al. 1994, Yoon et al. 2000, Chizzonite et al. 1992 , Gubler et al. 1991). The data from cross linking and surface labeling experiments suggest that only heterodimeric receptors bind IL12.
Dimerization of the receptor does not depend on IL12 binding to the receptor subunits but if the IL12 is pre-bound to either receptor subunit, the resulting binding pattern does not change (Chua et al. 1994).
Regulation:
IL12B monomer can be secreted and interact with the Interleukin 12 receptor. Human IL12B homodimers can be produced by cells containing expression constructs (Ling et al. 1995, Alloza & Vandenbroeck 2015) but not under natural conditions (Carra et al. 2000). IL12B homodimers do not mediate biological activity, rather they act as a competitive antagonist by competition with IL12 (Ling et al. 1995).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-447226",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-447226"
}
]
},
{
"id": "R-HSA-447252",
"name": "IL12RB1:TYK2 binds IL12RB2:JAK2",
"equation": "",
"summary": "Interleukin-12 receptor beta 2 (IL12RB2) is a type I transmembrane protein with a 595-amino-acid-long extracellular domain and a cytoplasmic tail of 216 amino acids that contains three tyrosine residues. It binds Interleukin-12 with low affinity. IL12RB2 binds Interleukin 12 receptor beta 1 subunit (IL12RB1) forming the high affinity Interleukin-12 receptor (Presky et al. 1996a, 1996b), which signals via JAK2 and TYK2 (Zou et al. 1997).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-447252",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-447252"
}
]
},
{
"id": "R-HSA-448427",
"name": "Interleukin-27 binds Interleukin-27 receptor",
"equation": "",
"summary": "Interleukin-27 is a heterodimer composed of Interleukin-27 subunit alpha (IL27) and Epstein-Barr virus-induced gene 3 (EBI3). It binds to the Interleukin-27 heterodimeric receptor, which is composed of Interleukin-27 receptor subunit alpha (IL27RA, WSX-1) and Interleukin-6 receptor subunit beta (IL6ST, gp130). IL6ST is a signal transducing protein that is a component of several other cytokine receptors including the Interleukin-6 and Interleukin-11 receptors (Pflanz et al. 2004). In the absence of IL27RA, Interleukin-27 can bind to IL6ST but with low affinity (Jia et al. 2016).
Regulation: IL27RA can be cleaved releasing a soluble form (sIL27RA) that can bind to Interleukin-27 and antagonize Interleukin-27 binding to its heterodimer receptor (Dietrich et al. 2014).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-448427",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-448427"
}
]
},
{
"id": "R-HSA-449976",
"name": "IL11:IL11RA binds IL6ST:JAK1,JAK2,(TYK2)",
"equation": "",
"summary": "Interleukin-11 receptor alpha subunit (IL11RA) binds interleukin-11 (IL11) with low affinity but for high affinity binding and signaling must associate with interleukin-6 receptor beta subunit (IL6ST, gp130).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-449976",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-449976"
}
]
},
{
"id": "R-HSA-450031",
"name": "Interleukin-3 receptor alpha: Interleukin-3 binds IL3RB:JAK2",
"equation": "",
"summary": "The alpha subunit of the IL3 receptor binds IL 3 with low affinity. Binding of this dimer to the common beta subunit (Bc) confers high affinity binding. Recent models of receptor activation suggest a sequential activation that is initiated by the low-affinity interaction of ligand with the alpha chain to form a binary complex. This binary complex is then able to bind preformed Bc dimers generating a 2:2:2 hexameric complex (Hansen et al. 2008). Covalent linkage of the receptor subunits is required for receptor signalling (Stomski et al. 1996).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-450031",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-450031"
}
]
},
{
"id": "R-HSA-453104",
"name": "Phosphorylated SHC1 recruits GRB2:GAB2",
"equation": "",
"summary": "Phosphorylated Shc recruits Grb2 and Gab2, probably by binding to Grb2 in the Grb2:Gab2 complex. Gab2 associates with Grb2, Shc, Shp2 and the p85 subunit of PI3K (Gu et al. 1998). The association of Grb2 with Gab2 has been suggested to be constitutive (Gu et al. 2000, Kong et al. 2003, Harkiolaki et al. 2009), so Gab2 may be recruited to Shc1 with Grb2. Alternatively, Gab2 has been suggested to associate constitutively with Shc (Kong et al 2003). In either case, the result is a complex of Shc:Grb2:Gab2. Gab2 binding to p85 (Gu et al. 1998) links Shc1 to PI3K activity and subsequent activation of kinases such as Akt (Gu et al. 2000).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-453104",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-453104"
}
]
},
{
"id": "R-HSA-453111",
"name": "Phosphorylated SHC recruits GRB2:SOS1",
"equation": "",
"summary": "Shc is tyrosine phosphorylated by an unidentified kinase, creating a docking site for the SH2 domain of Grb2 (Zhu et al. 1994). Grb2 is an adaptor protein believed to be constitutively associated with the guanine nucleotide exchange protein Sos1 (often abbreviated to Sos). Recruitment of the Grb2:Sos1 complex leads to activation of the Ras pathway (Ravichandran & Burakoff 1994) and consequently activation of the MAPK pathway.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-453111",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-453111"
}
]
},
{
"id": "R-HSA-508247",
"name": "Gab2 binds the p85 subunit of Class 1A PI3 kinases",
"equation": "",
"summary": "Shc promotes Gab2 tyrosine phosphorylation via Grb2 (Gu et al. 2000). This promotes binding of Gab2 to p85alpha, a component of Class 1A PI3Ks (Gu et al. 1998). JAK1 may also be involved in PI3K recruitment (Migone et al. 1998). Binding of p85 activates PI3K kinase activity, with consequent effects on many processes including Akt activation. This is one of two mechanisms described for the recruitment of PI3K to the IL-3/IL-5/GM-CSF receptors, the other is mediated by Serine-585 phosphorylation of the common beta chain.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"P42336-1",
"O60674-1",
"P42338-1",
"O00329-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-508247",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-508247"
}
]
},
{
"id": "R-HSA-5672965",
"name": "RAS GEFs promote RAS nucleotide exchange",
"equation": "",
"summary": "The human genome is predicted to encode 27 RAS guanine nucleotide exchange factors (GEFs) that promote the exchange of GDP for GTP on membrane-associated RAS in response to RAS-MAPK pathway activation by growth factors, hormones, cytokines and other stimuli (reviewed in Cherfils and Zeghouf, 2013; Cargnello and Roux, 2011). Nucleotide exchange stimulates a conformational change in RAS to facilitate its interaction with RAF, ultimately promoting the phosphorylation of downstream effectors MAPK3 and MAPK1 (also known as ERK1 and ERK2) (reviewed in Cseh et al, 2014; Vigil et al, 2010).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P07949-1",
"P22455-1",
"P52333-1",
"P16234-1",
"O60674-1",
"Q9UQM7-1",
"P00533-1",
"P04626-1",
"P06241-1",
"P10721-1",
"Q13554-1",
"Q02763-1",
"P01112-1",
"P36888-1",
"P09619-1",
"P18433-5",
"Q05397-1",
"Q13557-1",
"P08581-1",
"P23458-1",
"Q13555-1"
],
"evidence": [
{
"id": "R-HSA-5672965",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5672965"
}
]
},
{
"id": "R-HSA-5672969",
"name": "Phosphorylation of RAF",
"equation": "",
"summary": "Downstream of RAF dimerization and allosteric activation, RAF monomers and KSR1 undergo a series of activating phosphorylations in both the activation loop (AL) and, in the case of ARAF, RAF1 and KSR1, in the NtA . Phosphorylation of the activation loop residues (T491, S494 in RAF1, T452, T455 in ARAF and T599, S602 in BRAF) contributes to full kinase activity, although this may be less critical for ARAF, and RAFs in general, than for other kinases due to their regulation by 14-3-3 binding (Zhu et al, 2005; Zhang et al, 2000; Baljuls et al, 2008, reviewed in Matallanas et al, 2011; Udell et al, 2011). AL phosphorylation may occur through cis-autophosphorylation within the RAF dimer, although phosphorylation by other kinases is also possible (Hu et al, 2013; reviewed in Matallanas et al, 2011).
Phosphorylation in the RAF NtA region is required for full kinase activity, for interaction with MAP2K substrates and for the ability of activated RAF to act as an allosteric activator of other RAF monomers (Marais et al, 1995; Diaz et al, 1997; Xiang et al, 2002; Edin et al, 2005; Hu et al, 2013; Mason et al, 1999). Phosphorylation of these residues (S338 and Y441 in RAF1, S299 and Y302 in ARAF and Y602 in KSR1) may be mediated by a kinase of the SRC, JAK or PAK family kinases, by MAP2K kinases, calmodulin kinase CaMKII or through autophosphorylation by RAF itself (Marais et al, 1995; Xia et al, 1996; King et al, 1998; Sun et al, 2000; Tran et al, 2003; Tran et al, 2005; Salzano et al. 2012, Hu et al, 2013; reviewed in Matallanas et al, 2011). The phosphorylated NtA of RAF1 is also the binding site for the negative regulator PEPB1, also known as RKIP. PEBP1 binding to RAF1 prevents phosphorylation of the MAP2K substrates (Park et al, 2006; Rath et al, 2008; reviewed in Shin et al, 2009).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"O60674-1",
"Q9UQM7-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"Q13554-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q13557-1",
"Q13555-1"
],
"evidence": [
{
"id": "R-HSA-5672969",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5672969"
}
]
},
{
"id": "R-HSA-5696482",
"name": "CTF1 binds LIFR:JAKs",
"equation": "",
"summary": "Cardiotrophin-1 (CTF1/CT-1) is a member of the IL-6 family of cytokines which was originally discovered as a factor which can induce hypertrophy of cardiac myocytes both in vitro and in vivo (Pennica et al. 1995a). Subsequently, CTF1 has been shown to have a wide variety of different effects on cardiac and non cardiac cells including the ability to stimulate the survival of both cardiac and neuronal cells (Latchman 1999). Leukemia inhibitory factor (LIF), CTF1, and oncostatin M (OSM) are four helix bundle cytokines acting through a common heterodimeric receptor composed of gp130 and LIF receptor (LIFR) (Pennica et al. 1995b).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-5696482",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5696482"
}
]
},
{
"id": "R-HSA-6783524",
"name": "OSM,LIF,CTF1 receptor complex binds gp130",
"equation": "",
"summary": "Glycoprotein (gp)130 is the common signal transducer for LIF, OSM and CTF1 receptor complexes. gp130/OSMRbeta complex is used solely by OSM, the gp130/LIFR complex is shared by the three receptors LIF, OSM and CTF1. Binding of OSM to either the gp130/LIFR or the gp130/OSMRbeta complex triggers the activation of multiple members of the Janus kinase (JAK) family.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6783524",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6783524"
}
]
},
{
"id": "R-HSA-6783530",
"name": "gp130:JAKs bind CNTFR",
"equation": "",
"summary": "Members of the interleukin-6 (IL-6) cytokines, IL-6, IL-11, leukemia inhibitory factor (LIF), oncostatin M (OSM) cardiotrophin-1 (CT-1) and cardiotrophin-like cytokine (CLC) share one or both of the receptor signal transducing subunits glycoprotein (gp) 130 and LIFR in their respective receptor complexes (Taga et al. 1997). gp130 (also known as CD130) is the central signal transducer of the interleukin-6 (IL6)-related cytokines. It is expressed in almost all organs, including heart, kidney, spleen, liver, lung, placenta, and brain. Mice lacking gp130 gene results in embryonic lethality at day 12.5 (Yoshida et al. 1996). CNTFR alpha bound to CNTFR or CLCF1:CRLF1 complex recruits gp130 by binding to the cytokine-binding domain (CBD) of gp130 (Man et al. 2003).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6783530",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6783530"
}
]
},
{
"id": "R-HSA-6783552",
"name": "OSM binds LIFR:JAKs,OSMR:JAKs",
"equation": "",
"summary": "Oncostatin M (OSM) is a multifunctional cytokine produced by bone microenvironment by cells of both mesenchymal and hematopoietic origin, including osteocytes, osteoblasts, macrophages and T lymphocytes (Brown et al. 1987, Malik et al. 1989). It belongs to the interleukin-6 (IL-6) subfamily and shares properties with all the members of the family but is closely related to leukemia inhibitory factor (LIF) structurally and functionally and it infact utilizes the LIF receptor (LIFR) in addition to its specific receptor OSMR. In humans, there are two types of functional OSM receptor complexes: the type I OSM receptor complex consisting of gp130 and LIF receptor (LIFR) subunits, and the type II OSM receptor complex consisting of gp130 and OSM receptor beta (OSMRbeta) subunits (Chen & Benveniste 2004, Thoma et al. 1994, Gomez-Lechon 1999). Upon association with its specific receptor complexes OSM, then activates two major signaling pathways: Janus Kinase-Signal Transducers and Activators of Transcription (JAK-STAT) and Mitogen-Activated Protein Kinase (MAPK), to regulate downstream events. OSM is involved in the regulation of complex cellular processes such as growth regulation, differentiation, gene expression, and cell survival in humans (Tanaka & Miyajima 2004).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6783552",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6783552"
}
]
},
{
"id": "R-HSA-6783556",
"name": "LIFR:JAKs bind gp130:JAKs:CNTFR",
"equation": "",
"summary": "The cytokine receptor gp130 is the shared signalling subunit of the interleukin (IL)-6-type cytokines. IL-6 and IL-11 signal through gp130 homodimer whereas leukaemia inhibitory factor (LIF), ciliary neurotrophic factor receptor (CNTFR), Cardiotrophin-like cytokine factor 1 (CLCF1), Cardiotrophin-1 (CT-1) and Oncostatin-M (OSM) exerts its action through a heterodimer of gp130 and the LIF receptor (LIFR) (Heinrich et al. 2003, Giese et al. 2005). LIFR beta structure closely resembles that of gp130 and upon ligand binding forms gp130:LIFR beta heterodimer. Finally CNTFR alpha complexed with this signal transducing heterodimer converts into functional tripartite CNTF receptor and induces phosphorylation of both gp130 and LIFR beta (Davis et al. 1993, Stahl & Yancopoulos 1994). Formation of the tripartite complex then leads to activation of Janus family kinases, JAK1, 2, 3, and TYK2 and phosphorylation of tyrosine residues on the cytoplasmic domain of gp130 (Kass 2011).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6783556",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6783556"
}
]
},
{
"id": "R-HSA-6783681",
"name": "LIF binds LIFR",
"equation": "",
"summary": "Leukemia inhibitory factor (LIF), initially named for its ability to cause myeloid leukemic cells to differentiate into macrophages (Gearing et al. 1987) is a member of the interleukin-6 (IL-6)-related cytokines. It possesses overlapping function with other IL-6 family members. The pleiotrophic effects of LIF in many physiological systems include proliferation, differentiation, and cell survival (Hilton 1992, Metcalf 1992). It exerts numerous effects in the nervous system, promote gliogenesis, support neural stem cell (NSC) renewal (Bonni et al. 1997, Hermanson et al. 2002, Pitman et al. 2004) and also been implicated in the expression of various cytokines. LIF exerts its effects by binding to a bipartite membrane receptor complex that consists of the LIF receptor subunit (LIFR) and the glycoprotein (gp)130 subunit and activates STAT3. LIF initially binds LIFR and the LIFR Ig-like domains contributes to LIF binding (Bitard et al. 2003).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6783681",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6783681"
}
]
},
{
"id": "R-HSA-6784189",
"name": "JAKs bind LIFR",
"equation": "",
"summary": "Leukemia inhibitory factor receptor (LIFR) beta and Oncostatin M receptor (OSMR) constitutively associates with the JAK-TYK family of cytoplasmic protein tyrosine kinases in the absence of ligand. Activation of these kinases occur as a result of ligand-induced heterodimerzation of LIFR beta or OSMR with gp130 (Stahl et al. 1994, Hermanns et al. 2000).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6784189",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6784189"
}
]
},
{
"id": "R-HSA-6784204",
"name": "JAKs bind OSMR",
"equation": "",
"summary": "Leukemia inhibitory factor receptor (LIFR) beta and Oncostatin M receptor (OSMR) constitutively associates with the JAK-TYK family of cytoplasmic protein tyrosine kinases in the absence of ligand. Activation of these kinases occur as a result of ligand-induced heterodimerzation of LIFR beta or OSMR with gp130 (Stahl et al. 1994, Hermanns et al. 2000).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6784204",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6784204"
}
]
},
{
"id": "R-HSA-6785821",
"name": "SOCS5,(SOCS1) bind IL4RA",
"equation": "",
"summary": "SOCS5 can bind the type I IL4R, reducing its association with JAK1, which results in the inhibition of IL4-mediated STAT6 activation (Seki et al. 2002). Similarly SOCS1 serves as a regulator of IL-4 signaling, diminishing the magnitude and duration of STAT6 activation (Dickensheets et al. 2007).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-6785821",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6785821"
}
]
},
{
"id": "R-HSA-6785898",
"name": "IL4R binds JAK2",
"equation": "",
"summary": "The interleukin-4 receptor (IL4R) constitutively binds Janus kinase 2 (JAK2) (Roy et al. 2002).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-6785898",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6785898"
}
]
},
{
"id": "R-HSA-6786050",
"name": "IL4R, IL13RA, JAK2 and TYK2 are tyrosine phosphorylated",
"equation": "",
"summary": "Interleukin-4 receptor alpha subunit (IL4R) and Interleukin-13 receptor subunit alpha 1 (IL13RA1) are phosphorylated on tyrosines in response to Interleukin-13 (IL13) in human blood monocytes (Roy et al. 2002, Bhattacharjee et al. 2013). The associated Janus-kinase (JAK) family kinases JAK2 and TYK2 are also phosphorylated (Roy & Cathcart 1998, Bhattacharjee et al. 2013). Although JAK1 binds to IL4R in response to IL13, it does not appear to be phosphorylated in response to IL13 (Roy & Cathcart 1998, Bhattacharjee et al. 2013).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6786050",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6786050"
}
]
},
{
"id": "R-HSA-6786058",
"name": "JAK1 binds IL4R in IL4-bound IL4R1",
"equation": "",
"summary": "In human blood monocytes, where the type I interleukin-4 (IL4) receptor (IL4R1) is the predominant IL4 receptor type, IL4 leads to tyrosine phosphorylation of Janus kinase 1 (JAK1), rather than constitutively bound JAK2, JAK3 or Non-receptor associated tyrosine kinase 2 (TYK2). JAK1 was found to be essential for IL4-mediated expression of 15-lipoxygenase while JAK2 and TYK2 antisense inhibition had no effect (Bhattacharjee et al. 2013). As JAK1 binds IL4RA in response to IL13 binding (Roy et al. 2002), it is believed that IL4 similarly triggers binding of JAK1 to IL4 receptor complexes. The molecular trigger for JAK1 binding is not clear.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6786058",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6786058"
}
]
},
{
"id": "R-HSA-6786070",
"name": "IL4:IL4R:JAK2 binds IL13RA1:TYK2",
"equation": "",
"summary": "Interleukin-13 receptor subunit alpha-1 (IL13RA1), with associated Non-receptor tyrosine-protein kinase 2 (TYK2), binds the IL4:IL4R:JAK2 complex to form the ligand-bound Type II IL4 receptor complex (IL4R2). IL4R2 is predominantly expressed on the surface of non-hematopoietic cells. It is also a receptor for Interleukin-13 (IL13) (Obiri et al. 1995, Aman et al. 1996, Hilton et al. 1996). Crystal structures of the IL4:IL4R:IL13RA1 and IL13:IL4R:IL13RA1 complexes have been determined (LaPorte et al. 2008).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-6786070",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6786070"
}
]
},
{
"id": "R-HSA-6786072",
"name": "p-Y705-STAT3,p-Y641-STAT6 dissociate",
"equation": "",
"summary": "Once phosphorylated, Signal transducer and activator of transcription 3 (STAT3) and STAT6 dissociate from the IL4 receptor/JAK1 complex.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6786072",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6786072"
}
]
},
{
"id": "R-HSA-6786092",
"name": "IL4:IL4R:JAK2 binds IL2RG:JAK3",
"equation": "",
"summary": "Interleukin 2 receptor gamma subunit (IL2RG), with constitutively-associated Janus kinase 3 (JAK3), binds the IL4:IL4R:JAK2 complex, interacting with IL4 and IL4R to form the ligand-bound type I IL4 receptor complex, IL4R1 (LaPorte et al. 2008).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-6786092",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6786092"
}
]
},
{
"id": "R-HSA-6786095",
"name": "JAK1 phosphorylates STAT3,STAT6",
"equation": "",
"summary": "Signal transducer and activator of transcription 3 (STAT3) and STAT6 are phosphorylated by Janus kinase 1 (JAK1) in response to Interleukin-4 (IL4) (Bhattacharjee et al. 2013). STAT3 is phosphorylated on Y705, STAT6 is phosphorylated on Y641, residues critical for their function (Schindler & Darnell 1995, Mikita et al. 1996).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6786095",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6786095"
}
]
},
{
"id": "R-HSA-6786096",
"name": "IL4R, IL2RG, JAK1 in IL4-bound IL4R1:JAK1 are phosphorylated",
"equation": "",
"summary": "Interleukin-4 receptor subunit apha (IL4R), Interleukin-2 receptor subunit gamma (IL2RG) and Janus kinase 1 (JAK1), but not Non-receptor associated tyrosine kinase 2 (TYK2), JAK2 or JAK3 are tyrosine phosphorylated in response to IL4 (Bhattacharjee et al. 2013). The order of these phosphorylation events is not clear. Based on studies of other interleukin receptors and their associated JAKs it is likely that JAK1 autophosphorylates and then phosphorylates IL4R and IL2RG.
IL4R contains 5 conserved tyrosine residues, Y497, Y575, Y603, Y631, and Y713, which can all play a role in signaling through this receptor. Structure-function analyses have revealed that Y497 is part of the IL4R motif that is necessary for the recruitment of IRS1 and IRS2 to IL4R and is critical for IL4-dependent cell proliferation (Keegan et al. 1994). STAT6 signaling requires one of tyrosines Y575, Y603, and Y631 (Ryan et al. 1996). Y713 is part of an immunotyrosine-based inhibitory motif (ITIM) shown to be important in the negative regulation of IL4 and IL13 responses (Kashiwada et al. 2001).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6786096",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6786096"
}
]
},
{
"id": "R-HSA-6786101",
"name": "IL4 binds IL4R:JAK2",
"equation": "",
"summary": "The first step in the formation of both types of IL4 receptor is the binding of Interleukin-4 (IL4) with Interleukin-4 receptor subunit alpha (IL4R) , which has Janus kinase 2 (JAK2) constitutively associated (Hoffman et al. 1995, Shen et al. 1996, Hage et al. 1999).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-6786101",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6786101"
}
]
},
{
"id": "R-HSA-6786110",
"name": "JAK1 binds IL4R in IL13-bound IL13R type II",
"equation": "",
"summary": "In response to Interleukin-13 ( IL13) binding, Janus kinase 1 (JAK1) binds to Interleukin-4 receptor alpha subunit (IL4R) (Roy et al. 2002). IL4R has 2 JAK binding motifs so it is believed that IL4R can bind JAK2 constitutively and additionally bind JAK1 upon ligand binding. The molecular trigger for JAK1 binding is not clear.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6786110",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6786110"
}
]
},
{
"id": "R-HSA-6786114",
"name": "IL13:IL13RA:TYK2 binds IL4R:JAK2",
"equation": "",
"summary": "Interleukin-13 receptor alpha subunit (IL13RA1) binds Interleukin-13 (IL13) with a relatively low affinity, but when paired with Interleukin-4 receptor subunit alpha (IL4R), binds with much higher affinity (Kd = 400 pmol/L) and forms a functional IL13 receptor that is capable of signaling (Miloux et al. 1997). This type II IL13 receptor complex is also the alternative type II receptor for IL4.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-6786114",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6786114"
}
]
},
{
"id": "R-HSA-6786124",
"name": "STAT3,STAT6 bind p-Y-IL4R",
"equation": "",
"summary": "Signal transducer and activator of transcription 6 (STAT6) binds to tyrosine-phosphorylated Interleukin-4 receptor subunit alpha (IL4R) (Hou et al. 1994, Schindler et al. 1996, Mikita et al. 1998). Binding of STAT3 has also been reported (Rahaman et al. 2005, Bhattacharjee et al. 2013) but is sometimes reported to be dependent on interleukin-13 receptor subunit alpha (IL13RA) rather than IL4R (Umeshita-Suyama et al. 2000). Other reports have suggested that STAT3 is not phosphorylated in response to IL4 (Friedrich et al. 1999). Consistent with the fact that IL4 and IL13 receptors both incorporate IL4R, they also share common signaling pathways. IL4R is believed to be the signaling component of both IL4 and IL13 receptors because treatment with either generates intermediates that are characteristic of IL4 responses, including phosphorylation of IL4R, insulin receptor substrate 2 (IRS2), Janus kinase 1 (JAK1), and Non-receptor tyrosine-protein kinase 2 (TYK2) (Welham et al. 1995). STAT6-deficient mice suggest that IL13 signaling, like IL4 signaling, uses STAT6 (Takeda et al. 1996, Kaplan et al. 1996). STAT1 activation in response to IL4 has been reported (Wang et al. 2004) but also disputed (Bhattacharjee et al. 2013).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6786124",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6786124"
}
]
},
{
"id": "R-HSA-6788571",
"name": "STAT1,STAT3,STAT6 bind IL13:IL13R type II",
"equation": "",
"summary": "Characterisation of Signal transducer and activator of transcription 6 (STAT6)-deficient mice suggests that Interleukin-13 (IL13) signaling, like Interleukin-4 (IL4) signaling, uses STAT6 (Takeda et al. 1996, Kaplan et al. 1996). In humans STAT6 is activated in response to IL4 and IL13 (Wang et al. 2004) and can bind tyrosine-phosphorylated Interleukin-4 receptor subunit alpha (IL4R) (Hou et al. 1994, Schindler et al. 1996, Mikita et al. 1998), but in response to IL13, STAT6 binds Interleukin-13 receptor subunit alpha 1 (IL13RA1), to be phosphorylated by Non-receptor associated tyrosine kinase 2 (TYK2) (Bhattacharjee et al. 2013).
Binding and phosphorylation of STAT3 has been reported in response to IL13 (Rahaman et al. 2005, Bhattacharjee et al. 2013) but not IL4 (Friedrich et al. 1999), suggesting that STAT3 binding might depend on IL13RA, but recently STAT3 was reported to associate with IL4R and be phosphorylated by Janus kinase 2 (JAK2) (Umeshita-Suyama et al. 2000, Bhattacharjee et al. 2013).
STAT1 is activated in response to IL13 (Wang et al. 2004) and reported to bind IL13RA1 and be phosphorylated by TYK2 (Bhattacharjee et al. 2013).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6788571",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6788571"
}
]
},
{
"id": "R-HSA-6788582",
"name": "STAT1,STAT3,STAT6 phosphorylation",
"equation": "",
"summary": "Once bound to the Interleukin-13 (IL13) type II receptor, Signal transducer and activator of transcription 3 (STAT3) is tyrosine phosphorylated by Janus kinase 2 (JAK2), while STAT1 and STAT6 are phosphorylated by Non-receptor tyrosine kinase 2 (TYK2) (Bhattacharjee et al. 2013).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6788582",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6788582"
}
]
},
{
"id": "R-HSA-6788628",
"name": "p-Y-STATs dissociate",
"equation": "",
"summary": "Once phosphorylated, Signal transducer and activator of transcription family members (STATs) dissociate from the receptor complex and translocate to the nucleus.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6788628",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6788628"
}
]
},
{
"id": "R-HSA-6802916",
"name": "RAF is phosphorylated downstream of moderate kinase activity BRAF mutants",
"equation": "",
"summary": "Homo- or heterodimerization (with RAF1, also known as CRAF) downstream of moderate kinase activity BRAF mutants leads to phosphorylation and activation of the 'receiver' kinase. Unlike the case for the highly active V600E BRAF mutation, pathway activation downstream of moderately activated BRAF mutants depends both on RAS binding and on dimerization (Wan et al, 2004; Roring et al, 2012; Freeman et al, 2013; reviewed in Samatar and Poulikakos, 2014; Lavoie and Therrien, 2015)
",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"O60674-1",
"Q9UQM7-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"Q13554-1",
"P01112-1",
"P36507-1",
"Q02750-1",
"Q13557-1",
"Q13555-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802916",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802916"
}
]
},
{
"id": "R-HSA-6802924",
"name": "RAF is phosphorylated downstream of oncogenic RAS",
"equation": "",
"summary": "In many cancer types, RAF1 (also known as CRAF) appears to be a critical initial effector of the ERK pathway downstream of activated RAS and also mediates pathway activation in the presence of WT BRAF plus BRAF inhibitors (Rushworth et al, 2006; Dumaz et al, 2006; Garnett et al, 2005; Karreth et al, 2011; Poulikakos et al, 2010; Heidorn et al, 2010; Roring et al, 2012; reviewed in Samatar et al, 2014; Lito et al, 2013). This activation depends largely on heterodimerization with BRAF, although homodimers also contribute (Weber et al, 2001; Rushworth et al, 2006). Activation of RAF downstream of mutant RAS appears to require full phosphorylation of the N-region and the activation loop, unlike the case in BRAF mutant cells, where RAF N-loop phosphorylation is dispensable (Garnett et al, 2005).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"O60674-1",
"Q9UQM7-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"Q13554-1",
"P01112-1",
"P36507-1",
"Q02750-1",
"Q13557-1",
"Q13555-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802924",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802924"
}
]
},
{
"id": "R-HSA-6802927",
"name": "BRAF and RAF fusion mutant dimers are phosphorylated",
"equation": "",
"summary": "Fusion mutants of BRAF and RAF1 are believed to form constitutive dimers and activate downstream signaling independent of RAS and external stimuli (Jones et al, 2008; Cin et al, 2011; Palanisamy et al, 2010; Ciampi et al, 2005; Stransky et al, 2014; Hutchinson et al, 2013; Zhang et al, 2013; Lee et al, 2012; Ricarte-Filho et al, 2013; reviewed in Lavoie and Therrien et al, 2015). The RAF portion of the fusion mutants may undergo phosphorylation of the N-region and activation loops similar to WT as shown in this reaction, although this has not been studied in detail. While WT RAF phosphorylation happens in the context of a complex with with RAS, this is unlikely to be the case for the fusion mutants, as many of these proteins lack the N-terminal RAS binding domain (reviewed in Lavoie and Therrien, 2015).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O15164-1",
"Q6ZMT4-1",
"O60674-1",
"Q9UQM7-1",
"P12931-1",
"Q53H12-1",
"P04049-1",
"P10398-1",
"P15056-1",
"Q13554-1",
"P36507-1",
"Q7KZF4-1",
"Q02750-1",
"Q13557-1",
"Q5XG87-1",
"Q13555-1"
],
"evidence": [
{
"id": "R-HSA-6802927",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802927"
}
]
},
{
"id": "R-HSA-6802941",
"name": "RAF is paradoxically phosphorylated downstream of kinase-inactive RAF",
"equation": "",
"summary": "The enhanced dimerization of inhibited or kinase dead versions of BRAF to RAF1/CRAF stimulates the phosphorylation and transactivation of RAF1 (Wan et al, 2004; Garnett et al, 2005; Heidorn et al, 2010; Poulikakos et al, 2010; Hatzivassiliou et al, 2010; reviewed in Samatar and Poulikakos, 2014; Lavoie and Therrien, 2015). Other evidence suggests that paradoxical activation of RAF1 by inhibited or inactive BRAF may result from relief of an inhibitory CRAF autophosphorylation event (Holderfield et al, 2013; reviewed in Holderfield, 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"O60674-1",
"Q9UQM7-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"Q13554-1",
"P01112-1",
"P36507-1",
"Q02750-1",
"Q13557-1",
"Q13555-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802941",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802941"
}
]
},
{
"id": "R-HSA-6809140",
"name": "IL35 binds IL-12RB2:IL6ST receptor",
"equation": "",
"summary": "Interleukin-35 (IL35) is a heteromeric complex of Interleukin-12 subunit alpha (IL12A) and Interleukin-27 subunit beta (EBI3, IL27B) ) induces hetero and homodimers of Interleukin 6 receptor beta precursor (IL6ST, gp130) and Interleukin 12 receptor beta 2 (IL12RB2).; These results suggested that Interleukin 35 is bound to these three receptor subunits providing insight into the partial resistance to Interleukin 35 mediated suppression observed after the deletion of a single chain. Moreover there is the possibility of the assembly of higher structures by Interleukin 35, as has been suggested for Interleukin 6 receptor subunit beta precursor.; IL12RB2 and IL6ST represent the most plausible components of Interleukin 35 receptor. However, additional molecules might facilitate cytokine binding or downstream signaling, although this would be unprecedented in the Interleukin 6 receptor and Interleukin 12 receptor families (Collison et al. 2012); ; Moreover Interleukin 35 (IL35) uses an unique heterodimer of receptor chains Interleukin 12 receptor subunit beta (IL 12RB2) and Interleukin 6 receptor subunit beta (gp130 or IL6ST) for its signal transduction.; The composition of Interleukin 35 heterodimeric receptor is not totally elucidated, but Interleukin 35\u2013Interleukin 35 receptor interaction and assembly given the `site 1 2 3' follows an architectural paradigm originally established for Interleukin 6 (IL 6) (Boulanger et al. 2003).; ; Computational analysis suggests 3 potential conformations of Interleukin 35/Interleukin 35 Receptor complex: ; First, IL6ST binds to site 2 in the Interleukin 6(IL 6), Ciliary neurotrophic factor (CNTF) and LIF (Leukemia inhibitory factor) complexes and thus could do so in the IL 35 IL35R complex, leaving IL12RB2 to bind site 3. ; Second, the Interleukin 35\u2013Interleukin 35 receptor complex could form symmetric homohexameric assemblies (2:2:2) analogous to the Interleukin 6 receptor complex, thus allowing IL 12RB2 and IL6ST to each bind to site 3 on IL12A. ; Third, IL6ST and IL12RB2 could both be capable of binding to site 2 and site 3 and therefore exist in an interchanging equilibrium of heterotetrameric complexes (at a ratio of 1:1:1:1, IL6ST to IL12RB2 to Interleukin 27 beta subunit (EBI3). Indeed, studies of the Interleukin 6 ligand receptor complex suggest that it may be able to signal as tetrameric or hexameric assembly. ; ; Finally, a previously unknown mode of binding may exist that uses the site 1 2 3 model in a manner not predicted on the basis of the existing structural information for IL 6, LIF and CNTF (Collison et al. 2012).; ; As it is not clear whether the dimeric receptor can form in the absence of ligand, formation of the receptor dimer is represented here as a black box event.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-6809140",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6809140"
}
]
},
{
"id": "R-HSA-873918",
"name": "Transphosphorylation of JAK1",
"equation": "",
"summary": "The initial phosphorylation of JAK1 and JAK2 is mediated by JAK2. Autophosphorylated JAK2 may transphopshorylate JAK1 bound to IFNGR1 chain. Tyrosine 1033 in the activation loop of the JAK1 kinase domain may be the target for transphosphorylation (phosphorylation site mentioned here is based on sequence similarity with all the other JAK kinases).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29350-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-873918",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-873918"
}
]
},
{
"id": "R-HSA-873919",
"name": "Phosphorylation of JAK2",
"equation": "",
"summary": "IFN-gamma binding to the receptor complex, induces JAK2 autophosphorylation and activation. Like all protein tyrosine kinases (PTKs) JAK2 activity also depends on the phosphorylation of tandem tyrosine residues within the activation loop that results in the removal of the activation loop from the active site. Multiple phosphorylation sites have been identified in JAK2 (tyrosines 221, 570, 868, 966, 972, 1007 and 1008 ) of which phosphorylation of tyrosine 1007 is essential for kinase activity. Tyrosine 1007 is in the activation loop and phosphorylation allows access of the catalytic loop to the ATP in the ATP binding domain. Of all the predicted phoshorylation sites only tyrosine 1007 is represented in the reaction.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-873919",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-873919"
}
]
},
{
"id": "R-HSA-873921",
"name": "Binding of STAT1 to p-IFNGR1",
"equation": "",
"summary": "The phosphorylated tyrosine residue 440 in the 440YDKPH444 motif on IFNGR1 chain serves as a docking site and recruits STAT1, an SH2 domain-containing transcription factor to the functional receptor unit.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-873921",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-873921"
}
]
},
{
"id": "R-HSA-873922",
"name": "Phosphorylation of STAT1 by JAK kinases",
"equation": "",
"summary": "STAT1 pair recruited to the receptor complex is phosphorylated near the C-terminus at residue Y701, probably by JAK2. This phosphorylation enables the STAT1 homodimer formation which is further phosphorylated on residue S727.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-873922",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-873922"
}
]
},
{
"id": "R-HSA-873924",
"name": "Phosphorylation of IFNGR1 by JAK kinases",
"equation": "",
"summary": "The phosphorylated active JAK1 kinase inturn phosphorylates tyrosine residue 440 on each of the IFNGR1 chains to form two adjacent docking sites for the latent STAT1 SH2 domains.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-873924",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-873924"
}
]
},
{
"id": "R-HSA-873926",
"name": "IFNG dimer binds IFNGR",
"equation": "",
"summary": "The IFNG receptor complex is a pre-assembled entity, as constitutive interactions are seen between IFNGR1 and IFNGR2, and between two IFNGR2 chains in the absence of ligand IFNG. JAK1 and JAK2 constitutively associate with the intracellular domains of the subunits of the IFNG receptor complex, providing it with tyrosine kinase activity. In unstimulated cells JAK1 preferentially associates with IFNGR1 and while JAK2 associates with IFNGR2 chains. JAK1 enhances the interaction between IFNGR1 and IFNGR2 chains, and thus has a major role in the pre-assembly of the IFNGR complex, in contrast the kinase activity of JAK2 is required to observe any signaling by IFNG.
IFNG binds directly to both the receptor chains IFNGR1 and IFNGR2. IFNGR1 is a high affinity receptor and binds directly to IFNG whereas IFNGR2 binds to IFNG in presence of IFNGR1. According to Krause et al. model IFNG binds to IFNGR1 chains first and then IFNGR2 chains interact with the IFNGR1:IFNG:IFNGR1 complex.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-873926",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-873926"
}
]
},
{
"id": "R-HSA-873927",
"name": "Release of STAT1 dimer from active receptor unit",
"equation": "",
"summary": "The phosphorylated STAT1 on IFNGR1 chains homodimerize through reciprocal SH2-phosphotyrosine interactions to form p-STAT1 homodimer called gamma-activated-factor (GAF). This phosphorylated STAT1 homodimer disassociates from the receptor complex and translocates to the nucleus.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-873927",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-873927"
}
]
},
{
"id": "R-HSA-877269",
"name": "SOCS-1 and SOCS-3 binds to p-JAK2",
"equation": "",
"summary": "SOCS-1 and SOCS-3 coprecipitates with JAK kinases upon IFNG stimulation and are able to inhibit the JAK-STAT pathway, although with different affinity and kinetics. SOCS1 and SOCS3 binds to phosphorylated JAK1/2 and prevent the tyrosine kinase activity of JAKs through their kinase inhibitory region (KIR), thereby inhibiting downstream IFNG signaling. SOCS1 may also prevent IFNG signaling by targeting the signaling machinery to ubiquitin-proteasomal degradation pathway.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-877269",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-877269"
}
]
},
{
"id": "R-HSA-877308",
"name": "Dephosphorylation of JAKs by PTPs",
"equation": "",
"summary": "Protein tyrosine phosphatases (PTPs) SHP1 and SHP2 down regulate the IFNG signaling by dephosphorylating the tyrosine residues critical to the activation of JAK kinases. PTP1B interacts directly with JAK2 but not JAK1 and dephosphorylate the tyrosine Y1007 on JAK2.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"Q06124-2",
"P29350-1",
"P18031-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-877308",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-877308"
}
]
},
{
"id": "R-HSA-879907",
"name": "Tyrosine kinases phosphorylate the receptor",
"equation": "",
"summary": "Phosphorylation of the receptor common beta chain (Bc) creates binding sites for proteins that trigger subsequent signaling cascades (Pawson & Scott, 1997). The cytoplasmic region of Bc contains several tyrosines that become phosphorylated on cytokine binding (Sorensen et al. 1989, Duronio et al. 1992, Sakamaki et al. 1992, Pratt et al. 1996). One site is Y766 (numbered as Y750 by Sakamaki et al. 1992 and many other publications). Phosphorylation of Bc in response to GM-CSF/IL3 is observed at low temperatures (4 degrees C) that prevent the phosphorylation of other proteins, suggesting that the kinase responsible is likely to be physically associated with the receptor complex prior to stimulation (Miyajima et al. 1993). JAK2 is activated in response to IL-3, IL-5 and GM-CSF but signaling via JAK/STAT is not dependent on Bc tyrosine phosphorylation (Okuda et al. 1997). Based on these observations and the role of JAK1/3 in IL-2 signaling, JAK2 is believed to be the most likely candidate responsible for the phosphorylation of Bc (Guthridge et al. 1998). To represent the possible phosphorylation of Bc by kinases other than JAK2, this reaction includes receptor complexes with both active and inactive JAK2. Phosphorylation is represented only where this is necesssary for subsequent signaling; phosphorylation at other positions is probable.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-879907",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-879907"
}
]
},
{
"id": "R-HSA-879909",
"name": "Activation of STAT5a/b by JAK2",
"equation": "",
"summary": "JAK2 phosphorylates STAT5; phosphorylated STAT5 dimerizes and translocates to the nucleus (Darnell et al., 1994), binds DNA and activates target genes including c-fos, pim-1, oncostatin M, and Id-1 (Mui et al. 1996). STAT5 activation is believed to be the primary signaling mechanism for Bc (Ihle, 2001).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-879909",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-879909"
}
]
},
{
"id": "R-HSA-879910",
"name": "JAK2 is phosphorylated, activated",
"equation": "",
"summary": "JAK2 is tyrosine phosphorylated in response to IL-3 (Silvennoinen et al. 1993), GM-CSF (Quelle et al. 1994) and IL-5 (Cornelis et al. 1995) leading to kinase activity. Although structures of JAK kinase domains exist (e.g. Lucet et al. 2006) no complete structures of Janus kinases (JAKs) are available and the activation mechanism is poorly understood. Activation is believed to be a consequence of conformational changes, propagated from conformational changes in the common beta chain (Bc) following alpha-beta dimerization. This is believed to result in a trans-activation event whereby JAKs bound to activated, dimerized receptors phosphorylate and thereby activate each other (Quelle et al. 1994, Hou et al. 2002). This model is similar to IL2R activation of JAK1/3. In addition to the observed activation of JAK2 following stimulation with IL-3, IL-5 or GM-CSF, other supporting observations include: phosphorylation of JAK2 at Y1007 is critical for kinase activation (Feng et al. 1997, Lucet et al. 2006) and autophosphorylation at several other sites appears to regulate activity (e.g. Feener et al. 2004, Argetsinger et al. 2004, 2010). Only the critical Y1007 phosphorylation is represented for this reaction.
Constitutive activation of JAK2 resulting from the V617F mutation is present in over 95% of Polycythemia Vera patients (Dusa et al. 2010). F595 is indispensible for constitutive activation by V617F, but not for JAK2 activation, suggesting that this is not part of the cytokine-induced mechansim of JAK2 activation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-879910",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-879910"
}
]
},
{
"id": "R-HSA-879925",
"name": "SHC1 bound to the common beta chain becomes tyrosine phosphorylated",
"equation": "",
"summary": "IL-3, IL-5 and GM-CSF all induce tyrosine phosphorylation of Shc (Dorsch et al. 1994). Three sites are known to mediate specific downstream associations; tyrosine Y427 (Salcini et al. 1994) mediates the subsequent association of Shc with Grb2 (Salcini et al. 1994). The identity of the kinase is unknown. Y349 and Y350 phosphorylation is not required for Ras-MAPK signaling but are involved in IL-3-induced cell survival (Gotoh et al. 1996).
Residue numbering used here refers to Uniprot P29353 where the p66 isoform has been selected as the canonical form. Literature references given here refer to the p52 isoform which lacks the first 110 residues, so Y427 is referred to as Y317 in Salcini et al. 1994, Y349 and Y350 as Y239 and Y240 in Gotoh et al. 1996.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-879925",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-879925"
}
]
},
{
"id": "R-HSA-879930",
"name": "STAT5 is recruited by JAK2",
"equation": "",
"summary": "Activated JAK2 binds to unphosphorylated STAT5; cytokine treatment of cells leads to JAK2 activation and promotes binding of JAK2 to unphosphorylated STAT5.
STAT5 proteins are considered the main targets of IL-3, IL-5 and GM-CSF signaling (Mui et al. 1995a, Mui et al. 1995b, Ihle, 2001), but other members of this family including STAT3 and STAT1 (Chin et al. 1996) can be involved, the STAT family member activated appears to depend on the cell line used in the study, rather than the cytokine (Reddy et al. 2000). IL-5 and GM-CSF increase STAT3 and 5 signaling (Caldenhoven et al. 1995, Stout et al. 2004).
Unphosphorylated STATs are cytoplasmic; tyrosine phosphorylation facilitates dimerization and translocation to the nucleus where they act as transcription factors. STATs were originally described as ligand-induced transcription factors in interferon-treated cells, subsequently they were shown to be critical in many signal transduction pathways associated with cytokines and neurokines including several interleukins, the interferons, erythropoietin, prolactin, growth hormone, oncostatin M (OSM), and ciliary neurotrophic factor (Darnell 1997, Reddy et al. 2000). JAK-STAT signaling is widely accepted as a primary signaling route for receptors that share the common beta subunit (Bc).
The role of the receptor itself in STAT5 binding is somewhat controversial because while STAT proteins can be recruited to tyrosine phosphorylated receptors via their SH2 domains (Greenlund et al. 1995, Li et al. 1997) binding of STAT5 to Bc has not been formally demonstrated (Guthridge et al. 1998), though tyrosine-phosphorylated peptides of Bc have been demonstrated to associate with STAT5, and anti-Bc or phosphotyrosine antibodies inhibited GM-CSF induced STAT5 DNA binding activity (Sakurai et al. 2000). Binding of JAK2 to STAT5 can occur in vitro when no receptor is present (Flores-Morales et al. 1998). STAT5 activation was seen when all six conserved cytoplasmic tyrosines in Bc were mutated to P (Okuda et al. 1997), but a C-terminal deletion mutant of Bc while able to activate JAK2 was unable to activate STAT5 (Smith et al. 1997). These observations suggest that JAK2 activation is a critical step in STAT signaling from Bc-containing receptors, but other factors may be required. It is not clear whether Bc is directly involved or not in STAT5 activation, but the specificity for particular STAT members is believed to be determined by STAT docking sites present on the receptor molecules, not JAK kinase preference (Reddy et al. 2000).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-879930",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-879930"
}
]
},
{
"id": "R-HSA-879934",
"name": "Recruitment of SHC1 is mediated by Y593 of the common beta chain",
"equation": "",
"summary": "Upon receptor activation, Shc is recruited to the receptor complex, where it becomes tyrosine phosphorylated. The recruitment of Shc is mediated by Y593 (Y577 in the mature peptide) of the common beta chain (Bc), which binds the PTB domain of Shc (Pratt et al. 1996).; Phosphorylated Shc interacts with Grb2 within a Grb2:Gab2 complex, promoting tyrosine phosphorylation of Gab2. The p85 subunit of PI3Kinases associates with phosphorylated Gab, and this induces activation of the catalytic p110 PI3K subunit leading to activation of Akt kinase, thereby regulating cell survival and/or proliferation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-879934",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-879934"
}
]
},
{
"id": "R-HSA-879937",
"name": "The common beta chain IL3RB binds JAK2",
"equation": "",
"summary": "JAK2 associates with IL3 receptor beta chain (IL3RB) better known as the cytokine recetpor common beta chain (Bc). This association was not found to be dependent upon, or influenced by, the presence of GM-CSF or the GM-CSF receptor alpha chain, suggesting that JAK2 and Bc may be constitutively associated (Quelle et al. 1994).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-879937",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-879937"
}
]
},
{
"id": "R-HSA-879942",
"name": "The receptor is activated",
"equation": "",
"summary": "Upon ligand binding to the alpha subunit, the alpha and Bc subunits asociate, forming a high affinity receptor. Subsequent signaling may require a disulfide-linked association between the alpha and beta chains (Stomski et al. 1996). While the formation of a 1:1:1 complex of interleukin:alpha subunit:common beta subunit represents a high-affinity binding complex, receptor activation involves the formation of higher order multimeric structures. The stoichiometry of endogenous active receptor complexes is not clear, but studies using dominant-negative, chimeric, and mutant receptors and modeling studies all suggest that a minimum of two Bc subunits are required for receptor activation and signaling (Guthridge et al. 1998, Hansen et al. 2008).
The cytoplasmic region of Bc contains several tyrosines that become phosphorylated on cytokine binding (Sorensen et al. 1989, Duronio et al. 1992, Sakamaki et al. 1992, Pratt et al. 1996). One such site is Y766, numbered according to the Uniprot canonical sequence. Note that in many publications this position is numbered as 750, referring to the mature sequence with signal peptide removed. These phosphorylations are mediated by receptor-associated kinases with JAK2 as the most likely candidate (Quelle et al. 1994, Guthridge et al. 1998). Specific phosphorylations appear to mediate association with different signaling components (Sato et al. 1993), e.g. substitution of F for Y766 prevents Shc phosphorylation (Inhorn et al. 1995) but not JAK2 phosphorylation. Modeling and structural data suggest that the active receptor is at least a dimer of ligand:alpha subunit:common beta subunit complexes (Bagley et al. 1997, Guthridge et al. 1998, Hansen et al. 2008). This fits a model of receptor activation whereby dimerization leads to Jak2 activation by transphosphorylation of the activation sites (Ihle et al. 1995, Guthridge et al. 1998, Hansen et al. 2008), leading to Bc activation by phosphorylation. The active receptors are represented here as dimers of ligand:alpha subunit:common beta subunit complexes.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-879942",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-879942"
}
]
},
{
"id": "R-HSA-8942607",
"name": "Tyrosine kinases phosphorylate Cip/Kip inhibitors bound to CDK4/6:CCND complexes",
"equation": "",
"summary": "Phosphorylation of Cip/Kip cyclin-dependent kinase (CDK) inhibitors CDKN1A (p21Cip), CDKN1B (p27Kip1) and CDKN1C (p57Kip2) on conserved tyrosine residues Y77, Y88 and Y91, respectively, can convert them from bound inhbitors to bound non-inhibitors of CDK4 or CDK6 complexes with D cyclins by dislodging them from the active site of CDK4 or CDK6. This mechanism was studied in most detail on the example of CDKN1B associated with the CDK2:CCNA complex (Grimmler et al. 2007) and the CDK4:CCND1 complex (James et al. 2008, Patel et al. 2015). For a review of this topic, please refer to Blain 2008.
CDKN1A can be phosphorylated at tyrosine residue Y77 by protein tyrosine kinase ABL1 (Hukkelhoven et al. 2012). CDKN1B can be phosphorylated at tyrosine residue Y88, and probably also at the adjacent Y89, by protein tyrosine kinases ABL1 (Grimmler et al. 2007, James et al. 2008, Ray et al. 2009, Ou et al. 2011), LYN (Grimmler et al. 2007), SRC (Larrea et al. 2008), JAK2 (Jakel et al. 2011) and PTK6 (Patel et al. 2015). CDKN1C can be phosphorylated at tyrosine residue Y91 by protein tyrosine kinase ABL1 (Borriello et al. 2011).
Dislodgment of the tyrosine phosphorylated 3-10 helix of Cip/Kip CDK inhibitors from the active site of cyclin D-bound CDK4 or CDK6 results in increased catalytic activity of CDK4 or CDK6 by allowing ATP binding to the active site, but also by enabling activating phosphorylation of the T-loop of CDK4 or CDK6 phosphorylation by CDK7 in complex with cyclin H (Ray et al. 2009).
SRC-mediated phosphorylation of CDKN1B on tyrosine residue Y88 was shown to reduce protein stability of CDKN1B (Chu et al. 2007).
Without overexpression of BCR-ABL or SRC-family tyrosine kinases in several cell systems, tyrosine phosphorylated p27 is either undetectable or a very low abundance species (Ishida et al. 2000, Jaimes et al. 2008, Grimmler et al. 2007) that does not bind preferentially to CDK4 (Jaimes et al. 2008). Therefore, tyrosine phosphorylation of p27 is unlikely to be the sole explanation of the full activity of p27-bound CDK4:CCND complexes reported in previous studies (Blain et al. 1997, Coulonval et al. 2003, Bockstaele et al. 2006). It has been proposed that stoichiometry of the Cip/Kip complex with CDK4 or CDK6 and cyclin D, in addition to or alternative to tyrosine phosphorylation of Cip/Kip CDK inhibitors, determines their inhibitory role where binding of more than one molecule of CDKN1A, CDKN1B or CDKN1C would be needed to achieve inhibition of the CDK4/6:CCND complex (reviewed by Paternot et al. 2010).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13882-1",
"O60674-1",
"P00519-1",
"P07948-1",
"P11802-1",
"Q00534-1"
],
"evidence": [
{
"id": "R-HSA-8942607",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8942607"
}
]
},
{
"id": "R-HSA-8950063",
"name": "IL12RB2 binds JAK2",
"equation": "",
"summary": "Inferred from human protein interaction:
Tyrosine-protein kinase JAK2 (JAK2) can associates with the intacellular domain of Interleukin-12 recetor subunit beta 2 (IL12RB2). Interleukin-12 receptor subunit beta 1 (IL12RB1) and Non-receptor tyrosine-protein kinase TYK2 (TYK2) are not required (Zou et al.1997, Floss et al. 2016 ,Yamamoto et al. 1999).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-8950063",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950063"
}
]
},
{
"id": "R-HSA-8950128",
"name": "Interleukin-12 dissociates from Interleukin-12 receptor",
"equation": "",
"summary": "Based on competition experiments with Iodine125-labeled Interleukin-12 (IL12) it was determined that IL12 can dissociate from the Interleukin-12 receptor. The association kinetics suggest mostly subsequent internalization of the IL12 (Chizzonite et al. 1992).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-8950128",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950128"
}
]
},
{
"id": "R-HSA-8950210",
"name": "Interleukin-27 dissociates from Interleukin-27 receptor",
"equation": "",
"summary": "Interleukin-27 heterodimer (IL27) binds a heterodimeric receptor formed by Interleukin-27 subunit alpha (IL27RA) and Interleukin-6 receptor subunit beta (IL6ST, gp130). In the absence of IL27RA IL27 can bind IL6ST with low affinity. Dissociation rate constants for binding of IL27 to the heterodimeric receptor indicate a slow dissociation rate, resulting in very high binding affinity. Blocking both receptor chains completely blocks IL27 induced STAT1 and STAT3 phosphorylation and IL27 induced proliferation (Jia et al. 2016).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8950210",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950210"
}
]
},
{
"id": "R-HSA-8950269",
"name": "STAT3, STAT4 are phosphorylated by p-JAK2, p-TYK2 in IL23:IL23 receptor",
"equation": "",
"summary": "Interleukin-23 (IL23) induces Signal transducer and activator of transcription 3 (STAT3) and STAT4 phosphorylation. Non-receptor tyrosine-protein kinase TYK2 (TYK2) and Tyrosine-protein kinase JAK2 (JAK2) are believed to phosphorylate STAT3 and STAT4 (Parham et al. 2002). STAT3 is the most prominent STAT activated by IL23, contrasting with Interleukin-12 (IL12) which predominantly induces STAT4 activation (Parham et al. 2002). IL23 induces phosphorylation of STAT3 and STAT4 in NK-like T cells but neither in NK cells (van de Wetering et al. 2009). Phosphorylation results in STAT3:STAT4 heterodimer formation (Parham et al. 2002).
This is a black box event because the exact mechanism and order of STAT3/STAT4 binding is unknown.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-8950269",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950269"
}
]
},
{
"id": "R-HSA-8950340",
"name": "IL27RA and IL6ST are phosphorylated after IL27:IL27 receptor interaction and JAK's phosphorylation",
"equation": "",
"summary": "Interleukin-27 receptor is formed by Interleukin-27 receptor subunit alpha (IL27RA, WSX-1) and Interleukin-27 receptor subunit beta (IL6ST, gp130). Both subunits can be tyrosine phosphorylated after ligand-receptor interaction (Pflanz et al. 2004, Takeda et al. 2003). There is general agreement that ligand binding to cytokine receptors results in the activation of prebound Jak kinases, which auto- and transphosphorylate then phosphorylate key tyrosine residues on the receptor (O'Shea et al 2002), but for the interleukin-27 receptor the pattern of phosphorylations is not clear, hence this is represented as a black box event.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8950340",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950340"
}
]
},
{
"id": "R-HSA-8950354",
"name": "STAT4 is phosphorylated by p-JAK2 and/or p-Y-TYK2 after IL12:IL12R interaction",
"equation": "",
"summary": "Inferred from mouse:
Signal transducer and activator of transcription 4 (STAT4) is activated via interaction with tyrosine-800 of Interleukin-12 receptor beta 2 subunit (IL12RB2). Based on experiments with murine-specific peptides, STAT4 activation depends on interaction with the peptide sequence pYLPSNID, where pY represents phosphotyrosine. STAT1 and STAT3 are not activated directly through the Interleukin-12 heterodimeric receptor (Naeger et al. 1999).
As the pattern of phosphorylations required for this event is unclear, it is represented here as a black box event.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8950354",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950354"
}
]
},
{
"id": "R-HSA-8950364",
"name": "IL23R in IL23:IL23 receptor complex is phosphorylated",
"equation": "",
"summary": "Inferred from mouse:
Interleukin-23 receptor subunit (Il23r) can be phosphoryated at various intracellular Tyrosin residues. Tyr-542 and Tyr-626 aminoacid residues in murine Il23r are responsible for SH2 domain dependent Signal transducer and activator of transcription 3 (Stat3) activation (Floss et al. 2013). Moreover Western blot data demostrated Interleukin-23 dependent trysoine phosphorylation of Stat3 in cotransfected parental cell lines(2C4, 2fTGH) and Tyrosine-protein kinase JAK1(Jak1)-deficient cells (U4C) (Floss et al.2016).
As the process of phosphorylation is not clear this reaction is represented here as a black box event.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-8950364",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950364"
}
]
},
{
"id": "R-HSA-8950405",
"name": "JAK1/JAK2 bound to IL35:IL6ST:IL12RB2 receptor are phosphorylated",
"equation": "",
"summary": "Interleukin 35 (IL35) may presumably signal via a complex that includes Tyrosine protein kinase JAK1 (JAK1) and JAK2 associated with Interleukin 6 receptor beta subunit (IL6ST) and Interleukin 12 receptor beta 2 subunit (IL12RB2) (Collison et al. 2012). These JAKs are believed to phosphorylate Signal transducer and activator of transcription 1 (STAT) (Stark GR and Darnell JE, 2012). As the series of events that induces JAK/STAT phosphorylation events in response to IL35 are not clear, this event is represented as a black box.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8950405",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950405"
}
]
},
{
"id": "R-HSA-8950423",
"name": "JAK2, TYK2 in IL12A:IL12RB1:TYK2:IL12B:IL12RB2:JAK2 are phosphorylated",
"equation": "",
"summary": "Interleukin-12 phosphorylates and thereby activates Tyrosine-protein kinase JAK2 (JAK2) and non-receptor tyrosine-protein kinase TYK2 (TYK2) (Bacon et al.1995, Kanda & Watanabe 2008).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-8950423",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950423"
}
]
},
{
"id": "R-HSA-8950441",
"name": "p-Y701-STAT1 and p-Y705-STAT3 dissociate from IL27:IL27 receptor",
"equation": "",
"summary": "Signal transducer and activator of transcription 1-alpha/beta (STAT1) and Signal transducer and activator of transcription 3 (STAT3) dissociate from the receptor complex after activation.
This is a BlackBox event since the exact mechanism of this dissociation is unknown.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8950441",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950441"
}
]
},
{
"id": "R-HSA-8950448",
"name": "STAT4 binds to IL12RB2 in Interleukin-12 receptor complex",
"equation": "",
"summary": "Signal transducer and activator of transcription 4 (STAT4) binds to phosphorylated tyrosine-800 and a few surronding amino acids on Interleukin-12 receptor subunit beta 2 (IL12RB2) (Yao et al. 1999).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8950448",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950448"
}
]
},
{
"id": "R-HSA-8950453",
"name": "JAK1/JAK2 bound to IL12RB2:IL6ST receptor phosphorylates STAT1 and STAT4",
"equation": "",
"summary": "Interleukin-35 (IL35) binding activates the IL35 receptor complex and facilitates Tyrosine-protein kinase JAK (JAK) phosphorylation. Subsequently, Signal transducer and activator of transcription 1-alpha/beta (STAT1) and STAT4 bind to the receptor complex and are activated by tyrosine phosphorylation (Collison et al. 2012). Although it is known that JAKs are involved in STATs phosphorylation (Stark GR and Darnell JE, 2012), it is not clear how other components of the IL35 receptor complex contribute to STAT1/STAT4 phosphorylation. For this reason, this event is assigned a black box status.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8950453",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950453"
}
]
},
{
"id": "R-HSA-8950485",
"name": "STAT3 and STAT1 are phosphorylated by JAKs after IL27:IL27R interaction",
"equation": "",
"summary": "Signal transducer and activator of transcription 3 (STAT3) and Signal transducer and activator of transcription 1 alpha/beta (STAT1) are phosphorylated after Interleukin-27 (IL27) binds the Interleukin-27 receptor. In Interleukin-2 activated T cells, Interleukin-6 receptor beta subunit (IL6ST, gp130) has STAT3-docking sites, the result of tyrosine phosphorylation by Tyrosine protein-kinase JAK2 (JAK2) and/or Non receptor Tyrosine-protein kinase 2 (TYK2) and JAK1.
In human keratynocytes, Interleukin-12 (IL12) enhanced tyrosine phosphorylation and transcriptional activity of STAT3, possibly mediated by JAK2, which is associated with Interleukin-12 receptor beta 2 subunit (IL12RB2). However Interleukin-23 (IL23) and IL27 did not activate STAT3 in keratinocytes although JAK2 was activated (Kanda & Watanabe 2008)
Inferred from mouse:
As further background, the heterodimeric proteins IL12, IL23 and IL27 activate JAK2 and Non-receptor tyrosine-protein kinase TYK2 (TYK2). IL27 simultaneously activates JAK1. STAT3 is required for IL27 induced up-regulation of c-Myc and Pim-1 and consequent cell proliferation. IL27-induced STAT3 activation is mediated through four tyrosine residues in the YXXQ motif of the cytoplasmic region of IL6ST, as observed with IL6. On the other hand, STAT3 is dispensable for IL27-induced augmentation of Th1 differentiation and IL27 induced supression of proinflammatory cytokine production.
In human keratynocytes IL27 induced both tyrosine phosphorylation and the transcriptional activity of STAT1 in parallel with the activation of JAK1. In IL27-activated naive T cells, the cytoplasmic domain of interleukin-27 receptor alpha subunit (IL27RA, WSX-1) is tyrosine phosphorylated by constitutively associated JAK1, providing a docking site for STAT1 which leads to its phosphorylation and activation by JAK1 (Kanda & Watanabe 2008). Moreover STAT1 silencing in human monocytic THP-1 cells demostrated that IL27 strongly increases STAT1 protein expression. Concomitant with increased STAT1 expression, Interleukin-10 (IL10) induced increased levels of STAT1 tyrosine phosphorylation in monocytes. All of these observations are consistent with results obtained with STAT1-deficient mice, which indicate that STAT1 activation is important for IL27-induced cell proliferation (Owaki et al. 2008).
This is a black box event because the exact mechanism and order of STAT1 and STAT3 binding is unknown.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8950485",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950485"
}
]
},
{
"id": "R-HSA-8950518",
"name": "STAT1, STAT3 bind p-Y611-IL27RA from Interleukin-27:Interleukin-27 receptor complex",
"equation": "",
"summary": "Signal transducer and activator of transcription 1 (STAT1) and STAT3 are both known to be phosphorylated by Interleukin-27 (IL27) in human cells (Hibbert et al 2003 ).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8950518",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950518"
}
]
},
{
"id": "R-HSA-8950537",
"name": "JAK1, JAK2, TYK2 in IL27:EBI3:IL27RA:JAK1:IL6ST:(JAK1,JAK2,TYK2) are phosphorylated",
"equation": "",
"summary": "Interleukin 27 phosphorylates/activates Tyrosine protein kinase JAK2 (JAK2) , non receptor tyrosine protein kinase TYK2 (TYK2) and Tyrosine protein kinase JAK1 (JAK1) (Kanda & Watanabe 2008). JAK1 interacts with IL27RA (Takeda et al 2003 )
As the phosphorylation required for Interleukin 27 induced activation are not clear, this is represented here as a black box event.
",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8950537",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950537"
}
]
},
{
"id": "R-HSA-8950583",
"name": "STAT3 binds to p-Y-IL23R in IL23:IL23 receptor",
"equation": "",
"summary": "Inferred from mouse :
Signal transducer and activator of transcription 3 (STAT3) binds tyrosine residues of the Interleukin-23 receptor (IL23R) after cytokine-receptor interaction (Dumoutier et al. 2009, Floss et al. 2013). This is a black box event because STAT3 binding as a consequence of Interleukin-23 stimulation has not been directly demonstrated. IL23R can also bind STAT4, this alternative binding is not represented here only because the evidence for STAT3 binding is inferred from mouse/human chimeras while STAT4 binding evidence was obtained with human protein data.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-8950583",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950583"
}
]
},
{
"id": "R-HSA-8950591",
"name": "JAK2, TYK2 in IL23A:IL12B:IL23R:JAK2:IL12RB1:TYK2 are phosphorylated",
"equation": "",
"summary": "In human cells IL-23 binding leads to phosphorylation and activation of TYK2 and JAK2 (Parham et al 2002).; Inferred from mouse:
The intracellular domain of Interleukin 12 receptor beta 1 subunit (Il12rb1), spanning amino acid residues 592\u2013656, is crucial for Interleukin 23 complex\u2013induced cellular proliferation and Signal transducer and activator of transcription 3 (Stat3) phosphorylation (Floss et al. 2016).
As it is not clear what induces JAK2 and TYK2 kinase phosphorylation this is represented here as a black box event.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [
"R-HSA-447186"
],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-8950591",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950591"
}
]
},
{
"id": "R-HSA-8950737",
"name": "IL23R binds JAK2",
"equation": "",
"summary": "Inferred from mouse:
Interleukin-23 heterodimeric receptor, formed by Interleukin-23 receptor (Il23r) and Interleukin-12 receptor beta 1 subunit (Il12rb1), can bind Tyrosine-protein kinase JAK2 (Jak2). This association is essential for Interleukin-23 signaling (Floss et al. 2016).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-8950737",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950737"
}
]
},
{
"id": "R-HSA-8950757",
"name": "IL12RB2 in IL12A:IL12RB1:p-Y-TYK2:IL12B:IL12RB2:p-JAK2 is phosphorylated",
"equation": "",
"summary": "Phosphorylated residues in the cytoplasmic region of Interleukin-12 receptor subunit beta 2 (IL12RB2) enable binding and activation of Signal transducer and activator of transcription 4 (STAT4) by means of Tyrosine-protein kinase JAK2 (JAK2).
STAT4 was found to bind only phosphorylated tyrosine-800, and not to phosphorylated tyrosines 678 or 767 when phosphorylated. Although required, phosphorylated tyrosine-800 was not sufficient for binding of STAT4, as other residues in IL12RB2, specifically at -4, -1 and +1 relative to the tyrosine, contribute to the specificity of STAT4 binding (Yao et al. 1999).
As the pattern of phosphorylations required for receptor activation is unknown, this is a black box event.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8950757",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8950757"
}
]
},
{
"id": "R-HSA-8952749",
"name": "STAT4 binds p-Y-IL23R in IL23:IL23 receptor",
"equation": "",
"summary": "Signal transducer and activator of transcription 4 (STAT4) is believed to bind Interleukin-23 receptor (IL23R) in response to Interleukin-23 (IL23). The sequence GY484KPQIS in IL23R is thought to be the STAT4 binding site as it resembles the STAT4 binding motif in IL12RB2 (Naeger at al. 1999, Yao et al. 1999). ; This is a black box event because there is no direct evidence of STAT4 binding in response to IL23. Note that theris no evidence to suggest that STAT3 binding precedes STAT4 association.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-8952749",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8952749"
}
]
},
{
"id": "R-HSA-8952807",
"name": "p-Y693-STAT4 dissociates after IL12:IL12R interaction",
"equation": "",
"summary": "Phosphorylated Signal transducer and activator of transcription 4 (STAT4) dissociates from the receptor, dimerizes, translocates to the nucleus and binds to STAT target sequences in Interleukin-12 responsive genes (Cho et al.1996, Bacon et al. 1995).
This is a Black Box Event since the exact mechanism of association and dissociation of STATs is not described.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8952807",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8952807"
}
]
},
{
"id": "R-HSA-8952823",
"name": "p-Y693-STAT4, p-Y705-STAT3 dissociate from IL23:IL23 receptor",
"equation": "",
"summary": "Activated Signal transducer and activator of transcription 4 (STAT4) and STAT3 are released as subunits after Interleukin-23 (IL23) binds the Interleukin-23 heterodimeric receptor (Parham et al. 2002, Silvanesan et al. 2016).
This is a Black box event since the exact mechanisms of STAT3 and STAT4 binding, phosphorylation, dissociation and dimerization are unknown.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-8952823",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8952823"
}
]
},
{
"id": "R-HSA-8981093",
"name": "IL12 bound to IL12R internalises",
"equation": "",
"summary": "Association kinetics based on competition experiments with Iodine125-labeled Interleukin-12 (IL12) in human PHA-activated lymphoblasts suggested that upon binding of IL12 to the IL-12 receptor the IL12 and probably its receptor are subsequently internalized (Chizzonite et al. 1992). ; Using confocal laser microscopy in human B cells and primary T cells it was shown that after binding of IL12 to the IL-12 receptor heterodimer IL12:IL12RB1:IL12RB2 is indeed internalised into the cell (Durali et al. 2003). This is a black box event because the mechanism is uncertain.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1"
],
"evidence": [
{
"id": "R-HSA-8981093",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8981093"
}
]
},
{
"id": "R-HSA-8983518",
"name": "IL35 binds IL6ST:IL6ST receptor",
"equation": "",
"summary": "Interleukin-35 (IL35) is a heteromeric complex conformed by Interleukin-12 subunit alpha (IL12A) and Interleukin-27 subunit alpha (IL27). IL35 can stimulate Janus Kinase (JAK)-bound homodimers of Interleukin-6 receptor beta precursor (IL6ST or gp130). JAKs are believed to be associated with the receptor before receptor activation (Behrmann et al., 2004). Subsequently, this triggers the phosphorylation of STAT1 downstream. The physiological consequence of this signalling is the suppression of T-cell response. The event is represented as a black box due to the incomplete knowledge about the ligand binding to monomers followed by dimerization or binding directly to the dimers.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8983518",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8983518"
}
]
},
{
"id": "R-HSA-8983519",
"name": "IL35 binds IL12RB2:IL12RB2 receptor",
"equation": "",
"summary": "Interleukin 35 (IL35) is a heteromeric complex conformed by Interleukin 12 subunit alpha (IL12A) and Interleukin 27 subunit alpha (IL27). IL35 may presumably stimulate Janus Kinase (JAK) bound homodimers of Interleukin 12 receptor beta 2 (IL12RB2). JAKs are believed to be associated with the receptor before receptor activation (Behrmann et al., 2004). Subsequently, this triggers the phosphorylation of STAT4 downstream. The physiological consequence of this signalling is the suppression of T cell response. The event is represented as a black box due to the incomplete knowledge about the ligand binding to monomers followed by dimerization or binding directly to the dimers.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-8983519",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8983519"
}
]
},
{
"id": "R-HSA-8983834",
"name": "JAK1/JAK2/TYK2 bound to IL6ST:IL6ST are phosphorylated",
"equation": "",
"summary": "Interleukin 35 (IL35) may presumably signal via a complex that includes Tyrosine protein kinase JAK1 (JAK1) and JAK2 associated with Interleukin 6 receptor beta subunit (IL6ST) dimers (Collison et al. 2012). These JAKs are believed to phosphorylate Signal transducer and activator of transcription 1 (STAT) (Stark GR and Darnell JE, 2012). As the series of events that induces JAK/STAT phosphorylation events in response to IL35 are not clear, this event is represented as a black box.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8983834",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8983834"
}
]
},
{
"id": "R-HSA-8983835",
"name": "JAK1/JAK2/TYK2 bound to IL6ST:IL6ST phosphorylate STAT1",
"equation": "",
"summary": "Interleukin-35 (IL35) binding activates the IL35 receptor complex and facilitates Tyrosine-protein kinase JAK (JAK) phosphorylation. Subsequently, Signal transducer and activator of transcription 1-alpha/beta (STAT1) binds to the receptor complex and is activated by tyrosine phosphorylation (Collison et al. 2012). Although it is known that JAKs are involved in STATs phosphorylation (Stark GR and Darnell JE, 2012), it is not clear how other components of the IL35 receptor complex contribute to STAT1 phosphorylation. For this reason, this event is assigned a black box status.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8983835",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8983835"
}
]
},
{
"id": "R-HSA-8983841",
"name": "STAT1 associates with IL6ST:IL6ST",
"equation": "",
"summary": "Interleukin-35 (IL35) binding activates the IL35 receptor complex and facilitates JAKs phosphorylation. Subsequently, Signal transducer and activator of transcription 1-alpha/beta (STAT1) binds to the receptor complex and is activated by tyrosine phosphorylation (Collison et al. 2012). This is a black box event because the receptor subunit responsible for STAT1 binding to the receptor is unclear.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8983841",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8983841"
}
]
},
{
"id": "R-HSA-8983845",
"name": "p-STAT1 dissociates from IL6ST:IL6ST",
"equation": "",
"summary": "Interleukin-35 (IL35) can signal via IL35 receptors triggering the JAK/STAT pathway downstream. Signal transducer and activator of transcription 1-alpha/beta (STAT1) binds to the JAK associated-IL35 receptor complex and is activated via phosphorylations. Subsequently, phosphorylated p-STAT1 dissociates from the receptor complex (Collison et al. 2012). This is a black box event because there is no literature evidence about the exact mechanism of the release of STAT1 from the receptor complex.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8983845",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8983845"
}
]
},
{
"id": "R-HSA-8983870",
"name": "JAK2 in IL12RB2:IL12RB2 receptor is phosphorylated",
"equation": "",
"summary": "Interleukin 35 (IL35) may presumably signal via a complex that includes Tyrosine protein kinase JAK2 (JAK2) associated with Interleukin 12 receptor beta 2 (IL12RB2) dimers (Collison et al. 2012). JAKs are believed to phosphorylate Signal transducers and activator of transcription (STATs) (Stark GR and Darnell JE, 2012). As the series of events that induce JAK/STAT phosphorylation events in response to IL35 are not clear, this event is represented as a black box.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-8983870",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8983870"
}
]
},
{
"id": "R-HSA-8983872",
"name": "JAK2 bound to IL12RB2:IL12RB2 phosphorylate STAT4",
"equation": "",
"summary": "Interleukin 35 (IL35) binding activates the IL35 receptor complex and may facilitate Tyrosine protein kinase JAK (JAK) phosphorylation. Subsequently, Signal transducer and activator of transcription 4 alpha/beta (STAT4) may bind to the receptor complex and is activated by tyrosine phosphorylation (Collison et al. 2012). JAK2 is known to be involved in the phosphorylation of STAT1 (Higashi T et al., 2005).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-8983872",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8983872"
}
]
},
{
"id": "R-HSA-8983876",
"name": "STAT4 binds IL12RB2:IL12RB2",
"equation": "",
"summary": "Interleukin-35 (IL35) binding activates the IL35 receptor complex and facilitates JAKs phosphorylation. Subsequently, Signal transducer and activator of transcription 4-alpha/beta (STAT4) binds to the receptor complex and is activated by tyrosine phosphorylation (Collison et al. 2012). This is a black box event because the receptor subunit responsible for STAT4 binding to the receptor is unclear.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-8983876",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8983876"
}
]
},
{
"id": "R-HSA-8983878",
"name": "p-STAT4 dissociates from IL12RB2:IL12RB2 receptor",
"equation": "",
"summary": "Interleukin-35 (IL35) can signal via IL35 receptors triggering the JAK/STAT pathway downstream. Signal transducer and activator of transcription 4-alpha/beta (STAT4) binds to the JAK associated-IL35 receptor complex and are activated via phosphorylations. Subsequently, phosphorylated p-STAT4 dissociates from the receptor complex (Collison et al. 2012). This is a black box event because there is no literature evidence about the exact mechanism of the release of STAT4 from the receptor complex.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-8983878",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8983878"
}
]
},
{
"id": "R-HSA-8983983",
"name": "p-STAT1 and p-STAT4 dissociate from IL12RB2:IL6ST receptor",
"equation": "",
"summary": "Signal transducer and activator of transcription 1-alpha/beta(STAT1) and Signal transducer and activator of transcription 4 (STAT4) after phosphorylation dissociates from the complex of ligand receptor and will dimerize (Delgoffe & Vignali 2013). This is a Black Box event because the mechanism of the release of STAT1 and STAT4 from the receptor complex is unclear. However, it is reported that simultaneous activation of IL12RB2 or IL6ST homodimer receptors do not promote the formation of pSTAT1:pSTAT4 and only the activation of the IL12RB2:IL6ST heteromeric receptor favours pSTAT1:pSTAT4 formation. For this reason, STAT1 and STAT4 are simultaneously considered in the binding, activation and release events.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8983983",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8983983"
}
]
},
{
"id": "R-HSA-8983996",
"name": "STAT1 and STAT4 associate with IL12RB2:IL6ST receptor",
"equation": "",
"summary": "Interleukin-35 (IL35) binding activates the IL35 receptor complex and facilitates JAKs phosphorylation. Subsequently, Signal transducer and activator of transcription 1-alpha/beta (STAT1) and STAT4 bind to the receptor complex and are activated by tyrosine phosphorylation (Collison et al. 2012). This is a black box event because the receptor subunit responsible for STAT4 binding to the receptor is unclear. However, it is reported that simultaneous activation of IL12RB2 or IL6ST homodimer receptors do not promote the formation of pSTAT1:pSTAT4 and only the activation of the IL12RB2:IL6ST heteromeric receptor favours pSTAT1:pSTAT4 formation. For this reason, STAT1 and STAT4 are simultaneously considered in the binding, activation and release events.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8983996",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8983996"
}
]
},
{
"id": "R-HSA-8984001",
"name": "IL35 binds IL27RA:IL12RB2 receptor",
"equation": "",
"summary": "Interleukin 35 (IL35) is a heteromeric complex of Interleukin 12 subunit alpha (IL12A) and Interleukin 27 subunit alpha (IL27). IL35 can trigger the activation of the Janus Kinase (JAK) bound heterodimeric receptor composed of Interleukin 27 receptor subunit alpha (Il27RA) and Interleukin 12 recetor subunit beta 2 (IL12RB2). JAKs are believed to be associated with the receptor before receptor activation (Behrmann et al., 2004). Consequently, IL12RB2:IL27RA facilitates the phosphorylation of STAT1:STAT3 heteromer downstream. Physiologically, this may result in the expansion of regulatory B cells and suppression of T and B cell proliferation. As it is not clear whether the dimeric receptor can form in the absence of ligand, formation of the receptor dimer is represented here as a black box event.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8984001",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8984001"
}
]
},
{
"id": "R-HSA-8984012",
"name": "JAK1,JAK2 bound to IL27RA:IL12RB2 receptor are phosphorylated",
"equation": "",
"summary": "Interleukin 35 (IL35) presumably signal via a complex that includes Interleukin 27 receptor subunit alpha (Il27RA), Interleukin 12 receptor subunit beta 2 (IL12RB2) and the associated Tyrosine protein kinase JAK1 (JAK1) and JAK2 (Wang et al. 2014). Downstream, these JAKs are believed to phosphorylate Signal transducer and activator of transcription 1 (STAT1) and STAT3 (Stark GR and Darnell JE, 2012). As the series of events that induces JAK/STAT phosphorylation events in response to IL35 are not clear, this event is represented as a black box.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8984012",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8984012"
}
]
},
{
"id": "R-HSA-8984014",
"name": "JAK1,JAK2 bound to IL27RA:IL12RB2 receptor phosphorylate STAT1,STAT3",
"equation": "",
"summary": "Interleukin 35 (IL35) binding activates the IL35 receptor complex and may presumably facilitate Tyrosine protein kinase JAK (JAK) phosphorylation. Subsequently, Signal transducer and activator of transcription 1 alpha/beta (STAT1) and Signal transducer and activator of transcription 3 alpha/beta (STAT3) may bind to the receptor complex and are activated by tyrosine phosphorylation. Although it is known that JAKs are involved in STATs phosphorylation (Stark GR and Darnell JE, 2012), it is not clear how other components of the IL35 receptor complex contribute to STAT1/STAT3 phosphorylation. For this reason, this event is assigned a black box status.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8984014",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8984014"
}
]
},
{
"id": "R-HSA-8984021",
"name": "STAT1,STAT3 associate with IL27RA:IL12RB2 receptor",
"equation": "",
"summary": "Interleukin 35 (IL35) binding activates the IL35 receptor complex and facilitates JAKs phosphorylation. Subsequently, Signal transducer and activator of transcription 1 alpha/beta (STAT1) and Signal transducer and activator of transcription 3 alpha/beta (STAT3) bind to the receptor complex and are activated by tyrosine phosphorylation (Wang et al. 2014). This is a black box event because the receptor subunit responsible for STAT1 and STAT3 binding to the receptor is unclear.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8984021",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8984021"
}
]
},
{
"id": "R-HSA-8984023",
"name": "p-STAT1, p-STAT3 dissociate from IL27RA:IL12RB2 receptor",
"equation": "",
"summary": "Interleukin 35 (IL35) can signal via IL35 receptors triggering the JAK/STAT pathway downstream. Signal transducer and activator of transcription 1 alpha/beta (STAT1) and Signal transducer and activator of transcription 3 alpha/beta (STAT3) bind to the JAK associated IL35 receptor complex and are activated via phosphorylations. Subsequently, phosphorylated p STAT1:p STAT3 dissociates from the receptor complex (Wang et al. 2014). This is a black box event because there is no literature evidence about the exact mechanism of the release of STAT1 and STAT3 from the receptor complex.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8984023",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8984023"
}
]
},
{
"id": "R-HSA-8987104",
"name": "IL20:IL20RA:JAK1:IL20RB:pJAK2,pJAK3 binds STAT3",
"equation": "",
"summary": "Signal transducer and activator of transcription 3 (STAT3)and STAT5 are believed to bind the receptor complex following the phosphorylation of JAK2 and JAK3 within the IL20:IL20RA receptor complex, because Interleukin-20 (IL20) stimulation leads to STAT3 nuclear translocation (Blumberg et al. 2001, Parrish-Novak et a. 2002)). Phosphorylation of STAT5 at Tyr-694 has been observed in response to IL20 but it is not clear which IL20 receptor was involved (Tritsaris et al. 2007). This is a black box event because there is no direct evidence of STAT3 or STAT5 binding, which is inferred to be a prerequisite for STAT phosphorylation in response to IL20.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8987104",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8987104"
}
]
},
{
"id": "R-HSA-8987141",
"name": "IL20:IL20RA:JAK1:IL20RB:p-JAK3,p-JAK2:STAT3 phosphorylates STAT3",
"equation": "",
"summary": "Signal transducer and activator of transcription 5A and 5B (STAT5A, STAT5B) is phosphorylated after binding the Interleukin-20 (IL20) receptor complex, which consist of IL20, Interleukin-20 receptor subunit alpha (IL20RA), phosphorylated Tyrosine-protein kinase JAK1 (JAK1), Interleukin-20 receptor subunit beta (IL20RB), phosphorylated Tyrosine-protein kinase JAK2 (JAK2), Tyrosine-protein kinase JAK3 (JAK3) and STAT5. After IL20 stimulation STAT5 is phosphorylated at Tyr-694 (Tritsaris et al. 2007). It is not clear which kinase subunit of the receptor complex is responsible for STAT5 phosphorylation.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8987141",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8987141"
}
]
},
{
"id": "R-HSA-8987156",
"name": "p-STAT3 dissociates from IL20:IL20RA:JAK1:IL20RB:p-Y1007,Y1008-JAK2,p-JAK3",
"equation": "",
"summary": "Phosphorylated Signal transducer and activator of transcription 5A or 5B (STAT5) dissociates from the Interleukin-20 (IL20) receptor complex (Tristaris et al. 2007). This is a black box event because dissociation is inferred from the signalling events of other Interleukins where phosphorylated STATs translocate to the nucleus, as with Interleukin-3 (Hirose et al. 2014).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8987156",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8987156"
}
]
},
{
"id": "R-HSA-8987179",
"name": "IL20:IL20RA:JAK1:IL20RB:JAK2,JAK3 phosphorylates JAK2,JAK3",
"equation": "",
"summary": "Tyrosine-protein kinase JAK2 (JAK2) or Tyrosine-protein kinase JAK3 (JAK3) are phosphorylated after the binding of Interleukin-20 (IL20) to a heterodimeric receptor complex formed by Interleukin-20 receptor subunit alpha (IL20RA) associated with Tyrosine-protein kinase JAK1 (JAK1) and Interleukin-20 receptor subunit beta (IL20RB).
JAK2 is phosphorylated at Tyr-1007/1008 (Tritsaris et al. 2007). JAK3 is also phosphorylated (Lee et al. 2012).
This is a black box event because it is unclear whether JAK2 and JAK3 are phosphorylated simultaneously or sequentially during IL20 stimulation.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8987179",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8987179"
}
]
},
{
"id": "R-HSA-8987220",
"name": "IL20:IL20RA:JAK1:IL20RB binds JAK2,JAK3",
"equation": "",
"summary": "Tyrosine-protein kinase JAK2 (JAK2) or Tyrosine-protein kinase JAK3 (JAK3) are believed to bind the complex formed by Interleukin-20 (IL20), Interleukin-20 Receptor subunit alpha (IL20RA), which is associated with Tyrosine-protein kinase JAK1 (JAK1) and Interleukin-20 receptor subunit beta (IL20RB). JAK2 was phosphorylated in response to IL20 in porcine aorta endothelial cells (Tritsaris et al. 2007). JAK2 and JAK3 were phosphorylated after IL20 stimulation of human 253J bladder cancer cells (Lee et al. 2012).
This is a black box event since it is unclear whether JAK2/3 are constitutively associated or bind to the receptor after IL20 stimulation.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-8987220",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8987220"
}
]
},
{
"id": "R-HSA-9006323",
"name": "Phospho-JAK2 phosphorylates EPOR",
"equation": "",
"summary": "Phosphorylated JAK2 phosphorylates 8 tyrosine residues in the cytoplasmic tail of EPOR (Dusanter-Fourt et al. 1992, McGraw et al. 2012, and inferred from mouse homologs). The phosphorylated residues then serve as binding sites for scaffold proteins such as CRKL and GAB1 and downstream signaling proteins such as STAT5, phospholipase C, and phosphatidylinositol 3-kinase.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9006323",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9006323"
}
]
},
{
"id": "R-HSA-9006325",
"name": "EPO binds EPOR:JAK2:LYN:IRS2",
"equation": "",
"summary": "Extracellular Erythropoietin (EPO) binds the EPO receptor (EPOR) located in the plasma membrane of the target cell (Jones et al. 1990, Syed et al. 1998, Remy et al. 1999, and inferred from mouse homologs). EPOR is a dimer that appears to be preassociated with downstream signaling proteins JAK2 (inferred from mouse homologs) and LYN (Chin et al. 1998, and inferred from mouse homologs) and the scaffold protein IRS2 (Verdier et al. 1997). Binding of EPO to EPOR causes a change in the conformation of the dimer which activates JAK2 (Syed et al. 1998, Remy et al. 1999, Kubatzky et al. 2001).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9006325",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9006325"
}
]
},
{
"id": "R-HSA-9006332",
"name": "JAK2 transphosphorylates and is activated in response to Erythropoietin",
"equation": "",
"summary": "Upon binding EPO, the EPOR dimer changes conformation, resulting in activation of JAK2 associated with box 1 and box 2 of the cytoplasmic domain of each EPOR (inferred from mouse homologs). One JAK2 transphosphorylates 12 tyrosine residues of the other JAK2 thereby activating JAK2 to phosphorylate EPOR and other substrates (Arcasoy et al. 1999, Watowich et al. 1999, Erickson-Miller et al. 2000, and inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9006332",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9006332"
}
]
},
{
"id": "R-HSA-9012650",
"name": "JAK2 and LYN phosphorylate STAT5 in EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2",
"equation": "",
"summary": "After STAT5 binds the EPO:EPOR complex, phosphorylated JAK2 and LYN phosphorylate STAT5 (STAT5A or STAT5B) (Gouilleux et al. 1995, Pallard et al. 1995, Hoefsloot et al. 1997, Miura et al. 1998, Oda et al. 1998, Okajima et al. 1998, Erickson-Miller et al. 2000, and inferred from mouse homologs). STAT5A (MGH-STAT5) is phosphorylated on tyrosine-694 (Gouilleux et al. 1995, Arcasoy et al. 1999). Activation of STAT5 appears to be impaired in myelodysplastic syndrome (Hoefsloot et al. 1997). IGF-I enhances STAT5 phosphorylation in response to EPO (Okajima et al. 1998).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9012650",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9012650"
}
]
},
{
"id": "R-HSA-9012651",
"name": "p-STAT5 dissociates from EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2",
"equation": "",
"summary": "After being phosphorylated, phospho-STAT5 (STAT5A or STAT5B) dissociates from the EPO:EPOR complex, dimerizes, and transits to the nucleus where it activates transcription of target genes (Oda et al. 1998, and inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9012651",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9012651"
}
]
},
{
"id": "R-HSA-9012654",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2 binds STAT5",
"equation": "",
"summary": "STAT5 (STAT5A or STAT5B) binds the phosphorylated cytoplasmic domain of EPOR via phosphotyrosine-343 and phosphotyrosine-479 of EPOR (Chretien et al. 1996, McGraw et al. 2012, and inferred from mouse homologs). STAT5 may also bind the EPOR complex indirectly via CRKL (Ota et al. 1998).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9012654",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9012654"
}
]
},
{
"id": "R-HSA-9012657",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:phospho-IRS2 binds PI3K",
"equation": "",
"summary": "Phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) binds phosphorylated IRS2 associated with the phosphorylated EPOR (Bouscary et al. 2003).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"O60674-1",
"P48736-1",
"P07948-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-9012657",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9012657"
}
]
},
{
"id": "R-HSA-9021627",
"name": "EPOR-associated PI3K phosphorylates PIP2 to PIP3",
"equation": "",
"summary": "Phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) associated with EPOR phosphorylates phosphatidylinositol 4,5-bisphosphate to yield phosphatidyl 3,4,5-trisphosphate (Kubota et al. 2001, Schmidt et al. 2004). PI3K binds the phosphorylated EPOR directly or indirectly via phosphorylated IRS2 or phosphorylated GAB1 (Bouscary et al. 2003).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"O60674-1",
"P48736-1",
"P07948-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-9021627",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9021627"
}
]
},
{
"id": "R-HSA-9024723",
"name": "EPO:p-EPOR:p-JAK2:LYN:IRS2 binds CRKL:RAPGEF1",
"equation": "",
"summary": "CRKL, in a constitutive complex with RAPGEF1 (C3G, a nucleotide exchange factor for RAP1), binds the cytoplasmic domain of EPOR in the region of phosphotyrosine-460 (Arai et al. 2001).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9024723",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9024723"
}
]
},
{
"id": "R-HSA-9024726",
"name": "LYN phosphorylates CRKL in EPO:p-8Y-EPOR:p-12Y-JAK2:LYN:IRS2:CRKL:RAPGEF1",
"equation": "",
"summary": "LYN, in a complex with EPOR, phosphorylates CRKL bound to RAPGEF1 (Arai et al. 2001).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9024726",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9024726"
}
]
},
{
"id": "R-HSA-9027272",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2 phosphorylates IRS2",
"equation": "",
"summary": "IRS2 is constitutively associated with EPOR and is phosphorylated on tyrosine residues in response to EPO (Verdier et al. 1997, Bouscary et al. 2003). The phosphorylated IRS2 serves as a docking site for downstream signaling proteins, notably phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) (Bouscary et al. 2003).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9027272",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027272"
}
]
},
{
"id": "R-HSA-9027273",
"name": "JAK2 phosphorylates GAB1 in EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:GAB1",
"equation": "",
"summary": "Phosphorylated JAK2 in a complex with EPOR and GAB1 phosphorylates GAB1 on unknown tyrosine residues (Lecoq-Lafon et al. 1999, Wickrema et al. 1999, Bouscary et al. 2003, Fukumoto et al. 2009). Phosphorylated GAB1 serves as a scaffold for binding downstream signaling molecules including phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) (Bouscary et al. 2003).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9027273",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027273"
}
]
},
{
"id": "R-HSA-9027274",
"name": "EPO:p-8Y-EPOR:p-12Y-JAK2:LYN:IRS2:p-CRKL:RAPGEF1 binds SHC1",
"equation": "",
"summary": "After stimulation by EPO, CRKL associates with EPOR, is phosphorylated, and binds SHC1 (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9027274",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027274"
}
]
},
{
"id": "R-HSA-9027275",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:phospho-GAB1 binds PI3K",
"equation": "",
"summary": "Phosphorylated GAB1 in a complex with EPOR binds the p85 subunit of phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) (Lecoq-Lafon et al. 1999, Wickrema et al. 1999, Bouscary et al. 2003).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"O60674-1",
"P48736-1",
"P07948-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-9027275",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027275"
}
]
},
{
"id": "R-HSA-9027280",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2 binds PI3K",
"equation": "",
"summary": "Phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) can directly bind phosphotyrosine-479 in the cytosolic domain of EPOR (Kubota et al. 2001, Bouscary et al. 2003, and inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"O60674-1",
"P48736-1",
"P07948-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-9027280",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027280"
}
]
},
{
"id": "R-HSA-9027281",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2 binds GAB1",
"equation": "",
"summary": "GAB1 binds directly to phosphotyrosines 344 and 402 of the EPOR (Bouscary et al. 2003, Montoye et al. 2005). GAB1 can also indirectly bind the EPOR via SHC1 or GRB2. GAB2 is absent from human erythroid progenitors but present in mouse erythroid progenitors (Wickrema et al. 1999).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9027281",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027281"
}
]
},
{
"id": "R-HSA-9027373",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2 binds PLCgamma",
"equation": "",
"summary": "PLCG2 (PLCgamma2) binds phosphotyrosine-432 and phosphotyrosine-480 of EPOR (Montoye et al. 2005, and inferred from moue homologs). PLCG1 can also bind the phosphorylated EPOR (inferred from mouse homologs). After binding, PLCG2 is phosphorylated (Ren et al. 1994)",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P19174-1",
"P07948-1",
"P16885-1"
],
"evidence": [
{
"id": "R-HSA-9027373",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027373"
}
]
},
{
"id": "R-HSA-9027425",
"name": "LYN phosphorylates PLCG1,2 in EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:PLCG1,2",
"equation": "",
"summary": "PLCG1 (Phospholipase C gamma1) or PLCG2 bound to the activated EPOR is phosphorylated on tyrosine residues by the kinase LYN (Ren et al. 1994, and inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P19174-1",
"P07948-1",
"P16885-1"
],
"evidence": [
{
"id": "R-HSA-9027425",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027425"
}
]
},
{
"id": "R-HSA-9029149",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:phospho-CRKL:RAPGEF1:phospho-SHC1 binds GRB2:SOS1",
"equation": "",
"summary": "Phosphorylated SHC1 in the EPOR complex serves as a scaffold to bind GRB2 bound to SOS1 (Damen et al. 1993, Odai et al. 1997). GRB2 may be pre-associated with VAV1 or SOS1, which are guanine nucleotide exchange factors for RAS, or with CBL, an ubiquitin ligase (Odai et al. 1997).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9029149",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9029149"
}
]
},
{
"id": "R-HSA-9029150",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:phospho-CRKL:RAPGEF1:phospho-SHC1 binds GRB2:VAV1",
"equation": "",
"summary": "Phosphorylated SHC1 in a complex with the activated EPOR binds GRB2 bound to VAV1 (Hanazono et al. 1995, Hanazono et al. 1996, Odai et al. 1997). GRB2 exists in pre-assembled complexes with VAV1 (Hanazono et al. 1995), SOS1 (Odai et al. 1997), or CBL (Odai et al. 1997). VAV1 and SOS1 are guanine nucleotide exchange factors that activate the RAS signaling pathway.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9029150",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9029150"
}
]
},
{
"id": "R-HSA-9029151",
"name": "JAK2 phosphorylates VAV1 in EPO:p-8Y-EPOR:p-12Y-JAK2:LYN:IRS2:p-Y-CRKL:RASGEF1:p-Y-SHC1:GRB2:VAV1",
"equation": "",
"summary": "Phosphorylated JAK2 phosphorylates VAV1 bound to GRB2 in a large complex assembled on the phosphorylated EPOR (Odai et al. 1997, Shigematsu et al. 1997). Phosphorylation of VAV1 activates its guanine nucleotide exchange activity (inferred from the mouse homolog).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9029151",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9029151"
}
]
},
{
"id": "R-HSA-9029155",
"name": "JAK2 phosphorylates SHC1 in EPO:p-8Y-EPOR:p-12Y-JAK2:LYN:p-CRKL:RABGEF1:SHC1",
"equation": "",
"summary": "Phosphorylated JAK2 associated with the EPOR complex phosphorylates SHC1 (Damen et al. 1993, Verma et al. 2014) bound to CRKL in the EPOR complex. The phosphorylated SHC1 serves as a scaffold to bind downstream effectors including GRB2:VAV1 and GRB2:SOS1.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9029155",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9029155"
}
]
},
{
"id": "R-HSA-9029158",
"name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:phospho-CRKL:RAPGEF1:GRB2-1:SOS1,phospho-VAV1 mediates exchange of GTP for GDP bound to RAS",
"equation": "",
"summary": "SOS1 and phospho-VAV1 bound to GRB2 in a complex with the activated EPOR catalyze the exchange of GDP for GTP bound to RAS proteins, yielding RAS:GTP (Komatsu et al. 1992, Torti et al. 1992). RAS:GTP then activates RAF1 and ERK1 and ERK2. EPO is observed to activate HRAS (Komatsu et al. 1992, Torti et al. 1992), KRAS, and NRAS (inferred from mouse homologs). KRAS appears to be particularly important for erythropoiesis since deletion of KRAS causes anemia in mouse.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"O60674-1",
"P07948-1",
"P01112-1"
],
"evidence": [
{
"id": "R-HSA-9029158",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9029158"
}
]
},
{
"id": "R-HSA-9032478",
"name": "EPOR-associated PLCG hydrolyzes 1-Phosphatidyl-1D-myo-inositol 4,5-bisphosphate",
"equation": "",
"summary": "Phospholipase C gamma (PLCG1 or PLCG2) bound to the phosphorylated cytoplasmic domain of the EPO receptor (EPOR) hydrolyzes 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate to yield the second messengers diacylglycerol and 1D-myo-inositol 1,4,5-trisphosphate (Ren et al. 1994, and inferred from mouse). Erythropoietin may also activate the hydrolysis of phosphatidylcholine and phosphatidylethanolamine (inferred from mouse homologs),",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P19174-1",
"P07948-1",
"P16885-1"
],
"evidence": [
{
"id": "R-HSA-9032478",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9032478"
}
]
},
{
"id": "R-HSA-909552",
"name": "Phosphorylation of STAT1 at Ser727",
"equation": "",
"summary": "Kinases like Protein kinase C delta (PKC-delta) and Calcium/calmodulin-dependent protein kinase II (CaMK II ) can phosphorylate STAT1 at serine 727 (S727). This phosphorylation is not required for STAT1 homodimer formation, nuclear translocation and DNA binding. However, it is essential for the full transcriptional activation of STAT1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q05655-1",
"O60674-1",
"Q9UQM7-1",
"Q13554-1",
"Q13557-1",
"P23458-1",
"Q13555-1"
],
"evidence": [
{
"id": "R-HSA-909552",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-909552"
}
]
},
{
"id": "R-HSA-909738",
"name": "SHP1 and SHP2 bind the common beta chain",
"equation": "",
"summary": "The common beta chain (Bc) has at least at least one direct binding site for SHP-1/SHP-2 (PTPN6/PTPN11). The SH2 domains of SHP1 and SHP2 associate with Y628 of Bc following IL-3 stimulation (Pei et al. 1994, Bone et al. 1997). SHPs act as regulators of signaling. SHP1 is thought to be a negative regulator of growth that terminates signals. Binding of SHP1 to EpoR leads to SHP1 activation and dephosphorylation of JAK2, terminating proliferative signals (Klingmuller et al. 1995). SHP1 has also been shown to interact directly and dephosphorylate JAK2 (Jiao et al. 1996). Although SHP-2 competes for the same binding site, it is thought to be a positive modulator. SHP2 associates with JAK1/2 and is phosphorylated at Y304 by these kinases, creating a GRB2 recognition motif (Yin et al. 1997). IL-3 induces the phosphorylation of SHP2 and its association with Grb2 (Welham et al. 1994). SHP2 could thereby act as an adaptor between Bc and Grb2 leading to activation of the ras/mitogen-activated protein kinase pathway. SHP2 can also associate with the p85 subunit of phosphatidylinositol 3-kinase (Welham et al. 1994) so SHP2 may also regulate this pathway.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"Q06124-2",
"P29350-1"
],
"evidence": [
{
"id": "R-HSA-909738",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-909738"
}
]
},
{
"id": "R-HSA-912527",
"name": "SHC1 mediates cytokine-induced phosphorylation of GAB2",
"equation": "",
"summary": "Binding of Gab2 to tyrosine phosphorylated Shc promotes the phosphorylation of Gab2 by an unknown kinase. Gab2 becomes tyrosine phosphorylated in response to IL-2 (Brockdorff et al. 2001) and IL-3 (Gu et al. 1998). Chimeric receptors were used to demonstrate that Shc is sufficient for Gab2 tyrosine phosphorylation. In response to IL-3, Grb2 was also required, reflecting that Gab2 is recruited to the activated cytokine receptor complex as a complex of Gab2:Grb2 (Gu et al. 2000).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-912527",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912527"
}
]
},
{
"id": "R-HSA-912757",
"name": "p-S585-IL3RB binds 14-3-3 proteins",
"equation": "",
"summary": "The common beta chain (Bc), binds 14-3-3 zeta at a site that requires phosphorylation of Serine 585 (Stomski et al. 1999). Bc modifications that prevent Ser-585 phosphorylation do not recruit 14-3-3 zeta (Guthridge et al. 2000).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-912757",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912757"
}
]
},
{
"id": "R-HSA-913370",
"name": "Interleukin-5:Interleukin-5 receptor alpha binds IL3RB:JAK2",
"equation": "",
"summary": "The alpha subunit of the IL5 receptor binds IL-5 with relatively low affinity. Binding of this dimer to the common beta subunit (Bc) confers high affinity binding. Recent models of receptor activation suggest a sequential activation that is initiated by the low-affinity interaction of ligand with the alpha chain to form a binary complex. This binary complex may bind preformed Bc dimers generating a 2:2:2 hexameric complex (Hansen et al. 2008).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-913370",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-913370"
}
]
},
{
"id": "R-HSA-913371",
"name": "GM-CSF receptor alpha:GM-CSF binds Bc",
"equation": "",
"summary": "The alpha subunit of the GM-CSF receptor binds GM-CSF with relatively low affinity. Binding of this dimer to the common beta subunit (Bc) confers high affinity binding. Recent models of receptor activation suggest a sequential activation that is initiated by the low-affinity interaction of GM-CSF with the alpha chain to form a binary complex. This binary complex is then able to bind preformed Bc dimers generating a 2:2:2 hexameric complex (Hansen et al. 2008).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-913371",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-913371"
}
]
},
{
"id": "R-HSA-913374",
"name": "Phosphorylated SHC1 recruits SHIP",
"equation": "",
"summary": "SHIP dephosphorylates PIP3 and may limit the magnitude or duration of signaling events that are dependent upon PIP3-mediated membrane recruitment of plextrin homology (PH) domain signalling proteins such as PI3K and Akt (Aman et al. 1998). The PTB domain of SHC1 binds to phosphorylated tyrosine residues on SHIP. Mutations that inactivate the PTB domain prevent this binding and substitution of F for Y917 and Y1020 on SHIP prevents creation of the phosphotyrosine motifs that are recognized by the SHC1 PTB domain, blocking the interaction (Lamkin et al. 1997). A functional SHIP SH2 domain is also reported as a requirement for association of SHIP with Shc (Liu et al. 1997). GRB2 stabilizes the SHC1/SHIP complex (Harmer & DeFranco 1999), presumably by simultaneously binding via its SH3 domains to SHIP and via its SH2 domain to phosphotyrosines on SHC1, forming a ternary complex of SHC1:GRB2:SHIP described as inducible by IL-3, IL-5 or GM-CSF by many authors (Jucker et al. 1997, Lafrancone et al. 1995, Odai et al. 1997). SHIP2 also associates with SHC1 but does not appear to require Grb2 for stability (Wisniewskiet al. 1999).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"O15357-1",
"Q92835-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-913374",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-913374"
}
]
},
{
"id": "R-HSA-913424",
"name": "The SHC1:SHIP1 complex is stabilized by GRB2",
"equation": "",
"summary": "Grb2 stabilizes the Shc/SHIP complex (Harmer & DeFranco 1999), presumably by simultaneously binding via its SH3 domains to SHIP and via its SH2 domain to phosphotyrosines on Shc. This forms a ternary complex of SHC1:GRB2:SHIP described as an outcome of IL-3, IL-5 or GM-CSF stimulation (Lafrancone et al. 1995, Odai et al. 1997). SHIP2 also associates with SHC1 but does not appear to require Grb2 for stability (Wisniewskiet al. 1999).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"O60674-1",
"P29350-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-913424",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-913424"
}
]
},
{
"id": "R-HSA-913451",
"name": "IL3RB is phosphorylated on Ser-585",
"equation": "",
"summary": "GM-CSF and IL-3 application lead to Ser-585 phosphorylation of the Common beta chain (Bc) shared with the IL-3 and IL-5 receptors (Stomski et al. 1999, Guthridge et al. 2000). PKA was identified as capable of phosphorylating Bc at S585 (Guthridge et al. 2000).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P17612-1"
],
"evidence": [
{
"id": "R-HSA-913451",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-913451"
}
]
},
{
"id": "R-HSA-914036",
"name": "SHP1 and SHP2 dephosphorylate Y628 of IL3RB",
"equation": "",
"summary": "Synthetic phosphopeptides based on Bc were dephosphorylated by SHP1 and SHP2, peptides phosphorylated at Y628 were the best substrate followed by those phosphorylated at Y766.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"Q06124-2",
"P29350-1"
],
"evidence": [
{
"id": "R-HSA-914036",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-914036"
}
]
},
{
"id": "R-HSA-914182",
"name": "14-3-3 zeta binding allows recruitment of PI3K",
"equation": "",
"summary": "Immunoprecipitation and kinase activity experiments demonstrated that Ser-585 phosphorylation of the common beta chain (Bc) was required for activation of PI3K activity in response to IL-3 and co-precipitation of Bc, 14-3-3 zeta and the p85 subunit of Class 1A PI3 kinases (Guthridge et al. 2000). Subsequent experiments confirmed that Ser-585 phosphorylation and PI3K activation are required to promote cell survival in response to GM-CSF, but not for proliferation responses, and that this mechanism is independent of Bc tyrosine phosphorylation (Guthridge et al. 2004). This is one of two mechanisms described for the recruitment of PI3K to the IL-3/IL-5/GM-CSF receptors; the other involves Bc tyrosine-593 phosphorylation-mediated recruitment of SHC1, GRB2 and GAB2.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"O60674-1",
"P42338-1",
"O00329-1"
],
"evidence": [
{
"id": "R-HSA-914182",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-914182"
}
]
},
{
"id": "R-HSA-921155",
"name": "p-STAT5 dissociates from the receptor complex",
"equation": "",
"summary": "Deletion mutants have demonstrated that STAT dimerization can occur independently of the binding of 2 STAT molecules by a dimeric receptor. Although this does not exclude the possibility that STATs may dimerize while still associated with the receptor complex, dimerization is believe to occur following the release of phosphorylated monomers (e.g. Turkson & Jove 2000).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-921155",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-921155"
}
]
},
{
"id": "R-HSA-9656212",
"name": "Phosphorylation of RAF1 mutants",
"equation": "",
"summary": "RAF1 mutants in cancer and germline disorders such as Noonan syndrome undergo enhanced dimerization and activation with BRAF, leading to high levels of downstream signaling. This has been observed even in cases of RAF1 mutations with abrogated or impaired kinase activity (Razzaque et al, 2007; Pandit et al, 2007; Kobayashi et al, 2010; Wu et al, 2012; Krauthammer et al, 2015; reviewed in Rauen, 2013).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"O60674-1",
"Q9UQM7-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"Q13554-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q13557-1",
"Q13555-1"
],
"evidence": [
{
"id": "R-HSA-9656212",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9656212"
}
]
},
{
"id": "R-HSA-9670412",
"name": "Phosphorylation of STATs downstream of KIT mutants",
"equation": "",
"summary": "Extracellular- , juxtamembrane- and kinase-domain mutants of KIT have been shown to activate the STAT pathway, as assessed by STAT phosphorylation. The biological relevance of each STAT isoform varies between tumor types (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hara et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004; reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670412",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670412"
}
]
},
{
"id": "R-HSA-9670413",
"name": "JAK2 binds to p-KIT mutants",
"equation": "",
"summary": "Activation of STAT signaling has been observed downstream of a number of oncogenic KIT mutants, both juxtamembrane and kinase domain mutants, although the biological relevance or each STAT isoform varies between tumor types (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hana et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004). Although the pathway details haven't been examined in all cases, this likely occurs through the recruitment of JAK2 and SRC family kinases, as is the case for the wild type receptor (reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670413",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670413"
}
]
},
{
"id": "R-HSA-9670416",
"name": "Recruitment of STATs by KIT mutants",
"equation": "",
"summary": "Extracellular- , juxtamembrane- and kinase-domain mutants of KIT have been shown to signal through the STAT pathway, although the biological relevance or each STAT isoform varies between tumor types (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hara et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004). Although the pathway details haven't been examined in all cases, STAT pathway activation likely occurs through the recruitment of JAK2 and SRC family kinases, as is the case for the wild type receptor (reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670416",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670416"
}
]
},
{
"id": "R-HSA-9670417",
"name": "Dimerization of STATs downstream of KIT mutants",
"equation": "",
"summary": "Activation of STAT signaling suggests that STATs dimerize downstream of activating KIT mutations as is the case with the wild-type receptor, although this hasn't been directly demonstrated in all cases (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hara et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004; reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670417",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670417"
}
]
},
{
"id": "R-HSA-9670418",
"name": "Phosphorylation of JAK2 downstream of KIT mutants",
"equation": "",
"summary": "Although the details haven't been examined in detail in all cases, phosphorylation of JAK2 likely occurs downstream of oncogenic mutations of KIT, as is the case for the wild-type receptor (Brizzi et al, 1999; Ning et al, 2001; Hirota et al, 1998; reviewed in Lennartsson and Roonstrand, 2012).; ;",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670418",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670418"
}
]
},
{
"id": "R-HSA-9670426",
"name": "Disassociation and translocation of STATs to the nucleus downstream of KIT mutants",
"equation": "",
"summary": "STATs are assumed to dissociate from the receptor and translocate to the nucleus downstream of activated KIT receptors to propagate STAT-dependent signaling (Brizzi et al, 1999; Ning et al, 2001; Frost et al, 2002; Growney et al, 2005; Hara et al, 2017; Obata et al, 2017; Duensing et al, 2004; Bauer et al, 2007; Deberry et al, 1997; Ronnstrand, 2004; reviewed in Lennartsson and Roonstrand, 2012).",
"cellular_location": "cytosol, nucleoplasm, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670426",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670426"
}
]
},
{
"id": "R-HSA-9674562",
"name": "CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2 binds STAT1,3,5",
"equation": "",
"summary": "The STAT proteins STAT1 (Tian et al. 1994), STAT3 (Tian et al. 1994, Tian et al. 1996, Ward et al. 1999, Marino and Roguin 2008), and STAT5 (STAT5A and STAT5B) (Tian et al. 1996) bind phosphotyrosines of the cytosolic domain of CSF3R. The membrane-proximal region of the cytosolic domain of CSF3R is sufficient to activate STAT1 and STAT5. Activation of STAT3 by low concentrations of CSF3 (G-CSF) requires a membrane-distal region of CSF3R (Ward et al. 1999).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9674562",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674562"
}
]
},
{
"id": "R-HSA-9674563",
"name": "CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2:p-Y-STAT1,3,5 dissociates yielding CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2 and p-Y-STAT1,3,5",
"equation": "",
"summary": "After phosphorylation while bound to phospho-CSF3R at the plasma membrane, p-STAT1,3,5 dissociates from CSF3R prior to dimerizing and transiting to the nucleus (Tian et al. 1994, Tian et al. 1996, Ward et al. 1999, also inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9674563",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674563"
}
]
},
{
"id": "R-HSA-9674567",
"name": "p-Y-JAK1,2 phosphorylates STAT1,3,5 in CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1:p-Y-JAK2:p-TYK2",
"equation": "",
"summary": "Phosphorylated JAK1 (p-Y-JAK1) phosphorylates the STAT proteins STAT1 (Tian et al. 1994, Tian et al. 1996, Shimoda et al. 1997, also inferred from mouse homologs), STAT3 (Tian et al. 1994, Tian et al. 1996, Shimoda et al. 1997, Ward et al. 1999, Marino and Roguin 2008, Kumar et al. 2014, also inferred from mouse homologs), and STAT5 (Tian et al. 1994, Tian et al. 1996, Shimoda et al. 1997, also inferred from mouse homologs) at the cytosolic domain of CSF3R (G-CSFR). Phosphorylated JAK2 acts redundantly with p-Y-JAK1 to phosphorylate STAT proteins (Kumar et al. 2014, also inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9674567",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674567"
}
]
},
{
"id": "R-HSA-9674808",
"name": "CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1:p-JAK2:p-TYK2 binds and phosphorylates SHC1, GRB2, GAB2, and PTPN11 (SHP2)",
"equation": "",
"summary": "Proteins involved in RAS-RAF-ERK signaling bind the phosphorylated cytosolic domain of CSF3R (GCSFR) and are phosphorylated (Wang et al. 2008 and inferred from mouse homologs). GRB2, GAB2, and SHC1 bind phosphorylated CSF3R directly. PTPN11 (SHP2) directly binds the phosphorylated cytosolic domain of CSF3R (inferred from mouse homologs) and also appears to bind CSF3R indirectly via phosphorylated GAB2 (inferred from mouse homologs). LYN is required for phosphorylation of GAB2 9inferred from mouse homologs). The order of binding and phosphorylation is unknown.",
"cellular_location": "plasma membrane",
"input_participant_list": [
"R-HSA-162563",
"R-HSA-508239",
"R-HSA-8983328"
],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"Q06124-2",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9674808",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674808"
}
]
},
{
"id": "R-HSA-9674816",
"name": "p-Y546,Y584-PTPN11 (in CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2:SHC:GRB2:PTPN11) dephosphorylates KRAS",
"equation": "",
"summary": "CSF3 (G-CSF) signaling activates ERKs (ERK1, ERK2) via RAS. One possible mechanism of RAS activation is the dephosphorylation of KRAS (the dominant isoform of RAS in hematopoietic cells) by phosphorylated PTPN11 (also known as SHP-2 or SHP2) (Kano et al. 2019, also inferred from dephosphorylation of the HRAS paralog in Bunda et al. 2015) bound to phosphorylated CSF3R. Dephosphorylation of RAS increases the association of RAS with its downstream effector RAF. Inhibition of PTPN11 in mouse cells indicates that this pathway accounts for most but not all activation of ERKs in response to CSF3 (Jack et al. 2009, Zhang and Friedman 2011). Guanyl nucleotide exchange factors SOS or VAV bound to GRB2 may also be responsible for some activation of RAS in response to CSF3, but this has not yet been demonstrated.",
"cellular_location": "plasma membrane",
"input_participant_list": [
"R-HSA-9674821"
],
"output_participant_list": [
"R-HSA-9674814"
],
"enzyme_list": [
"O60674-1",
"P07948-1",
"Q06124-2",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-9674816",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9674816"
}
]
},
{
"id": "R-HSA-9676071",
"name": "CSF3 dimer:2xp-4Y-CSF3R:LYN:p-Y-JAK1 binds and activates JAK2, TYK2, SYK, and HCK",
"equation": "",
"summary": "The kinases JAK2 (Shimoda et al. 1997, Marino and Roguin 2008), TYK2 (Shimoda et al. 1997, Marino and Roguin 2008), HCK, and SYK (Kasper et al. 1999) bind phosphorylated tyrosine residues of the cytosolic domain of CSF3R and are activated by phosphorylation (also inferred from mouse homologs). The order of their binding and the kinases responsible for their phosphorylation are incompletely characterized.",
"cellular_location": "plasma membrane",
"input_participant_list": [
"R-HSA-210620",
"R-HSA-877348",
"R-HSA-58268",
"R-HSA-167708"
],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9676071",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9676071"
}
]
},
{
"id": "R-HSA-9678561",
"name": "IFNGR1:JAK1:INFGR2:JAK2 binds JAK1,2 inhibitors",
"equation": "",
"summary": "Janus Kinase 2 (JAK2) binds and is inhibited by several small molecule drugs (Clark et al. 2014, Fridman et al. 2010, Hanan et al. 2012). The Janus kinases (JAKs) are a family of intracellular tyrosine kinases that play an essential role in the signaling of numerous cytokines that have been implicated in the pathogenesis of inflammatory diseases. Drugs that inhibit these kinases such as baricitinib, tofacitinib and ruxolitinib are thus plausible candidates for treatment of severe host inflammatory reactions to viral infection (Peterson et al. 2020, Richardson et al. 2020).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9678561",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9678561"
}
]
},
{
"id": "R-HSA-9705467",
"name": "SOCS1,3 binds p-4Y-CSF3R:CSF3 dimer:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2",
"equation": "",
"summary": "SOCS3 (Hortner et al. 2002) or SOCS1 binds phosphotyrosine-729 (phosphotyrosine-727 of isoform 1) of CSF3R. SOCS3 also interacts with phosphotyrosine-1007 of JAK2 (Sasaki et al. 1999). SOCS1 and especially SOCS3 inhibit the phosphorylation activity of JAK2 (van de Geijn et al. 2004).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9705467",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9705467"
}
]
},
{
"id": "R-HSA-9705726",
"name": "SOCS1,3:p-4Y-CSF3R:CSF3 dimer:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2 is endocytosed",
"equation": "",
"summary": "After binding CSF3 (G-CSF), the CSF3 receptor CSF3R is internalized into endosomes (Aarts et al. 2004). Only a minor portion of CSF3R is located at the plasma membrane. Most CSF3R is located internally in the Golgi, endosomes, and lysosomes (Aarts et al. 2004). Endocytosis depends on a dileucine motif in the C-terminal region of CSF3R (inferred from mouse homologs).",
"cellular_location": "plasma membrane, endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9705726",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9705726"
}
]
},
{
"id": "R-HSA-9705729",
"name": "SOCS1,3:p-4Y-CSF3R:CSF3 dimer:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2 binds CUL5, ELOB, ELOC, RNF7",
"equation": "",
"summary": "SOCS1 and SOCS3 recruit Elongin B (ELOB), Elongin C (ELOC), Cullin5 (CUL5), and RNF7 to CSF3R to form a ubiquitin E3 ligase complex (Kamura et al. 2004 and inferred from mouse homologs). SOCS3 has 100-fold higher affinity for CUL5 than SOCS1 has (inferred from mouse homologs).",
"cellular_location": "endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9705729",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9705729"
}
]
},
{
"id": "R-HSA-9705738",
"name": "SOCS1,3 ubiquitinates CSF3R in SOCS1,3:p-4Y-CSF3R:CSF3 dimer:LYN:p-Y-JAK1:p-JAK2:p-SYK:p-HCK:p-TYK2:CUL5:ELOB:ELOC:RNF7",
"equation": "",
"summary": "A ubiquitin E3 ligase complex assembled by SOCS3 or SOCS1 polyubiquitinates a membrane proximal lysine residue of CSF3R (K632 of the mature protein which corresponds to K655 of the preprotein) (Irandoust et al. 2007, W\u00f6lfler et al. 2009).",
"cellular_location": "endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P51668-1",
"P61077-1",
"P62837-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9705738",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9705738"
}
]
},
{
"id": "R-HSA-9707977",
"name": "CSF3 dimer:2xK48polyUb-K655,p-4Y-CSF3R:LYN:p-Y-JAK1:p-JAK2:p-Y-SYK:p-HCK:p-TYK2 translocates from the endocytic vesicle membrane to the lysosomal membrane",
"equation": "",
"summary": "Polyubiquitinated CSF3R, believed to be in a complex with with CSF3 and other signaling molecules, transits from endosomes to lysosomes (Aarts et al. 2004, Irandoust et al. 2007, W\u00f6lfler et al. 2009).",
"cellular_location": "lysosomal membrane, endocytic vesicle membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1",
"P08631-1",
"P43405-1",
"P29597-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9707977",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9707977"
}
]
},
{
"id": "R-HSA-9709454",
"name": "EPOR binds EPOR agonists",
"equation": "",
"summary": "Erythropoietin (EPO) is a growth factor produced in the kidneys that stimulates the production of red blood cells. It works by promoting the division and differentiation of committed erythroid progenitors in the bone marrow. EPO binds to the erythropoietin receptor (EPOR) and triggers the JAK2/STAT5 signalling cascade which ultimately signals the activatation of nuclear target genes involved in cell division or differentiation, including the apoptosis inhibitor Bcl-x. The inhibition of apoptosis is critical in erythroid differentiation. EPO also activates other intracellular proteins involved in erythroid cell proliferation and survival.
The PEGylated functional analogue of EPO (peginesatide) and recombinant EPO forms (the epoetins) are used for the treatment of patients with anemia associated with various clinical conditions, such as chronic renal failure, antiviral drug therapy and chemotherapy (Bennet et al. 2004, Singh et al. 2006, Besarab et al. 2012, Zabaneh et al. 2015, Fishbane & Shah 2015, Zadeh 2017)",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9709454",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9709454"
}
]
},
{
"id": "R-HSA-9732729",
"name": "Activated JAK1 binds RAF1",
"equation": "",
"summary": "In response to IFNG (interferon-gamma) stimulation, RAF1 forms a complex with JAK1 in a RAS-independent manner (Sakatsume et al. 1998).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P04049-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9732729",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9732729"
}
]
},
{
"id": "R-HSA-9732738",
"name": "JAK1-mediated phosphorylation of RAF1",
"equation": "",
"summary": "In response to IFNG (interferon-gamma) treatment, JAK1 mediates phosphorylation of RAF1 on an unknown tyrosine residue. As there is direct binding between JAK1 and RAF1, and as JAK1 tyrosine kinase activity is necessary, it is plausible that JAK1 is the tyrosine kinase that acts on RAF1, but indirect JAK1-mediated phosphorylation of RAF1 has not been excluded (Sakatsume et al. 1998).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1",
"P04049-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9732738",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9732738"
}
]
},
{
"id": "R-HSA-9732753",
"name": "JAK1-activated RAF1 phosphorylates MAPKs",
"equation": "",
"summary": "RAF1, activated downstream of IFNG (interferon-gamma) in a JAK1-dependent and RAS-independent manner, phosphorylates ERKs: MAPK1 (ERK2) and MAPK3 (ERK1) (Sakatsume et al. 1998). IFNG-mediated activation of ERKs may contribute to transient attenuation of TGF-beta signaling through ERK-mediated phosphorylation of SMAD2 and SMAD3, but a long-term effect depends on IFNG-mediated transcription of SMAD7, an inhibitor of TGF-beta signaling (Ulloa et al. 1999).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P27361-1",
"O60674-1",
"P04049-1",
"P28482-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9732753",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9732753"
}
]
},
{
"id": "R-HSA-9734547",
"name": "JAK2-activated MAPKs phosphorylate YBX1",
"equation": "",
"summary": "Interferon-gamma (IFNG) signaling was shown to induce nuclear translocation of YBX1 and its binding to the promoter of the collagen I gene COL1A2 (Higashi et al. 2003). IFNG signaling also induces YBX1-mediated repression of COL1A1 gene transcription, which is dependent on JAK1 activity (Dooley et al. 2006). Based on studies in mice, phosphorylation of YBX1 on serine residues S32 and S36 (S30 and S34 in mouse Ybx1) by MAPK1 and/or MAPK3 (ERK2 and ERK1, respectively) is needed for the nuclear translocation of YBX1 and depends on JAK2, which may promote the interaction between YBX1 and ERKs (Jayavelu et al. 2020).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [
"R-HSA-9736840"
],
"output_participant_list": [
"R-HSA-9736837"
],
"enzyme_list": [
"P27361-1",
"O60674-1",
"P28482-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-9734547",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9734547"
}
]
},
{
"id": "R-HSA-976991",
"name": "Prolactin receptor ligands bind the prolactin receptor",
"equation": "",
"summary": "Human PRLR binds at least 3 related peptide ligands namely prolactin, placental lactogen (PL) and growth hormone (GH). In non primates, GH is not able to bind the PRLR. Human GH binding to the PRLR is zinc-dependent (Cunningham et al. 1990). All three ligands bind the extracellular domain and have apparently identical actions. Two disulfide-linked cysteines in the D1 subdomain are involved in ligand binding while the WSXWS motif in the D2 subdomain is probably required for folding and cellular trafficking.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P62877-1",
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-976991",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-976991"
}
]
},
{
"id": "R-HSA-982768",
"name": "GH:GHR:JAK2 complex undergoes a conformational change",
"equation": "",
"summary": "Classical models of GHR activation suggest that GH binds sequentially to two GHR molecules, leading to receptor dimerization and activation. More recently, evidence from FRET, BRET, Co-IP (Brown et al. 2005) and molecular simulations (Poger & Mark 2010) suggest that dimerization occurs before ligand binding, and that activation is a consequence of conformational changes caused by ligand binding, namely a relative rotation of the receptor dimer so that the catalytic domains of JAK2 molecules bound to the cytoplasmic tails are brought into close proximity and are consequently able to phosphorylate each other (Rowlinson et al. 2008). Realignment of the receptor subunits and consequent JAK2 activation is supported by crystal structures of the related erythropoietin receptor (Livnah et al. 1999); similar proposals have been made for many receptors, including the prolactin and erythropoietin receptors (Brooks & Waters 2010).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-982768",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-982768"
}
]
},
{
"id": "R-HSA-982775",
"name": "Growth hormone receptor dimerizes",
"equation": "",
"summary": "The growth hormone receptor forms dimers (Cunningham et al. 1991) that subsequently signal via JAK2 (Argetsinger et al. 1993). Early studies suggested that dimerization occured following ligand binding, but it is now generally accepted that dimerization is independent of ligand binding and involves the transmembrane and juxtamembrane domains (van den Eijnden et al. 2006, Brown et al. 2005). Binding of growth hormone binding protein (GHBP) to growth hormone receptor (GHR) produces 'unproductive' dimers that prevent formation of signaling-capable GHR dimers (Ross et al. 1997).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-982775",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-982775"
}
]
},
{
"id": "R-HSA-982778",
"name": "Growth hormone binds the growth hormone receptor",
"equation": "",
"summary": "The growth hormone receptor (GHR) belongs to the superfamily of transmembrane proteins that includes the prolactin receptor and a number of class 1 cytokine receptors. It exists in two forms, full-length membrane-bound receptor with a single transmembrane region, and growth hormone binding protein (GHBP), a shorter soluble form corresponding to the extracellular domain of the full-length receptor. In rodents GHBP is encoded by a specific mRNA variant while in humans it results from proteolytic cleavage of the membrane receptor by a metalloprotease. The classical view is that growth hormone sequentially binds 2 molecules of GHR inducing dimerization, but it is now widely accepted that GHR dimers exist prior to ligand binding (Poger & Mark 2010).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-982778",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-982778"
}
]
},
{
"id": "R-HSA-982792",
"name": "Growth hormone receptor binds JAK2",
"equation": "",
"summary": "JAKs bind to the box1 motif (residues 297-305) of the Growth Hormone Receptor (GHR) (Argetsinger et al. 1993), a proline-rich region just inside the cell membrane. Binding is mediated largely by the JAK N-terminal FERM domain (Frank et al. 1995, He et al. 2003). JAK 2 binding enhances the stability of GHR (He et al. 2005).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-982792",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-982792"
}
]
},
{
"id": "R-HSA-982807",
"name": "JAK2 phosphorylation of GHR",
"equation": "",
"summary": "Activated JAK2 phosphorylates multiple tyrosine residues on GHR (Argetsinger et al. 1993, VanderKuur et al. 1994) including Y332 (VanderKuur 1995), Y487, Y534, Y566, and Y627 (Wang et al. 1996). Wang et al. using the porcine receptor found that phosphorylation at any of the positions they examined (all conserved in humans) was sufficient for STAT5 phosphorylation. While STAT5 activation requires phosphorylation of the distal region of GHR, this has no effect on STAT1 or STAT3 activation (Yi et al. 1996) suggesting different mechanisms. Mutation of Y332 to F in a truncated form of GHR with only the first 54 residues of the cytoplasmic domain had no effect on JAK2 activation or cell proliferation presumed to be mediated by ERK (Wang et al. 1995) so the significance of phosphorylation at this position is unclear. SHP2 binds to Y595 of rat GHR (identical numbering in humans) and to a lesser extent Y487; mutation of these residues impairs the association (Stofega et al. 2000). SOCS3 binds to rat GHR Y333 (equivalent of human Y332), Y338 (not conserved in humans) (Ram & Waxman 1999) and Y487 (Hansen et al. 1999). ; ; SOCS-1 has been implicated as a direct inhibitor of JAK kinases (Yasukawa et al. 1999).; ; This reaction represents the phosphorylation of all GHR tyrosines known to be phosphorylated by JAK2.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-982807",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-982807"
}
]
},
{
"id": "R-HSA-982810",
"name": "JAK2 phosphorylation",
"equation": "",
"summary": "Similar models explain JAK activation by the cytokine-like hormone receptors (GHR and PRLR) and interleukin receptors. JAK2 activation is believed to occur as mutual transactivation whereby JAK2 bound to one receptor chain phosphorylates JAK2 bound to the other receptor chain in the dimeric receptor. Transactivation is widely accepted (Herrington & Carter-Su 2001) having been originally proposed in the 1990's (Quelle et al. 1994, Hou et al. 2002). JAK phosphorylation is thought to lock the kinase domain in an active state; prior to this JAK2 is held in an inactive state by interactions between its kinase and pseudokinase domains (Giordanetto & Kroemer 2002). Although there are structures of JAK kinase domains (e.g. Lucet et al. 2006), no complete JAK structures are available and the activation mechanism remains poorly understood (Brooks & Waters 2010). The trigger for JAK activation is believed to be a conformational change in the receptor when ligand is bound, leading to a rotation of the cytoplasmic regions which brings the catalytic domains of bound JAK2 molecules into close proximity and frees them from inhibition by the pseudokinase domains. Supporting observations for cytokine-like hormone receptors include: JAK2 becomes tyrosine phosphorylated as a consequence of GHR activation by GH (Argetsinger et al. 1993); JAK2 is activated following PRLR activation (Campbell et al. 1994, Rui et al. 1994); forced dimerization of GH receptor domains is sufficient to activate signaling (Behncken et al. 2000); phosphorylation of JAK2 at Y1007 is critical for kinase activation (Feng et al. 1997, Lucet et al. 2006); JAK autophosphorylation at several other sites appears to regulate activity (e.g. Feener et al. 2004, Argetsinger et al. 2004, 2010). Only the Y1007 phosphorylation is represented in this reaction.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-982810",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-982810"
}
]
},
{
"id": "R-HSA-997237",
"name": "SH2B proteins bind JAK2",
"equation": "",
"summary": "The SH2B family has 3 members sharing a common domain structure, including a dimerization domain, a pleckstrin homology (PH) region, and a SH2 domain. The SH2 domain binds phosphotyrosines of various signal-transducing proteins such as c-Kit, MPL, EpoR. All are able to bind JAK2 phosphorylated at Tyr-813 (Bersenev et al. 2008, Kurzer et al. 2004, 2006), inhibiting JAK2 proliferative signaling (Gery et al. 2009).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O60674-1"
],
"evidence": [
{
"id": "R-HSA-997237",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-997237"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-HSA-162563",
"participant_name": "PTPN11 [cytosol]",
"crossref": [
{
"id": "Q06124",
"database": "UniProt",
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{
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{
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{
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{
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{
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{
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{
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{
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{
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"database": "PDB",
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{
"id": "Q06124",
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{
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{
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{
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{
"id": "7TVJ",
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{
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{
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"database": "PDB",
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},
{
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{
"id": "4OHE",
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{
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{
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{
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"database": "PDB",
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},
{
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{
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{
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}
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{
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{
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{
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},
{
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}
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]
},
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},
{
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},
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]
},
{
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},
{
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},
{
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}
]
},
{
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}
]
},
{
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}
]
}
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},
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{
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}
]
},
{
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}
]
}
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},
{
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},
{
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}
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}
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}
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},
{
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}
]
}
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{
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"activity": "",
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}
]
},
{
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},
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}
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}
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}
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},
{
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}
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}
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}
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},
{
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}
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]
},
{
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]
}
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},
{
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]
}
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},
{
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]
}
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},
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}
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},
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]
},
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]
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{
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]
}
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]
},
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}
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}
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]
}
]
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}
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}
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}
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},
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]
}
]
},
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]
},
{
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]
}
]
},
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]
},
{
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]
}
]
},
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{
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}
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},
{
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}
]
}
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},
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}
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}
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{
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]
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]
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]
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}
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]
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]
}
]
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]
},
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]
}
]
},
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]
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]
}
]
},
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]
},
{
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]
}
]
},
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{
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]
},
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