{
"uniprot_canonical_ac": "P06239-1",
"uniprot_ac": "P06239",
"uniprot_id": "LCK_HUMAN",
"mass": {
"chemical_mass": 58001.0,
"monoisotopic_mass": 58001.0
},
"refseq": {
"ac": "NP_001036236",
"name": "tyrosine-protein kinase Lck isoform a",
"summary": "This gene is a member of the Src family of protein tyrosine kinases (PTKs). The encoded protein is a key signaling molecule in the selection and maturation of developing T-cells. It contains N-terminal sites for myristylation and palmitylation, a PTK domain, and SH2 and SH3 domains which are involved in mediating protein-protein interactions with phosphotyrosine-containing and proline-rich motifs, respectively. The protein localizes to the plasma membrane and pericentrosomal vesicles, and binds to cell surface receptors, including CD4 and CD8, and other signaling molecules. Multiple alternatively spliced variants encoding different isoforms have been described. [provided by RefSeq, Aug 2016].",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001036236"
},
"gene_names": [
{
"name": "LCK",
"resource": "UniProtKB",
"type": "recommended",
"url": "https://www.uniprot.org/uniprot/P06239",
"id": "P06239"
},
{
"name": "IMD22; LSK; p56lck; pp58lck; YT16",
"resource": "RefSeq",
"type": "synonym",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001036236",
"id": "NP_001036236"
},
{
"name": "LCK",
"resource": "RefSeq",
"type": "synonym",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001036236",
"id": "NP_001036236"
}
],
"protein_names": [
{
"name": "Tyrosine-protein kinase Lck",
"resource": "UniProtKB",
"type": "recommended",
"url": "",
"id": "P06239"
},
{
"name": "2.7.10.2",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "P06239"
},
{
"name": "LSK",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "P06239"
},
{
"name": "Leukocyte C-terminal Src kinase",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "P06239"
},
{
"name": "Lymphocyte cell-specific protein-tyrosine kinase",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "P06239"
},
{
"name": "Protein YT16",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "P06239"
},
{
"name": "Proto-oncogene Lck",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "P06239"
},
{
"name": "T cell-specific protein-tyrosine kinase",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "P06239"
},
{
"name": "T-lymphocyte specific protein tyrosine kinase p56lck; p56(LSTRA) protein-tyrosine kinase; proto-oncogene tyrosine-protein kinase LCK; leukocyte C-terminal Src kinase; t cell-specific protein-tyrosine kinase; lymphocyte cell-specific protein-tyrosine kinase",
"resource": "RefSeq",
"type": "synonym",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001036236",
"id": "NP_001036236"
},
{
"name": "p56-LCK",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "P06239"
},
{
"name": "tyrosine-protein kinase Lck isoform a",
"resource": "RefSeq",
"type": "synonym",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001036236",
"id": "NP_001036236"
}
],
"function": [
{
"annotation": "A Novel Biallelic LCK Variant Resulting in Profound T-Cell Immune Deficiency and Review of the Literature. Review article Erratum:[J Clin Immunol. 2024 Jan 16;44(1):41. PMID: 38225415] Publication Status: Online-Only",
"evidence": [
{
"database": "RefSeq",
"id": "NP_001036236",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001036236"
},
{
"database": "PubMed",
"id": "38100037",
"url": "https://glygen.org/publication/PubMed/38100037"
}
]
},
{
"annotation": "Combined Immunodeficiency Caused by a Novel Nonsense Mutation in LCK. Publication Status: Online-Only",
"evidence": [
{
"database": "RefSeq",
"id": "NP_001036236",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001036236"
},
{
"database": "PubMed",
"id": "38112969",
"url": "https://glygen.org/publication/PubMed/38112969"
}
]
},
{
"annotation": "Identification of Breast Cancer LCK Proto-Oncogene as a Master Regulator of TNBC Neutrophil Enrichment and Polarization. Publication Status: Online-Only",
"evidence": [
{
"database": "RefSeq",
"id": "NP_001036236",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001036236"
},
{
"database": "PubMed",
"id": "37686072",
"url": "https://glygen.org/publication/PubMed/37686072"
}
]
},
{
"annotation": "LCK facilitates DNA damage repair by stabilizing RAD51 and BRCA1 in the nucleus of chemoresistant ovarian cancer. Publication Status: Online-Only",
"evidence": [
{
"database": "RefSeq",
"id": "NP_001036236",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001036236"
},
{
"database": "PubMed",
"id": "37370140",
"url": "https://glygen.org/publication/PubMed/37370140"
}
]
},
{
"annotation": "Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosine residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP70, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP. Interacts with FYB2 (PubMed:27335501).",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239#function"
},
{
"database": "PubMed",
"id": "20851766",
"url": "https://glygen.org/publication/PubMed/20851766"
},
{
"database": "PubMed",
"id": "21269457",
"url": "https://glygen.org/publication/PubMed/21269457"
},
{
"database": "PubMed",
"id": "16339550",
"url": "https://glygen.org/publication/PubMed/16339550"
},
{
"database": "PubMed",
"id": "27335501",
"url": "https://glygen.org/publication/PubMed/27335501"
},
{
"database": "PubMed",
"id": "16709819",
"url": "https://glygen.org/publication/PubMed/16709819"
},
{
"database": "PubMed",
"id": "20028775",
"url": "https://glygen.org/publication/PubMed/20028775"
},
{
"database": "PubMed",
"id": "22080863",
"url": "https://glygen.org/publication/PubMed/22080863"
},
{
"database": "PubMed",
"id": "20100835",
"url": "https://glygen.org/publication/PubMed/20100835"
}
]
},
{
"annotation": "This gene is a member of the Src family of protein tyrosine kinases (PTKs). The encoded protein is a key signaling molecule in the selection and maturation of developing T-cells. It contains N-terminal sites for myristylation and palmitylation, a PTK domain, and SH2 and SH3 domains which are involved in mediating protein-protein interactions with phosphotyrosine-containing and proline-rich motifs, respectively. The protein localizes to the plasma membrane and pericentrosomal vesicles, and binds to cell surface receptors, including CD4 and CD8, and other signaling molecules. Multiple alternatively spliced variants encoding different isoforms have been described. [provided by RefSeq, Aug 2016].",
"evidence": [
{
"database": "RefSeq",
"id": "NP_001036236",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_001036236"
}
]
}
],
"disease": [
{
"disease_id": "DOID:0111937",
"recommended_name": {
"id": "DOID:0111937",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:0111937",
"name": "immunodeficiency 22",
"description": "A severe combined immunodeficiency characterized by severe combined immunodeficiency, selective CD4 lymphopenia, and lack of CD28 expression on CD8+ T cells that has_material_basis_in homozygous or compound heterozygous mutation in the LCK gene on chromosome 1p35.2."
},
"synonyms": [
{
"id": "DOID:0111937",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:0111937",
"name": "IMD22",
"description": ""
},
{
"id": "DOID:0111937",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:0111937",
"name": "severe combined immunodeficiency due to lymphocyte-specific protein tyrosine kinase deficiency",
"description": ""
},
{
"id": "DOID:0111937",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:0111937",
"name": "SCID due to LCK deficiency",
"description": ""
},
{
"id": "DOID:0111937",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:0111937",
"name": "severe combined immunodeficiency due to LCK deficiency",
"description": ""
},
{
"id": "DOID:0111937",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:0111937",
"name": "SCID due to lymphocyte-specific protein tyrosine kinase deficiency",
"description": ""
},
{
"id": "MONDO:0014334",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0014334",
"name": "severe combined immunodeficiency due to LCK deficiency",
"description": ""
},
{
"id": "MONDO:0014334",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0014334",
"name": "SCID due to LCK deficiency",
"description": ""
},
{
"id": "MONDO:0014334",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0014334",
"name": "SCID due to lymphocyte-specific protein tyrosine kinase deficiency",
"description": ""
},
{
"id": "MONDO:0014334",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0014334",
"name": "immunodeficiency type 22",
"description": ""
},
{
"id": "MONDO:0014334",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0014334",
"name": "severe combined immunodeficiency due to lymphocyte-specific protein tyrosine kinase deficiency",
"description": ""
},
{
"id": "MONDO:0014334",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0014334",
"name": "IMD22",
"description": ""
},
{
"id": "MONDO:0014334",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0014334",
"name": "immunodeficiency 22",
"description": ""
},
{
"id": "MIM:615758",
"resource": "MIM",
"url": "https://www.omim.org/entry/615758",
"name": "Immunodeficiency 22",
"description": "Immunodeficiency 22"
}
],
"evidence": [
{
"id": "615758",
"database": "MIM",
"url": "https://www.omim.org/entry/615758"
}
]
}
],
"snv": [],
"mutagenesis": [
{
"start_pos": 154,
"end_pos": 154,
"sequence_org": "R",
"sequence_mut": "K",
"comment": "No effect on interaction with SQSTM1.",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
},
{
"database": "PubMed",
"id": "8618896",
"url": "https://glygen.org/publication/PubMed/8618896"
}
]
},
{
"start_pos": 59,
"end_pos": 59,
"sequence_org": "S",
"sequence_mut": "E",
"comment": "Allows interaction with SQSTM1.",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
},
{
"database": "PubMed",
"id": "8618896",
"url": "https://glygen.org/publication/PubMed/8618896"
}
]
}
],
"expression_tissue": [
{
"tissue": {
"name": "Adult mammalian kidney",
"namespace": "UBERON",
"id": "0000082",
"url": "http://purl.obolibrary.org/obo/UBERON_0000082"
},
"score": "63.28",
"present": "MEDIUM",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000182866",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000182866"
}
]
},
{
"tissue": {
"name": "Oral cavity",
"namespace": "UBERON",
"id": "0000167",
"url": "http://purl.obolibrary.org/obo/UBERON_0000167"
},
"score": "73.73",
"present": "HIGH",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000182866",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000182866"
}
]
},
{
"tissue": {
"name": "Stomach",
"namespace": "UBERON",
"id": "0000945",
"url": "http://purl.obolibrary.org/obo/UBERON_0000945"
},
"score": "79.98",
"present": "HIGH",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000182866",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000182866"
}
]
},
{
"tissue": {
"name": "Uterus",
"namespace": "UBERON",
"id": "0000995",
"url": "http://purl.obolibrary.org/obo/UBERON_0000995"
},
"score": "68.65",
"present": "MEDIUM",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000182866",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000182866"
}
]
},
{
"tissue": {
"name": "Esophagus",
"namespace": "UBERON",
"id": "0001043",
"url": "http://purl.obolibrary.org/obo/UBERON_0001043"
},
"score": "61.19",
"present": "MEDIUM",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000182866",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000182866"
}
]
},
{
"tissue": {
"name": "Rectum",
"namespace": "UBERON",
"id": "0001052",
"url": "http://purl.obolibrary.org/obo/UBERON_0001052"
},
"score": "80.53",
"present": "HIGH",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000182866",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000182866"
}
]
},
{
"tissue": {
"name": "Colon",
"namespace": "UBERON",
"id": "0001155",
"url": "http://purl.obolibrary.org/obo/UBERON_0001155"
},
"score": "73.03",
"present": "HIGH",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000182866",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000182866"
}
]
},
{
"tissue": {
"name": "Urinary bladder",
"namespace": "UBERON",
"id": "0001255",
"url": "http://purl.obolibrary.org/obo/UBERON_0001255"
},
"score": "65.41",
"present": "MEDIUM",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000182866",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000182866"
}
]
},
{
"tissue": {
"name": "Thyroid gland",
"namespace": "UBERON",
"id": "0002046",
"url": "http://purl.obolibrary.org/obo/UBERON_0002046"
},
"score": "68.77",
"present": "MEDIUM",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000182866",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000182866"
}
]
},
{
"tissue": {
"name": "Lung",
"namespace": "UBERON",
"id": "0002048",
"url": "http://purl.obolibrary.org/obo/UBERON_0002048"
},
"score": "73.5",
"present": "HIGH",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000182866",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000182866"
}
]
},
{
"tissue": {
"name": "Liver",
"namespace": "UBERON",
"id": "0002107",
"url": "http://purl.obolibrary.org/obo/UBERON_0002107"
},
"score": "66.77",
"present": "MEDIUM",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000182866",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000182866"
}
]
},
{
"tissue": {
"name": "Prostate gland",
"namespace": "UBERON",
"id": "0002367",
"url": "http://purl.obolibrary.org/obo/UBERON_0002367"
},
"score": "69.17",
"present": "MEDIUM",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000182866",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000182866"
}
]
},
{
"tissue": {
"name": "Thoracic mammary gland",
"namespace": "UBERON",
"id": "0005200",
"url": "http://purl.obolibrary.org/obo/UBERON_0005200"
},
"score": "69.64",
"present": "MEDIUM",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000182866",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000182866"
}
]
}
],
"expression_disease": [
{
"significant": "No",
"trend": "up",
"name": "Prostate cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:10283",
"evidence": [
{
"database": "BioXpress",
"id": "P06239",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P06239"
}
],
"disease": [
{
"disease_id": "DOID:10283",
"recommended_name": {
"id": "DOID:10283",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:10283",
"name": "prostate cancer",
"description": "A male reproductive organ cancer that is located_in the prostate."
},
"synonyms": [
{
"id": "DOID:10283",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:10283",
"name": "NGP - new growth of prostate",
"description": ""
},
{
"id": "DOID:10283",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:10283",
"name": "hereditary prostate cancer",
"description": ""
},
{
"id": "DOID:10283",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:10283",
"name": "malignant tumor of the prostate",
"description": ""
},
{
"id": "DOID:10283",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:10283",
"name": "prostate cancer, familial",
"description": ""
},
{
"id": "DOID:10283",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:10283",
"name": "prostate neoplasm",
"description": ""
},
{
"id": "DOID:10283",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:10283",
"name": "prostatic cancer",
"description": ""
},
{
"id": "DOID:10283",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:10283",
"name": "prostatic neoplasm",
"description": ""
},
{
"id": "DOID:10283",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:10283",
"name": "tumor of the prostate",
"description": ""
},
{
"id": "MONDO:0012597",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012597",
"name": "prostate cancer, hereditary, 9",
"description": ""
},
{
"id": "MONDO:0012597",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012597",
"name": "prostate cancer, hereditary, 9",
"description": ""
},
{
"id": "MONDO:0012597",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012597",
"name": "prostate cancer, hereditary, type 9",
"description": ""
},
{
"id": "MONDO:0012597",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012597",
"name": "HPC9",
"description": ""
},
{
"id": "MONDO:0012741",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012741",
"name": "prostate cancer, hereditary, 12",
"description": "Any familial prostate cancer in which the cause of the disease is a mutation in the EHBP1 gene."
},
{
"id": "MONDO:0012741",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012741",
"name": "EHBP1 familial prostate cancer",
"description": ""
},
{
"id": "MONDO:0012741",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012741",
"name": "familial prostate cancer caused by mutation in EHBP1",
"description": ""
},
{
"id": "MONDO:0012741",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012741",
"name": "prostate cancer, hereditary, 12",
"description": ""
},
{
"id": "MONDO:0012741",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012741",
"name": "prostate cancer, hereditary, type 12",
"description": ""
},
{
"id": "MONDO:0012741",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012741",
"name": "HPC12",
"description": ""
},
{
"id": "MONDO:0012244",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012244",
"name": "prostate cancer, hereditary, 5",
"description": ""
},
{
"id": "MONDO:0012244",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012244",
"name": "prostate cancer, hereditary, 5",
"description": ""
},
{
"id": "MONDO:0012244",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012244",
"name": "prostate cancer, hereditary, type 5",
"description": ""
},
{
"id": "MONDO:0012244",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012244",
"name": "HPC5",
"description": ""
},
{
"id": "MONDO:0012093",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012093",
"name": "prostate cancer, hereditary, 3",
"description": ""
},
{
"id": "MONDO:0012093",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012093",
"name": "prostate cancer, hereditary, 3",
"description": ""
},
{
"id": "MONDO:0012093",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012093",
"name": "prostate cancer, hereditary, type 3",
"description": ""
},
{
"id": "MONDO:0012093",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012093",
"name": "prostate cancer, susceptibility to, 3",
"description": ""
},
{
"id": "MONDO:0012093",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012093",
"name": "HPC3",
"description": ""
},
{
"id": "MONDO:0012094",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012094",
"name": "prostate cancer, hereditary, 4",
"description": ""
},
{
"id": "MONDO:0012094",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012094",
"name": "prostate cancer, hereditary, 4",
"description": ""
},
{
"id": "MONDO:0012094",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012094",
"name": "prostate cancer, hereditary, type 4",
"description": ""
},
{
"id": "MONDO:0012094",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012094",
"name": "prostate cancer, susceptibility to, 4",
"description": ""
},
{
"id": "MONDO:0012094",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012094",
"name": "HPC4",
"description": ""
},
{
"id": "MONDO:0012094",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012094",
"name": "prostate cancer, hereditary, on chromosome 7",
"description": ""
},
{
"id": "MONDO:0012758",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012758",
"name": "prostate cancer, hereditary, 13",
"description": "Any familial prostate cancer in which the cause of the disease is a mutation in the MSMB gene."
},
{
"id": "MONDO:0012758",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012758",
"name": "MSMB familial prostate cancer",
"description": ""
},
{
"id": "MONDO:0012758",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012758",
"name": "familial prostate cancer caused by mutation in MSMB",
"description": ""
},
{
"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": "P06239",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P06239"
}
],
"disease": [
{
"disease_id": "DOID:10534",
"recommended_name": {
"id": "DOID:10534",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:10534",
"name": "stomach cancer",
"description": "A gastrointestinal system cancer that is located_in the stomach."
},
"synonyms": [
{
"id": "DOID:10534",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:10534",
"name": "gastric cancer",
"description": ""
},
{
"id": "DOID:10534",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:10534",
"name": "gastric neoplasm",
"description": ""
},
{
"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": "No",
"trend": "down",
"name": "Urinary bladder cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:11054",
"evidence": [
{
"database": "BioXpress",
"id": "P06239",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P06239"
}
],
"disease": [
{
"disease_id": "DOID:11054",
"recommended_name": {
"id": "DOID:11054",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:11054",
"name": "urinary bladder cancer",
"description": "An urinary system cancer that results_in malignant growth located_in the urinary bladder."
},
"synonyms": [
{
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"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:11054",
"name": "bladder cancer",
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},
{
"id": "DOID:11054",
"resource": "Disease Ontology",
"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",
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},
{
"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",
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},
{
"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": "Yes",
"trend": "up",
"name": "Head and neck cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:11934",
"evidence": [
{
"database": "BioXpress",
"id": "P06239",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P06239"
}
],
"disease": [
{
"disease_id": "DOID:11934",
"recommended_name": {
"id": "DOID:11934",
"resource": "Disease Ontology",
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"name": "head and neck cancer",
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},
"synonyms": [
{
"id": "DOID:11934",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:11934",
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},
{
"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",
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},
{
"id": "DOID:11934",
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}
]
}
]
},
{
"significant": "No",
"trend": "down",
"name": "Lung cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:1324",
"evidence": [
{
"database": "BioXpress",
"id": "P06239",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P06239"
}
],
"disease": [
{
"disease_id": "DOID:1324",
"recommended_name": {
"id": "DOID:1324",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1324",
"name": "lung cancer",
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},
"synonyms": [
{
"id": "MONDO:0012159",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012159",
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"description": ""
},
{
"id": "MONDO:0012159",
"resource": "MONDO",
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"description": ""
},
{
"id": "MONDO:0012159",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012159",
"name": "lung cancer susceptibility",
"description": ""
},
{
"id": "MONDO:0012159",
"resource": "MONDO",
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"name": "lung cancer susceptibility 1",
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},
{
"id": "MONDO:0012942",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0012942",
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},
{
"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",
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"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",
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},
{
"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",
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"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",
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"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",
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"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",
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},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "nonsmall cell lung cancer, susceptibility to, autosomal dominant, somatic mutation",
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},
{
"id": "MONDO:0008903",
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"url": "https://monarchinitiative.org/disease/MONDO:0008903",
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"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",
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},
{
"id": "MIM:211980",
"resource": "MIM",
"url": "https://www.omim.org/entry/211980",
"name": "Lung cancer",
"description": "Lung cancer"
}
]
}
]
},
{
"significant": "Yes",
"trend": "up",
"name": "Breast cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:1612",
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}
],
"disease": [
{
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},
"synonyms": [
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},
{
"id": "DOID:1612",
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},
{
"id": "DOID:1612",
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},
{
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
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},
{
"id": "DOID:1612",
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},
{
"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",
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"name": "familial cancer of breast",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "familial cancer of the breast",
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},
{
"id": "MONDO:0016419",
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},
{
"id": "MONDO:0016419",
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},
{
"id": "MONDO:0016419",
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"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": "P06239",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P06239"
}
],
"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": "up",
"name": "Kidney cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:263",
"evidence": [
{
"database": "BioXpress",
"id": "P06239",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P06239"
}
],
"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": "No",
"trend": "down",
"name": "Liver cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:3571",
"evidence": [
{
"database": "BioXpress",
"id": "P06239",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P06239"
}
],
"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": "up",
"name": "Uterine cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:363",
"evidence": [
{
"database": "BioXpress",
"id": "P06239",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P06239"
}
],
"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": ""
}
]
}
]
},
{
"significant": "Yes",
"trend": "up",
"name": "Esophageal cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:5041",
"evidence": [
{
"database": "BioXpress",
"id": "P06239",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P06239"
}
],
"disease": [
{
"disease_id": "DOID:5041",
"recommended_name": {
"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": [
{
"id": "DOID:5041",
"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",
"url": "http://disease-ontology.org/term/DOID:5041",
"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",
"resource": "MONDO",
"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",
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"name": "malignant tumor of proximal third of esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
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"name": "malignant tumor of the middle third of the esophagus",
"description": ""
},
{
"id": "MONDO:0007576",
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"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"
}
]
}
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},
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"url": "https://www.uniprot.org/uniprot/P06239"
}
],
"pmid": ""
},
{
"name": "protein kinase binding",
"id": "GO:0019901",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019901",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
}
],
"pmid": ""
},
{
"name": "identical protein binding",
"id": "GO:0042802",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042802",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
}
],
"pmid": ""
},
{
"name": "ATPase binding",
"id": "GO:0051117",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051117",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
}
],
"pmid": ""
},
{
"name": "protein serine/threonine phosphatase activity",
"id": "GO:0004722",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004722",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
}
],
"pmid": ""
},
{
"name": "CD4 receptor binding",
"id": "GO:0042609",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042609",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
}
],
"pmid": ""
},
{
"name": "SH2 domain binding",
"id": "GO:0042169",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042169",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
}
],
"pmid": ""
},
{
"name": "T cell receptor binding",
"id": "GO:0042608",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042608",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
}
],
"pmid": ""
},
{
"name": "protein phosphatase binding",
"id": "GO:0019903",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019903",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
}
],
"pmid": ""
},
{
"name": "phospholipase activator activity",
"id": "GO:0016004",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0016004",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
}
],
"pmid": ""
},
{
"name": "phospholipase binding",
"id": "GO:0043274",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043274",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
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}
],
"pmid": ""
},
{
"name": "CD8 receptor binding",
"id": "GO:0042610",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042610",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
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}
],
"pmid": ""
},
{
"name": "phosphatidylinositol 3-kinase binding",
"id": "GO:0043548",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043548",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
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}
],
"pmid": ""
}
]
},
{
"name": "Biological Process",
"total": 25,
"go_terms": [
{
"name": "phosphorylation",
"id": "GO:0016310",
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{
"database": "UniProtKB",
"id": "P06239",
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}
],
"pmid": ""
},
{
"name": "Fc-gamma receptor signaling pathway",
"id": "GO:0038094",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0038094",
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{
"database": "UniProtKB",
"id": "P06239",
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}
],
"pmid": ""
},
{
"name": "protein phosphorylation",
"id": "GO:0006468",
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"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
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}
],
"pmid": ""
},
{
"name": "transmembrane receptor protein tyrosine kinase signaling pathway",
"id": "GO:0007169",
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{
"database": "UniProtKB",
"id": "P06239",
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],
"pmid": ""
},
{
"name": "peptidyl-tyrosine phosphorylation",
"id": "GO:0018108",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0018108",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
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}
],
"pmid": ""
},
{
"name": "intracellular signal transduction",
"id": "GO:0035556",
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"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
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],
"pmid": ""
},
{
"name": "peptidyl-tyrosine autophosphorylation",
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{
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"id": "P06239",
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}
],
"pmid": ""
},
{
"name": "innate immune response",
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{
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],
"pmid": ""
},
{
"name": "T cell costimulation",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0031295",
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{
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"id": "P06239",
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],
"pmid": ""
},
{
"name": "T cell receptor signaling pathway",
"id": "GO:0050852",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050852",
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{
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"id": "P06239",
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],
"pmid": ""
},
{
"name": "activation of cysteine-type endopeptidase activity involved in apoptotic process",
"id": "GO:0006919",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006919",
"evidence": [
{
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"id": "P06239",
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],
"pmid": ""
},
{
"name": "platelet activation",
"id": "GO:0030168",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030168",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
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],
"pmid": ""
},
{
"name": "positive regulation of T cell receptor signaling pathway",
"id": "GO:0050862",
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{
"database": "UniProtKB",
"id": "P06239",
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],
"pmid": ""
},
{
"name": "B cell receptor signaling pathway",
"id": "GO:0050853",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050853",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
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],
"pmid": ""
},
{
"name": "leukocyte migration",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050900",
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{
"database": "UniProtKB",
"id": "P06239",
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],
"pmid": ""
},
{
"name": "release of sequestered calcium ion into cytosol",
"id": "GO:0051209",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051209",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
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}
],
"pmid": ""
},
{
"name": "hemopoiesis",
"id": "GO:0030097",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030097",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
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],
"pmid": ""
},
{
"name": "positive regulation of intrinsic apoptotic signaling pathway",
"id": "GO:2001244",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:2001244",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
}
],
"pmid": ""
},
{
"name": "response to xenobiotic stimulus",
"id": "GO:0009410",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0009410",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
}
],
"pmid": ""
},
{
"name": "positive regulation of T cell activation",
"id": "GO:0050870",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050870",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
}
],
"pmid": ""
},
{
"name": "intracellular zinc ion homeostasis",
"id": "GO:0006882",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006882",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
}
],
"pmid": ""
},
{
"name": "T cell differentiation",
"id": "GO:0030217",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030217",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
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}
],
"pmid": ""
},
{
"name": "positive regulation of heterotypic cell-cell adhesion",
"id": "GO:0034116",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0034116",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
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],
"pmid": ""
},
{
"name": "regulation of lymphocyte activation",
"id": "GO:0051249",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051249",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
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}
],
"pmid": ""
},
{
"name": "positive regulation of leukocyte cell-cell adhesion",
"id": "GO:1903039",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:1903039",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
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],
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]
}
]
},
"pro_annotation": [],
"site_annotation": [
{
"start_pos": 131,
"end_pos": 133,
"annotation": "n_glycosylation_sequon"
},
{
"start_pos": 211,
"end_pos": 213,
"annotation": "n_glycosylation_sequon"
},
{
"start_pos": 321,
"end_pos": 323,
"annotation": "n_glycosylation_sequon"
},
{
"start_pos": 40,
"end_pos": 42,
"annotation": "n_glycosylation_sequon"
}
],
"ptm_annotation": [
{
"annotation": "Autophosphorylated on Tyr-394, increasing enzymatic activity, this site is dephosphorylated by PTN22. Phosphorylated on Tyr-505 by CSK, decreasing activity. Dephosphorylated by PTPRC/CD45. Dephosphorylation at Tyr-394 by PTPN2 negatively regulates T-cell receptor signaling.",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
},
{
"database": "PubMed",
"id": "8631775",
"url": "https://glygen.org/publication/PubMed/8631775"
},
{
"database": "PubMed",
"id": "1639064",
"url": "https://glygen.org/publication/PubMed/1639064"
},
{
"database": "PubMed",
"id": "8139546",
"url": "https://glygen.org/publication/PubMed/8139546"
},
{
"database": "PubMed",
"id": "22080863",
"url": "https://glygen.org/publication/PubMed/22080863"
}
]
},
{
"annotation": "Palmitoylation regulates association with the plasma membrane and could be mediated by ZDHHC2.",
"evidence": [
{
"database": "UniProtKB",
"id": "P06239",
"url": "https://www.uniprot.org/uniprot/P06239"
},
{
"database": "PubMed",
"id": "22034844",
"url": "https://glygen.org/publication/PubMed/22034844"
}
]
}
],
"interactions": [],
"reactions": [
{
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"name": "",
"equation": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]",
"summary": "",
"cellular_location": "",
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"Q03137-1",
"Q60751-1",
"Q62137-1",
"P28867-1",
"P25911-1",
"P48025-1",
"Q9WTL4-1",
"P41242-1",
"P05532-1",
"P06240-1",
"P08103-1",
"P15208-1",
"Q03526-1",
"Q9WVS7-1",
"P70236-1",
"P31938-1",
"P47809-1",
"Q61846-1",
"Q60805-1",
"Q63932-1",
"O09110-1",
"P26618-1",
"Q8CE90-1",
"P16056-1",
"P05622-1",
"P15209-1",
"Q6VNS1-1",
"Q61006-1",
"Q3UFB7-1",
"Q5RJI4-1",
"Q9JJ78-1",
"P58801-1",
"Q8VCT9-1",
"O70146-1",
"Q62190-1",
"Q62270-1",
"P35546-1",
"P35761-1",
"Q9Z138-1",
"Q9R117-1",
"O88697-1",
"P05480-2",
"Q01887-1",
"Q02858-1",
"Q06806-1",
"Q00993-1",
"Q64434-1",
"Q6J9G1-1",
"Q99ML2-1",
"Q78DX7-1",
"P55144-1",
"P43404-1",
"P35917-1",
"P47810-1",
"P35918-1",
"Q04736-1",
"Q66JT0-1",
"O54804-1",
"P52480-1",
"P14680-1",
"P21965-1",
"P22216-1",
"P32490-1",
"P06784-1",
"P08018-1",
"P32350-1",
"P32491-1",
"P54199-1",
"Q54G28-1",
"Q54N73-1",
"Q54R58-1",
"P18160-1",
"P18161-1",
"Q54BC9-1",
"Q54I36-1",
"Q54QV3-1",
"Q552C6-1",
"Q55CL6-1",
"Q75JK0-1",
"Q76NV1-1",
"Q23977-1",
"P18475-1",
"P13368-1",
"Q24145-1",
"Q24488-1",
"Q27324-1",
"P08630-1",
"P00522-1",
"P00528-1",
"P04412-1",
"Q9V422-1",
"Q9V6K3-1",
"Q9V9J3-1",
"Q9VBW3-1",
"P09208-1",
"P49762-1",
"P83102-1",
"Q24324-1",
"Q9VPC0-1",
"P49657-1",
"P54350-1",
"P18106-4",
"Q07407-1",
"Q09147-1",
"Q24592-1",
"Q9I7F7-1",
"Q9V3D5-1",
"Q9VZI2-1",
"Q8INJ8-1",
"Q7KJ08-1",
"Q9VJ04-1",
"E1JHB7-1",
"Q9VE06-1",
"O61444-1",
"O62602-1",
"Q9VZA8-1",
"Q7KT06-1"
],
"evidence": [
{
"id": "10596",
"database": "Rhea",
"url": "https://www.rhea-db.org/rhea/10596"
}
]
},
{
"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-1433428",
"name": "GRB2 is indirectly recruited to p-KIT through SHP2",
"equation": "",
"summary": "GRB2 can be recruited indirectly to KIT through SHP2 (Tauchi et al. 1994). Y279, Y304, Y546 and Y584 (usually referred to as Y542 and Y580 in literature based on the SHP2 short isoform) are the potential sites of SHP2 tyrosyl phosphorylation and that Y546 is the major GRB2 binding site (Feng, et al. 1993, Araki, et al. 2003). This brings Grb2:SOS1 into proximity with the plasma membrane, where it can activate Ras.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1",
"Q06124-2"
],
"evidence": [
{
"id": "R-HSA-1433428",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1433428"
}
]
},
{
"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-1433454",
"name": "Phosphorylation of GAB2 by SFKs",
"equation": "",
"summary": "GAB2 bound to GRB2 on KIT is then phosphorylated on a number of tyrosine residues through the action of Src family kinases (SFKs).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1",
"Q06124-2"
],
"evidence": [
{
"id": "R-HSA-1433454",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1433454"
}
]
},
{
"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-1433488",
"name": "Phosphorylation of SHP2 by SFKs",
"equation": "",
"summary": "Following association with KIT, Tauchi et al. had observed phosphorylation of SHP2 (Tauchi et al. 1994). Tyrosine residues Y546 and Y584 (usually referred to as Y542 and Y580 in literature based on the short isoform) are the major sites of SHP2 tyrosyl phosphorylation. Src family kinases (SFKs) are candidates for this phosphorylation (Araki et al. 2003). The phosphorylated tyrosine residues on SHP2 can recruit the adapter protein GRB2 (Tauchi et al. 1994), but it is unclear whether GRB2 binding to SHP2 is important for KIT mediated SHP2 signaling or whether the effect of SHP2 on the RAS/ERK pathway goes through its catalytic activity.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1",
"Q06124-2"
],
"evidence": [
{
"id": "R-HSA-1433488",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1433488"
}
]
},
{
"id": "R-HSA-1433506",
"name": "Phosphorylation of APS",
"equation": "",
"summary": "APS bound to KIT is phosphorylated by tyrosine kinases in response to SCF stimulation (Wollberg et al, 2003). The C-terminal tyrosine 629 may be the target site of phosphorylation in APS (Wakioka et al, 1999).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-1433506",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1433506"
}
]
},
{
"id": "R-HSA-1433514",
"name": "Synthesis of PIP3 from PIP2 by PI3K",
"equation": "",
"summary": "PI3 kinases catalyze the production of phosphatidylinositol-3, 4, 5-triphosphate (PIP3) by phosphorylating phosphatidylinositol-4, 5-bisphosphate (PIP2). PIP3 bound to the inner lipid bilayer of the plasma membrane promotes the recruitment and activation of AKT. Active AKT subsequently phosphorylates the pro-apoptotic factor BAD at Ser136. Phosphorylated BAD binds 14-3-3 proteins, sequestering BAD from interaction with the anti-apoptotic molecule BCL-XL and leaving BCL-Xl free to inhibit BAX-triggered apoptosis. In this way, AKT-mediated BAD phosphorylation promotes cell survival. The alternative route for c-Kit mediated survival is through AKT-mediated phosphorylation and inactivation of the forkhead transcription factor (FoxO3a) (Engstrom et al, 2003; Lennartson et al, 2005).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1",
"Q06124-2"
],
"evidence": [
{
"id": "R-HSA-1433514",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1433514"
}
]
},
{
"id": "R-HSA-1433542",
"name": "Phosphorylation and activation of VAV1",
"equation": "",
"summary": "The Src and PI3-kinase signaling pathways converge to activate Rac1 and JNK after c-Kit activation, promoting mast cell proliferation but not for suppression of apoptosis (Timokhina et al. 1998). PI3K and Src are considered mediators of c-Kit induced Rac1 activation via the guanine nucleotide exchange factor (GEF) VAV1. Stimulation of c-Kit receptor results in rapid tyrosine phosphorylation of VAV1 (Timokhina et al. 1998).
VAV1 exists in an auto-inhibitory state folded in such a way as to inhibit the GEF activity of its Dbl homology domain (DH) domain. PI3K is thought to modulate the activation of VAV1 by influencing its degree of tyrosine phosphorylation and its recruitment to membrane. VAV1 is recruited to membrane by binding to PtdIns(3,4,5)P3 (PIP3) and this interaction relieves an intramolecular interaction between pleckstrin homology (PH) and DH domains, thus facilitating tyrosine phosphorylation on Y174 and so further opening of the DH/PH domains, binding of Rac-GDP and catalysis (Welch et al, 2003). In VAV1, tyrosine 174 (Y174) binds to the DH domain and inhibits its GEF activity. Src kinases phosphorylate this Y174 and this causes the tyrosine to move away from the DH domain thereby reliving the auto-inhibition.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [
"R-HSA-195066"
],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-1433542",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1433542"
}
]
},
{
"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-1472121",
"name": "Phosphorylation of p-KIT on Y900 by Src kinases",
"equation": "",
"summary": "Src family of tyrosine kinases phosphorylate KIT on Y900 located in the second part of the tyrosine kinase domain. This phosphorylated tyrosine acts as a docking site for p85alpha regulatory subunit of PI3K and the adapter protein CRKII. CRKII does not interact directly with KIT but is recruited indirectly by binding to p85alpha subunit of PI3K. Thus, in this case the p85 subunit acts as an adapter between KIT and CRKII, and not to recruit PI3-kinase. (Lennartsson et al. 2003).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-1472121",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1472121"
}
]
},
{
"id": "R-HSA-1562641",
"name": "Indirect recruitment of PI3K to KIT via p(Y)-GAB2",
"equation": "",
"summary": "Phosphorylated GAB2 recruits the p85 subunit of the PI3K complex and activates the PI3K/AKT pathway. This is one of two mechanisms described for the recruitment of PI3K to KIT.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1",
"Q06124-2"
],
"evidence": [
{
"id": "R-HSA-1562641",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1562641"
}
]
},
{
"id": "R-HSA-167566",
"name": "Nef mediated disruption of CD4:Lck Complex",
"equation": "",
"summary": "Nef disrupts the CD4 Lck complex",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-167609"
],
"enzyme_list": [
"P06239-1"
],
"evidence": [
{
"id": "R-HSA-167566",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-167566"
}
]
},
{
"id": "R-HSA-200954",
"name": "Nef Binds and activates the Src-family tyrosine kinase Lck",
"equation": "",
"summary": "The Nef protein of the primate lentiviruses, including human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV), is a myristylated protein associated with increased viral replication and enhanced pathogenicity. Both the potentiation of T-lymphocyte activation and the enhanced serine-phosphorylation of HIV-1 capsid by Nef correlate with increased viral replication. The Nef proteins from HIV-1 and SIV bind to Lck. The SH3 and SH2 domains of Lck are sufficient for coprecipitation with non-tyrosine-phosphorylated Nef proteins. The conserved core region of HIV-1 Nef is essential for the interaction with Lck and is also important for enhanced HIV-1 replication in T-lymphocytes. The SIV and HIV-1 Nef proteins are differentially tyrosine-phosphorylated. The kinase-active Lck tyrosine-phosphorylates SIVmac239 Nef but does not phosphorylate HIV-1 Nef.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06239-1"
],
"evidence": [
{
"id": "R-HSA-200954",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-200954"
}
]
},
{
"id": "R-HSA-202165",
"name": "Phosphorylation of ITAM motifs in CD3 complexes",
"equation": "",
"summary": "The autophosphorylated, active Lck is now proximally positioned to phosphorylate specific tyrosine residues within ITAMs (immunoreceptor tyrosine-based activation motifs) located within the CD3 and the TCR zeta signaling chains of the TCR. ITAMs consist of evolutionarily conserved amino-acid sequence motifs of D/ExYxxLx(6-8)YxxL. Both the tyrosine residues in the motif are phosphorylated by Lck and the TCR complex include 10 ITAMs with one ITAM in each of the CD3 chains including the three tandem ITAMs in each zeta chains.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06239-1"
],
"evidence": [
{
"id": "R-HSA-202165",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-202165"
}
]
},
{
"id": "R-HSA-202168",
"name": "Phosphorylation of ZAP-70 by Lck",
"equation": "",
"summary": "In ZAP-70 there are multiple phosphorylation sites (Y292, Y315, Y319, Y492, Y493) which have both positive and negative regulatory effect on its catalytic activity. Tyrosine 493 is a conserved regulatory site found within the activation loop of the kinase domain. This site has shown to be a positive regulatory site required for ZAP-70 kinase activity and is phosphorylated by Lck. This phosphorylation contribute to the active conformation of the catalytic domain.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06239-1",
"P43403-1"
],
"evidence": [
{
"id": "R-HSA-202168",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-202168"
}
]
},
{
"id": "R-HSA-202174",
"name": "Activation of ZAP-70",
"equation": "",
"summary": "Later ZAP-70 undergoes trans-autophosphorylation at Y315 and Y319. These sites appear to be positive regulatory sites. ZAP-70 achieve its full activation after the trans-autophosphorylation. Activated ZAP-70 phosphorylates T-cell-specific adaptors, such as LAT and SLP-76 leading to the recruitment and activation of other kinase families and enzymes, resulting in secondary messenger generation and culminating in T cell activation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06239-1",
"P43403-1"
],
"evidence": [
{
"id": "R-HSA-202174",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-202174"
}
]
},
{
"id": "R-HSA-202214",
"name": "Dephosphorylation of Lck-pY505 by CD45",
"equation": "",
"summary": "TCR stimulation induce the transient dephosphorylation of PAG thereby release the Csk from its plasma membrane anchor. The release of Csk from its proximity with Lck may serve to facilitate the activation of Lck.Protein tyrosine phosphtase CD45 (PTPRC) and CD148 (PTPRJ) have dual function in TCR signalling. They act both in activation as well as inactivation of Src family kinases (SFKs) which are involved in the initiation of TCR signal transduction (Stepanek et al. 2011). The activatory role is to dephosphorylate an inhibitory site tyrosine 505 (Y505) at the C-terminal end of Lck, which is needed to enable Lck to an open conformation and expose the activation loop (A-loop) containing the activating tyrosine 394 (Y394) (Xu et al. 1993. McNeill et al. 2007, Zikherman et al. 2010, Stepanek et al. 2011, Salmond et al. 2009).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08575-3",
"P06239-1",
"Q12913-1"
],
"evidence": [
{
"id": "R-HSA-202214",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-202214"
}
]
},
{
"id": "R-HSA-202216",
"name": "Phosphorylation of SLP-76",
"equation": "",
"summary": "Once SLP-76 is recruited to Gads its rapidly phosphorylated on the tyrosine residues in the N-terminal acidic domain. This domain contains three tyrosine phosphorylation sites, Y113, Y128 and Y145. These tyrosine residues are phosphorylated by tyrosine kinase ZAP-70 and these phosphorylated tyrosine residues provide the binding site for the SH2 domains of the incoming signaling proteins like Vav, Itk and PLC-gamma1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06239-1",
"P43403-1"
],
"evidence": [
{
"id": "R-HSA-202216",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-202216"
}
]
},
{
"id": "R-HSA-202233",
"name": "Inactivation of Lck by Csk",
"equation": "",
"summary": "Lck is a member of the Src family tyrosine kinases and these members have the following domains in common: N-terminal Myristoylation site for saturated fatty acid addition, a unique region, a Src-homology 3 (SH3) domain, an SH2 domain, a tyrosine kinase domain (SH1), and a C-terminal negative regulatory domain. Myristoylation engenders Lck with the ability to attach to cellular membranes. This interaction is mediated by both myristic acid and palmitic acid that are bound to the amino terminal glycine and Cys-3 and/or Cys-5.
The unique region of Lck is thought to be involved in the interaction with the cytoplasmic tails of coreceptors CD4 and CD8. The Lck/CD4 interaction require conserved cysteine motifs: a CxCP motif in CD4 and a CxxC motif in the Lck unique domain. The SH3 and SH2 domains of Lck are involved in intramolecular and intermolecular regulation by mediating protein-protein interactions via poly-proline and phosphotyrosine-specific interactions, respectively.
Lck adopts specific conformation that largely dictate its level of activity. The C-ter tail has an autoinhibitory phosphorylation site (tyr 505). When the Y505 is phosphorylated, Lck adopts a closed conformation, where the pY505 residue creates an intramolecular binding motif for the SH2 domain, effectively inactivating the kinase domain. The inactivating phosphorylation on Y505 is carried out by the Src-specific kinase Csk.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P08575-3",
"P41240-1",
"P06239-1",
"Q12913-1"
],
"evidence": [
{
"id": "R-HSA-202233",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-202233"
}
]
},
{
"id": "R-HSA-202245",
"name": "Phosphorylation of TBSMs in LAT",
"equation": "",
"summary": "The adaptor molecule LAT (Linker for the Activation of T cells) is a membrane protein that links the TCR signal to the cell activation. It has a total 10 (Y36, Y45, Y64, Y110, Y156, Y161, Y200, Y220, and Y255) conserved TBSMs (tyrosine based signaling motifs) in its cytoplasmic region. These tyrosine residues are phosphorylated by the activated ZAP-70 upon TCR/CD3 complex engagement. Phosphorylation of LAT creates binding sites for the Src homology 2 (SH2) domains of other proteins, including PLC-gamma1, Grb2 and Gads, and indirectly binds SOS, Vav, SLP-76, and Itk. The residues Y200, Y220 and Y255 are responsible for Grb2 binding, Y200 and Y220 but not Y255, are necessary for Gads binding and Y161 for the PLC-gamma1 binding (numbering based on Uniprot isoform 1).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-202364"
],
"enzyme_list": [
"P06239-1",
"P43403-1"
],
"evidence": [
{
"id": "R-HSA-202245",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-202245"
}
]
},
{
"id": "R-HSA-202248",
"name": "Phosphorylation of PLC-gamma1",
"equation": "",
"summary": "Three tyrosine residues at positions 771, 783 and 1254 in PLC-gamma1 have been identified as the sites of receptor tyrosine kinase phosphorylation. Of these Y783 and Y1254 are required for activation of PLC-gamma1. The phosphorylation of the tyrosine residues and the activation of PLC-gamma1 is mediated by both Syk tyrosine kinase ZAP-70 and Tec kinase ITK.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P19174-1",
"P06239-1",
"P43403-1",
"Q08881-1"
],
"evidence": [
{
"id": "R-HSA-202248",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-202248"
}
]
},
{
"id": "R-HSA-202291",
"name": "Activation of Lck",
"equation": "",
"summary": "The binding of CD4/CD8 to non-polymorphic regions of MHC brings Lck in to proximity with TCR subunits phosphorylation. Lck is further phosphorylated to promote the active conformation and to increase their catalytic activity. The C-term domain contain a regulatory activation loop, which is the site of activating Tyr 394 phosphorylation. This tyrosine is auto-phosphorylated to attain an active conformation on TCR stimulation. Now Lck through its kinase activity phosphorylates the ITAMs in TCR zeta and CD3 members.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06239-1"
],
"evidence": [
{
"id": "R-HSA-202291",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-202291"
}
]
},
{
"id": "R-HSA-202307",
"name": "Change of PKC theta conformation",
"equation": "",
"summary": "PKC theta localizes at the interface between T cells and antigen presenting cells. Upon the T cell activation and release of the second messengers Ca++ and DAG by PLC-gamma1, DAG binds to the C1 domain of the PKC theta thereby enhances the attachment to the plasma membrane. Upon membrane translocation, PKC theta is phosphorylated at tyrosine 90 in the C2 like domain. This phosphorylation is mediated by the tyrosine kinase Lck. These association and, most likely, other regulatory interactions, lead to a change in PKC theta conformation into an open, active state whereby it can now access its substrates and phosphorylate them.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06239-1",
"Q04759-1"
],
"evidence": [
{
"id": "R-HSA-202307",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-202307"
}
]
},
{
"id": "R-HSA-202344",
"name": "Recruitment of ZAP-70 to phosphorylated ITAMs",
"equation": "",
"summary": "Phosphorylation of the ITAMs by Lck is followed by the recruitment of the ZAP-70 a member of Syk family PTK, to the receptor complex. ZAP-70 is exclusively expressed in T cells and NK cells. The dually phosphorylated ITAMs provide a high-affinity docking site for the tandem SH2-domains of the ZAP-70. Once recruited, ZAP-70 is activated by phosphorylation and will be responsible for the phosphorylation of further downstream molecules. Due to the presence of 10 ITAMs in the TCR complex, up to 10 ZAP-70 molecules may cluster on the fully phosphorylated receptors.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06239-1",
"P43403-1"
],
"evidence": [
{
"id": "R-HSA-202344",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-202344"
}
]
},
{
"id": "R-HSA-205205",
"name": "Interaction of Src family kinases with p-KIT",
"equation": "",
"summary": "Binding of SCF to KIT induces the activation and rapid increase in kinase activity of multiple Src family kinases (SFK), including Src, Lck, Tec, Fyn, and Lyn (Timokhina et al. 1998, Krystal et al. 1998, Linnekin et al. 1997, Lennartsson et al. 1999, Tang et al. 1994, Samayawardhena et al. 2007). The tyrosine residues Y568 and Y570 in KIT juxtamembrane region are involved in the association of SFKs (Price et al. 1997).
SFKs recruited to KIT induce proliferation and chemotaxis in primary hematopoietic progenitor cells or bone marrow derived mast cells (O'Laughlin-Bunner et al. 2001). SCF activated SFKs also mediate a critical signal for lymphocyte development (Agosti et al. 2004). Timokhina et al. demonstrated that Src kinase and PI3-kinase signaling pathways converge to activate Rac1 and JNK after SCF stimulation in BMMC, promoting cell proliferation (Timokhina et al., 1998, Reber et al. 2006 ).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-205205",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-205205"
}
]
},
{
"id": "R-HSA-205234",
"name": "Indirect recruitment of GAB2 to p-KIT",
"equation": "",
"summary": "The scaffolding adapter GAB2 plays a role in KIT dependent PI3K/AKT activation. GAB2 interacts with KIT indirectly via the adapter protein GRB2 which is bound to KIT on phosphorylated Y703 and Y936 (Sun et al. 2008, Yu et al. 2006).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1",
"Q06124-2"
],
"evidence": [
{
"id": "R-HSA-205234",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-205234"
}
]
},
{
"id": "R-HSA-205238",
"name": "SHP2 interacts with p-KIT",
"equation": "",
"summary": "SHP2 is a protein tyrosine phosphatase (PTP) with two NH2-terminal SH2 domains, a PTP domain, a -COOH tail with two tyrosyl phosphorylation sites at Y546 and Y584, and an interposed proline-rich domain. SHP2 binds to activated KIT on tyrosine-568 in the juxtamembrane region, which also constitutes the docking site for a number of other signal transduction molecules, such as SFKs, Csk homologous kinase (CHK), CBL, LNK and Adapter protein with PH and SH2 domains (APS) (Kozlowski et al. 1998, Price et al. 1997, Gueller et al. 2008).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1",
"Q06124-2"
],
"evidence": [
{
"id": "R-HSA-205238",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-205238"
}
]
},
{
"id": "R-HSA-205244",
"name": "Recruitment of CBL to KIT",
"equation": "",
"summary": "The phosphotyrosine residue in APS creates a putative binding site for CBL. CBL is an ubiquitin E3 ligase that attaches ubiquitin to KIT leading to KIT's ubiquitination followed by internalization and degradation. GRB2 in addition to its role in positive signaling via RAS/ERK pathway also mediates negative regulation of KIT by recruiting CBL (Sun et al, 2007). CBL has also been shown to bind directly to both Y568 and Y936 in KIT (Masson et al. 2006). CBL bound to KIT ubiquitinates KIT and targets it to lysosomal degradation (Masson et al. 2006)",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P10721-1",
"P22681-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-205244",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-205244"
}
]
},
{
"id": "R-HSA-205319",
"name": "Interaction of APS and p-KIT",
"equation": "",
"summary": "APS adapter protein has been identified as a KIT binding partner using yeast two-hybrid screening. APS contains a PH domain and an SH2 domain. The SH2 domain interacts with c-Kit phosphotyrosine residues Y568 and Y936 (Wollberg et al. 2003).",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-205319",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-205319"
}
]
},
{
"id": "R-HSA-210289",
"name": "Recruitment of SYK to p-DAP12",
"equation": "",
"summary": "Phosphorylated ITAM on DAP12 serves as the docking site for the two SH2 domains of SYK or ZAP70. Binding leads to SYK activation (Lanier et al. 1998, McVicar et al. 1998).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P06239-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-210289",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-210289"
}
]
},
{
"id": "R-HSA-210291",
"name": "Phosphorylation of PECAM-1 by Fyn or Lyn or c-Src",
"equation": "",
"summary": "PECAM-1 is capable of transmitting information into the cell following its engagement and becomes tyrosine-phosphorylated during the platelet aggregation process. The Src family of tyrosine kinases (more specifically, Src, Lyn, and c-src) has been widely implicated in the phosphorylation of PECAM-1. Conserved tyrosine residues (Tyr663 and Tyr686) within the PECAM-1 cytoplasmic ITIM motif have been shown to become phosphorylated. Tyrosine phosphorylation of PECAM-1 prompts its association with intracellular signal transduction molecules.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-210291",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-210291"
}
]
},
{
"id": "R-HSA-2316434",
"name": "PI3K phosphorylates PIP2 to PIP3",
"equation": "",
"summary": "A number of different extracellular signals converge on PI3K activation. PI3K can be activated downstream of receptor tyrosine kinases (RTKs) such as FGFR (Ong et al. 2001, Eswarakumar et al. 2005), KIT (Chian et al. 2001, Ronnstrand 2004, Reber et al. 2006), PDGF (Coughlin et al. 1989, Fantl et al. 1992, Heldin et al. 1998), insulin receptor IGF1R (Hadari et al. 1992, Kooijman et al. 1995), and EGFR and its family members (Rodrigues et al. 2000, Jackson et al. 2004, Kainulainen et al. 2000, Junttila et al. 2009). Other proteins, such as CD28 (Pages et al. 1996, Koyasu 2003, Kane and Weiss, 2003) and TRAT1 (Bruyns et al. 1998, Koyasu 2003, Kolsch et al. 2006), can also trigger PI3K activity.
In unstimulated cells, PI3K class IA exists as an inactive heterodimer of a p85 regulatory subunit (encoded by PIK3R1, PIK3R2 or PIK3R3) and a p110 catalytic subunit (encoded by PIK3CA, PIK3CB or PIK3CD). Binding of the iSH2 domain of the p85 regulatory subunit to the ABD and C2 domains of the p110 catalytic subunit both stabilizes p110 and inhibits its catalytic activity. This inhibition is relieved when the SH2 domains of p85 bind phosphorylated tyrosines on activated RTKs or their adaptor proteins. Binding to membrane-associated receptors brings activated PI3K in proximity to its membrane-localized substrate, PIP2 (Mandelker et al. 2009, Burke et al. 2011).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22455-1",
"P16234-1",
"P42336-1",
"Q9NWZ3-1",
"P00533-1",
"P04626-1",
"P06241-1",
"P10721-1",
"P12931-1",
"P63000-1",
"P06239-1",
"Q06124-2",
"Q9Y4K3-1",
"P36888-1",
"P09619-1",
"P42338-1",
"O00329-1",
"P08581-1",
"Q01638-1",
"P51617-1"
],
"evidence": [
{
"id": "R-HSA-2316434",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2316434"
}
]
},
{
"id": "R-HSA-2395412",
"name": "Phosphorylation of SYK",
"equation": "",
"summary": "The binding of SYK to DAP12 induces conformational changes that result in SYK activation. Around ten autophosporylated tyrosine residues have been identified in SYK, regulating activity and serving as docking sites for other proteins. Sites include Y131 of interdomain A, Y323, Y348, and Y352 of interdomain B, Y525 and Y526 within the activation loop of the kinase domain and Y630 in the C-terminus (Zhang et al. 2002, Lupher et al. 1998, Furlong et al. 1997).
SYK is phosphorylated by Src family kinases and this acts as an initiating trigger by generating a few molecules of activated SYK, which then initiate SYK autophosphorylation (Hillal et al. 1997, Castro et al. 2010)",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P06239-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-2395412",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2395412"
}
]
},
{
"id": "R-HSA-2395439",
"name": "Phosphorylation of DAP12",
"equation": "",
"summary": "Crosslinking of receptors associated with DAP12 leads to phosphorylation of tyrosine residues in their cytoplasmic ITAM by SRC family kinases (Turnbull & Colonna 2007). This initiates downstream signaling. FYN and LCK have both been found physically and functionally associated with receptors using DAP12 signaling and have been demonstrated to be involved in DAP12 phosphorylation (Mason et al. 2006).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P06239-1"
],
"evidence": [
{
"id": "R-HSA-2395439",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2395439"
}
]
},
{
"id": "R-HSA-2395801",
"name": "Phosphorylation of LAT by p-SYK",
"equation": "",
"summary": "LAT is palmitoylated and membrane-associated adaptor protein. It rapidly becomes tyrosine-phosphorylated upon receptor engagement. LAT has nine conserved tyrosine residues of which five have been shown to undergo phosphorylation (Y127, Y132, Y171, Y191 and Y226). Src family kinases, SYK and ZAP-70 efficiently phosphorylate LAT on these tyrosine residues (Jiang & Cheng 2007, Paz et al. 2001). Phosphorylation of LAT creates binding sites for the Src homology 2 (SH2) domain proteins PLC-gamma1, GRB2 and GADS, which indirectly bind SOS, VAV, SLP-76 and ITK (Wange 2000).",
"cellular_location": "plasma membrane",
"input_participant_list": [
"R-HSA-2396548"
],
"output_participant_list": [
"R-HSA-2396597"
],
"enzyme_list": [
"P06241-1",
"P06239-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-2395801",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2395801"
}
]
},
{
"id": "R-HSA-2396594",
"name": "Phosphorylation of SLP-76 by p-SYK",
"equation": "",
"summary": "SLP-76 lacks intrinsic catalytic activity and acts as a scaffold, recruiting other proteins for correct localization during molecular signal transduction (Bogin et al. 2007). Activation of DAP12-associated receptors leads to tyrosine phosphorylation of SLP-76 (Gross et al. 1999). SLP-76 has three potential tyrosine phosphorylation sites within its amino terminus region: Y113, Y128, and Y145. Phosphorylation may be mediated by SYK, analogous to the role of ZAP-70 in phosphorylating T-cell SLP-76 (Bubeck-Wardenberg et al. 1996).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P19174-1",
"P06239-1",
"P16885-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-2396594",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2396594"
}
]
},
{
"id": "R-HSA-2400009",
"name": "PI3K inhibitors block PI3K catalytic activity",
"equation": "",
"summary": "A variety of inhibitors capable of blocking the phosphoinositide kinase activity of PI3K have been developed. These inhibitors display differential selectivity and inhibit kinase activity of their substrates by distinct mechanisms. For example, the first-generation PI3K inhibitor wortmannin (Wymann et al. 1996) covalently and irreversibly binds all classes of PI3K enzymes, as well as other kinases including mTOR, at a residue critical for catalytic activity. Although wortmannin is precluded from in vivo and clinical use due to its toxicity, it has proven to be a useful tool for in vitro laboratory studies. Newer inhibitors, such as BEZ235, are currently being investigated in Phase I clinical trials. BEZ235 is a dual pan-class I PI3K/mTOR inhibitor that blocks kinase activity by binding competitively to the ATP-binding pocket of these enzymes (Serra et al. 2008, Maira et al. 2008). BGT226 (Chang et al. 2011) and XL765 (Prasad et al. 2011) also inhibits both PI3K class I enzymes and mTOR. Other inhibitors in clinical trials, such as BKM120 (Maira et al. 2012), GDC0941 (Folkes et al. 2008, Junttila et al. 2009) and XL147 (Chakrabarty et al. 2012), are specific for class I PI3Ks and exhibit no activity against mTOR. Current research aims to identify isoform-specific PI3K inhibitors. Small molecule inhibitors that selectively inhibit PIK3CA (p110alpha), e.g. PIK-75 and A66, were used to study the role of p110alpha in signaling and growth of tumor cells (Knight et al. 2006, Sun et al. 2010, Jamieson et al. 2011, Utermark et al. 2012). The PIK3CB (p110beta) specific inhibitor TGX221 has been used in in vitro models of vascular injury (Jackson et al. 2005), and the TGX221 derivative KIN-193 has been shown to block AKT activity and tumor growth in mice with p110beta activation or PTEN loss (Ni et al. 2012). CAL-101 is a PIK3CD (p110delta) specific inhibitor that is being clinically investigated as a therapeutic for lymphoid malignancies (Herman et al. 2010). It is hoped that, in the future, more specific inhibitors, such as those targeting selective PI3K isoforms, will provide optimum treatment while minimizing unwanted side effects. For a recent review, please refer to Liu et al. 2009.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P22455-1",
"P16234-1",
"P42336-1",
"P00533-1",
"P04626-1",
"P06241-1",
"P10721-1",
"P12931-1",
"P63000-1",
"P06239-1",
"Q06124-2",
"P36888-1",
"P09619-1",
"P42338-1",
"O00329-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-2400009",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2400009"
}
]
},
{
"id": "R-HSA-2424480",
"name": "PI3K phosphorylates PIP2 to PIP3",
"equation": "",
"summary": "Activated PI3K phosphorylates phosphatidylinositol (PI) 4-phosphate and PI 4,5-bisphosphate (PIP2) to generate PI 3,4-bisphosphate and PI 3,4,5-triphosphate (PIP3) and these second messengers recruit other signaling proteins containing plecstrin homology (PH) domain. Products of PI3K are involved in the regulation of PLC-gamma 1 and VAV activation. The PH domain of PLC-gamma 1 binds to PIP3 and is targeted to the membrane. PIP3 binds to the PH domain of VAV2/VAV3 and increases it activity and PI3K may also strongly stimulate VAV activity by converting an inhibitory regulator VAV to an activator (Toker & Cantley 1997, Fischer et al. 1998, Falasca et al. 1998).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P06241-1",
"P06239-1",
"P43405-1",
"P42338-1"
],
"evidence": [
{
"id": "R-HSA-2424480",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2424480"
}
]
},
{
"id": "R-HSA-2424482",
"name": "p85 regulatory unit of PI3K binds p-6Y-SYK",
"equation": "",
"summary": "Phosphoinositide 3-kinases (PI3Ks) are one of the downstream effectors of activated SYK. The p85 alpha regulatory subunit of PI3K has been shown to interact with SYK phospho-tyrosine Y323. In DAP12 signaling SYK acts via the PI3K-dependent pathway to control NK cell-mediated cytotoxicity. SYK-coupled PI3K is rapidly activated and triggers a sequential activation of VAV2/VA3, RAC1, PAK1, MEK and ERK to mediate NK cell-mediated lysis (Jiang et al. 2002, Moon et al. 2005).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P06241-1",
"P06239-1",
"P43405-1",
"P42338-1"
],
"evidence": [
{
"id": "R-HSA-2424482",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2424482"
}
]
},
{
"id": "R-HSA-2424484",
"name": "Phosphorylation of BTK by p-SYK",
"equation": "",
"summary": "In myeloid cells BTK is phosphorylated on Y551 upon DAP12 activation in a SYK kinase-dependent manner. Y551 is located in the activation loop of BTK, known to be required for activation and kinase activity. Y223 in the SH3 domain of BTK is autophosphorylated, which may also be involved in BTK activation (Ormsby et al. 2010, Rawlings et al. 1996).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P19174-1",
"Q06187-1",
"P06239-1",
"P16885-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-2424484",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2424484"
}
]
},
{
"id": "R-HSA-2424486",
"name": "Phosphorylation and activation of VAV2/VAV3 by SYK",
"equation": "",
"summary": "VAV exists in an auto-inhibitory state, folded in such a way as to inhibit the GEF activity of its DH domain. This folding is mediated through binding of tyrosines in the acidic domain to the DH domain and through binding of the calponin homology (CH) domain to the C1 region. Activation of VAV may involve three events which relieve this auto-inhibition: phosphorylation of tyrosines in the acidic domain causes them to be displaced from the DH domain; binding of a ligand to the CH domain may cause it to release the C1 domain; binding of the PI3K product PIP3 to the PH domain may alter its conformation (Aghazadeh et al. 2000). VAV2/3 are phosphorylated on Y172/Y173 respectively in the acidic domain. This is mediated by SYK and Src-family tyrosine kinases (Deckert et al. 1996, Schuebel et al. 1998). Once activated, VAV2/VAV3 are involved in the activation of RAC1, PAK1, MEK and ERK.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P19174-1",
"Q06187-1",
"P06239-1",
"P16885-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-2424486",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2424486"
}
]
},
{
"id": "R-HSA-2424487",
"name": "Phosphorylation of PLC-gamma by p-BTK/p-SYK",
"equation": "",
"summary": "Three tyrosine residues at positions 771, 783 and 1254 in PLCgamma1 have been identified as the sites of receptor tyrosine kinase phosphorylation. Of these Y783 and Y1254 are required for PLC-gamma1 activation.
In myeloid cells phosphorylation of the tyrosine residues of PLC-gamma1 is mediated by SYK and BTK kinases (Ormsby et al. 2010, Kim et al. 1994, Law et al. 1996, Watanabe et al. 2001).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P19174-1",
"Q06187-1",
"P06239-1",
"P16885-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-2424487",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2424487"
}
]
},
{
"id": "R-HSA-388814",
"name": "Grb2 binds CD28",
"equation": "",
"summary": "CD28 is capable of binding the Src homology 3 (SH3) domains of several proteins, including Grb2. The phospho-YMNM motif in CD28's cytoplasmic domain facilitates tandem SH2\u2013SH3 domain binding. Grb-2 has been shown to bind to the CD28 YMNM motif with additional SH3 domain binding to the diproline motif in the C-terminal portion of the cytoplasmic domain of CD28.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P06239-1"
],
"evidence": [
{
"id": "R-HSA-388814",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-388814"
}
]
},
{
"id": "R-HSA-388829",
"name": "SHP2 phosphatase binds CTLA-4",
"equation": "",
"summary": "CTLA4 associates with the SH2 domain containing tyrosine phosphatase SHP2 and this interaction is mediated through the YVKM motif of CTLA-4. Phosphorylation of tyrosine in the YVKM motif recruits SHP-2.
Still the association of SHP-2 with CTLA-4 is unclear and remains controversial. Several other studies have reported that CTLA-4 does not directly associate with SHP-2. The interaction between the phosphatase and CTLA-4 may be an indirect event, possibly mediated by PI3-kinase/SHP-2 binding.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P06239-1",
"P07947-1",
"P07948-1",
"Q06124-2"
],
"evidence": [
{
"id": "R-HSA-388829",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-388829"
}
]
},
{
"id": "R-HSA-388831",
"name": "Phosphorylation of CD28",
"equation": "",
"summary": "The interaction of CD28 with its ligands, B7-1 (CD80) and B7-2 (CD86) on antigen-presenting cells enhances a number of TCR-mediated responses like production of interleukins. CD28 mediated costimulation is dependent upon phosphorylation of tyrosine residue 191 of the CD28 cytoplasmic tail, present in a 'YMNM' motif. p56Lck and p59Fyn phosphorylate CD28 and the phosphorylated residue allows the recruitment of PI3K, growth factor receptor-bound protein 2 (GRB2) and Grb2-related adaptor downstream of SHC (GADS) via their src-homology region 2 (SH2) domains.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-388831",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-388831"
}
]
},
{
"id": "R-HSA-388832",
"name": "PI3K binds CD28",
"equation": "",
"summary": "PI3K inducibly associates with CD28: the SH2 domains of the PI3K p85 adaptor subunit interact with a cytoplasmic YMNM consensus motif at residues 173-176 of CD28.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P06241-1",
"P06239-1"
],
"evidence": [
{
"id": "R-HSA-388832",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-388832"
}
]
},
{
"id": "R-HSA-388833",
"name": "Phosphorylation of CTLA-4",
"equation": "",
"summary": "Upon TCR-CTLA-4 complex formation, CTLA4 is tyrosine phosphorylated. Src family tyrosine kinases Fyn, Lyn, and Lck associate with CTLA-4 and phosphorylate both Y-201 and Y-218 that are mainly responsible for interaction with Fyn through its SH2 domain (Marengere et al. 1996). Once tyrosine 165 is phosphorylated, PP2A is activated and disassociates from CTLA4; this correlates with T cell inactivation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P67775-1",
"P06239-1",
"P07947-1",
"P07948-1",
"P62714-1"
],
"evidence": [
{
"id": "R-HSA-388833",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-388833"
}
]
},
{
"id": "R-HSA-389158",
"name": "CD28 bound PI3K phosphorylates PIP2 to PIP3",
"equation": "",
"summary": "PI3K enzyme bound to co-stimulatory protein CD28 catalyzes the phosphorylation of phosphatidylinositol 4,5-bisphosphate (PIP2) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). This PIP3 acts as a membrane anchor for the downstream proteins like PDK1 and PKB.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P06241-1",
"P06239-1"
],
"evidence": [
{
"id": "R-HSA-389158",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389158"
}
]
},
{
"id": "R-HSA-389348",
"name": "Activation of Rac1 by pVav1",
"equation": "",
"summary": "Vav1, once activated by PIP3 binding and phosphorylation by Fyn, stimulates the GDP/GTP exchange activity of Rac. Vav1 is selective for Rac and catalyses exchange of bound GDP for GTP.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P63000-1",
"P06239-1"
],
"evidence": [
{
"id": "R-HSA-389348",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389348"
}
]
},
{
"id": "R-HSA-389350",
"name": "Activation of Cdc42 by pVav1",
"equation": "",
"summary": "Vav1 serves as a GEF for Cdc42-GTPase. It interacts with and activates Cdc42. The activated Cdc42 in turn transmits its signals through the downstream target, the PAK1 kinase.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P60953-2",
"P06239-1"
],
"evidence": [
{
"id": "R-HSA-389350",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389350"
}
]
},
{
"id": "R-HSA-389352",
"name": "Translocation of Vav1 to CD28",
"equation": "",
"summary": "Vav1 protein is a cytoplasmic guanine nucleotide exchange factor (GEF) for Rho-family GTPases. CD28 co-stimulation resulted in a prolonged and sustained phosphorylation and membrane localization of Vav1 in comparison to T-cell receptor activation alone. Vav1 contains a unique arrangement of signaling motifs a calponin homology domain, an acidic domain, a DBL homology (DH) domain, a pleckstrin homology (PH) domain, a cysteine-rich domain (CR), and a SH2 domain flanked by two proline-binding SH3 domains. Vav-1 may be recruited to the membrane through its PH domain by binding PI(3,4,5)P3 produced by CD28-bound PI3K and also by binding to CD28:Grb2 complexes by the dimerized SH3 domains in both the molecules.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P06239-1"
],
"evidence": [
{
"id": "R-HSA-389352",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389352"
}
]
},
{
"id": "R-HSA-389354",
"name": "Activation of Vav1",
"equation": "",
"summary": "Vav1 exists in an auto-inhibitory state folded in such a way as to inhibit the GEF activity of its DH domain. This folding is mediated through binding of tyrosines in the acidic domain to the DH domain and through binding of the CH domain to the C1 region. Activation of Vav may involve at least three different events to relieve this auto-inhibition. Phosphorylation of the tyrosines causes them to be displaced from the DH domain, binding of a ligand to the CH domain may cause it to release the C1 domain and PIP3 may bind to the PH domain, altering its conformation. Vav1 is phosphorylated on at least three tyrosines (Y142, Y160 and Y174) in the acidic domain, and this phosphorylation results in an increase in GEF activity. Fyn tyrosine kinase phosphorylates Vav1 after CD28 ligation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P06239-1"
],
"evidence": [
{
"id": "R-HSA-389354",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389354"
}
]
},
{
"id": "R-HSA-389381",
"name": "Gads binds CD28",
"equation": "",
"summary": "Gads (Grb2-related adaptor protein 2) is essential for CD28 mediated NF-kB activation. This signal is mediated by the binding of Gads to the CD28 YMNM motif. The CD28 cytoplasmic PxxP motif is also required for this association.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P06239-1"
],
"evidence": [
{
"id": "R-HSA-389381",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389381"
}
]
},
{
"id": "R-HSA-389758",
"name": "Dephosphorylation of CD3-zeta by PD-1 bound phosphatases",
"equation": "",
"summary": "PD-1 delivers inhibitory signals and downregulates antigen receptor signaling through direct dephosphorylation of signaling intermediates. The phosphatases SHP-1 and SHP-2 dephosphorylate CD3 zeta and inhibit the phosphorylation of ZAP-70 and PKC theta.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P41240-1",
"P06239-1",
"Q06124-2",
"P29350-1"
],
"evidence": [
{
"id": "R-HSA-389758",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389758"
}
]
},
{
"id": "R-HSA-389759",
"name": "Interaction of SHP-1 or SHP-2 with phospho PD-1",
"equation": "",
"summary": "Once phosphorylated, SH2-domain containing tyrosine phosphatases SHP-1 and SHP-2 bind to the ITIM and ITSM motifs of PD-1. The association between SHP-1 and PD-1 appears to be weaker than the interaction of PD-1 with SHP-2.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P41240-1",
"P06239-1",
"Q06124-2",
"P29350-1"
],
"evidence": [
{
"id": "R-HSA-389759",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389759"
}
]
},
{
"id": "R-HSA-389762",
"name": "Phosphorylation of PD-1",
"equation": "",
"summary": "The cytoplasmic domain of PD-1 has two tyrosine motifs, ITIM and ITSM. On engagement with B7 ligands B7DC and B7H1, PD-1 is phosphorylated on tyrosine residues 223 and 248 within these motifs. Kinases Lck and Csk also bind to these motifs and these kinases may be involved in the phosphorylation of PD-1.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P41240-1",
"P06239-1"
],
"evidence": [
{
"id": "R-HSA-389762",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389762"
}
]
},
{
"id": "R-HSA-434836",
"name": "Syk/Lck phosphorylate LAT",
"equation": "",
"summary": "Activated Syk (or possibly the related kinase Lck) phosphorylates two key tyrosine residues of LAT.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [
"R-HSA-202322"
],
"output_participant_list": [
"R-HSA-434829"
],
"enzyme_list": [
"P06239-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-434836",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-434836"
}
]
},
{
"id": "R-HSA-452100",
"name": "SHC1 bound to IL2 receptor is phosphorylated",
"equation": "",
"summary": "Following IL2 stimulation of IL2R, Shc is known to be tyrosine phosphorylated (Zhu et al. 1994). The identity of the kinase is uncertain (Gesbert et al. 1998); JAK1 may be responsible but this has not been demonstrated, another candidate is Lck.
Following IL-3 treatment, Shc becomes tyrosyl phoshorylated at 3 sites, Y427 (Salcini et al. 1994), Y349 and Y350 (Gotoh et al. 1996). Y427 mediates the subsequent association with Grb2 (Salcini et al. 1994).
Numbering here refers to Uniprot P29353 where the p66 isoform has been selected as the canonical form. Literature references used 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": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P52333-1",
"P06239-1",
"P23458-1"
],
"evidence": [
{
"id": "R-HSA-452100",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-452100"
}
]
},
{
"id": "R-HSA-8852200",
"name": "Inactivation of LCK by PTPN22",
"equation": "",
"summary": "Protein tyrosine phosphatase PTPN22 (LYP, PEP) (Cohen et al. 1999) dephosphorylates tyrosine residue Y394 of LCK, thus inactivating LCK and down-regulating TCR signaling (Wu et al. 2006, Vang et al. 2012).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06239-1",
"Q9Y2R2-1"
],
"evidence": [
{
"id": "R-HSA-8852200",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8852200"
}
]
},
{
"id": "R-HSA-8855381",
"name": "PTPN22 dephosphorylates ZAP70",
"equation": "",
"summary": "Protein tyrosine phosphatase PTPN22 (LYP, PEP) dephosphorylates ZAP70 adaptor protein on tyrosine residue Y493, resulting in reduced activation of ZAP70. Dephosphorylation of ZAP70 contributes to PTPN22-mediated downregulation of TCR signaling (Wu et al. 2006).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06239-1",
"P43403-1",
"Q9Y2R2-1"
],
"evidence": [
{
"id": "R-HSA-8855381",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8855381"
}
]
},
{
"id": "R-HSA-8857925",
"name": "Inhibition of PP2A activity by phosphorylation of the catalytic subunit at tyrosine Y307",
"equation": "",
"summary": "SRC family tyrosine kinases, such as SRC and LCK, as well as receptor tyrosine kinases, such as EGFR and insulin receptor, can phosphorylate the catalytic subunit of serine/threonine protein phosphatase PP2A at tyrosine residue Y307. Phosphorylation at Y307 inhibits the catalytic activity of PP2A. Phosphatidylinositol-5-phosphate (PI5P) positively regulates phosphorylation of the catalytic subunit of PP2A at Y307.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P67775-1",
"P06239-1",
"P06213-1",
"P62714-1"
],
"evidence": [
{
"id": "R-HSA-8857925",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8857925"
}
]
},
{
"id": "R-HSA-9018758",
"name": "RHOH binds effectors at the plasma membrane",
"equation": "",
"summary": "RHOH plays an important role in development of T lymphocytes and binds to several kinases involved in T lymphocyte activation, including:
ZAP70 (Gu et al. 2006, Chae et al. 2010, Wang et al. 2011)
LCK (Chae et al. 2010, Wang et al. 2011)
CSK (Wang et al. 2010).
Additional RHOH interactors include:
PAK1 (Wang et al. 2010; Tajadura Ortega et al. 2018)
PAK2 (Tajadura Ortega et al. 2018)
PAK4 (Tajadura Ortega et al. 2018)
PAK5 (Wu and Frost 2006; Tajadura Ortega et al. 2018)
PAK6 (Tajadura Ortega et al. 2018)
The following RHOH interactors have only been reported in a high throughput screen by Bagci et al. 2020, and are therefore annotated as candidate RHOH effectors:
CAV1 (Bagci et al. 2020).
DBN1 (Bagci et al. 2020)
DBT (Bagci et al. 2020)
FAM91A1 (Bagci et al. 2020)
JUP (Bagci et al. 2020)
LAMTOR1 (Bagci et al. 2020)
MTR (Bagci et al. 2020)
NIPSNAP2 (Bagci et al. 2020)
NSFL1C (Bagci et al. 2020)
OSBPL11 (Bagci et al. 2020)
RAB7A (Bagci et al. 2020)
RALGAPA1 (Bagci et al. 2020)
ROCK1 (Bagci et al. 2020)
ROCK2 (Bagci et al. 2020)
SLC1A5 (Bagci et al. 2020)
SLC4A7 (Bagci et al. 2020)
STOM (Bagci et al. 2020)
TFRC (Bagci et al. 2020)
TMEM59 (Bagci et al. 2020)
TUBA1B (Bagci et al. 2020)
UACA (Bagci et al. 2020)
VAMP3 (Bagci et al. 2020)
VANGL1 (Bagci et al. 2020)
VCP (Bagci et al. 2020)
WDR11 (Bagci et al. 2020)",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q13464-1",
"P41240-1",
"Q99707-1",
"P11182-1",
"O75116-1",
"P55072-1",
"P06239-1",
"Q13153-1",
"Q13177-1",
"P68363-1",
"Q9P286-1",
"P43403-1",
"O96013-1",
"Q9NQU5-1",
"P51149-1"
],
"evidence": [
{
"id": "R-HSA-9018758",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9018758"
}
]
},
{
"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-9670414",
"name": "KIT mutants bind SFKs",
"equation": "",
"summary": "Signaling downstream of KIT mutants occurs in part through SRC family kinases, as is the case for the wild-type receptor (Paronetto et al, 2004; Krystal et al, 1998; Schittenhelm et al, 2006; Tatton et al, 2003; Timokhina et al, 1998; reviewed in Lanneartsson and Roonstrand, 2012). The dependence of different KIT mutants on SRC family signaling varies, however, with mutants such as the common D816V showing less requirement for SFK-mediated signaling (Sun et al, 2009).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06241-1",
"P10721-1",
"P06239-1",
"P07947-1",
"P07948-1"
],
"evidence": [
{
"id": "R-HSA-9670414",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9670414"
}
]
},
{
"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-9706312",
"name": "Active FLT3 binds to LCK",
"equation": "",
"summary": "SRC family of non-receptor tyrosine kinase LCK binds to tyrosine-phosphorylated FLT3. LCK-binding stimulates STAT signaling downstream of FLT3-ITD mutants and promotes cellular proliferation and tumor formation in mouse models (Marhall et al, 2017).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P06239-1",
"P36888-1"
],
"evidence": [
{
"id": "R-HSA-9706312",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9706312"
}
]
}
],
"reaction_participants": [
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"participant_name": "LCK [cytosol]",
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