{
"uniprot_canonical_ac": "P12931-1",
"uniprot_ac": "P12931",
"uniprot_id": "SRC_HUMAN",
"mass": {
"chemical_mass": 59835.0,
"monoisotopic_mass": 59835.0
},
"refseq": {
"ac": "NP_005408",
"name": "proto-oncogene tyrosine-protein kinase Src",
"summary": "This gene is highly similar to the v-src gene of Rous sarcoma virus. This proto-oncogene may play a role in the regulation of embryonic development and cell growth. The protein encoded by this gene is a tyrosine-protein kinase whose activity can be inhibited by phosphorylation by c-SRC kinase. Mutations in this gene could be involved in the malignant progression of colon cancer. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_005408"
},
"gene_names": [
{
"name": "SRC",
"resource": "UniProtKB",
"type": "recommended",
"url": "https://www.uniprot.org/uniprot/P12931",
"id": "P12931"
},
{
"name": "ASV; c-SRC; p60-Src; SRC1; THC6",
"resource": "RefSeq",
"type": "synonym",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_005408",
"id": "NP_005408"
},
{
"name": "SRC1",
"resource": "UniProtKB",
"type": "synonym",
"url": "https://www.uniprot.org/uniprot/P12931",
"id": "P12931"
},
{
"name": "SRC",
"resource": "RefSeq",
"type": "synonym",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_005408",
"id": "NP_005408"
}
],
"protein_names": [
{
"name": "Proto-oncogene tyrosine-protein kinase Src",
"resource": "UniProtKB",
"type": "recommended",
"url": "",
"id": "P12931"
},
{
"name": "2.7.10.2",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "P12931"
},
{
"name": "Proto-oncogene c-Src",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "P12931"
},
{
"name": "p60-Src",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "P12931"
},
{
"name": "pp60c-src",
"resource": "UniProtKB",
"type": "synonym",
"url": "",
"id": "P12931"
},
{
"name": "proto-oncogene tyrosine-protein kinase Src",
"resource": "RefSeq",
"type": "synonym",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_005408",
"id": "NP_005408"
},
{
"name": "tyrosine-protein kinase SRC-1; tyrosine kinase pp60c-src; protooncogene SRC, Rous sarcoma; proto-oncogene c-Src; v-src avian sarcoma (Schmidt-Ruppin A-2) viral oncogene homolog",
"resource": "RefSeq",
"type": "synonym",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_005408",
"id": "NP_005408"
}
],
"function": [
{
"annotation": "An allosteric switch between the activation loop and a c-terminal palindromic phospho-motif controls c-Src function. Publication Status: Online-Only",
"evidence": [
{
"database": "RefSeq",
"id": "NP_005408",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_005408"
},
{
"database": "PubMed",
"id": "37848415",
"url": "https://glygen.org/publication/PubMed/37848415"
}
]
},
{
"annotation": "Identification and functional validation of SRC and RAPGEF1 as new direct targets of miR-203, involved in regulation of epidermal homeostasis. Publication Status: Online-Only",
"evidence": [
{
"database": "RefSeq",
"id": "NP_005408",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_005408"
},
{
"database": "PubMed",
"id": "37635193",
"url": "https://glygen.org/publication/PubMed/37635193"
}
]
},
{
"annotation": "MiR-654-3p targets SRC to suppress tumor growth in non-small cell lung cancer. Publication Status: Online-Only",
"evidence": [
{
"database": "RefSeq",
"id": "NP_005408",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_005408"
},
{
"database": "PubMed",
"id": "37329531",
"url": "https://glygen.org/publication/PubMed/37329531"
}
]
},
{
"annotation": "Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (PubMed:21411625). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (By similarity). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1 (PubMed:11389730). Plays a role in EGF-mediated calcium-activated chloride channel activation (PubMed:18586953). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (Probable). Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus (PubMed:7853507). Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:8755529, PubMed:14585963). Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation (PubMed:16186108). Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731' (PubMed:20100835, PubMed:21309750). Enhances RIGI-elicited antiviral signaling (PubMed:19419966). Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376' (PubMed:14585963). Phosphorylates BCAR1 at 'Tyr-128' (PubMed:22710723). Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity (PubMed:20525694). Phosphorylates synaptic vesicle protein synaptophysin (SYP) (By similarity). Involved in anchorage-independent cell growth (PubMed:19307596). Required for podosome formation (By similarity). Mediates IL6 signaling by activating YAP1-NOTCH pathway to induce inflammation-induced epithelial regeneration (PubMed:25731159). Phosphorylates OTUB1, promoting deubiquitination of RPTOR (PubMed:35927303).",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931#function"
},
{
"database": "PubMed",
"id": "9442882",
"url": "https://glygen.org/publication/PubMed/9442882"
},
{
"database": "PubMed",
"id": "8759729",
"url": "https://glygen.org/publication/PubMed/8759729"
},
{
"database": "PubMed",
"id": "11389730",
"url": "https://glygen.org/publication/PubMed/11389730"
},
{
"database": "UniProtKB",
"id": "P05480",
"url": "https://www.uniprot.org/uniprot/P05480#function"
},
{
"database": "PubMed",
"id": "22710723",
"url": "https://glygen.org/publication/PubMed/22710723"
},
{
"database": "PubMed",
"id": "8755529",
"url": "https://glygen.org/publication/PubMed/8755529"
},
{
"database": "UniProtKB",
"id": "Q9WUD9",
"url": "https://www.uniprot.org/uniprot/Q9WUD9#function"
},
{
"database": "PubMed",
"id": "11964124",
"url": "https://glygen.org/publication/PubMed/11964124"
},
{
"database": "PubMed",
"id": "12615910",
"url": "https://glygen.org/publication/PubMed/12615910"
},
{
"database": "PubMed",
"id": "19307596",
"url": "https://glygen.org/publication/PubMed/19307596"
},
{
"database": "PubMed",
"id": "18586953",
"url": "https://glygen.org/publication/PubMed/18586953"
},
{
"database": "PubMed",
"id": "25731159",
"url": "https://glygen.org/publication/PubMed/25731159"
},
{
"database": "PubMed",
"id": "14585963",
"url": "https://glygen.org/publication/PubMed/14585963"
},
{
"database": "PubMed",
"id": "20100835",
"url": "https://glygen.org/publication/PubMed/20100835"
},
{
"database": "PubMed",
"id": "21411625",
"url": "https://glygen.org/publication/PubMed/21411625"
},
{
"database": "PubMed",
"id": "21309750",
"url": "https://glygen.org/publication/PubMed/21309750"
},
{
"database": "PubMed",
"id": "19419966",
"url": "https://glygen.org/publication/PubMed/19419966"
},
{
"database": "PubMed",
"id": "20525694",
"url": "https://glygen.org/publication/PubMed/20525694"
},
{
"database": "PubMed",
"id": "8672527",
"url": "https://glygen.org/publication/PubMed/8672527"
},
{
"database": "PubMed",
"id": "16186108",
"url": "https://glygen.org/publication/PubMed/16186108"
},
{
"database": "PubMed",
"id": "7853507",
"url": "https://glygen.org/publication/PubMed/7853507"
},
{
"database": "PubMed",
"id": "35927303",
"url": "https://glygen.org/publication/PubMed/35927303"
}
]
},
{
"annotation": "Non-receptor protein tyrosine kinase which phosphorylates synaptophysin with high affinity.",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931#function"
},
{
"database": "UniProtKB",
"id": "Q9WUD9",
"url": "https://www.uniprot.org/uniprot/Q9WUD9#function"
}
]
},
{
"annotation": "Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr-419 and subsequent activation (By similarity). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (By similarity). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (By similarity). Plays a role in neurite elongation (By similarity).",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931#function"
},
{
"database": "UniProtKB",
"id": "Q9WUD9",
"url": "https://www.uniprot.org/uniprot/Q9WUD9#function"
}
]
},
{
"annotation": "SQLE promotes pancreatic cancer growth by attenuating ER stress and activating lipid rafts-regulated Src/PI3K/Akt signaling pathway. Publication Status: Online-Only",
"evidence": [
{
"database": "RefSeq",
"id": "NP_005408",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_005408"
},
{
"database": "PubMed",
"id": "37542052",
"url": "https://glygen.org/publication/PubMed/37542052"
}
]
},
{
"annotation": "The activated CD36-Src axis promotes lung adenocarcinoma cell proliferation and actin remodeling-involved metastasis in high-fat environment. Publication Status: Online-Only",
"evidence": [
{
"database": "RefSeq",
"id": "NP_005408",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_005408"
},
{
"database": "PubMed",
"id": "37612265",
"url": "https://glygen.org/publication/PubMed/37612265"
}
]
},
{
"annotation": "This gene is highly similar to the v-src gene of Rous sarcoma virus. This proto-oncogene may play a role in the regulation of embryonic development and cell growth. The protein encoded by this gene is a tyrosine-protein kinase whose activity can be inhibited by phosphorylation by c-SRC kinase. Mutations in this gene could be involved in the malignant progression of colon cancer. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008].",
"evidence": [
{
"database": "RefSeq",
"id": "NP_005408",
"url": "https://www.ncbi.nlm.nih.gov/protein/NP_005408"
}
]
}
],
"disease": [
{
"disease_id": "MONDO:0014837",
"recommended_name": {
"id": "MONDO:0014837",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0014837",
"name": "thrombocytopenia 6",
"description": ""
},
"synonyms": [
{
"id": "MONDO:0014837",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0014837",
"name": "hereditary thrombocytopenia with early-onset myelofibrosis",
"description": ""
},
{
"id": "MONDO:0014837",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0014837",
"name": "thrombocytopenia 6",
"description": ""
},
{
"id": "MONDO:0014837",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0014837",
"name": "thrombocytopenia type 6",
"description": ""
},
{
"id": "MONDO:0014837",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0014837",
"name": "THC6",
"description": ""
},
{
"id": "MONDO:0014837",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0014837",
"name": "thrombocytopenia, autosomal dominant, 6",
"description": ""
},
{
"id": "MIM:616937",
"resource": "MIM",
"url": "https://www.omim.org/entry/616937",
"name": "Thrombocytopenia 6",
"description": "Thrombocytopenia 6"
}
],
"evidence": [
{
"id": "616937",
"database": "MIM",
"url": "https://www.omim.org/entry/616937"
}
]
}
],
"snv": [
{
"evidence": [
{
"id": "rs1251001677",
"database": "dbSNP",
"url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs1251001677"
},
{
"id": "rs1251001677",
"database": "gnomAD",
"url": "http://gnomad.broadinstitute.org/awesome?query=rs1251001677"
}
],
"glycoeffect": [
"n-glyco-sequon-gain"
],
"start_pos": 10,
"end_pos": 10,
"sequence_org": "D",
"sequence_mut": "N",
"comment": "Germline mutation passed 1 out of 1 filters: n-glyco-sequon-gain (DAS->NAS).",
"chr_id": "20",
"chr_pos": "37384181",
"ref_nt": "A",
"alt_nt": "null",
"minor_allelic_frequency": "",
"site_lbl": "D10",
"keywords": [
"ebi",
"germline"
]
},
{
"evidence": [
{
"id": "rs956880395",
"database": "dbSNP",
"url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs956880395"
},
{
"id": "rs956880395",
"database": "TOPMed",
"url": "https://www.ncbi.nlm.nih.gov/snp/rs956880395#frequency_tab"
},
{
"id": "rs956880395",
"database": "gnomAD",
"url": "http://gnomad.broadinstitute.org/awesome?query=rs956880395"
}
],
"glycoeffect": [
"n-glyco-sequon-loss"
],
"start_pos": 68,
"end_pos": 68,
"sequence_org": "N",
"sequence_mut": "D",
"comment": "Germline mutation passed 1 out of 1 filters: n-glyco-sequon-loss (NSS->DSS).",
"chr_id": "20",
"chr_pos": "37384355",
"ref_nt": "G",
"alt_nt": "null",
"minor_allelic_frequency": "",
"site_lbl": "N68",
"keywords": [
"ebi",
"germline"
]
},
{
"evidence": [
{
"id": "rs1432925945",
"database": "dbSNP",
"url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs1432925945"
},
{
"id": "rs1432925945",
"database": "gnomAD",
"url": "http://gnomad.broadinstitute.org/awesome?query=rs1432925945"
}
],
"glycoeffect": [
"n-glyco-sequon-loss",
"o-glyco-site-loss"
],
"start_pos": 69,
"end_pos": 69,
"sequence_org": "S",
"sequence_mut": "P",
"comment": "Germline mutation passed 1 out of 1 filters: n-glyco-sequon-loss (NSS->NPS).",
"chr_id": "20",
"chr_pos": "37384358",
"ref_nt": "C",
"alt_nt": "null",
"minor_allelic_frequency": "",
"site_lbl": "S69",
"keywords": [
"ebi",
"germline"
]
}
],
"mutagenesis": [
{
"start_pos": 298,
"end_pos": 298,
"sequence_org": "K",
"sequence_mut": "M",
"comment": "Kinase inactive. Abolishes ubiquitination promoted by CBLC.",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
},
{
"database": "PubMed",
"id": "14661060",
"url": "https://glygen.org/publication/PubMed/14661060"
}
]
},
{
"start_pos": 302,
"end_pos": 302,
"sequence_org": "P",
"sequence_mut": "E",
"comment": "Kinase active. Interacts with PDLIM4; when associated with E-307 and F-419.",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
},
{
"database": "PubMed",
"id": "19307596",
"url": "https://glygen.org/publication/PubMed/19307596"
}
]
},
{
"start_pos": 307,
"end_pos": 307,
"sequence_org": "P",
"sequence_mut": "E",
"comment": "Kinase active. Interacts with PDLIM4; when associated with E-302 and F-419.",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
},
{
"database": "PubMed",
"id": "19307596",
"url": "https://glygen.org/publication/PubMed/19307596"
}
]
},
{
"start_pos": 419,
"end_pos": 419,
"sequence_org": "Y",
"sequence_mut": "F",
"comment": "Loss of kinase activity. Loss of interaction with PDLIM4.",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
},
{
"database": "PubMed",
"id": "19307596",
"url": "https://glygen.org/publication/PubMed/19307596"
}
]
}
],
"expression_tissue": [
{
"tissue": {
"name": "Adult mammalian kidney",
"namespace": "UBERON",
"id": "0000082",
"url": "http://purl.obolibrary.org/obo/UBERON_0000082"
},
"score": "78.24",
"present": "MEDIUM",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000197122",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000197122"
}
]
},
{
"tissue": {
"name": "Oral cavity",
"namespace": "UBERON",
"id": "0000167",
"url": "http://purl.obolibrary.org/obo/UBERON_0000167"
},
"score": "73.28",
"present": "MEDIUM",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000197122",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000197122"
}
]
},
{
"tissue": {
"name": "Stomach",
"namespace": "UBERON",
"id": "0000945",
"url": "http://purl.obolibrary.org/obo/UBERON_0000945"
},
"score": "87.29",
"present": "HIGH",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000197122",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000197122"
}
]
},
{
"tissue": {
"name": "Uterus",
"namespace": "UBERON",
"id": "0000995",
"url": "http://purl.obolibrary.org/obo/UBERON_0000995"
},
"score": "84.33",
"present": "HIGH",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000197122",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000197122"
}
]
},
{
"tissue": {
"name": "Esophagus",
"namespace": "UBERON",
"id": "0001043",
"url": "http://purl.obolibrary.org/obo/UBERON_0001043"
},
"score": "91.97",
"present": "HIGH",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000197122",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000197122"
}
]
},
{
"tissue": {
"name": "Rectum",
"namespace": "UBERON",
"id": "0001052",
"url": "http://purl.obolibrary.org/obo/UBERON_0001052"
},
"score": "96.33",
"present": "HIGH",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000197122",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000197122"
}
]
},
{
"tissue": {
"name": "Colon",
"namespace": "UBERON",
"id": "0001155",
"url": "http://purl.obolibrary.org/obo/UBERON_0001155"
},
"score": "72.68",
"present": "MEDIUM",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000197122",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000197122"
}
]
},
{
"tissue": {
"name": "Urinary bladder",
"namespace": "UBERON",
"id": "0001255",
"url": "http://purl.obolibrary.org/obo/UBERON_0001255"
},
"score": "89.47",
"present": "HIGH",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000197122",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000197122"
}
]
},
{
"tissue": {
"name": "Thyroid gland",
"namespace": "UBERON",
"id": "0002046",
"url": "http://purl.obolibrary.org/obo/UBERON_0002046"
},
"score": "84.5",
"present": "HIGH",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000197122",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000197122"
}
]
},
{
"tissue": {
"name": "Lung",
"namespace": "UBERON",
"id": "0002048",
"url": "http://purl.obolibrary.org/obo/UBERON_0002048"
},
"score": "69.71",
"present": "MEDIUM",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000197122",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000197122"
}
]
},
{
"tissue": {
"name": "Liver",
"namespace": "UBERON",
"id": "0002107",
"url": "http://purl.obolibrary.org/obo/UBERON_0002107"
},
"score": "75.16",
"present": "MEDIUM",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000197122",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000197122"
}
]
},
{
"tissue": {
"name": "Prostate gland",
"namespace": "UBERON",
"id": "0002367",
"url": "http://purl.obolibrary.org/obo/UBERON_0002367"
},
"score": "96.03",
"present": "HIGH",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000197122",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000197122"
}
]
},
{
"tissue": {
"name": "Thoracic mammary gland",
"namespace": "UBERON",
"id": "0005200",
"url": "http://purl.obolibrary.org/obo/UBERON_0005200"
},
"score": "87.64",
"present": "HIGH",
"evidence": [
{
"database": "Bgee",
"id": "ENSG00000197122",
"url": "https://bgee.org/?page=gene&gene_id=ENSG00000197122"
}
]
}
],
"expression_disease": [
{
"significant": "No",
"trend": "down",
"name": "Prostate cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:10283",
"evidence": [
{
"database": "BioXpress",
"id": "P12931",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P12931"
}
],
"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": "Yes",
"trend": "up",
"name": "Stomach cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:10534",
"evidence": [
{
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{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "nonsmall cell lung cancer, somatic",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "nonsmall cell lung cancer, susceptibility to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "Nonsmall cell lung cancer",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "alveolar cell carcinoma",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "lung cancer, protection against",
"description": ""
},
{
"id": "MONDO:0008903",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0008903",
"name": "lung neoplasm",
"description": ""
},
{
"id": "MIM:211980",
"resource": "MIM",
"url": "https://www.omim.org/entry/211980",
"name": "Lung cancer",
"description": "Lung cancer"
}
]
}
]
},
{
"significant": "Yes",
"trend": "up",
"name": "Breast cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:1612",
"evidence": [
{
"database": "BioXpress",
"id": "P12931",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P12931"
}
],
"disease": [
{
"disease_id": "DOID:1612",
"recommended_name": {
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
"name": "breast cancer",
"description": "A thoracic cancer that originates in the mammary gland."
},
"synonyms": [
{
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
"name": "breast tumor",
"description": ""
},
{
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
"name": "malignant neoplasm of breast",
"description": ""
},
{
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
"name": "malignant tumor of the breast",
"description": ""
},
{
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
"name": "mammary cancer",
"description": ""
},
{
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
"name": "mammary tumor",
"description": ""
},
{
"id": "DOID:1612",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:1612",
"name": "primary breast cancer",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "hereditary breast carcinoma",
"description": "Breast carcinoma that has developed in relatives of patients with history of breast carcinoma."
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer susceptibility, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, early-onset, susceptibility to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, invasive ductal, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, lobular, somatic",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, male, susceptibility to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, protection against, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, somatic",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, susceptibility to, autosomal dominant, somatic mutation",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "familial breast cancer",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "familial breast carcinoma",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "familial cancer of breast",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "familial cancer of the breast",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "hereditary breast cancer",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "hereditary breast carcinoma",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, familial",
"description": ""
},
{
"id": "MONDO:0016419",
"resource": "MONDO",
"url": "https://monarchinitiative.org/disease/MONDO:0016419",
"name": "breast cancer, familial Male",
"description": ""
},
{
"id": "MIM:114480",
"resource": "MIM",
"url": "https://www.omim.org/entry/114480",
"name": "Breast cancer",
"description": "Breast cancer"
}
]
}
]
},
{
"significant": "Yes",
"trend": "up",
"name": "Thyroid cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:1781",
"evidence": [
{
"database": "BioXpress",
"id": "P12931",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P12931"
}
],
"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": "P12931",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P12931"
}
],
"disease": [
{
"disease_id": "DOID:263",
"recommended_name": {
"id": "DOID:263",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:263",
"name": "kidney cancer",
"description": "A urinary system cancer that is located_in the kidney."
},
"synonyms": [
{
"id": "DOID:263",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:263",
"name": "malignant neoplasm of kidney except pelvis",
"description": ""
},
{
"id": "DOID:263",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:263",
"name": "malignant tumour of kidney",
"description": ""
},
{
"id": "DOID:263",
"resource": "Disease Ontology",
"url": "http://disease-ontology.org/term/DOID:263",
"name": "renal cancer",
"description": ""
}
]
}
]
},
{
"significant": "Yes",
"trend": "up",
"name": "Liver cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:3571",
"evidence": [
{
"database": "BioXpress",
"id": "P12931",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P12931"
}
],
"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": "No",
"trend": "up",
"name": "Uterine cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:363",
"evidence": [
{
"database": "BioXpress",
"id": "P12931",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P12931"
}
],
"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": "No",
"trend": "up",
"name": "Esophageal cancer [DO disease name]",
"url": "http://disease-ontology.org/term/DOID:5041",
"evidence": [
{
"database": "BioXpress",
"id": "P12931",
"url": "https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/P12931"
}
],
"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",
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"description": "Regulation of RUNX3 expression and activity"
},
{
"id": "R-HSA-9009391",
"name": "Extra-nuclear estrogen signaling",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9009391",
"resource": "Reactome",
"description": "Extra-nuclear estrogen signaling"
},
{
"id": "R-HSA-9013420",
"name": "RHOU GTPase cycle",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9013420",
"resource": "Reactome",
"description": "RHOU GTPase cycle"
},
{
"id": "R-HSA-9032500",
"name": "Activated NTRK2 signals through FYN",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9032500",
"resource": "Reactome",
"description": "Activated NTRK2 signals through FYN"
},
{
"id": "R-HSA-9603381",
"name": "Activated NTRK3 signals through PI3K",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9603381",
"resource": "Reactome",
"description": "Activated NTRK3 signals through PI3K"
},
{
"id": "R-HSA-9620244",
"name": "Long-term potentiation",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9620244",
"resource": "Reactome",
"description": "Long-term potentiation"
},
{
"id": "R-HSA-9634597",
"name": "GPER1 signaling",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9634597",
"resource": "Reactome",
"description": "GPER1 signaling"
},
{
"id": "R-HSA-9649948",
"name": "Signaling downstream of RAS mutants",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9649948",
"resource": "Reactome",
"description": "Signaling downstream of RAS mutants"
},
{
"id": "R-HSA-9656223",
"name": "Signaling by RAF1 mutants",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9656223",
"resource": "Reactome",
"description": "Signaling by RAF1 mutants"
},
{
"id": "R-HSA-9680350",
"name": "Signaling by CSF1 (M-CSF) in myeloid cells",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9680350",
"resource": "Reactome",
"description": "Signaling by CSF1 (M-CSF) in myeloid cells"
}
],
"orthologs": [
{
"uniprot_canonical_ac": "P05480-2",
"protein_name": "Proto-oncogene tyrosine-protein kinase Src",
"gene_name": "Src",
"tax_id": 10090,
"organism": "Mus musculus",
"sequence": {
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"length": 535
},
"evidence": [
{
"id": "45921156",
"url": "http://www.informatics.jax.org/homology/45921156",
"database": "MGI"
},
{
"id": "P12931",
"url": "https://omabrowser.org/oma/group/P12931/",
"database": "OMA"
}
],
"common_name": "Mouse"
},
{
"uniprot_canonical_ac": "Q9WUD9-1",
"protein_name": "Proto-oncogene tyrosine-protein kinase Src",
"gene_name": "Src",
"tax_id": 10116,
"organism": "Rattus norvegicus",
"sequence": {
"sequence": "MGSNKSKPKDASQRRRSLEPAENVHGAGGAFPASQTPSKPASADGHRGPNAAFVPPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMNKGSLLDFLKGETGKYLRLPQLVDMSAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL",
"length": 536
},
"evidence": [
{
"id": "45921156",
"url": "http://www.informatics.jax.org/homology/45921156",
"database": "MGI"
},
{
"id": "P12931",
"url": "https://omabrowser.org/oma/group/P12931/",
"database": "OMA"
}
],
"common_name": "Rat"
}
],
"go_annotation": {
"categories": [
{
"name": "Molecular Function",
"total": 22,
"go_terms": [
{
"name": "connexin binding",
"id": "GO:0071253",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0071253",
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{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "protein kinase activity",
"id": "GO:0004672",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004672",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "protein tyrosine kinase activity",
"id": "GO:0004713",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004713",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "non-membrane spanning protein tyrosine kinase activity",
"id": "GO:0004715",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0004715",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "signaling receptor binding",
"id": "GO:0005102",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005102",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "insulin receptor binding",
"id": "GO:0005158",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005158",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "integrin binding",
"id": "GO:0005178",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005178",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "ATP binding",
"id": "GO:0005524",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005524",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "enzyme binding",
"id": "GO:0019899",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0019899",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "ephrin receptor binding",
"id": "GO:0046875",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0046875",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "ATPase binding",
"id": "GO:0051117",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051117",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "transmembrane transporter binding",
"id": "GO:0044325",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0044325",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "phosphoprotein binding",
"id": "GO:0051219",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051219",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "protein kinase C binding",
"id": "GO:0005080",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005080",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cadherin binding",
"id": "GO:0045296",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045296",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "SH2 domain binding",
"id": "GO:0042169",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042169",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "heme binding",
"id": "GO:0020037",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0020037",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "scaffold protein binding",
"id": "GO:0097110",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0097110",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "nuclear estrogen receptor binding",
"id": "GO:0030331",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030331",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "phospholipase activator activity",
"id": "GO:0016004",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0016004",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "phospholipase binding",
"id": "GO:0043274",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043274",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "BMP receptor binding",
"id": "GO:0070700",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070700",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
}
]
},
{
"name": "Biological Process",
"total": 116,
"go_terms": [
{
"name": "positive regulation of TORC1 signaling",
"id": "GO:1904263",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:1904263",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "regulation of early endosome to late endosome transport",
"id": "GO:2000641",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:2000641",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "regulation of bone resorption",
"id": "GO:0045124",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045124",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of Ras protein signal transduction",
"id": "GO:0046579",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0046579",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of small GTPase mediated signal transduction",
"id": "GO:0051057",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051057",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "DNA biosynthetic process",
"id": "GO:0071897",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0071897",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of ovarian follicle development",
"id": "GO:2000386",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:2000386",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "regulation of caveolin-mediated endocytosis",
"id": "GO:2001286",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:2001286",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "primary ovarian follicle growth",
"id": "GO:0001545",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0001545",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of platelet-derived growth factor receptor-beta signaling pathway",
"id": "GO:2000588",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:2000588",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cellular response to progesterone stimulus",
"id": "GO:0071393",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0071393",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of non-membrane spanning protein tyrosine kinase activity",
"id": "GO:1903997",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:1903997",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cell adhesion",
"id": "GO:0007155",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007155",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "signal transduction",
"id": "GO:0007165",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007165",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "integrin-mediated signaling pathway",
"id": "GO:0007229",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007229",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "spermatogenesis",
"id": "GO:0007283",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007283",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "learning or memory",
"id": "GO:0007611",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007611",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "negative regulation of gene expression",
"id": "GO:0010629",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0010629",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "peptidyl-tyrosine phosphorylation",
"id": "GO:0018108",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0018108",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cell differentiation",
"id": "GO:0030154",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030154",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "forebrain development",
"id": "GO:0030900",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030900",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cellular response to insulin stimulus",
"id": "GO:0032869",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0032869",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "intracellular signal transduction",
"id": "GO:0035556",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035556",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of apoptotic process",
"id": "GO:0043065",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043065",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "negative regulation of apoptotic process",
"id": "GO:0043066",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043066",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "innate immune response",
"id": "GO:0045087",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045087",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "ephrin receptor signaling pathway",
"id": "GO:0048013",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0048013",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction",
"id": "GO:0051897",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051897",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of ERK1 and ERK2 cascade",
"id": "GO:0070374",
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{
"database": "UniProtKB",
"id": "P12931",
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}
],
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},
{
"name": "macroautophagy",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0016236",
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "T cell costimulation",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0031295",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "response to nutrient levels",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "negative regulation of cysteine-type endopeptidase activity involved in apoptotic process",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043154",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "regulation of heart rate by cardiac conduction",
"id": "GO:0086091",
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"database": "UniProtKB",
"id": "P12931",
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],
"pmid": ""
},
{
"name": "transforming growth factor beta receptor signaling pathway",
"id": "GO:0007179",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "positive regulation of protein processing",
"id": "GO:0010954",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0010954",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "regulation of cell-cell adhesion",
"id": "GO:0022407",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0022407",
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
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],
"pmid": ""
},
{
"name": "positive regulation of bone resorption",
"id": "GO:0045780",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045780",
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{
"database": "UniProtKB",
"id": "P12931",
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],
"pmid": ""
},
{
"name": "cellular response to lipopolysaccharide",
"id": "GO:0071222",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0071222",
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{
"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "cellular response to hypoxia",
"id": "GO:0071456",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0071456",
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cell-cell adhesion",
"id": "GO:0098609",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0098609",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of cytokine production",
"id": "GO:0001819",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0001819",
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{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "negative regulation of inflammatory response to antigenic stimulus",
"id": "GO:0002862",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0002862",
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{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "response to mechanical stimulus",
"id": "GO:0009612",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0009612",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "platelet activation",
"id": "GO:0030168",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030168",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "negative regulation of telomere maintenance via telomerase",
"id": "GO:0032211",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0032211",
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{
"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "positive regulation of Notch signaling pathway",
"id": "GO:0045747",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045747",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "protein autophosphorylation",
"id": "GO:0046777",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0046777",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "epidermal growth factor receptor signaling pathway",
"id": "GO:0007173",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007173",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "substrate adhesion-dependent cell spreading",
"id": "GO:0034446",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0034446",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "Fc-gamma receptor signaling pathway involved in phagocytosis",
"id": "GO:0038096",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0038096",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "angiotensin-activated signaling pathway",
"id": "GO:0038166",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0038166",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "regulation of vascular permeability",
"id": "GO:0043114",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043114",
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"database": "UniProtKB",
"id": "P12931",
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],
"pmid": ""
},
{
"name": "positive regulation of peptidyl-tyrosine phosphorylation",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050731",
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"database": "UniProtKB",
"id": "P12931",
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],
"pmid": ""
},
{
"name": "leukocyte migration",
"id": "GO:0050900",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050900",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "response to mineralocorticoid",
"id": "GO:0051385",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051385",
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cellular response to hydrogen peroxide",
"id": "GO:0070301",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070301",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "positive regulation of vascular associated smooth muscle cell proliferation",
"id": "GO:1904707",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:1904707",
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{
"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "bone resorption",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045453",
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}
],
"pmid": ""
},
{
"name": "positive regulation of protein serine/threonine kinase activity",
"id": "GO:0071902",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0071902",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "cell cycle",
"id": "GO:0007049",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007049",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "negative regulation of protein-containing complex assembly",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "vascular endothelial growth factor receptor signaling pathway",
"id": "GO:0048010",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0048010",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "focal adhesion assembly",
"id": "GO:0048041",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0048041",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "negative regulation of focal adhesion assembly",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051895",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "adherens junction organization",
"id": "GO:0034332",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0034332",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "osteoclast development",
"id": "GO:0036035",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0036035",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "odontogenesis",
"id": "GO:0042476",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042476",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "response to electrical stimulus",
"id": "GO:0051602",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051602",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cellular response to peptide hormone stimulus",
"id": "GO:0071375",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0071375",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of glucose metabolic process",
"id": "GO:0010907",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0010907",
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of canonical Wnt signaling pathway",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0090263",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "negative regulation of extrinsic apoptotic signaling pathway",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:2001237",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "positive regulation of insulin receptor signaling pathway",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0046628",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "response to interleukin-1",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070555",
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "neurotrophin TRK receptor signaling pathway",
"id": "GO:0048011",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0048011",
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "response to xenobiotic stimulus",
"id": "GO:0009410",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0009410",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of protein localization to nucleus",
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"url": "https://www.ebi.ac.uk/QuickGO/term/GO:1900182",
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"database": "UniProtKB",
"id": "P12931",
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}
],
"pmid": ""
},
{
"name": "response to acidic pH",
"id": "GO:0010447",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0010447",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "transcytosis",
"id": "GO:0045056",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045056",
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of lamellipodium morphogenesis",
"id": "GO:2000394",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:2000394",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of epithelial cell migration",
"id": "GO:0010634",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0010634",
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "protein destabilization",
"id": "GO:0031648",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0031648",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cellular response to platelet-derived growth factor stimulus",
"id": "GO:0036120",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0036120",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of podosome assembly",
"id": "GO:0071803",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0071803",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "stress fiber assembly",
"id": "GO:0043149",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043149",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "platelet-derived growth factor receptor signaling pathway",
"id": "GO:0048008",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0048008",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "oogenesis",
"id": "GO:0048477",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0048477",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "regulation of epithelial cell migration",
"id": "GO:0010632",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0010632",
"evidence": [
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"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "negative regulation of intrinsic apoptotic signaling pathway",
"id": "GO:2001243",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:2001243",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of protein transport",
"id": "GO:0051222",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051222",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of integrin activation",
"id": "GO:0033625",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0033625",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "stimulatory C-type lectin receptor signaling pathway",
"id": "GO:0002223",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0002223",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "myoblast proliferation",
"id": "GO:0051450",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051450",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of hippo signaling",
"id": "GO:0035332",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035332",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of smooth muscle cell migration",
"id": "GO:0014911",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0014911",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "negative regulation of mitochondrial depolarization",
"id": "GO:0051902",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051902",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "negative regulation of anoikis",
"id": "GO:2000811",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:2000811",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cellular response to fluid shear stress",
"id": "GO:0071498",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0071498",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "regulation of intracellular estrogen receptor signaling pathway",
"id": "GO:0033146",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0033146",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "entry of bacterium into host cell",
"id": "GO:0035635",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035635",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "intestinal epithelial cell development",
"id": "GO:0060576",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0060576",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of dephosphorylation",
"id": "GO:0035306",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035306",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "ERBB2 signaling pathway",
"id": "GO:0038128",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0038128",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "signal complex assembly",
"id": "GO:0007172",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007172",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "uterus development",
"id": "GO:0060065",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0060065",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "branching involved in mammary gland duct morphogenesis",
"id": "GO:0060444",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0060444",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "negative regulation of telomerase activity",
"id": "GO:0051974",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0051974",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "regulation of cell projection assembly",
"id": "GO:0060491",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0060491",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cellular response to fatty acid",
"id": "GO:0071398",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0071398",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "positive regulation of male germ cell proliferation",
"id": "GO:2000256",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:2000256",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "interleukin-6-mediated signaling pathway",
"id": "GO:0070102",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070102",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cellular response to prolactin",
"id": "GO:1990646",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:1990646",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "progesterone receptor signaling pathway",
"id": "GO:0050847",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050847",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "skeletal muscle cell proliferation",
"id": "GO:0014856",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0014856",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "regulation of toll-like receptor 3 signaling pathway",
"id": "GO:0034139",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0034139",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
}
]
},
{
"name": "Cellular Component",
"total": 24,
"go_terms": [
{
"name": "glutamatergic synapse",
"id": "GO:0098978",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0098978",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "nucleoplasm",
"id": "GO:0005654",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005654",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cytoplasm",
"id": "GO:0005737",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005737",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "mitochondrion",
"id": "GO:0005739",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005739",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "mitochondrial inner membrane",
"id": "GO:0005743",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005743",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cytosol",
"id": "GO:0005829",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005829",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "actin filament",
"id": "GO:0005884",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005884",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "plasma membrane",
"id": "GO:0005886",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005886",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "focal adhesion",
"id": "GO:0005925",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005925",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "cell junction",
"id": "GO:0030054",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030054",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "extrinsic component of cytoplasmic side of plasma membrane",
"id": "GO:0031234",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0031234",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "neuronal cell body",
"id": "GO:0043025",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043025",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "membrane raft",
"id": "GO:0045121",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045121",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "perinuclear region of cytoplasm",
"id": "GO:0048471",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0048471",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "extracellular exosome",
"id": "GO:0070062",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0070062",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "lysosome",
"id": "GO:0005764",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005764",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "podosome",
"id": "GO:0002102",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0002102",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "late endosome",
"id": "GO:0005770",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005770",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "caveola",
"id": "GO:0005901",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005901",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "ruffle membrane",
"id": "GO:0032587",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0032587",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "synaptic membrane",
"id": "GO:0097060",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0097060",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "dendritic growth cone",
"id": "GO:0044294",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0044294",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "dendritic filopodium",
"id": "GO:1902737",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:1902737",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
},
{
"name": "postsynaptic specialization, intracellular component",
"id": "GO:0099091",
"url": "https://www.ebi.ac.uk/QuickGO/term/GO:0099091",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
}
],
"pmid": ""
}
]
}
]
},
"pro_annotation": [],
"site_annotation": [
{
"start_pos": 115,
"end_pos": 117,
"annotation": "n_glycosylation_sequon"
},
{
"start_pos": 290,
"end_pos": 292,
"annotation": "n_glycosylation_sequon"
},
{
"start_pos": 4,
"end_pos": 6,
"annotation": "n_glycosylation_sequon"
},
{
"start_pos": 68,
"end_pos": 70,
"annotation": "n_glycosylation_sequon"
}
],
"ptm_annotation": [
{
"annotation": "Dephosphorylated at Tyr-530 by PTPRJ (By similarity). Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-419. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-530, the SH3 domain engaged with the SH2-kinase linker, and Tyr-419 dephosphorylated. Dephosphorylation of Tyr-530 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-530, Tyr-419 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-530 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-75 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity. Phosphorylated by PTK2B/PYK2; this enhances kinase activity. Upon activation of IL6ST by IL6, Tyr-419 is phosphorylated and Tyr-530 dephosphorylated (PubMed:25731159).",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
},
{
"database": "PubMed",
"id": "6273838",
"url": "https://glygen.org/publication/PubMed/6273838"
},
{
"database": "PubMed",
"id": "22888118",
"url": "https://glygen.org/publication/PubMed/22888118"
},
{
"database": "PubMed",
"id": "21442427",
"url": "https://glygen.org/publication/PubMed/21442427"
},
{
"database": "PubMed",
"id": "14661060",
"url": "https://glygen.org/publication/PubMed/14661060"
},
{
"database": "PubMed",
"id": "25731159",
"url": "https://glygen.org/publication/PubMed/25731159"
},
{
"database": "PubMed",
"id": "18936167",
"url": "https://glygen.org/publication/PubMed/18936167"
},
{
"database": "PubMed",
"id": "7525268",
"url": "https://glygen.org/publication/PubMed/7525268"
}
]
},
{
"annotation": "Myristoylated at Gly-2, and this is essential for targeting to membranes.",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
},
{
"database": "PubMed",
"id": "7525268",
"url": "https://glygen.org/publication/PubMed/7525268"
}
]
},
{
"annotation": "Ubiquitinated in response to CDK5-mediated phosphorylation. Ubiquitination mediated by CBLC requires SRC autophosphorylation at Tyr-419 and may lead to lysosomal degradation.",
"evidence": [
{
"database": "UniProtKB",
"id": "P12931",
"url": "https://www.uniprot.org/uniprot/P12931"
},
{
"database": "PubMed",
"id": "6273838",
"url": "https://glygen.org/publication/PubMed/6273838"
},
{
"database": "PubMed",
"id": "22888118",
"url": "https://glygen.org/publication/PubMed/22888118"
},
{
"database": "PubMed",
"id": "14661060",
"url": "https://glygen.org/publication/PubMed/14661060"
},
{
"database": "PubMed",
"id": "18936167",
"url": "https://glygen.org/publication/PubMed/18936167"
}
]
}
],
"interactions": [],
"reactions": [
{
"id": "10596",
"name": "",
"equation": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]",
"summary": "",
"cellular_location": "",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
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"P57760-1",
"P35739-1",
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"O08680-1",
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"P54757-1",
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"Q64725-1",
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"P24062-1",
"Q924U5-1",
"Q63272-1",
"B2RYC7-1",
"P41243-1",
"M0RDA4-1",
"Q62838-1",
"Q63116-1",
"A0A8I6AM23-1",
"P50545-1",
"P57097-1",
"P97523-1",
"Q91ZT1-1",
"D4A7W7-1",
"F1LVI0-1",
"E9PSY0-1",
"A0A0G2K6M9-1",
"F1LSN4-1",
"F1MAJ0-1",
"A0A0R4J8U1-1",
"A0A8I6A5T6-1",
"D3ZDS3-1",
"D4ADZ5-1",
"F1LSG7-1",
"F1LRZ0-1",
"D3ZBN3-1",
"F1M0N1-1",
"G3V6K6-1",
"D3ZD03-1",
"D3ZZK3-1",
"E9PT20-1",
"D4A584-1",
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"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",
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"P32490-1",
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"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-112333",
"name": "SRC autophosphorylation is positively regulated by InlA-bound CDH1",
"equation": "",
"summary": "SRC activation involves autophosphorylation at tyrosine residue Y419 (Brown and Cooper 1996). Binding of the Listeria monocytogenes cell wall protein InlA to E-cadherin (CDH1) triggers SRC autophosphorylation at Y419 through an unknown mechanism (Sousa et al. 2007). CDH1 engagement (adhesion) at cell-cell contacts is also known to induce SRC autophosphorylation (Fujita et al. 2002, McLachlan et al. 2007) and may involve integrins (Avizienyte et al. 2002, Martinez-Rico et al. 2010), but the process has not been fully elucidated.",
"cellular_location": "cytosol, plasma membrane, peptidoglycan-based cell wall",
"input_participant_list": [
"R-HSA-8876922"
],
"output_participant_list": [
"R-HSA-1810408",
"R-LMO-8876505"
],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-112333",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-112333"
}
]
},
{
"id": "R-HSA-1252013",
"name": "Translocation of ERBB4s80 to the nucleus",
"equation": "",
"summary": "The soluble intracellular domain of ERBB4 s80 (E4ICD) is able to translocate from the cytosol to the nucleus (Ni et al. 2001). Translocation of ERBB4s80 to the nucleus is negatively regulated by binding of ERBB4s80 to activated SRC kinase (Ishibashi et al. 2012).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-1252013",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1252013"
}
]
},
{
"id": "R-HSA-177923",
"name": "Sustained activation of SRC kinase by SHP2",
"equation": "",
"summary": "SHP2 can dephosphorylate paxillin, which leads to CSK dissociation from the paxillin-SRC complex and SRC activation. SRC is an SHP2 effector in EGF-stimulated ERK activation and cell migration.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-180499"
],
"enzyme_list": [
"P41240-1",
"P00533-1",
"P12931-1",
"Q06124-2"
],
"evidence": [
{
"id": "R-HSA-177923",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-177923"
}
]
},
{
"id": "R-HSA-186819",
"name": "SH2 domain of Src binds to the active receptor",
"equation": "",
"summary": "The Src family of tyrosine kinases are characterized by a SH3 and a SH2 domain in addition to the kinase domain.Src is activated when the SH2 domain binds to autophosphorylation sites on PDGF receptors (Tyr579 and 581 in the beta-receptor, Tyr572 and 574 in the alpha receptor), in conjuction with dephosporylation of the COOH-terminal phosphorylated tyrosine 527.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P16234-1",
"P12931-1",
"P09619-1"
],
"evidence": [
{
"id": "R-HSA-186819",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-186819"
}
]
},
{
"id": "R-HSA-1963586",
"name": "SRC family kinases phosphorylate ERBB2",
"equation": "",
"summary": "Dissociation of HSP90 from ERBB2 upon formation of ERBB2 heterodimers (with either EGFR, ERBB3 or ERBB4) enables phosphorylation of ERBB2 on the tyrosine residue Y877, mediated by one of SRC family kinases - SRC, FYN or YES1. Although not a mandatory prerequisite of ERBB2 catalytic activity, the phosphorylation at Y877 significantly increases the kinase activity of ERBB2.",
"cellular_location": "cytosol, extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00533-1",
"P04626-1",
"P06241-1",
"P12931-1",
"P07947-1"
],
"evidence": [
{
"id": "R-HSA-1963586",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1963586"
}
]
},
{
"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-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-354066",
"name": "Translocation of PTK2 to Focal complexes",
"equation": "",
"summary": "As integrins do not have an intrinsic catalytic activity, the signals initiated by the ECM-integrin interactions are transduced into cells through the integrin bound protein-tyrosine kinases. PTK2 (protein-tyrosine kinase 2, also known as Focal adhesion kinase 1; FADK1, FAK) is one of the protein tyrosine kinases that plays a prominent role in integrin signaling. PTK2 has been implicated in controlling cell motility and transmitting a cell survival signal from ECM.
PTK2 is recruited to sites of integrin clustering by directly binding to integrin associated c-Src.
",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P61224-1",
"P62834-1",
"P12931-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-354066",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-354066"
}
]
},
{
"id": "R-HSA-354073",
"name": "Autophosphorylation of PTK2 at Y397",
"equation": "",
"summary": "The co-localization of PTK2/FAK with integrins in focal adhesions and the actin cytoskeleton is essential for the activation and phosphorylation of PTK2/FAK.
PTK2/FAK has six tyrosine phosphorylation sites and tyrosine 397 is the main auto-phosphorylation site present upstream of the kinase domain.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P61224-1",
"P62834-1",
"P12931-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-354073",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-354073"
}
]
},
{
"id": "R-HSA-354077",
"name": "Integrin alphaIIb beta3 activation",
"equation": "",
"summary": "The interaction between talin and integrin alphaIIb beta3 breaks the putative salt bridge between the alphaIIb (R995) and beta3 (D723) integrin chains and induces conformational changes in their external domains increasing their affinity for fibrinogen and other ECM ligands. Breaking of this salt bridge is necessary but not sufficient for full activation.
The Talin F3 subdomain of the FERM domain has a phosphotyrosine binding (PTB) domain fold. This domain interacts with the membrane-proximal (MP) region within the integrin beta3 chain. The primary function of this interaction is to provide an initial strong linkage between talin and integrin and this interaction holds the key to the molecular recognition required for activation. In platelets SRC kinase and its negative regulator CSK associates constitutively with integrin alphaIIbbeta3. SRC is involved in alphaIIbbeta3 dependent activation of SYK, and both SRC and SYK are required to initiate cytoskeletal events responsible for platelet spreading on fibrinogen.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-354077",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-354077"
}
]
},
{
"id": "R-HSA-354087",
"name": "Recruitment of GRB2 to p-PTK2",
"equation": "",
"summary": "Phosphorylated tyrosine 925 in the FAT domain of PTK2/FAK creates a docking site for the SH2 domain of GRB2 and recruits the GRB2/SOS complex. PTK2 may use this mechanism to activate Ras and the MAP kinase pathway.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-354128"
],
"enzyme_list": [
"P61224-1",
"P62834-1",
"P12931-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-354087",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-354087"
}
]
},
{
"id": "R-HSA-354124",
"name": "Phosphorylation of pPTK2 by SRC",
"equation": "",
"summary": "The recruitment of FADK1 to active SRC leads to the efficient tyrosine phosphorylation of multiple additional sites on FADK1. SRC trans-phosphorylates FADK1 within the kinase doman activation loop (Y576 and Y577) and within the FADK1 C-terminal domain (Y861 and Y925).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P61224-1",
"P62834-1",
"P12931-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-354124",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-354124"
}
]
},
{
"id": "R-HSA-354149",
"name": "Interaction of integrin alphaIIb beta3 with Fibrinogen",
"equation": "",
"summary": "The overall shape of integrins is that of a globular 'head' supported by two rod like legs. The ligand-binding pocket is formed by the combination of A-domain or beta-I domain on the beta3 subunit and the putative beta-propeller fold on the alphaIIb subunit in the head regions. The binding of ligand to integrin is also dependent on divalent cations (usually Mn++ or Mg++or Ca++). A conserved motif, the metal ion-dependant adhesion site (MIDAS) is located in the alpha and the beta chains that coordinate the divalent cation at the top of the domain.
Active integrin alphaIIb beta3 interacts with a variety of plasma proteins such as fibrinogen, vWF, thrombin, thrombospondin, and fibronectin. The ability of alphaIIbbeta3 to bind fibrinogen plays a crucial role in platelet aggregation and hemostasis. Most of these matrix proteins have integrin binding sites of 3-6 amino acids length, of which the best known are the 'RGD' and 'KGD' motifs. The alpha and beta integrin subunits are both required for ligand binding.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-354149",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-354149"
}
]
},
{
"id": "R-HSA-354165",
"name": "Interaction of SOS with GRB2 bound to FADK1",
"equation": "",
"summary": "Son of sevenless protein homolog 1(SOS) is an activating nucleotide exchange factor for H-Ras (p21Ras). SOS is brought close to the H-Ras by interacting with the FADK1 bound GRB2.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [
"R-HSA-64847"
],
"output_participant_list": [
"R-HSA-74686"
],
"enzyme_list": [
"P61224-1",
"P62834-1",
"P12931-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-354165",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-354165"
}
]
},
{
"id": "R-HSA-372693",
"name": "Phosphorylation of BCAR1 by SRC-PTK2 complex",
"equation": "",
"summary": "SH3-mediated binding of BCAR1/p130Cas to PTK2 is linked to enhanced tyrosine phosphorylation of BCAR1 at multiple sites. The Cas substrate domain contains 15 separate YxxP motifs, a main site of tyrosine phosphorylation on the BCAR1 molecule. Once phosphorylated, this domain serves as a docking site for the SH2 domains of CRK or NCK adaptor proteins that affect the downstream MAPK signalling pathway, resulting in cell survival and increased motility.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P61224-1",
"P62834-1",
"P12931-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-372693",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-372693"
}
]
},
{
"id": "R-HSA-372697",
"name": "Crk binding to p130cas",
"equation": "",
"summary": "Crk is an adaptor protein with one SH2 and two SH3 domains. It is involved in integrin mediated signalling and is recruited to the focal adhesion complexes by interacting with p130Cas or paxillin through its SH2 domain.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P61224-1",
"P62834-1",
"P12931-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-372697",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-372697"
}
]
},
{
"id": "R-HSA-372705",
"name": "Recruitment of BCAR1 to PTK2 complex",
"equation": "",
"summary": "BCAR1 (breast cancer anti-estrogen resistance protein1, also known as Crk-associated substrate (Cas) or p130Cas) is an adaptor protein that promotes protein-protein interactions, leading to the multiprotein complexes. The interaction of ?BCAR1/p130Cas with other proteins modulates cell motility, survial and proliferation. BCAR1/P130Cas is one of the main phosphorylation targets of the PTK2/SRC complex. The BCAR1 SH3 domain binds to PR1 and PR2 (\u2018PxxP\u2019) domains in the PTK2 C-terminal domain.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P61224-1",
"P62834-1",
"P12931-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-372705",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-372705"
}
]
},
{
"id": "R-HSA-373716",
"name": "DCC interacting NCK-1",
"equation": "",
"summary": "DCC interacts with the SH3/SH2 adaptor NCK1 in commissural neurons. This interaction is direct and requires the SH3 but not SH2 domains of NCK1. NCK1 can recruit Rac, Cdc42 and their effectors Pak and N-WASP to the activated receptor, thereby providing a direct link between DCC, Rho GTPases and numerous downstream signaling components that regulate the actin cytoskeleton.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-373716",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-373716"
}
]
},
{
"id": "R-HSA-374701",
"name": "Phosphorylation of DCC by Fyn",
"equation": "",
"summary": "Netrin-1 stimulates phosphorylation of DCC on serine, threonine, and tyrosine residues. The experimental data suggest that tyrosine phosphorylation of DCC is a prerequisite step for DCC phosphorylation on serine and threonine residues. Fyn initiates the phosphorylation of the tyrosine residue 1420 in the DCC cytoplasmic domain. This phosphorylation of DCC in turn facilitates the DCC-Fyn interaction, forming a positive reinforcement cycle.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-374701",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-374701"
}
]
},
{
"id": "R-HSA-377640",
"name": "Autophosphorylation of SRC",
"equation": "",
"summary": "Clustering of Integrin alphaIIb beta3 complexes results in the trans auto-phosphorylation of SRC tyrosine residue 419 (often referred to as 418 in the literature, as the initiating methionine is cleaved in the mature peptide) in SRC's kinase activation loop.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P61224-1",
"P62834-1",
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-377640",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-377640"
}
]
},
{
"id": "R-HSA-377641",
"name": "Clustering of Integrin alphaIIb beta3 complexes",
"equation": "",
"summary": "The fibrinogen-bound integrin alphaIIb beta3 clusters platelets together to form a platelet plug and generates intracellular signals (outside-in) causing further platelet activation and platelet plug retraction.
Intracellular integrin alphaIIb beta3 clustering brings SRCs bound to integrin beta3 chains into proximity. SRC associates constitutively with integrin alphaIIb beta3. In unstimulated cells this SRC is inactive, auto-inhibited by an internal interaction between phosphorylated Y530 and the SH2 domain. CSK is selective for the Y530 residue and prevents access to SRC of PTP1B, a protein tyrosine phosphatase that is capable of de-phosphorylating Y530.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-377641",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-377641"
}
]
},
{
"id": "R-HSA-377643",
"name": "Dephosphorylation of inactive SRC by PTPB1",
"equation": "",
"summary": "The integrin alphaIIb beta3:Inactive SRC complex recruits PTP1B protein tyrosine phosphatase resulting in the dephosphorylation of SRC tyrosine 530. The phosphorylated tail of SRC tail interacts with the SH2 domain thereby repressing kinase activity; removal of phosphorylation activates SRC kinase activity.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P61224-1",
"P62834-1",
"P12931-1",
"P18031-1"
],
"evidence": [
{
"id": "R-HSA-377643",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-377643"
}
]
},
{
"id": "R-HSA-377644",
"name": "Release of CSK from SRC",
"equation": "",
"summary": "CSK bound to integrin alphaIIb beta3 negatively regulates SRC by phosphorylating the Tyr-530. Platelet adhesion to fibrinogen causes the disassociation of CSK from alphaIIb beta3 complex.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-377644",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-377644"
}
]
},
{
"id": "R-HSA-380780",
"name": "Activation of Src",
"equation": "",
"summary": "Activation of Src kinases involves displacement of Tyr527 from the SH2 domain and phosphorylation of other tyrosine residues in the kinase domain. Src activation appears to be important for the mitogenic response of PDGF.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P16234-1",
"P12931-1",
"P09619-1"
],
"evidence": [
{
"id": "R-HSA-380780",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-380780"
}
]
},
{
"id": "R-HSA-389159",
"name": "CSF1R trans-autophosphorylates on multiple tyrosine and serine residues",
"equation": "",
"summary": "Following dimerization of the CSF-1 receptor (CSF1R), it undergoes trans-autophosphorylation on multiple tyrosine residues by its intrinsic kinase activity (Rohrschneider et al. 1997, Chihara et al. 2010). Tyrosine-561 (tyrosine-559 in the mouse homolog) in the juxtamembrane domain inhibits the kinase activity of CSF1R and is phosphorylated first, thus activating the kinase activity of CSF1R (inferred from the mouse homolog). Other tyrosine residues that are autophosphorylated are tyrosine-546 in the juxtamembrane domain, tyrosines-699,708,723 in the kinase insert domain, tyrosine-809 in the kinase domain, and tyrosines-923,969 in the C-terminal domain (Chihara et al. 2010, reviewed in Hamilton 1997, and inferred from the mouse homolog).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P22681-1",
"P07947-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-389159",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-389159"
}
]
},
{
"id": "R-HSA-418850",
"name": "Activation of Cdc42",
"equation": "",
"summary": "RhoGEF complexed with Netrin-1-DCC induces guanine nucleotide exchange by Cdc42, activating it. Activated Cdc42 activates N-WASP, which promotes the nucleation of F-actin via the Arp2/3 complex. Netrin-1, via DCC, influences cellular motility by regulating actin-based membrane extension through the activation of Cdc42.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"P60953-2",
"Q05397-1",
"O75962-1"
],
"evidence": [
{
"id": "R-HSA-418850",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-418850"
}
]
},
{
"id": "R-HSA-418856",
"name": "Activation of Rac1",
"equation": "",
"summary": "Rho GEF's DOCK180 and Trio directly associate with DCC, activate Rac-1 on DCC stimulation and cause cell spreading.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"P63000-1",
"Q05397-1",
"O75962-1"
],
"evidence": [
{
"id": "R-HSA-418856",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-418856"
}
]
},
{
"id": "R-HSA-418858",
"name": "RhoGTPase GEF's recruited to DCC",
"equation": "",
"summary": "When Netrin-1 binds to the DCC-NCK1 complex, a conformational change in NCK1 promotes interaction between the SH2 domain proteins, leading to recruitment and activation of RhoGEFs DOCK180 and Trio. These GEFs mediate Netrin-1 signaling in axon outgrowth and guidance through their ability to activate Rac1 and Cdc42.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"Q05397-1",
"O75962-1"
],
"evidence": [
{
"id": "R-HSA-418858",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-418858"
}
]
},
{
"id": "R-HSA-418859",
"name": "Phosphorylation of Unc5C",
"equation": "",
"summary": "Multiple sites on UNC5C are phosphorylated after NTN1 (netrin-1) stimulation. An activated SRC tyrosine kinase induces phosphorylation of UNC5C at multiple cytoplasmic tyrosine residues including highly-conserved residues 449, 454, 568, 649 and 667. Phosphorylation of these residues creates potential binding sites for cytoplasmic signaling proteins.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-418859",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-418859"
}
]
},
{
"id": "R-HSA-418865",
"name": "Recruitment of ABLIM to the plasma membrane",
"equation": "",
"summary": "Unc-115/AbLIM is a key regulator of lamellipodia and filopodia in the growth cone during axon pathfinding and acts downstream of Rac GTPase signaling. It acts as a scaffold to recruit other actin-modulating complexes involved in lamellipodia and filopodia. Unc-115/AbLIM is locally recruited to the plasma membrane by activated Rac1 and subsequently dephosphorylated on serine 617. Dephosphorylated Unc-115/AbLIM then might interact with other molecules at the plasma membrane to induce formation of lamellipodia and filopodia by reorganization of the actin cytoskeleton.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"P63000-1",
"Q05397-1",
"O75962-1"
],
"evidence": [
{
"id": "R-HSA-418865",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-418865"
}
]
},
{
"id": "R-HSA-418868",
"name": "Recruitment of Src and Fyn to DCC:FADK1",
"equation": "",
"summary": "Activated (phosphorylated) FADK1 acts as a scaffold and recruits src tyrosine kinases Src and Fyn to DCC. These tyrosine kinases phosphorylate DCC which is critical for Netrin-1 signaling.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-418868",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-418868"
}
]
},
{
"id": "R-HSA-418874",
"name": "Recruitment and activation of N-WASP by Cdc42",
"equation": "",
"summary": "The adaptor protein Nck-1 binds to DCC and recruits Rac-1, Cdc42 and their effectors PAK-1 and N-WASP to the activated receptor. Both Cdc42 and Nck-1 are activators of N-WASP. Cdc42 in its active GTP bound form binds to the CRIB domain of N-WASP and this interaction along with PIP2 results in the activation of N-WASP. Nck-1 activate N-WASP via binding of its SH3 domain to the proline rich domain of N-WASP. Nck-1 also possess an SH2 domain that associates directly with activated tyrosine kinase receptors which can phosphorylate N-WASP.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"P60953-2",
"Q05397-1",
"O75962-1"
],
"evidence": [
{
"id": "R-HSA-418874",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-418874"
}
]
},
{
"id": "R-HSA-429415",
"name": "SYK binds to integrin alphaIIb beta3",
"equation": "",
"summary": "Integrin alphaIIb beta3 'outside-in' signalling involves multiple proteins including SRC, SYK, SLP-76 and PLCgamma2. SRC is constitutively associated with the C-terminal tail of integrin beta 3. SYK is recruited to the beta3 tail and subsequently activated by SRC.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P61224-1",
"P62834-1",
"P12931-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-429415",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-429415"
}
]
},
{
"id": "R-HSA-429441",
"name": "SYK activation by SRC",
"equation": "",
"summary": "SYK activation in integrin signalling is associated with increased tyrosine phosphorylation. SYK activation and phosphorylation of SYK targets can be blocked by SRC inhibitors or expression of dominant negative SRC mutants.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P61224-1",
"P62834-1",
"P12931-1",
"P43405-1"
],
"evidence": [
{
"id": "R-HSA-429441",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-429441"
}
]
},
{
"id": "R-HSA-432096",
"name": "Activated integrin alphaIIb beta3 binds SHC1",
"equation": "",
"summary": "The beta 3 integrin cytoplasmic tail binds SH2-containing protein (SHC), an adapter in Ras signaling. Phosphorylation of Y785 may be necessary for binding; phosphorylation of T779 inhibits SHC binding. Mice expressing a mutated beta 3 where Y773 and Y785 have been mutated to F exhibit rebleeding from tail wounds and subtle defects in clot retraction and platelet aggregation.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-432096",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-432096"
}
]
},
{
"id": "R-HSA-443905",
"name": "SHC1 bound to integrin alphaIIb beta3 is phosphorylated somehow",
"equation": "",
"summary": "In a mechanism that is presumed to be analagous to signaling of SHC downstream of the insulin and TrkA receptors, SHC becomes phosphorylated and dissociates from the integrin alphaIIb beta3 complex.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-443905",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-443905"
}
]
},
{
"id": "R-HSA-443910",
"name": "SHC1 dissociates from integrin alphaIIb beta3",
"equation": "",
"summary": "In a mechanism that is presumed to be analagous to signaling of SHC downstream of the insulin and TrkA receptors, SHC becomes phosphorylated and dissociates from the integrin alphaIIb beta3 complex.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-443910",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-443910"
}
]
},
{
"id": "R-HSA-5672969",
"name": "Phosphorylation of RAF",
"equation": "",
"summary": "Downstream of RAF dimerization and allosteric activation, RAF monomers and KSR1 undergo a series of activating phosphorylations in both the activation loop (AL) and, in the case of ARAF, RAF1 and KSR1, in the NtA . Phosphorylation of the activation loop residues (T491, S494 in RAF1, T452, T455 in ARAF and T599, S602 in BRAF) contributes to full kinase activity, although this may be less critical for ARAF, and RAFs in general, than for other kinases due to their regulation by 14-3-3 binding (Zhu et al, 2005; Zhang et al, 2000; Baljuls et al, 2008, reviewed in Matallanas et al, 2011; Udell et al, 2011). AL phosphorylation may occur through cis-autophosphorylation within the RAF dimer, although phosphorylation by other kinases is also possible (Hu et al, 2013; reviewed in Matallanas et al, 2011).
Phosphorylation in the RAF NtA region is required for full kinase activity, for interaction with MAP2K substrates and for the ability of activated RAF to act as an allosteric activator of other RAF monomers (Marais et al, 1995; Diaz et al, 1997; Xiang et al, 2002; Edin et al, 2005; Hu et al, 2013; Mason et al, 1999). Phosphorylation of these residues (S338 and Y441 in RAF1, S299 and Y302 in ARAF and Y602 in KSR1) may be mediated by a kinase of the SRC, JAK or PAK family kinases, by MAP2K kinases, calmodulin kinase CaMKII or through autophosphorylation by RAF itself (Marais et al, 1995; Xia et al, 1996; King et al, 1998; Sun et al, 2000; Tran et al, 2003; Tran et al, 2005; Salzano et al. 2012, Hu et al, 2013; reviewed in Matallanas et al, 2011). The phosphorylated NtA of RAF1 is also the binding site for the negative regulator PEPB1, also known as RKIP. PEBP1 binding to RAF1 prevents phosphorylation of the MAP2K substrates (Park et al, 2006; Rath et al, 2008; reviewed in Shin et al, 2009).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"O60674-1",
"Q9UQM7-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"Q13554-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q13557-1",
"Q13555-1"
],
"evidence": [
{
"id": "R-HSA-5672969",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5672969"
}
]
},
{
"id": "R-HSA-5672972",
"name": "MAP2Ks and MAPKs bind to the activated RAF complex",
"equation": "",
"summary": "RAF kinases have restricted substrate specificity and have as their primary substrates the two MAP2K proteins MAP2K1 and MAP2K2 (also known as MEK1 and 2). MAP2K1 knockout is embryonic lethal in mice, while MAP2K2 knockouts have no apparent abnormalities, suggesting that MAP2K1 can compensate for MAP2K2 in vivo (Giroux et al, 1999; Belanger et al, 2003). MAP2K proteins exist as stable homo- and heterodimers independent of growth factor stimulation and are generally recruited to activated RAF proteins in conjunction with a scaffolding protein and the MAP2K substrates, MAPK1 and 3 (also known as ERK1 and 2) (Ohren et al, 2004; Catalanotti et al, 2009; Catling et al, 1995; reviewed in Matallanas et al, 2011; Roskoski et al, 2012a; Roskoski et al, 2012b).
Scaffolding proteins promote signaling by providing a docking platform that colocalizes components of the signaling cascade, and provide specificity by controlling the spatial and temporal regulation of the pathway (reviewed in Brown and Sacks, 2009; Matallanas et al, 2011). KSR1 and 2, CNKSR1 and 2, IQGAP1 and the beta arrestins are among the known MAPK scaffold proteins that act at the plasma membrane upon MAPK pathway activation; in addition, paxillin localizes MAPK pathway components to focal adhesion sites in the plasma membrane (Roy et al, 2005; Ren et al, 2007; DeFea et al, 2000; Togho et al, 2003; Ishibe et al, 2003; reviewed in Claperon and Therrien, 2007; Brown and Sacks, 2009; Matallanas et al, 2011). Although this reaction depicts these scaffolding proteins acting equivalently, the details of how they promote pathway activation vary. For instance, KSR1 and 2 are constitutively bound to MAP2K dimers but recruit MAPKs only upon pathway stimulation, while IQGAP1 associates constitutively with both MAP2K and MAPK proteins in unstimulated cells and shows increased interaction with MAP2K1 upon pathway activation by EGF (Stewart et al, 1999; Cacace et al, 2000; Muller et al, 2000; Roy et al, 2004; Roy et al, 2005; reviewed in Brown and Sacks, 2009). Scaffolding complexes may be particularly important for the phosphorylation of cytosolic MAPK targets (reviewed in Casar et al, 2009).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-5672972",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5672972"
}
]
},
{
"id": "R-HSA-5672973",
"name": "MAP2Ks phosphorylate MAPKs",
"equation": "",
"summary": "Activated MAP2K phosphorylates MAPK on threonine and tyrosine residues in the activation loop (residues T202 and Y204 in MAPK3, residues T185 and Y187 in MAPK1) (Ray et al, 1988; reviewed in Roskoski, 2012b). MAPK3 and MAPK1 are 84% identical and appear to be stimulated in parallel by all known activators of the MAPK pathway (Lefloch et al, 2009; reviewed in Lloyd, 2006).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-5672973",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5672973"
}
]
},
{
"id": "R-HSA-5672978",
"name": "RAF phosphorylates MAP2K dimer",
"equation": "",
"summary": "Activated RAF phosphorylates the MEK kinases MAP2K1 and MAP2K2 on 2 serine residues in the MAP2K activation loop (S218 and S222 in MAP2K1 and S222 and S226 in MAP2K2 (Zheng and Guan, 1994; Alessi et al, 1994; Catling et al, 1995; Papin et al, 1995; Seger et al, 1994; reviewed in Roskoski, 2012a). Although all three RAF kinases can phosphorylate MAP2K1 and MAP2K2, BRAF appears to be the primary activator in vivo (Marais et al, 1997; Jaiswal et al, 1994; Pritchard et al, 1995; reviewed in Welbrock et al, 2004)",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-5672978",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5672978"
}
]
},
{
"id": "R-HSA-5672980",
"name": "Dissociation of RAS:RAF complex",
"equation": "",
"summary": "The mechanisms governing the dissociation or trafficking of activated MAPK signaling complexes at the plasma membrane are not fully worked out. Some active complexes may be endocytosed and targeted to other cellular locations, for example the Golgi complex (Lorentzen et al, 2010). Activated RAF monomers may dissociate and homo- or heterodimerize with additional inactive RAF monomers and in this way amplify the signal (reviewed in Matallanas et al, 2011; Cseh et al, 2014).
Ultimately, active RAF complexes are subject to PP5- and PP2A-mediated dephosphorylation, which promotes a return to the inactive state. Hydrolysis of RAS-bound GTP by the intrinsic GTPase activity, stimulated by association with RAS GAP proteins, ultimately promotes dissociation of RAS from RAF allowing a return to the quiescent state (reviewed in Wellbrock et al, 2004; Matallanas et al, 2011).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-5672980",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-5672980"
}
]
},
{
"id": "R-HSA-6802910",
"name": "Activated MAP2Ks phosphorylate MAPKs downstream of high kinase activity BRAF mutants",
"equation": "",
"summary": "Highly active BRAF mutants show constitutive phosphorylation of MAPKs that does not depend on RAS activation or RAF dimerization (Davies et al, 2002; Wan et al, 2004; Garnett et al, 2005; reveiwed in Lavoie and Therrien, 2015).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-6802910",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802910"
}
]
},
{
"id": "R-HSA-6802911",
"name": "High kinase activity BRAF complexes phosphorylate MAP2Ks",
"equation": "",
"summary": "Highly active BRAF mutants such as V600E are constitutively active and phosphorylate MAP2Ks in a RAS- and dimer interface-independent manner (Davies et al, 2002; Wan et al, 2004; Garnett et al, 2005; Roring et al, 2012; Poulikakos et al, 2010; reviewed in Lavoie and Therrien, 2015).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-6802911",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802911"
}
]
},
{
"id": "R-HSA-6802912",
"name": "High kinase activity BRAF mutants bind MAP2Ks and MAPKs",
"equation": "",
"summary": "High-kinase activity BRAF mutants such as the prevalent V600E mutant bind MAP2K and MAPK proteins to activate signaling in a constitutive, RAS-independent manner (Wan et al, 2004; Garnett et al, 2005; Ritt et al, 2010; Roring et al, 2012; Freeman et al, 2013; reviewed in Lavoie and Therrien, 2015). These highly active BRAF mutations are thought to disrupt interactions between the DFG motif and the P loop that are required to hold RAF in the inactive, \\DFG out\\ conformation. In this way, BRAF V600E and other highly active BRAF mutations render the protein constitutively active (Wan et al, 2004; reviewed in Lito et al, 2013; Lavoie and Therrien, 2015). Although highly active BRAF mutants can heterodimerize with and signal through RAF1, V600E BRAF is resistant to disruptions in the dimerization interface, has relaxed requirements for RAF1 activation loop phosphorylation, and is able to signal as a monomer (Garnett et al, 2005; Ritt et al, 2010; Roring et al, 2012; Freeman et al, 2013; reviewed in Lavoie and Therrien, 2015; Lito et al, 2013).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-6802912",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802912"
}
]
},
{
"id": "R-HSA-6802914",
"name": "RAS:GTP:moderate kinase activity p-RAF complexes bind MAP2Ks and MAPKs",
"equation": "",
"summary": "RAF dimerization and phosphorylation downstream of moderately activating BRAF mutations is associated with increased MAP2K and MAPK phosphorylation (Wan et al, 2004; Freeman et al, 2013; Roring et al, 2012; reviewed in Holderfield et al, 2014; Lavoie and Therrien, 2015). Although the interactions between oncogenic RAS or RAFs and downstream effectors hasn't been studied in detail, these disease pathways are presumed to recruit MAP2Ks and MAPKs in a scaffold-dependent manner similar to WT (reviewed in Matallanas et al, 2011).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802914",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802914"
}
]
},
{
"id": "R-HSA-6802916",
"name": "RAF is phosphorylated downstream of moderate kinase activity BRAF mutants",
"equation": "",
"summary": "Homo- or heterodimerization (with RAF1, also known as CRAF) downstream of moderate kinase activity BRAF mutants leads to phosphorylation and activation of the 'receiver' kinase. Unlike the case for the highly active V600E BRAF mutation, pathway activation downstream of moderately activated BRAF mutants depends both on RAS binding and on dimerization (Wan et al, 2004; Roring et al, 2012; Freeman et al, 2013; reviewed in Samatar and Poulikakos, 2014; Lavoie and Therrien, 2015)
",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"O60674-1",
"Q9UQM7-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"Q13554-1",
"P01112-1",
"P36507-1",
"Q02750-1",
"Q13557-1",
"Q13555-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802916",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802916"
}
]
},
{
"id": "R-HSA-6802918",
"name": "Activated MAP2Ks phosphorylate MAPKs downstream of inactive BRAF mutants",
"equation": "",
"summary": "Downstream of kinase-dead or inhibited forms of BRAF, activated MAP2K phosphorylates MAPK on threonine and tyrosine residues in the activation loop (Wan et al, 2004; Garnett et al, 2005; Heidorn et al, 2010; Poulikakos et al, 2010; Hatzivassilliou et al, 2010; reviewed in Samatar and Poulikakos, 2014; Lavoie and Therrien, 2015).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802918",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802918"
}
]
},
{
"id": "R-HSA-6802919",
"name": "RAS:GTP:moderate kinase activity p-RAF complexes phosphorylate MAP2Ks",
"equation": "",
"summary": "Recruitment of MAP2Ks and MAPKs downstream of moderately activated BRAF mutants leads to phosphorylation and activation of MAP2Ks, as in the WT pathway (Wan et al, 2004; Freeman et al, 2013; Roring et al, 2012; reviewed in Lavoie and Therrien, 2015).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802919",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802919"
}
]
},
{
"id": "R-HSA-6802921",
"name": "Activated MAP2Ks phosphorylate MAPKs downstream of moderate kinase activity BRAF mutants",
"equation": "",
"summary": "MAPKs are phosphorylated downstream of moderately activated BRAF mutants in a MAP2K-dependent manner (Wan et al, 2004; Roring et al, 2012; Freeman et al, 2013; reviewed in Lavoie and Therrien, 2015).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802921",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802921"
}
]
},
{
"id": "R-HSA-6802922",
"name": "Activated MAP2Ks phosphorylate MAPKs downstream of oncogenic RAS",
"equation": "",
"summary": "MAPK proteins are phosphorylated downstream of oncogenic RAS mutants; somewhat surprisingly, however, steady state levels of phospho-MAP2K and phospho-MAPKs are not always elevated in cancer cells (reviewed in Ramos, 2008; Neuzillet et al, 2014; Stephen et al, 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802922",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802922"
}
]
},
{
"id": "R-HSA-6802924",
"name": "RAF is phosphorylated downstream of oncogenic RAS",
"equation": "",
"summary": "In many cancer types, RAF1 (also known as CRAF) appears to be a critical initial effector of the ERK pathway downstream of activated RAS and also mediates pathway activation in the presence of WT BRAF plus BRAF inhibitors (Rushworth et al, 2006; Dumaz et al, 2006; Garnett et al, 2005; Karreth et al, 2011; Poulikakos et al, 2010; Heidorn et al, 2010; Roring et al, 2012; reviewed in Samatar et al, 2014; Lito et al, 2013). This activation depends largely on heterodimerization with BRAF, although homodimers also contribute (Weber et al, 2001; Rushworth et al, 2006). Activation of RAF downstream of mutant RAS appears to require full phosphorylation of the N-region and the activation loop, unlike the case in BRAF mutant cells, where RAF N-loop phosphorylation is dispensable (Garnett et al, 2005).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"O60674-1",
"Q9UQM7-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"Q13554-1",
"P01112-1",
"P36507-1",
"Q02750-1",
"Q13557-1",
"Q13555-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802924",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802924"
}
]
},
{
"id": "R-HSA-6802925",
"name": "Mutant RAS:p-RAF complexes bind MAP2Ks and MAPKs",
"equation": "",
"summary": "RAF dimerization and phosphorylation downstream of oncogenic RAS and RAF mutations is associated with increased MAP2K and MAPK phosphorylation (Wan et al, 2004; Garnett et al, 2005; reviewed in Holderfield et al, 2014). Although the interactions between oncogenic RAS or RAFs and downstream effectors hasn't been studied in detail, these disease pathways are presumed to recruit MAP2Ks and MAPKs in a scaffold-dependent manner similar to WT (reviewed in Matallanas et al, 2011).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802925",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802925"
}
]
},
{
"id": "R-HSA-6802926",
"name": "Mutant RAS:p-RAF complexes phosphorylate MAP2Ks",
"equation": "",
"summary": "MAP2K proteins are phosphorylated downstream of oncogenic RAS mutants; somewhat surprisingly, however, steady state levels of phospho-MAP2K and phospho-MAPKs are not always elevated in cancer cells (reviewed in Ramos, 2008; Neuzillet et al, 2014; Stephen et al, 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802926",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802926"
}
]
},
{
"id": "R-HSA-6802927",
"name": "BRAF and RAF fusion mutant dimers are phosphorylated",
"equation": "",
"summary": "Fusion mutants of BRAF and RAF1 are believed to form constitutive dimers and activate downstream signaling independent of RAS and external stimuli (Jones et al, 2008; Cin et al, 2011; Palanisamy et al, 2010; Ciampi et al, 2005; Stransky et al, 2014; Hutchinson et al, 2013; Zhang et al, 2013; Lee et al, 2012; Ricarte-Filho et al, 2013; reviewed in Lavoie and Therrien et al, 2015). The RAF portion of the fusion mutants may undergo phosphorylation of the N-region and activation loops similar to WT as shown in this reaction, although this has not been studied in detail. While WT RAF phosphorylation happens in the context of a complex with with RAS, this is unlikely to be the case for the fusion mutants, as many of these proteins lack the N-terminal RAS binding domain (reviewed in Lavoie and Therrien, 2015).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"O15164-1",
"Q6ZMT4-1",
"O60674-1",
"Q9UQM7-1",
"P12931-1",
"Q53H12-1",
"P04049-1",
"P10398-1",
"P15056-1",
"Q13554-1",
"P36507-1",
"Q7KZF4-1",
"Q02750-1",
"Q13557-1",
"Q5XG87-1",
"Q13555-1"
],
"evidence": [
{
"id": "R-HSA-6802927",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802927"
}
]
},
{
"id": "R-HSA-6802932",
"name": "Dissociation of BRAF/RAF fusion complex",
"equation": "",
"summary": "After phosphorylation by MAP2Ks, the scaffolded kinase complex assembled by BRAF and RAF fusion dimers presumably dissociates, as is the case for WT complexes (Jones et al, 2008; Cin et al, 2011; Palanisamy et al, 2010; Ciampi et al, 2005; Stransky et al, 2014; Hutchinson et al, 2013; Zhang et al, 2013; Lee et al, 2012; Ricarte-Filho et al, 2013; reviewed in Lavoie and Therrien et al, 2015).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P27361-1",
"O15164-1",
"Q6ZMT4-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"Q53H12-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P36507-1",
"Q7KZF4-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"Q5XG87-1"
],
"evidence": [
{
"id": "R-HSA-6802932",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802932"
}
]
},
{
"id": "R-HSA-6802933",
"name": "p-BRAF and RAF fusion dimers phosphorylate MAP2Ks",
"equation": "",
"summary": "BRAF and RAF fusion dimers constitutively phosphorylate MAP2Ks (Jones et al, 2008; Cin et al, 2011; Palanisamy et al, 2010; Ciampi et al, 2005; Stransky et al, 2014; Hutchinson et al, 2013; Zhang et al, 2013; Lee et al, 2012; Ricarte-Filho et al, 2013; reviewed in Lavoie and Therrien et al, 2015).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P27361-1",
"O15164-1",
"Q6ZMT4-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"Q53H12-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P36507-1",
"Q7KZF4-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"Q5XG87-1"
],
"evidence": [
{
"id": "R-HSA-6802933",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802933"
}
]
},
{
"id": "R-HSA-6802934",
"name": "p-BRAF and RAF fusion dimers bind MAP2Ks and MAPKs",
"equation": "",
"summary": "BRAF and RAF fusion proteins expressed in cancer constitutively activate downstream signaling and promote cellular transformation (Jones et al, 2008; Cin et al, 2011; Palanisamy et al, 2010; Ciampi et al, 2005; Stransky et al, 2014; Hutchinson et al, 2013; Zhang et al, 2013; Lee et al, 2012; Ricarte-Filho et al, 2013; reviewed in Lavoie and Therrien et al, 2015). Recruitment of MAP2Ks and MAPKs to the fusion dimers may occur in conjunction with scaffold proteins as is the case for WT RAF dimers, however this has not been studied in detail.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"O15164-1",
"Q6ZMT4-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"Q53H12-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q7KZF4-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"Q5XG87-1"
],
"evidence": [
{
"id": "R-HSA-6802934",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802934"
}
]
},
{
"id": "R-HSA-6802935",
"name": "MAPKs are phosphorylated downstream of BRAF and RAF fusion dimers",
"equation": "",
"summary": "MAPKs are phosphorylated downstream of constitutively active BRAF and RAF fusion proteins (Jones et al, 2008; Cin et al, 2011; Palanisamy et al, 2010; Ciampi et al, 2005; Stransky et al, 2014; Hutchinson et al, 2013; Zhang et al, 2013; Lee et al, 2012; Ricarte-Filho et al, 2013; reviewed in Lavoie and Therrien et al, 2015).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P27361-1",
"O15164-1",
"Q6ZMT4-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"Q53H12-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P36507-1",
"Q7KZF4-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"Q5XG87-1"
],
"evidence": [
{
"id": "R-HSA-6802935",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802935"
}
]
},
{
"id": "R-HSA-6802941",
"name": "RAF is paradoxically phosphorylated downstream of kinase-inactive RAF",
"equation": "",
"summary": "The enhanced dimerization of inhibited or kinase dead versions of BRAF to RAF1/CRAF stimulates the phosphorylation and transactivation of RAF1 (Wan et al, 2004; Garnett et al, 2005; Heidorn et al, 2010; Poulikakos et al, 2010; Hatzivassiliou et al, 2010; reviewed in Samatar and Poulikakos, 2014; Lavoie and Therrien, 2015). Other evidence suggests that paradoxical activation of RAF1 by inhibited or inactive BRAF may result from relief of an inhibitory CRAF autophosphorylation event (Holderfield et al, 2013; reviewed in Holderfield, 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"O60674-1",
"Q9UQM7-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"Q13554-1",
"P01112-1",
"P36507-1",
"Q02750-1",
"Q13557-1",
"Q13555-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802941",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802941"
}
]
},
{
"id": "R-HSA-6802942",
"name": "RAS:GTP:p-RAF complexes paradoxically bind MAP2Ks and MAPKs",
"equation": "",
"summary": "Dimerization of kinase-dead or inhibited versions of BRAF to RAF1/CRAF leads to the recruitment and phosphorylation of MAP2Ks and MAPKs (Wan et al, 2004; Garnett et al, 2005; Heidorn et al, 2010; Poulikakos et al, 2010; Hatzivassiliou et al, 2010; reviewed in Samatar and Poulikakos, 2014; Lavoie and Therrien, 2015). Although the interactions haven't been studied in detail, these disease pathways are presumed to recruit MAP2Ks and MAPKs in a scaffold-dependent manner similar to WT (reviewed in Matallanas et al, 2011).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802942",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802942"
}
]
},
{
"id": "R-HSA-6802943",
"name": "RAS:GTP:inactive p-RAF complexes phosphorylate MAP2Ks",
"equation": "",
"summary": "As in the WT pathway, activation of ERK signaling downstream of kinase-dead or inhibited forms of BRAF depends on phosphorylation of two serine residues in the activation loop of the MAP2K proteins (Wan et al, 2004; Garnett et al, 2005; Heidorn et al, 2010; Poulikakos et al, 2010; Hatzivassiliou et al, 2010; reviewed in Samatar and Poulikakos, 2014; Lavoie and Therrien, 2015).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6802943",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6802943"
}
]
},
{
"id": "R-HSA-6803227",
"name": "Dissociation of high activity BRAF complexes",
"equation": "",
"summary": "After phosphorylation by MAP2Ks, the scaffolded kinase complex assembled by highly active BRAF mutants dissociates, as is the case for WT complexes (reviewed in Lavoie and Therrien et al, 2015).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-6803227",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6803227"
}
]
},
{
"id": "R-HSA-6803230",
"name": "Dissociation of moderate activity BRAF complexes",
"equation": "",
"summary": "After phosphorylation by MAP2Ks, the scaffolded kinase complex assembled by moderately active BRAF mutants dissociates, as is the case for WT complexes (reviewed in Lavoie and Therrien et al, 2015).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6803230",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6803230"
}
]
},
{
"id": "R-HSA-6803233",
"name": "Dissociation of oncogenic RAS:RAF complex",
"equation": "",
"summary": "After phosphorylation by MAP2Ks, the scaffolded kinase complex assembled by oncogenic RAS presumably dissociates, as is the case for WT complexes (reviewed in Lavoie and Therrien et al, 2015; Stephen et al, 2014).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6803233",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6803233"
}
]
},
{
"id": "R-HSA-6803234",
"name": "Dissociation of paradoxically activated RAS:BRAF complexes",
"equation": "",
"summary": "After phosphorylation by MAP2Ks, the scaffolded kinase complex assembled by kinase dead or inhibited BRAF mutants dissociates, as is the case for WT complexes (reviewed in Lavoie and Therrien et al, 2015).",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-6803234",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-6803234"
}
]
},
{
"id": "R-HSA-8874080",
"name": "SRC phosphorylates PTK2",
"equation": "",
"summary": "SRC phosphorylates PTK2 (FAK1) at tyrosine residues Y576 and Y577 in the activation loop of PTK2. Phosphorylation of PTK2 at Y576 and Y577 is required for the full catalytic activity of PTK2 (Calelb et al. 1995, Lietha et al. 2007) and is facilitated by MET-mediated phosphorylation of PTK2 at Y194. MET is able to phosphorylate PTK2 at Y576 and Y577 in vitro, in the absence of SRC (Chen et al. 2011).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"Q05397-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8874080",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8874080"
}
]
},
{
"id": "R-HSA-8874082",
"name": "MET phosphorylates PTK2",
"equation": "",
"summary": "Activated MET phosphorylates PTK2 (FAK1) at tyrosine residue Y194. Phosphorylation of PTK2 at Y194 facilitates SRC-mediated phosphorylation of PTK2 at Y577, but it has not been tested whether MET-mediated phosphorylation precedes SRC binding. MET may also phosphorylate PTK2 at Y5, although no functional significance of Y5 phosphorylation has been demonstrated. Activated EGFR and PDGFR can also phosphorylate PTK2 at Y5 and Y194 (Chen et al. 2011).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"Q05397-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8874082",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8874082"
}
]
},
{
"id": "R-HSA-8874083",
"name": "p-Y397-PTK2 binds SRC",
"equation": "",
"summary": "Phosphorylated tyrosine Y397 in the FERM domain of PTK2 (FAK1), along with an adjacent proline-rich motif, creates a docking site for the SRC kinase (Schaller et al. 1994, Xing et al. 1994, Thomas et al. 1998). It has not been specifically tested in this context whether PTK2 promotes SRC activation, and SRC is therefore represented in its active form.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"Q05397-1",
"P08581-1"
],
"evidence": [
{
"id": "R-HSA-8874083",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8874083"
}
]
},
{
"id": "R-HSA-8876948",
"name": "SRC phosphorylates InlA-bound CDH1 and CTNNB1",
"equation": "",
"summary": "SRC-mediated phosphorylation of E-cadherin (CDH1) is needed for InlA-mediated entry of Listeria monocytogenes into host cells (Bonazzi et al. 2008). At cell adhesion sites, SRC is known to phosphorylate CDH1 at tyrosine residues Y753 and Y754 and CDH1-bound beta-catenin (CTNNB1) at an unknown tyrosine residue. SRC-phosphorylated tyrosines of CDH1 and CTNNB1 serve as docking sites for the E3 ubiquitin ligase Hakai (CBLL1) (Fujita et al. 2002, Mukherjee et al. 2012).",
"cellular_location": "cytosol, plasma membrane, peptidoglycan-based cell wall",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-8876948",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8876948"
}
]
},
{
"id": "R-HSA-8937682",
"name": "RUNX1 binds SRC",
"equation": "",
"summary": "Based on studies in mouse megakaryocytes and T cells, RUNX1 forms a complex with SRC in the nucleus (Huang et al. 2012).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-8937682",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8937682"
}
]
},
{
"id": "R-HSA-8937728",
"name": "SRC phosphorylates RUNX1",
"equation": "",
"summary": "Based on studies in developing mouse megakaryocytes and T cells, SRC phosphorylates RUNX1 at seven tyrosine residues in the negative regulatory domain (Y254, Y258, Y260, Y376, Y379, Y380 and Y387). Endogenous human RUNX1 is tyrosine phosphorylated, and tyrosine residues in murine Runx1 that are phosphorylated by Src are conserved in human RUNX1. SRC-mediated phosphorylation interferes with binding of RUNX1 to GATA1, thus negatively regulating differentiation of hematopoietic progenitors. SRC-mediated phosphorylation promotes association of RUNX1 with the SWI/SNF complex (Huang et al. 2012).",
"cellular_location": "nucleoplasm",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-8937690",
"R-HSA-8937712"
],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-8937728",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8937728"
}
]
},
{
"id": "R-HSA-8937792",
"name": "RUNX3 binds SRC",
"equation": "",
"summary": "Activated SRC binds to RUNX3 in the cytosol. The interaction involves the Runt domain of RUNX3 (Goh et al. 2010).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-8937792",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8937792"
}
]
},
{
"id": "R-HSA-8937807",
"name": "SRC phosphorylates RUNX3",
"equation": "",
"summary": "Activated SRC phosphorylates RUNX3 in the cytosol, on multiple tyrosine residues. There are eleven tyrosine residues in RUNX3, but SRC target sites have not been determined. SRC-mediated phosphorylation of RUNX3 inhibits translocation of RUNX3 to the nucleus and is the underlying cause of cytosolic localization of RUNX3 in gastric and breast cancer (Goh et al. 2010).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-8937805"
],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-8937807",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8937807"
}
]
},
{
"id": "R-HSA-8937814",
"name": "RUNX3 translocates to the nucleus",
"equation": "",
"summary": "Translocation of RUNX3 from the cytosol to the nucleus is stimulated by TGF-beta (TGFB1) treatment (Ito et al. 2005) and inhibited by SRC-mediated phosphorylation of RUNX3 on multiple tyrosine residues (Goh et al. 2010).",
"cellular_location": "cytosol, nucleoplasm",
"input_participant_list": [
"R-HSA-8937797"
],
"output_participant_list": [
"R-HSA-8865393"
],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-8937814",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8937814"
}
]
},
{
"id": "R-HSA-8937820",
"name": "SRC,YES1 bind YAP1",
"equation": "",
"summary": "Based on studies in rat osteosarcoma cell line, activated SRC and YES1 form a complex with YAP1 (Zaidi et al. 2004).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"P07947-1"
],
"evidence": [
{
"id": "R-HSA-8937820",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8937820"
}
]
},
{
"id": "R-HSA-8937844",
"name": "SRC,YES1 phosphorylate YAP1",
"equation": "",
"summary": "Based on studies in rat, activated SRC and/or YES1 tyrosine kinases phosphorylate YAP1 on an unknown tyrosine residue (Zaidi et al. 2004).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [
"R-HSA-8937843"
],
"enzyme_list": [
"P12931-1",
"P07947-1"
],
"evidence": [
{
"id": "R-HSA-8937844",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8937844"
}
]
},
{
"id": "R-HSA-8964242",
"name": "G protein alpha (i)-SRC complex catalyzes SRC to p-Y419-SRC",
"equation": "",
"summary": "G-Protein Coupled Receptors sense extracellular signals and activate different Guanine nucleotide binding proteins. Upon activation, the alpha subunit of the G protein (GNAI) can directly bind to SRC. In the presence of active GNAI, SRC can autophosphorylate the 419-tyrosine residue, which leads to the subsequent activation of SRC. Physiologically, the SRC family have implications in cell growth and cancer.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-8964242",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964242"
}
]
},
{
"id": "R-HSA-8964252",
"name": "G alpha (s):GTP:SRC catalyzes SRC to p-Y419-SRC",
"equation": "",
"summary": "G-Protein Coupled Receptors sense extracellular signals and activate different Guanine nucleotide binding proteins. Upon activation, the alpha subunit of the G protein (GNAS) can directly bind to SRC. In the presence of active GNAS, SRC can autophosphorylate the 419-tyrosine residue, which leads to the subsequent activation of SRC. Physiologically, the SRC family have implications in cell growth and cancer. GNAS increases SRC enzymatic activity by decreasing Km and not affecting Vm.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-8964252",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964252"
}
]
},
{
"id": "R-HSA-8964278",
"name": "G protein alpha (s):GTP binds SRC",
"equation": "",
"summary": "G-Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins. Upon activation, the Guanine nucleotide-binding protein G(s) subunit alpha (GNAS) can bind directly to proto-oncogene tyrosine-protein kinase Src (SRC) in vitro and in vivo. This binding results in autophosphorylation of SRC and subsequently its activation. Physiologically, the SRC family have implications in cell growth and cancer.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-8964278",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964278"
}
]
},
{
"id": "R-HSA-8964287",
"name": "G alpha (s):GTP:SRC dissociates",
"equation": "",
"summary": "Upon autophosphorylation, SRC dissociates from GNAS and is subsequently activated. GNAS increases SRC enzymatic activity by decreasing Km and not affecting Vm. Physiologically, the SRC family have implications in cell growth and cancer.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-8964287",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964287"
}
]
},
{
"id": "R-HSA-8964311",
"name": "G alpha (i):GTP binds SRC",
"equation": "",
"summary": "G-Protein Coupled Receptors (GPCR) sense extracellular signals and activate different Guanine nucleotide binding proteins. Upon activation, the Guanine nucleotide-binding protein G(i) subunit alpha (GNAI) can bind directly to proto-oncogene tyrosine-protein kinase Src (SRC) in vitro and in vivo. This binding results in autophosphorylation of SRC and subsequently its activation. Physiologically, the SRC family have implications in cell growth and cancer.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-8964311",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964311"
}
]
},
{
"id": "R-HSA-8964329",
"name": "G protein alpha (i)-SRC complex dissociates to G protein alpha (i) and Active SRC",
"equation": "",
"summary": "G-Protein Coupled Receptors sense extracellular signals and activate different Guanine nucleotide binding proteins. Upon activation, the Guanine nucleotide-binding protein G(i) subunit alpha (GNAI) can directly bind to proto-oncogene tyrosine-protein kinase Src (SRC). When bound to active GNAI, SRC can autophosphorylate the 416-tyrosine residue. Upon autophosphorylation, SRC dissociates from GNAI and is subsequently activated. GNAI increases SRC enzymatic activity by decreasing Km and not affecting Vm. Physiologically, the SRC family have implications in cell growth and cancer.",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-8964329",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8964329"
}
]
},
{
"id": "R-HSA-9011241",
"name": "SRC phosphorylates ROBO3.1 in response to NTN1",
"equation": "",
"summary": "In response to NTN1 (netrin-1)-mediated activation of DCC, based on mouse studies, SRC phosphorylates ROBO3.1 on a conserved tyrosine Y1019. The mechanism of SRC recruitment to ROBO3.1 in response to NTN1 is not known (Zelina et al. 2014). The biological significance of SRC-mediated phosphorylation of ROBO3.1 is not known.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-9011241",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9011241"
}
]
},
{
"id": "R-HSA-9021596",
"name": "Membrane estrogen receptors bind SRC",
"equation": "",
"summary": "Rapid signaling downstream of estrogen stimulation activates signaling through MAP kinase and PI3K/AKT signaling pathways, as well as initiating cross-talk with NF kappa beta and receptor tyrosine kinase pathways (reviewed in Hammes et al, 2007; Handa et al, 2012; Lange et al, 2017; Losel et al, 2003). Signaling through AKT regulates cell cycle progression through CREB-mediated upregulation of cyclin D1 and depends on recruitment of SRC and the p85 regulatory subunit of PI3K (Castoria et al, 2001; Marino et al, 2002; Marino et al, 2003; Castoria et al, 2012; reviewed in Castoria et al, 2010). Estrogen-stimulated nitric oxide (NO) release from endothelial cells likewise depends on the recruitment of SRC to the estrogen receptors at the plasma membrane (Haynes et al, 2003).
Once recruited, SRC is activated by autophosphorylation at tyrosine 419, which in turn is required for the recruitment and activation of PI3K and AKT, and ultimately for the activation of endothelial nitric oxide synthase (eNOS) and promotion of AKT-dependent cellular proliferation (Haynes et al, 2000; Simoncini et al, 2000; Haynes et al, 2003; Li et al, 2007; reviewed in Kim and Bender, 2005; Hammes and Levin, 2011; Le Romancer et al, 2011: Castoria et al, 2010). Formation of an eNOS signaling complex also depends on interaction between the estrogen receptor and heterotrimeric G-proteins (Wyckoff et al, 2001; reviewed in Schwartz, 2016).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-9021596",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9021596"
}
]
},
{
"id": "R-HSA-9021609",
"name": "ESR-associated SRC autophosphorylates",
"equation": "",
"summary": "Estrogen treatment stimulates autophosphorylation of SRC at tyrosine 419 (Haynes et al, 2003). SRC catalytic activity is required for signaling to PI3K, AKT and eNOS, as both a kinase dead version of SRC and treatment of cells with a SRC inhibitor abrogate phosphorylation of these downstream targets. SRC interacts with the p85 regulatory subunit of PI3K and in this way promotes assembly of an estrogen-responsive signaling complex in the caveolae (Simoncini et al, 2000; Hayes et al, 2003; Castoria et al, 2001; Castoria et al, 2012; Le Romancer et al, 2008).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-9021609",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9021609"
}
]
},
{
"id": "R-HSA-9021660",
"name": "PI3K binds membrane-associated estrogen receptors",
"equation": "",
"summary": "PI3K is recruited to the estrogen receptors at the plasma membrane by virtue of an estrogen-dependent interaction of the p85 regulatory subunit with the estrogen receptor. Estrogen stimulation increases PI3K activity in a manner that also depends on SRC and SRC kinase activity, and results in increased PIP3 production and activation of AKT signaling (Simoncini et al, 2000; Castoria et al, 2001; Castoria et al, 2012; Le Romancer et al, 2008). Activation of AKT signaling downstream of estrogen stimulation drives cellular proliferation through the upregulation of the G1/S cyclin CCND1 (Castoria et al, 2001; Castoria et al, 2004; reviewed in Castoria et al, 2010), and E2 is also required for recruitment of focal adhesion kinase (FAK, also known as PTK2) (Le Romancer et al, 2008). AKT activation additionally stimulates phosphorylation of eNOS at residue 1117, promoting NO release in endothelial cells (Simoncini et al, 2000; Haynes et al, 2000; Hisamoto et al, 2001; Li et al, 2003; Haynes et al, 2003; reviewed in Levin, 2011).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-9021660",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9021660"
}
]
},
{
"id": "R-HSA-9037040",
"name": "SRC,FYN phosphorylate NTRK2",
"equation": "",
"summary": "Activated SRC and, probably FYN, can phosphorylate NTRK2 (TRKB) on tyrosine residues Y706 and Y707 in the absence of ligand binding, thus increasing the catalytic activity of NTRK2 (Huang and McNamara 2010).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [
"R-HSA-6798236"
],
"output_participant_list": [
"R-HSA-9037044"
],
"enzyme_list": [
"Q16620-1",
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-9037040",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9037040"
}
]
},
{
"id": "R-HSA-9603419",
"name": "Activated NTRK3 binds SRC",
"equation": "",
"summary": "Endogenous SRC binds to endogenous, activated, NTRK3 (TRKC) in both human and mouse cells (Jin et al. 2008)",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"Q16288-1"
],
"evidence": [
{
"id": "R-HSA-9603419",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9603419"
}
]
},
{
"id": "R-HSA-9603420",
"name": "Activated NTRK3 promotes SRC autophosphorylation",
"equation": "",
"summary": "Binding of SRC to activated NTRK3 (TRKC) promotes activating SRC autophosphorylation (Jin et al. 2008).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"Q16288-1"
],
"evidence": [
{
"id": "R-HSA-9603420",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9603420"
}
]
},
{
"id": "R-HSA-9603437",
"name": "Activated NTRK3 binds IRS1",
"equation": "",
"summary": "Activated wild-type NTRK3 (TRKC), as well as constitutively active ETV6-NTRK3 oncogene, a product of translocation between ETV6 and NTRK3 gene loci in congenital fibrosarcoma and cellular mesoblastic nephroma, are able to bind to adaptor protein IRS1 (Morrison et al. 2002, Lannon et al. 2004, Jin et al. 2008). Binding of IRS1 to NTRK3 is enhanced in the presence of SRC (Jin et al. 2008).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1",
"Q16288-1"
],
"evidence": [
{
"id": "R-HSA-9603437",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9603437"
}
]
},
{
"id": "R-HSA-9603445",
"name": "Activated NTRK3 stimulates PI3K activity",
"equation": "",
"summary": "Activation of PI3K signaling downstream of NTRK3 (TRKC) is evident from PI3K-dependent activating phosphorylation of AKT in response to NTRK3 activity. SRC and IRS1 contribute to NTRK3-mediated induction of PI3K activity, but the exact mechanism is not known (Tognon et al. 2001, Jin et al. 2008).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P12931-1",
"Q16288-1"
],
"evidence": [
{
"id": "R-HSA-9603445",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9603445"
}
]
},
{
"id": "R-HSA-9612085",
"name": "SRC phosphorylates GluN2 (GRIN2) subunits of NMDARs",
"equation": "",
"summary": "Non-receptor tyrosine kinase SRC phosphorylates GluN2 (GRIN2, NR2) subunits of the GluN2-containing NMDA receptors. This increases NMDA receptor open time and activity (Yu et al. 1997) and plays a role in long-term potentiation. SRC-mediated phosphorylation of NMDA receptors (NMDARs) is reduced in schizophrenia. Activation of ERBB4 signaling negatively regulates phosphorylation of NMDARs by SRC. ERBB4 signaling is hyperactivated in schizophrenia (Pitcher et al. 2011, Banerjee et al. 2015).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"Q9UQM7-1",
"P12931-1",
"Q13554-1",
"Q13557-1",
"Q13555-1"
],
"evidence": [
{
"id": "R-HSA-9612085",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9612085"
}
]
},
{
"id": "R-HSA-9612219",
"name": "ERBB4s80 binds to SRC",
"equation": "",
"summary": "SRC tyrosine kinase, activated by EGFR signaling, binds to the cleaved intracellular fragment of ERBB4, ERBB4s80 (E4ICD), released in response to ERBB4 activation by NRG1. Tyrosine phosphorylation of ERBB4s80 is needed for SRC binding. It is not clear whether tyrosine phosphorylation sites are auto-phosphorylated or phosphorylated by SRC. SRC binding prevents translocation of ERBB4s80 to the nucleus (Ishibashi et al. 2012).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-9612219",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9612219"
}
]
},
{
"id": "R-HSA-9624014",
"name": "SHC1 is phosphorylated downstream of estrogen stimulation of GPER1",
"equation": "",
"summary": "E2 treatment stimulates phosphorylation of MAPK3 and MAPK1 (also known as ERK1 and ERK2) downstream of GPER1 in a SRC- and G-protein beta gamma complex-dependent manner (Filardo et al, 2000; Quin et al, 2009). ERK phosphorylation through this pathway is mediated by SRC-dependent phosphorylation of the SHC adaptor protein, consistent with G beta gamma signaling in other pathways (Filardo et al, 2000; Quinn et al, 2009; Touhara et al, 1995; van Biesen et al, 1995; Luttrell et al, 1996; reviewed in Filardo and Thomas, 2012). Estrogen-dependent signaling through the G beta gamma -SRC -SHC module establishes crosstalk with integrin alpha5beta2 pathway and ultimately cross-talks with EGFR signaling, activating MAPK phosphorylation (reviewed in Filardo and Thomas, 2012; Prossnitz and Barton, 2014; Gaudet et al, 2015; Filardo et al, 2018). The mechanisms by which SRC and G beta gamma impinge on SHC phosphorylation are not fully elucidated, and direct phosphorylation of SHC by SRC has not been demonstrated in this pathway.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-9624014",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9624014"
}
]
},
{
"id": "R-HSA-9632412",
"name": "PTK2 is recruited to methylated ESR1",
"equation": "",
"summary": "PTK2 (also known as FAK) is co-immunoprecipitated with methylated ESR1 and PI3K after stimulation with estrogen. This interaction depends on ESR1 methylation and on SRC activity, as it is abrogated in the presence of SRC inhibitors or upon PRMT1 depletion (Le Romancer et al, 2008). Phosphorylation of PTK2 appears to be dynamic, as it is lost within 15 minutes of estrogen stimulation, promoting disassembly of the complex. Interaction with PTK2 may contribute to estrogen-stimulated cell motility.",
"cellular_location": "cytosol",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P42336-1",
"P12931-1",
"Q05397-1"
],
"evidence": [
{
"id": "R-HSA-9632412",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9632412"
}
]
},
{
"id": "R-HSA-9656209",
"name": "Dissociation of RAS:RAF1 mutant complex",
"equation": "",
"summary": "After phosphorylation of MAPKs by complexes containing RAF1 mutants, activated MAPK signaling complexes dissociate in a manner similar to wildtype, although this has not been explicitly demonstrated in all cases. Active complexes may signal from other cellular locations or may amplify signaling through rounds of heterodimerization with other inactive RAF monomers (reviewed in Matallanas et al, 2011; Cseh et al, 2014).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-9656209",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9656209"
}
]
},
{
"id": "R-HSA-9656211",
"name": "MAP2Ks and MAPKs bind to the activated mutant RAF1 complex",
"equation": "",
"summary": "MAP2K and MAPK proteins are likely recruited to complexes containing mutant versions of RAF1 proteins, analagous to the wild type pathway, although this has not been explicitly demonstrated in all cases (reviewed in Rauen, 2013).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-9656211",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9656211"
}
]
},
{
"id": "R-HSA-9656212",
"name": "Phosphorylation of RAF1 mutants",
"equation": "",
"summary": "RAF1 mutants in cancer and germline disorders such as Noonan syndrome undergo enhanced dimerization and activation with BRAF, leading to high levels of downstream signaling. This has been observed even in cases of RAF1 mutations with abrogated or impaired kinase activity (Razzaque et al, 2007; Pandit et al, 2007; Kobayashi et al, 2010; Wu et al, 2012; Krauthammer et al, 2015; reviewed in Rauen, 2013).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"O60674-1",
"Q9UQM7-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"Q13554-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q13557-1",
"Q13555-1"
],
"evidence": [
{
"id": "R-HSA-9656212",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9656212"
}
]
},
{
"id": "R-HSA-9656214",
"name": "MAP2Ks phosphorylate MAPKs downstream of RAF1 mutants",
"equation": "",
"summary": "MAPK proteins are phosphorylated downstream of RAF1 mutants (Razzaque et al, 2007; Pandit et al, 2007; Kobayashi et al, 2010; Wu et al, 2012).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-9656214",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9656214"
}
]
},
{
"id": "R-HSA-9656215",
"name": "RAF1 mutant complexes phosphorylate MAP2K dimer",
"equation": "",
"summary": "MAPK2Ks are phosphorylated downstream of mutant RAF1 proteins (Razzaque et al, 2007; Pandit et al, 2007; Kobayashi et al, 2010; Wu et al, 2012).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-9656215",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9656215"
}
]
},
{
"id": "R-HSA-9657599",
"name": "Dual mechanism MAP2K inhibitors bind MAP2Ks",
"equation": "",
"summary": "Although mutations in MAP2K proteins are infrequent in human cancers, the position of these kinases downstream of RAS and RAF make them good candidates for therapeutic targeting. Dual mechanism inhibitors such as trametinib bind to non-phosphorylated MAP2K proteins, inhibiting their MAPK-directed kinase activity as well as preventing their phosphorylation by RAF proteins (Hatzivassiliou et al, 2013; Lito et al, 2014; Ishii et al, 2013; reviewed in Samatar and Poulikakos, 2014).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-9657599",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9657599"
}
]
},
{
"id": "R-HSA-9657603",
"name": "Dual mechanism MAPK inhibitors bind MAPKs",
"equation": "",
"summary": "A number of 'dual mechanism' MAPK inhibitors are in preclinical or clinical trials (reviewed in Roskoski, 2019). Dual mechanism inhibitors, including the ATP-competitive inhibitors SCH772984 and MK-8353, bind to the unphosphorylated MAPK and prevent both its own kinase activity and its phosphorylation by MAP2Ks (Morris et al, 2013; Deng et al 2014; Chaikuad et al, 2014; Boga et al, 2018; Moschos et al, 2019; reviewed in Samatar and Poulikakos, 2014). MAPK inhibitors offer the potential to mitigate the development of resistance to RAF and MAP2K inhibitors, which often involves reactivation of MAPK-dependent signaling. As a result, MAPK inhibitors are frequently used in combination with RAF and MAP2K-directed therapeutics (reviewed in Samatar and Poulikakos, 2014; Roskoski, 2019).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-9657603",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9657603"
}
]
},
{
"id": "R-HSA-9657606",
"name": "Single mechanism MAP2K inhibitors bind phosphorylated MAP2Ks",
"equation": "",
"summary": "Single mechanism MAP2K inhibitors bind to phosphorylated forms of MAP2K 1 and 2 and prevent their phosphorylation of MAPK proteins (Hatzivassiliou et al, 2013; reviewed in Samatar and Poulikakos, 2014).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-9657606",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9657606"
}
]
},
{
"id": "R-HSA-9657608",
"name": "Single mechanism MAPK inhibitors bind phosphorylated MAPK",
"equation": "",
"summary": "Single mechanism MAPK inhibitors such as ulixertinib and ravoxertinib bind to the activated forms of MAPK proteins and inhibit their intrinsic target-directed kinase activity (Germann et al, 2017; Blake et al, 2016; reviewed in Samatar and Poulikakos, 2014).",
"cellular_location": "cytosol, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P01111-1",
"P27361-1",
"P41240-1",
"P61224-1",
"P62834-1",
"P12931-1",
"P04049-1",
"P10398-1",
"P15056-1",
"P27448-5",
"P60709-1",
"P63261-1",
"P28482-1",
"P01112-1",
"P36507-1",
"Q8IVT5-1",
"Q02750-1",
"Q6VAB6-1"
],
"evidence": [
{
"id": "R-HSA-9657608",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9657608"
}
]
},
{
"id": "R-HSA-9680348",
"name": "PIK3R1:PIK3CA,B,G (PI3K), PLCG2 (PLCgamma2), SHC1 (SHC), PTPN11 (SHP2), GRB2:GAB2, GRB2:GAB3, GRAP2 (MONA), CBL:GRB2, INPP5D (SHIP1), INPPL1 (SHIP2) bind PolyUb,p-8Y-CSF1R and are activated",
"equation": "",
"summary": "The PIK3R1 (p85alpha) subunit of phosphatidylinositol 3-kinase (PI3K) is phosphorylated and binds CBL and CSF1R (inferred from mouse homologs). CBL also directly binds phosphorylated CSF1R (inferred from mouse homologs). GRB2:SOS1 transiently interacts with CSF1R (inferred from mouse homologs) and PI3K (Saleem et al. 1995) in response to CSF1. SHC1 (SHC) interacts with CBL and CSF1R (inferred from mouse homologs). CBL is constitutively bound to GRB2, CBL is phosphorylated, and phosphorylated CBL binds phosphorylated SHC (inferred from mouse homologs). PLCG2 (PLC-gamma2), expressed in the myeloid lineage, binds phosphorylated tyrosine-723 of CSF1R and PLCG2 is phosphorylated in a process that requires the activity of PI3K (inferred from mouse homologs). GRAP2 (MONA) binds phosphorylated tyrosine-699 of CSF1R. GRB2 also interacts with CSF1R (Kharbanda et al. 1995) via phosphotyrosine-699 ( inferred from mouse homologs). GRAP2 binds GAB3, which is then phosphorylated (inferred from mouse homologs). In response to CSF1, the scaffolding protein GAB2 associates with INPP5D (SHIP1) and other proteins involved in CSF1 signaling and GAB2 is phosphorylated directly or indirectly by CSF1R (inferred from mouse homologs). INPPD5D also interacts with the kinase LYN (Baran et al. 2003). INPPL1 (SHIP2), a homolog of INPPD5, binds CSF1R in response to CSF1 (inferred from mouse homologs). GAB3, a homolog of GAB2, associates with CSF1R, is phosphorylated, and interacts with PI3K and PTPN11 (SHP2) (inferred from mouse homologs). The SRC family kinases SRC, FYN, and YES1 (YES) bind phosphorylated CSF1R (Courtneidge et al. 1993, Li et al. 1997, also inferred from mouse homologs). STAT proteins STAT1 and STAT3 bind CSF1R and are phosphorylated (inferred from mouse homologs). STAT5 also appears to be phosphorylated in response to CSF1 (Knowlton et al. 2010). THOC5 (FMIP) binds CSF1R and is phosphorylated (inferred from mouse homologs). The order of binding and phosphorylation of the interactors of CSF1R is unknown. Different subpopulations of CSF1R may be bound to different sets of interactors (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [
"R-HSA-197940",
"R-HSA-202367",
"R-HSA-354251",
"R-HSA-200917",
"R-HSA-9628701",
"R-HSA-373640",
"R-HSA-913354",
"R-HSA-9682751"
],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P42336-1",
"P48736-1",
"P06241-1",
"P12931-1",
"P22681-1",
"O15357-1",
"P07947-1",
"P07948-1",
"P16885-1",
"Q06124-2",
"P08631-1",
"P42338-1",
"Q92835-1"
],
"evidence": [
{
"id": "R-HSA-9680348",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9680348"
}
]
},
{
"id": "R-HSA-9680385",
"name": "CSF1R-associated SOS1 mediates exchange of GTP for GDP bound to RAS",
"equation": "",
"summary": "SOS1 (SOS) is stably bound to GRB2, which transiently associates with phosphorylated CSF1R. In response to the activation of CSF1R by CSF1, SOS1 promotes RAS to exchange of GDP for GTP (inferred from mouse homologs) and thereby activates the RAS-RAF-MEK-ERK1,2 signaling pathway. Myeloid cells contain the KRAS isoform of RAS. KRAS:GTP enhances proliferation of macrophages (inferred from mouse homologs).
GRB2 has been shown to bind phosphotyrosine-699 of CSF1R (phosphotyrosine-697 of mouse Csf1r), however phosphorylation of tyrosines 544, 559, and 807 of mouse Csf1r are together sufficient for the full proliferative response mediated via the RS-RAF-MEK-ERK1,2 pathway (Yu et al. 2012) and mouse Csf1r lacking phosophotyrosine-697 can still activate ERK (Lee and States 2000), Csf1r phosphotyrosine-697 (human CSF1R phosphotyrosine-699) is likely not the only GRB2:SOS binding site",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P07947-1",
"P08631-1",
"P01116-1"
],
"evidence": [
{
"id": "R-HSA-9680385",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9680385"
}
]
},
{
"id": "R-HSA-9680388",
"name": "CSF1R-associated PLCG2 hydrolyzes phosphatidylcholine",
"equation": "",
"summary": "In response to CSF1, PLCG2 (phospholipase C gamma2) associates with CSF1R, is activated by phosphorylation, and hydrolyzes phosphatidylcholine to yield choline phosphate (ChoP, phosphocholine) and 1,2-diacylglycerol (Imamura et al. 1990, Nakamura et al. 1992, Obba et al. 2015, also inferred from mouse homologs). PLCG2 activates pathways that enhance differentiation of macrophages (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P42336-1",
"P48736-1",
"P06241-1",
"P12931-1",
"P22681-1",
"O15357-1",
"P07947-1",
"P07948-1",
"P16885-1",
"Q06124-2",
"P08631-1",
"P42338-1",
"Q92835-1"
],
"evidence": [
{
"id": "R-HSA-9680388",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9680388"
}
]
},
{
"id": "R-HSA-9680389",
"name": "CSF1R-associated phosphatidylinositol 3-kinase (PI3K) phosphorylates PI(4,5)P2",
"equation": "",
"summary": "Phosphatidylinositol 3-kinase (PI3K) associated with the activated receptor for CSF1, CSF1R (M-CSFR), phosphorylates phosphatidylinositol 4,5-bisphosphate (PIP2) to yield phosphatidylinositol 3,4,5-trisphosphate (PIP3) (Saleem et al. 1995, also inferred from mouse homologs). The regulatory subunit of PI3K, PIK3R1 (p85alpha), binds phosphotyrosine-723 (721 in the mouse homologs) of CSF1R (inferred from mouse homologs). PI3K is important for proliferation, migration, and anti-inflammatory activity of macrophages (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P42336-1",
"P48736-1",
"P06241-1",
"P12931-1",
"P22681-1",
"O15357-1",
"P07947-1",
"P07948-1",
"P16885-1",
"Q06124-2",
"P08631-1",
"P42338-1",
"Q92835-1"
],
"evidence": [
{
"id": "R-HSA-9680389",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9680389"
}
]
},
{
"id": "R-HSA-9726848",
"name": "SRC phosphorylates RHOU",
"equation": "",
"summary": "Based on studies conducted using human RHOU (Wrch-1) and mouse Src, SRC phosphorylates RHOU at the tyrosine residue Y254, located at the C-terminus of RHOU (Alan et al. 2010).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P12931-1"
],
"evidence": [
{
"id": "R-HSA-9726848",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9726848"
}
]
},
{
"id": "R-HSA-9733316",
"name": "p-Y-CBL autoubiquitinates and multiubiquitinates p-Y561-CSF1R in CSF1 dimer:p-Y561-CSF1R dimer:p-Y-CBL",
"equation": "",
"summary": "After CBL is phosphorylated and binds CSF1R, CBL autopolyubiquitinates and polyubiquitinates CSF1R (inferred from mouse homologs). The ubiquitination of CSF1R results in a subsequent wave of phosphorylation by CSF1R and the internalization and proteolysis of CSF1R (inferred from mouse homologs). Thus multiubiquitination of CSF1R is required for full activity of CSF1R and for termination of signaling by CSF1R.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P22681-1",
"P07947-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-9733316",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9733316"
}
]
},
{
"id": "R-HSA-9733323",
"name": "Src family kinases phosphorylate CBL in CSF1 dimer:p-Y561-CSF1R dimer:CBL",
"equation": "",
"summary": "CBL binds the phosphorylated CSF1R and is phosphorylated (inferred from mouse homologs). CBL is observed to bind phosphotyrosine-969 but mutation of tyrosine-561 has a greater effect on phosphoryation of CBL and multiubiquitination of CSF1R by CBL (inferred from mouse homologs). Based on response to inhibitors, the phosphorylation of CBL is catalyzed by SRC family kinases (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P22681-1",
"P07947-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-9733323",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9733323"
}
]
},
{
"id": "R-HSA-9733330",
"name": "CSF1 dimer,IL34 dimer:p-Y561-CSF1R dimer:SFK binds GRB2:SOS1",
"equation": "",
"summary": "After an initial wave of phosphorylation of CSF1R, the stable GRB2:SOS1 complex transiently binds phospho-CSF1R (inferred from mouse homologs). GRB2 has been shown to bind phosphotyrosine-699, though another phosphotyrosine residue may be involved in transient binding of GRB2 (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P07947-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-9733330",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9733330"
}
]
},
{
"id": "R-HSA-9733331",
"name": "CSF1 dimer,IL34 dimer:p-Y561-CSF1R:GRB2:SOS1 dissociates yielding CSF1 dimer,IL34 dimer:p-Y561-CSF1R:SFK and GRB2:SOS1",
"equation": "",
"summary": "GRB2:SOS1 transiently associates with phosphorylated CSF1R after CSF1R undergoes an initial wave of autophosphorylation (Wang et al. 1999). GRB2:SOS1 then dissociates from CSF1R.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P07947-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-9733331",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9733331"
}
]
},
{
"id": "R-HSA-9817983",
"name": "CSF1 dimer,IL34 dimer:p-Y561-CSF1R dimer:SFK binds CBL",
"equation": "",
"summary": "The ubiquitin E3 ligase CBL associates with the phosphorylated CSF1R.",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P22681-1",
"P07947-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-9817983",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9817983"
}
]
},
{
"id": "R-HSA-9818010",
"name": "CSF1 dimer,IL34 dimer:p-Y561-CSF1R dimer binds SRC family kinases FYN,HCK,SRC,YES1",
"equation": "",
"summary": "After phosphorylation of CSF-1R tyrosine-Y561, SFKs bind the phosphotyrosine-561 site (inferred from mouse homologs).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P07333-1",
"P06241-1",
"P12931-1",
"P07947-1",
"P08631-1"
],
"evidence": [
{
"id": "R-HSA-9818010",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9818010"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-HSA-180499",
"participant_name": "CSK [plasma membrane]",
"crossref": [
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{
"id": "CSK_HUMAN",
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{
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{
"id": "P41240",
"database": "ZINC target",
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{
"id": "2.7.10.2",
"database": "IntEnz",
"url": ""
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{
"id": "ENSP00000220003",
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"url": ""
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{
"id": "P41240",
"database": "UniProt",
"url": ""
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{
"id": "ENSG00000103653",
"database": "OpenTargets",
"url": ""
},
{
"id": "CSK_HUMAN",
"database": "ZINC - FDA approved",
"url": ""
},
{
"id": "CSK_HUMAN",
"database": "ZINC - Biogenic",
"url": ""
},
{
"id": "3EAZ",
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{
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{
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{
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{
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"url": ""
}
]
},
{
"participant_id": "R-HSA-1810408",
"participant_name": "MyrG-p-Y419-SRC [plasma membrane]",
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{
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{
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{
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{
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{
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{
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{
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{
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{
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{
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"url": ""
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{
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{
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{
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{
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{
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"url": ""
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{
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"url": ""
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"url": ""
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{
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"url": ""
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"url": ""
},
{
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"url": ""
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{
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"url": ""
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{
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"url": ""
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{
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"url": ""
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{
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"url": ""
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{
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"url": ""
},
{
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"database": "Ensembl",
"url": ""
},
{
"id": "SRC_HUMAN",
"database": "ZINC - Investigational",
"url": ""
},
{
"id": "7NG7",
"database": "PDB",
"url": ""
},
{
"id": "SRC_HUMAN",
"database": "ZINC - FDA approved",
"url": ""
},
{
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"url": ""
},
{
"id": "SRC_HUMAN",
"database": "ZINC - Metabolites",
"url": ""
},
{
"id": "ENST00000373558",
"database": "Ensembl",
"url": ""
},
{
"id": "2SRC",
"database": "PDB",
"url": ""
},
{
"id": "ENSG00000197122",
"database": "OpenTargets",
"url": ""
},
{
"id": "1SHD",
"database": "PDB",
"url": ""
},
{
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"database": "PDB",
"url": ""
},
{
"id": "1O46",
"database": "PDB",
"url": ""
},
{
"id": "4HXJ",
"database": "PDB",
"url": ""
},
{
"id": "SRC_HUMAN",
"database": "ZINC - Predictions - Purchasable",
"url": ""
},
{
"id": "1O4G",
"database": "PDB",
"url": ""
},
{
"id": "1YI6",
"database": "PDB",
"url": ""
},
{
"id": "ENSP00000362659",
"database": "Ensembl",
"url": ""
},
{
"id": "4K11",
"database": "PDB",
"url": ""
},
{
"id": "1O4F",
"database": "PDB",
"url": ""
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