{ "uniprot_canonical_ac": "O00329-1", "uniprot_ac": "O00329", "uniprot_id": "PK3CD_HUMAN", "mass": { "chemical_mass": 119479.0, "monoisotopic_mass": 119479.0 }, "refseq": { "ac": "NP_005017", "name": "phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform isoform 1", "summary": "Phosphoinositide 3-kinases (PI3Ks) phosphorylate inositol lipids and are involved in the immune response. The protein encoded by this gene is a class I PI3K found primarily in leukocytes. Like other class I PI3Ks (p110-alpha p110-beta, and p110-gamma), the encoded protein binds p85 adapter proteins and GTP-bound RAS. However, unlike the other class I PI3Ks, this protein phosphorylates itself, not p85 protein.[provided by RefSeq, Jul 2010].", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_005017" }, "gene_names": [ { "name": "PIK3CD", "resource": "UniProtKB", "type": "recommended", "url": "https://www.uniprot.org/uniprot/O00329", "id": "O00329" }, { "name": "APDS; IMD14; IMD14A; IMD14B; p110D; P110DELTA; PI3K; ROCHIS", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_005017", "id": "NP_005017" }, { "name": "PIK3CD", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_005017", "id": "NP_005017" } ], "protein_names": [ { "name": "Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform", "resource": "UniProtKB", "type": "recommended", "url": "", "id": "O00329" }, { "name": "2.7.1.137", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "O00329" }, { "name": "2.7.1.153", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "O00329" }, { "name": "PI3-kinase p110 subunit delta; phosphoinositide-3-kinase C; ptdIns-3-kinase subunit p110-delta; phosphatidylinositol-4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta; phosphoinositide-3-kinase, catalytic, delta polypeptide variant p37delta; PI3Kdelta; phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta short variant 8/20", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_005017", "id": "NP_005017" }, { "name": "PI3-kinase subunit delta", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "O00329" }, { "name": "PI3K-delta", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "O00329" }, { "name": "PI3Kdelta", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "O00329" }, { "name": "Phosphatidylinositol 4,5-bisphosphate 3-kinase 110 kDa catalytic subunit delta", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "O00329" }, { "name": "PtdIns-3-kinase subunit delta", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "O00329" }, { "name": "PtdIns-3-kinase subunit p110-delta", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "O00329" }, { "name": "p110delta", "resource": "UniProtKB", "type": "synonym", "url": "", "id": "O00329" }, { "name": "phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform isoform 1", "resource": "RefSeq", "type": "synonym", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_005017", "id": "NP_005017" } ], "function": [ { "annotation": "A PI3K gene expression signature predicts for recurrence in early-stage non-small cell lung cancer treated with stereotactic body radiation therapy.", "evidence": [ { "database": "RefSeq", "id": "NP_005017", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_005017" }, { "database": "PubMed", "id": "37560930", "url": "https://glygen.org/publication/PubMed/37560930" } ] }, { "annotation": "CBX3 promotes clear cell renal carcinoma through PI3K/AKT activation and aberrant immunity. Publication Status: Online-Only", "evidence": [ { "database": "RefSeq", "id": "NP_005017", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_005017" }, { "database": "PubMed", "id": "37674204", "url": "https://glygen.org/publication/PubMed/37674204" } ] }, { "annotation": "CircCDK1 blocking IGF2BP2-mediated m6A modification of CPPED1 promotes laryngeal squamous cell carcinoma metastasis via the PI3K/AKT signal pathway.", "evidence": [ { "database": "RefSeq", "id": "NP_005017", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_005017" }, { "database": "PubMed", "id": "37543219", "url": "https://glygen.org/publication/PubMed/37543219" } ] }, { "annotation": "KIRREL promotes the proliferation of gastric cancer cells and angiogenesis through the PI3K/AKT/mTOR pathway.", "evidence": [ { "database": "RefSeq", "id": "NP_005017", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_005017" }, { "database": "PubMed", "id": "37909722", "url": "https://glygen.org/publication/PubMed/37909722" } ] }, { "annotation": "Phosphoinositide 3-kinases (PI3Ks) phosphorylate inositol lipids and are involved in the immune response. The protein encoded by this gene is a class I PI3K found primarily in leukocytes. Like other class I PI3Ks (p110-alpha p110-beta, and p110-gamma), the encoded protein binds p85 adapter proteins and GTP-bound RAS. However, unlike the other class I PI3Ks, this protein phosphorylates itself, not p85 protein.[provided by RefSeq, Jul 2010].", "evidence": [ { "database": "RefSeq", "id": "NP_005017", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_005017" } ] }, { "annotation": "Phosphoinositide-3-kinase (PI3K) phosphorylates phosphatidylinositol (PI) and its phosphorylated derivatives at position 3 of the inositol ring to produce 3-phosphoinositides (PubMed:9235916). Uses ATP and PtdIns(4,5)P2 (phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3) (PubMed:15135396). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Mediates immune responses. Plays a role in B-cell development, proliferation, migration, and function. Required for B-cell receptor (BCR) signaling. Mediates B-cell proliferation response to anti-IgM, anti-CD40 and IL4 stimulation. Promotes cytokine production in response to TLR4 and TLR9. Required for antibody class switch mediated by TLR9. Involved in the antigen presentation function of B-cells. Involved in B-cell chemotaxis in response to CXCL13 and sphingosine 1-phosphate (S1P). Required for proliferation, signaling and cytokine production of naive, effector and memory T-cells. Required for T-cell receptor (TCR) signaling. Mediates TCR signaling events at the immune synapse. Activation by TCR leads to antigen-dependent memory T-cell migration and retention to antigenic tissues. Together with PIK3CG participates in T-cell development. Contributes to T-helper cell expansion and differentiation. Required for T-cell migration mediated by homing receptors SELL/CD62L, CCR7 and S1PR1 and antigen dependent recruitment of T-cells. Together with PIK3CG is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in NK cell receptor activation. Plays a role in NK cell maturation and cytokine production. Together with PIK3CG is involved in neutrophil chemotaxis and extravasation. Together with PIK3CG participates in neutrophil respiratory burst. Plays important roles in mast-cell development and mast cell mediated allergic response. Involved in stem cell factor (SCF)-mediated proliferation, adhesion and migration. Required for allergen-IgE-induced degranulation and cytokine release. The lipid kinase activity is required for its biological function. Isoform 2 may be involved in stabilizing total RAS levels, resulting in increased ERK phosphorylation and increased PI3K activity.", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329#function" }, { "database": "PubMed", "id": "20081091", "url": "https://glygen.org/publication/PubMed/20081091" }, { "database": "PubMed", "id": "22020336", "url": "https://glygen.org/publication/PubMed/22020336" }, { "database": "PubMed", "id": "9235916", "url": "https://glygen.org/publication/PubMed/9235916" }, { "database": "PubMed", "id": "15135396", "url": "https://glygen.org/publication/PubMed/15135396" } ] }, { "annotation": "Polymorphisms in PI3K/AKT genes and gene-smoking interaction are associated with susceptibility to tuberculosis.", "evidence": [ { "database": "RefSeq", "id": "NP_005017", "url": "https://www.ncbi.nlm.nih.gov/protein/NP_005017" }, { "database": "PubMed", "id": "38117222", "url": "https://glygen.org/publication/PubMed/38117222" } ] } ], "disease": [ { "disease_id": "DOID:0111936", "recommended_name": { "id": "DOID:0111936", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:0111936", "name": "immunodeficiency 14", "description": "A combined T cell and B cell immunodeficiency characterized by B- and T-cell abnormalities and onset of recurrent sinopulmonary and other infections in early childhood that has_material_basis_in heterozygous activating mutation in the PIK3CD gene on chromosome 1p36.22." }, "synonyms": [ { "id": "DOID:0111936", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:0111936", "name": "APDS", "description": "" }, { "id": "DOID:0111936", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:0111936", "name": "IMD14", "description": "" }, { "id": "DOID:0111936", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:0111936", "name": "PASLI disease", "description": "" }, { "id": "DOID:0111936", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:0111936", "name": "activated PI3K-delta syndrome", "description": "" }, { "id": "DOID:0111936", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:0111936", "name": "senescent T-cells-lymphadenopathy-immunodeficiency syndrome due to p110delta-activating mutation", "description": "" }, { "id": "MONDO:0014222", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0014222", "name": "immunodeficiency 14", "description": "" }, { "id": "MONDO:0014222", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0014222", "name": "immunodeficiency 14", "description": "" }, { "id": "MONDO:0014222", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0014222", "name": "immunodeficiency 14A, autosomal dominant", "description": "" }, { "id": "MONDO:0014222", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0014222", "name": "immunodeficiency type 14", "description": "" }, { "id": "MONDO:0014222", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0014222", "name": "Activated PI3K-Delta syndrome", "description": "" }, { "id": "MONDO:0014222", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0014222", "name": "IMD14", "description": "" }, { "id": "MONDO:0014222", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0014222", "name": "p110-Delta-Activating mutation causing senescent T cells, lymphadenopathy, and immunodeficiency", "description": "" }, { "id": "MIM:615513", "resource": "MIM", "url": "https://www.omim.org/entry/615513", "name": "Immunodeficiency 14A with lymphoproliferation, autosomal dominant", "description": "Immunodeficiency 14A with lymphoproliferation, autosomal dominant" } ], "evidence": [ { "id": "615513", "database": "MIM", "url": "https://www.omim.org/entry/615513" } ] }, { "disease_id": "MONDO:0013226", "recommended_name": { "id": "MONDO:0013226", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013226", "name": "combined immunodeficiency with faciooculoskeletal anomalies", "description": "Combined immunodeficiency with faciooculoskeletal anomalies is an extremely rare combined immunodeficiency disorder characterized by primary immunodeficiency manifesting with repeated bacterial, viral and fungal infections, in association with neurological manifestations (hypotonia, cerebellar ataxia, myoclonic seizures), developmental delay, optic atrophy, facial dysmorphism (high forehead, hypoplastic supraorbital ridges, palpebral edema, hypertelorism, flat nasal bridge, broad nasal root and tip, anteverted nares, thin lower lip overlapped by upper lip, square chin) and skeletal anomalies (short metacarpals/metatarsals with cone-shaped epiphyses, osteopenia)." }, "synonyms": [ { "id": "MONDO:0013226", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013226", "name": "Roifman-Chitayat syndrome", "description": "" }, { "id": "MONDO:0013226", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013226", "name": "Roifman-Chitayat syndrome, digenic", "description": "" }, { "id": "MONDO:0013226", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013226", "name": "ROIFMAN-Chitayat syndrome", "description": "" }, { "id": "MONDO:0013226", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0013226", "name": "combined immunodeficiency, Facial Dysmorphism, optic nerve atrophy, skeletal anomalies, and developmental delay", "description": "" }, { "id": "MIM:613328", "resource": "MIM", "url": "https://www.omim.org/entry/613328", "name": "Roifman-Chitayat syndrome", "description": "Roifman-Chitayat syndrome" } ], "evidence": [ { "id": "613328", "database": "MIM", "url": "https://www.omim.org/entry/613328" } ] }, { "disease_id": "MONDO:0023655", "recommended_name": { "id": "MONDO:0023655", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023655", "name": "immunodeficiency 14b, autosomal recessive", "description": "" }, "synonyms": [ { "id": "MONDO:0023655", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0023655", "name": "IMD14B", "description": "" }, { "id": "MIM:619281", "resource": "MIM", "url": "https://www.omim.org/entry/619281", "name": "Immunodeficiency 14B, autosomal recessive", "description": "Immunodeficiency 14B, autosomal recessive" } ], "evidence": [ { "id": "619281", "database": "MIM", "url": "https://www.omim.org/entry/619281" } ] } ], "snv": [ { "evidence": [ { "id": "rs1201485090", "database": "dbSNP", "url": "https://www.ncbi.nlm.nih.gov/SNP/snp_ref.cgi?type=rs&rs=rs1201485090" }, { "id": "rs1201485090", "database": "gnomAD", "url": "http://gnomad.broadinstitute.org/awesome?query=rs1201485090" } ], "glycoeffect": [ "n-glyco-sequon-gain", "o-glyco-site-loss" ], "start_pos": 202, "end_pos": 202, "sequence_org": "S", "sequence_mut": "N", "comment": "Germline mutation passed 1 out of 1 filters: n-glyco-sequon-gain (SFT->NFT).", "chr_id": "1", "chr_pos": "9716444", "ref_nt": "A", "alt_nt": "null", "minor_allelic_frequency": "", "site_lbl": "S202", "keywords": [ "ebi", "germline" ] }, { "evidence": [ { "id": "O00329", "database": "BioMuta", "url": "https://hive.biochemistry.gwu.edu/biomuta/proteinview/O00329" } ], "glycoeffect": [], "start_pos": 20, "end_pos": 20, "subjects_tested": "0", "subjects_positive": "0", "frequency": "0.0", "sequence_org": "V", "sequence_mut": "I", "comment": "Somatic mutation passed 1 out of 6 filters: num. of cancers (3).", "chr_id": "1", "chr_pos": "9710513", "ref_nt": "G", "alt_nt": "A", "minor_allelic_frequency": "", "site_lbl": "V20", "disease": [ { "disease_id": "DOID:2394", "recommended_name": { "id": "DOID:2394", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2394", "name": "ovarian cancer", "description": "A female reproductive organ cancer that is located_in the ovary." }, "synonyms": [ { "id": "DOID:2394", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2394", "name": "malignant Ovarian tumor", "description": "" }, { "id": "DOID:2394", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2394", "name": "malignant tumour of ovary", "description": "" }, { "id": "DOID:2394", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2394", "name": "ovarian neoplasm", "description": "" }, { "id": "DOID:2394", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2394", "name": "ovary neoplasm", "description": "" }, { "id": "DOID:2394", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2394", "name": "primary ovarian cancer", "description": "" }, { "id": "DOID:2394", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:2394", "name": "tumor of the Ovary", "description": "" }, { "id": "MONDO:0011931", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011931", "name": "ovarian cancer, susceptibility to, 1", "description": "" }, { "id": "MONDO:0011931", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011931", "name": "OVCAS1", "description": "" }, { "id": "MONDO:0011931", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011931", "name": "ovarian cancer, susceptibility to", "description": "" }, { "id": "MONDO:0011931", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0011931", "name": "ovarian cancer, susceptibility to, 1", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "ovarian cancer", "description": "A primary or metastatic malignant neoplasm involving the ovary. Most primary malignant ovarian neoplasms are either carcinomas (serous, mucinous, or endometrioid adenocarcinomas) or malignant germ cell tumors. Metastatic malignant neoplasms to the ovary include carcinomas, lymphomas, and melanomas." }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "ovarian neoplasm", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "ovary neoplasm", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "tumor of the ovary", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "tumour of the ovary", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "cancer of ovary", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "cancer of the ovary", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "malignant neoplasm of ovary", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "malignant neoplasm of the ovary", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "malignant ovarian neoplasm", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "malignant ovarian tumor", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "malignant ovarian tumour", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "malignant ovary neoplasm", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "malignant tumor of ovary", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "malignant tumor of the ovary", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "malignant tumour of ovary", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "malignant tumour of the ovary", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "ovarian cancer", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "ovarian cancer, somatic", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "ovarian malignant tumor", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "ovarian malignant tumour", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "ovary cancer", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "ovarian cancer, epithelial", "description": "" }, { "id": "MONDO:0008170", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0008170", "name": "primary ovarian cancer", "description": "" }, { "id": "MIM:167000", "resource": "MIM", "url": "https://www.omim.org/entry/167000", "name": "Ovarian cancer", "description": "Ovarian cancer" } ] }, { "disease_id": "DOID:9256", "recommended_name": { "id": "DOID:9256", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:9256", "name": "colorectal cancer", "description": "A large intestine cancer that is located_in the colon and/or located_in the rectum." }, "synonyms": [ { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "colorectal cancer", "description": "A primary or metastatic malignant neoplasm that affects the colon or rectum. Representative examples include carcinoma, lymphoma, and sarcoma." }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "cancer of colorectum", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "cancer of large bowel", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "cancer of large intestine", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "cancer of the large bowel", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "colon cancer, advanced, somatic", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "colon cancer, somatic", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "colorectal cancer", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "colorectal cancer with chromosomal instability, somatic", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "colorectal cancer, autosomal dominant, somatic mutation", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "colorectal cancer, somatic", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "colorectal cancer, susceptibility to, autosomal dominant, 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"https://monarchinitiative.org/disease/MONDO:0005575", "name": "malignant neoplasm of colorectum", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "malignant neoplasm of large bowel", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "malignant neoplasm of large intestine", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "malignant neoplasm of the large bowel", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "malignant neoplasm of the large intestine", "description": "" }, { "id": "MONDO:0005575", "resource": "MONDO", "url": "https://monarchinitiative.org/disease/MONDO:0005575", "name": "malignant tumor of large bowel", "description": "" 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"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": 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"https://hive.biochemistry.gwu.edu/bioxpress/transcriptview/O00329" } ], "disease": [ { "disease_id": "DOID:263", "recommended_name": { "id": "DOID:263", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:263", "name": "kidney cancer", "description": "A urinary system cancer that is located_in the kidney." }, "synonyms": [ { "id": "DOID:263", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:263", "name": "malignant neoplasm of kidney except pelvis", "description": "" }, { "id": "DOID:263", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:263", "name": "malignant tumour of kidney", "description": "" }, { "id": "DOID:263", "resource": "Disease Ontology", "url": "http://disease-ontology.org/term/DOID:263", "name": "renal cancer", "description": "" } ] } ] }, { "significant": "Yes", "trend": "down", "name": "Liver cancer [DO disease name]", "url": "http://disease-ontology.org/term/DOID:3571", "evidence": [ 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"MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSVALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNVSKDNRQ", "length": 1044, "header": "sp|O00329-1|PK3CD_HUMAN Isoform 1 of Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform OS=Homo sapiens OX=9606 GN=PIK3CD PE=1 SV=2 CANONICAL=O00329-1" }, "isoforms": [ { "isoform_ac": "A0A8V8TM62-1", "url": "", "sequence": { "sequence": "MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTSEMHVPSVALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNVSKDNRQ", "length": 996, "header": "tr|A0A8V8TM62-1|A0A8V8TM62_HUMAN Computationally mapped isoform of phosphatidylinositol-4,5-bisphosphate 3-kinase OS=Homo sapiens OX=9606 GN=PIK3CD PE=1 SV=1 CANONICAL=O00329-1" }, "locus": { "chromosome": "1", "start_pos": 9727043, "end_pos": 9710456, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000698714.1", "url": "https://www.ensembl.org/id/ENST00000698714.1" }, { "database": "Ensembl Peptide", "id": "ENSP00000513891.1", "url": "https://www.ensembl.org/id/ENSP00000513891.1" } ] } }, { "isoform_ac": "A0A8V8TML5-1", "url": "", "sequence": { "sequence": "MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWH", "length": 51, "header": "tr|A0A8V8TML5-1|PK3CD_HUMAN Computationally mapped isoform of Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform OS=Homo sapiens OX=9606 GN=PIK3CD PE=1 SV=1 CANONICAL=O00329-1" }, "locus": { "chromosome": "1", "start_pos": 9715552, "end_pos": 9710456, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000698707.1", "url": "https://www.ensembl.org/id/ENST00000698707.1" }, { "database": "Ensembl Peptide", "id": "ENSP00000513885.1", "url": "https://www.ensembl.org/id/ENSP00000513885.1" } ] } }, { "isoform_ac": "A0A8V8TMM0-1", "url": "", "sequence": { "sequence": "MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSVALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNVSKDNRQ", "length": 1040, "header": "tr|A0A8V8TMM0-1|A0A8V8TMM0_HUMAN Computationally mapped isoform of phosphatidylinositol-4,5-bisphosphate 3-kinase OS=Homo sapiens OX=9606 GN=PIK3CD PE=1 SV=1 CANONICAL=O00329-1" }, "locus": { "chromosome": "1", "start_pos": 9727043, "end_pos": 9710456, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000698716.1", "url": "https://www.ensembl.org/id/ENST00000698716.1" }, { "database": "Ensembl Peptide", "id": "ENSP00000513893.1", "url": "https://www.ensembl.org/id/ENSP00000513893.1" } ] } }, { "isoform_ac": "A0A8V8TNP1-1", "url": "", "sequence": { "sequence": "XEWRPELLWMRLHAEDSAPSRMIGVAMPGLGVLPGLVQAPGDAECSRLLQILELGRHSECVHVTEEELQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRAL", "length": 197, "header": "tr|A0A8V8TNP1-1|A0A8V8TNP1_HUMAN Computationally mapped isoform of Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit delta OS=Homo sapiens OX=9606 GN=PIK3CD PE=1 SV=1 CANONICAL=O00329-1" }, "locus": { "chromosome": "1", "start_pos": 9721547, "end_pos": 9720462, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000698789.1", "url": "https://www.ensembl.org/id/ENST00000698789.1" }, { "database": "Ensembl Peptide", "id": "ENSP00000513931.1", "url": "https://www.ensembl.org/id/ENSP00000513931.1" } ] } }, { "isoform_ac": "A0A8V8TNW9-1", "url": "", "sequence": { "sequence": "MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLVQVLNSEMHVPSVALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNVSKDNRQ", "length": 1012, "header": "tr|A0A8V8TNW9-1|A0A8V8TNW9_HUMAN Computationally mapped isoform of phosphatidylinositol-4,5-bisphosphate 3-kinase OS=Homo sapiens OX=9606 GN=PIK3CD PE=1 SV=1 CANONICAL=O00329-1" }, "locus": { "chromosome": "1", "start_pos": 9727043, "end_pos": 9710456, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000698709.1", "url": "https://www.ensembl.org/id/ENST00000698709.1" }, { "database": "Ensembl Peptide", "id": "ENSP00000513887.1", "url": "https://www.ensembl.org/id/ENSP00000513887.1" } ] } }, { "isoform_ac": "B7ZM44-1", "url": "", "sequence": { "sequence": "MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKILELGRHSECVHVTEEELQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSVALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNVSKDNRQ", "length": 1043, "header": "tr|B7ZM44-1|PK3CD_HUMAN Computationally mapped isoform of Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform OS=Homo sapiens OX=9606 GN=PIK3CD PE=1 SV=1 CANONICAL=O00329-1" }, "locus": { "chromosome": "1", "start_pos": 9727043, "end_pos": 9710456, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000698715.1", "url": "https://www.ensembl.org/id/ENST00000698715.1" }, { "database": "Ensembl Peptide", "id": "ENSP00000513892.1", "url": "https://www.ensembl.org/id/ENSP00000513892.1" } ] } }, { "isoform_ac": "F8W9P4-1", "url": "", "sequence": { "sequence": "MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQVQKPRAKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKLPGGMLLASREWRPELLWMRLHAEDSAPSRMIGVAMPGLGVLPGLVQAPGDAECSRLLQILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSVALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNVSKDNRQ", "length": 1068, "header": "tr|F8W9P4-1|F8W9P4_HUMAN Computationally mapped isoform of phosphatidylinositol-4,5-bisphosphate 3-kinase OS=Homo sapiens OX=9606 GN=PIK3CD PE=1 SV=1 CANONICAL=O00329-1" }, "locus": { "chromosome": "1", "start_pos": 9727043, "end_pos": 9710456, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000361110.6", "url": "https://www.ensembl.org/id/ENST00000361110.6" }, { "database": "Ensembl Peptide", "id": "ENSP00000354410.2", "url": "https://www.ensembl.org/id/ENSP00000354410.2" } ] } }, { "isoform_ac": "O00329-1", "url": "", "sequence": { "sequence": "MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSVALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNVSKDNRQ", "length": 1044, "header": "sp|O00329-1|PK3CD_HUMAN Isoform 1 of Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform OS=Homo sapiens OX=9606 GN=PIK3CD PE=1 SV=2 CANONICAL=O00329-1" }, "locus": { "chromosome": "1", "start_pos": 9727043, "end_pos": 9710456, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000698712.1", "url": "https://www.ensembl.org/id/ENST00000698712.1" }, { "database": "Ensembl Peptide", "id": "ENSP00000513889.1", "url": "https://www.ensembl.org/id/ENSP00000513889.1" } ] } }, { "isoform_ac": "O00329-2", "url": "", "sequence": { "sequence": "MPPGVDCPMEFWTKEENQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEVSPCVACGIQAALSMGSTSSVKLLSHPQAPLPQWHQMVFARCLCMCGAQLNVPPGELHLPGVHQGRAAGADGLCPAEEGHSVPAAAGGAAGRLHAAGERQA", "length": 301, "header": "sp|O00329-2|PK3CD_HUMAN Isoform 2 of Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform OS=Homo sapiens OX=9606 GN=PIK3CD PE=1 SV=2 CANONICAL=O00329-1" }, "locus": { "chromosome": "1", "start_pos": 9716579, "end_pos": 9710456, "strand": "-", "evidence": [ { "database": "Ensembl Transcript", "id": "ENST00000481137.2", "url": "https://www.ensembl.org/id/ENST00000481137.2" }, { "database": "Ensembl Peptide", "id": "ENSP00000513886.1", "url": "https://www.ensembl.org/id/ENSP00000513886.1" } ] } } ], "glycosylation": [ { "glytoucan_ac": "G49108TO", "type": "O-linked", "subtype": "O-GlcNAcylation", "site_category": "reported_with_glycan", "site_seq": "S", "relation": "attached", "comment": "O-GlcNAcylation", "start_pos": 950, "start_aa": "Ser", "end_pos": 950, "end_aa": "Ser", "residue": "Ser", "site_lbl": "Ser950", "evidence": [ { "id": "O00329", "database": "O-GlcNAc Database", "url": "https://www.oglcnac.mcw.edu/search/?query_protein=O00329" }, { "id": "29351928", "database": "PubMed", "url": "https://glygen.org/publication/PubMed/29351928" }, { "id": "O00329", "database": "O-GlcNAc Atlas", "url": "https://oglcnac.org/atlas/detail/O00329" } ] } ], "phosphorylation": [ { "start_pos": 1039, "end_pos": 1039, "kinase_uniprot_canonical_ac": "O00329-1", "kinase_gene_name": "PIK3CD", "residue": "Ser", "comment": "", "evidence": [ { "database": "iPTMnet", "id": "O00329", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/O00329" }, { "database": "PubMed", "id": "10064595", "url": "https://glygen.org/publication/PubMed/10064595" }, { "database": "PubMed", "id": "9113989", "url": "https://glygen.org/publication/PubMed/9113989" }, { "database": "phospho.ELM", "id": "O00329", "url": "http://phospho.elm.eu.org/byAccession/O00329.html" }, { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "site_lbl": "Ser1039" }, { "start_pos": 1039, "end_pos": 1039, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Ser", "comment": "Phosphoserine; by autocatalysis", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" }, { "database": "iPTMnet", "id": "O00329", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/O00329" }, { "database": "PubMed", "id": "10064595", "url": "https://glygen.org/publication/PubMed/10064595" }, { "database": "PubMed", "id": "19369195", "url": "https://glygen.org/publication/PubMed/19369195" }, { "database": "PubMed", "id": "23186163", "url": "https://glygen.org/publication/PubMed/23186163" } ], "site_lbl": "Ser1039" }, { "start_pos": 440, "end_pos": 440, "kinase_uniprot_canonical_ac": "", "kinase_gene_name": "", "residue": "Tyr", "comment": "", "evidence": [ { "database": "phospho.ELM", "id": "O00329", "url": "http://phospho.elm.eu.org/byAccession/O00329.html" }, { "database": "iPTMnet", "id": "O00329", "url": "http://research.bioinformatics.udel.edu/iptmnet/entry/O00329" }, { "database": "PubMed", "id": 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"MPPGVDCPMEFWTKEESQSVAVDFLLPTGVYLNFPVSRNANLSTIKQVLWHRAQYEPFFHMLSDPEAYVFTCVNQTAEQQELEDEQRRLCDIQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLRDPEVNDFRTKMRQFCEEAAAHRQQLGWVEWLQYSFPLQLEPSARGWRAGLLHVSNRPLLVNVKFEGSEESFTFQVSTKDMPLALMACALRKKATVFRQPLVERPEEYALQVNGRHEYLYGSYPLCHFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRVKPPPIPAKKPSSVSLWSLEQPFCIELIEGRKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVNVCSEPVWKQRLEFDISICDLPRMARLCFALYAVVEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELMNPAGTVRGNPNTESAAALVIYLPEVAPHPVYFPALEKILELGRHGERGRITEEEQLQLREILERRGSGELYEHEKDLVWKMRHEVQEHFPEALARLLLVTKWNKHEDVAQLSQMLYLLCSWPELPVLSALELLDFSFPDCYVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLGRALANRKIGHFLFWHLRSEMHVPSVALRFGLIMEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKASSQKTTKPQTKEMMHMCMRQETYMEALSHLQSPLDPSTLLEEVCVEQCTFMDSKMKPLWIMYSSEKAGGAGSVGIIFKNGDDLRQDMLTLQMIQLMDFLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLHSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNVSKDNRQ", "length": 1047 }, "evidence": [ { "id": "45924601", "url": "http://www.informatics.jax.org/homology/45924601", "database": "MGI" }, { "id": "O00329", "url": "https://omabrowser.org/oma/group/O00329/", "database": "OMA" } ], "common_name": "Rat" }, { "uniprot_canonical_ac": "O35904-1", "protein_name": "Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform", "gene_name": "Pik3cd", "tax_id": 10090, "organism": "Mus musculus", "sequence": { "sequence": "MPPGVDCPMEFWTKEESQSVVVDFLLPTGVYLNFPVSRNANLSTIKQVLWHRAQYEPLFHMLSDPEAYVFTCVNQTAEQQELEDEQRRLCDIQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLRDPEVNDFRTKMRQFCEEAAAHRQQLGWVEWLQYSFPLQLEPSARGWRAGLLRVSNRALLVNVKFEGSEESFTFQVSTKDMPLALMACALRKKATVFRQPLVEQPEEYALQVNGRHEYLYGNYPLCHFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFSIELIEGRKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVNVCSEPVWKQRLEFDISVCDLPRMARLCFALYAVVEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPAGTVRGNPNTESAAALVIYLPEVAPHPVYFPALEKILELGRHGERGRITEEELQLREILERRGSGELYEHEKDLVWKMRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCYVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLGRALANRKIGHFLFWHLRSEMHVPSVALRFGLIMEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKVSSQKTTKPQTKEMMHMCMRQETYMEALSHLQSPLDPSTLLEEVCVEQCTFMDSKMKPLWIMYSSEEAGSAGNVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLHSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKTKVNWLAHNVSKDNRQ", "length": 1043 }, "evidence": [ { "id": "45924601", "url": "http://www.informatics.jax.org/homology/45924601", "database": "MGI" } ], "common_name": "Mouse" } ], "go_annotation": { "categories": [ { "name": "Molecular Function", "total": 5, "go_terms": [ { "name": "ATP binding", "id": "GO:0005524", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005524", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "1-phosphatidylinositol-3-kinase activity", "id": "GO:0016303", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0016303", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity", "id": "GO:0046934", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0046934", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "kinase activity", "id": "GO:0016301", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0016301", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "1-phosphatidylinositol-4-phosphate 3-kinase activity", "id": "GO:0035005", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035005", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" } ] }, { "name": "Biological Process", "total": 37, "go_terms": [ { "name": "phosphorylation", "id": "GO:0016310", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0016310", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "phosphatidylinositol-mediated signaling", "id": "GO:0048015", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0048015", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "phosphatidylinositol phosphate biosynthetic process", "id": "GO:0046854", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0046854", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "natural killer cell differentiation", "id": "GO:0001779", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0001779", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "phosphatidylinositol-3-phosphate biosynthetic process", "id": "GO:0036092", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0036092", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "protein phosphorylation", "id": "GO:0006468", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006468", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "inflammatory response", "id": "GO:0006954", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006954", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "immune response", "id": "GO:0006955", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0006955", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "signal transduction", "id": "GO:0007165", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0007165", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "positive regulation of gene expression", "id": "GO:0010628", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0010628", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "positive regulation of cell migration", "id": "GO:0030335", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030335", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "innate immune response", "id": "GO:0045087", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045087", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "positive regulation of endothelial cell migration", "id": "GO:0010595", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0010595", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "T cell activation", "id": "GO:0042110", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042110", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "B cell activation", "id": "GO:0042113", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0042113", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "positive regulation of angiogenesis", "id": "GO:0045766", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0045766", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "T cell receptor signaling pathway", "id": "GO:0050852", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050852", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "positive regulation of cytokine production", "id": "GO:0001819", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0001819", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "positive regulation of endothelial cell proliferation", "id": "GO:0001938", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0001938", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "adaptive immune response", "id": "GO:0002250", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0002250", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "B cell chemotaxis", "id": "GO:0035754", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035754", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "B cell receptor signaling pathway", "id": "GO:0050853", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0050853", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "B cell differentiation", "id": "GO:0030183", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030183", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "phosphatidylinositol 3-kinase/protein kinase B signal transduction", "id": "GO:0043491", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043491", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "positive regulation of neutrophil apoptotic process", "id": "GO:0033031", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0033031", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "natural killer cell activation", "id": "GO:0030101", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030101", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "mast cell differentiation", "id": "GO:0060374", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0060374", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "respiratory burst involved in defense response", "id": "GO:0002679", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0002679", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "natural killer cell chemotaxis", "id": "GO:0035747", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0035747", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "T cell chemotaxis", "id": "GO:0010818", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0010818", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "T cell differentiation", "id": "GO:0030217", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030217", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "neutrophil chemotaxis", "id": "GO:0030593", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0030593", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "mast cell degranulation", "id": "GO:0043303", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0043303", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "mast cell chemotaxis", "id": "GO:0002551", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0002551", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "neutrophil extravasation", "id": "GO:0072672", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0072672", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "positive regulation of epithelial tube formation", "id": "GO:1905278", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:1905278", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "positive regulation of cell migration by vascular endothelial growth factor signaling pathway", "id": "GO:0038089", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0038089", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" } ] }, { "name": "Cellular Component", "total": 5, "go_terms": [ { "name": "cytoplasm", "id": "GO:0005737", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005737", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "cytosol", "id": "GO:0005829", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005829", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "plasma membrane", "id": "GO:0005886", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005886", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "phosphatidylinositol 3-kinase complex", "id": "GO:0005942", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005942", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" }, { "name": "phosphatidylinositol 3-kinase complex, class IA", "id": "GO:0005943", "url": "https://www.ebi.ac.uk/QuickGO/term/GO:0005943", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" } ], "pmid": "" } ] } ] }, "pro_annotation": [], "site_annotation": [ { "start_pos": 1037, "end_pos": 1039, "annotation": "n_glycosylation_sequon" }, { "start_pos": 17, "end_pos": 19, "annotation": "n_glycosylation_sequon" }, { "start_pos": 41, "end_pos": 43, "annotation": "n_glycosylation_sequon" }, { "start_pos": 74, "end_pos": 76, "annotation": "n_glycosylation_sequon" }, { "start_pos": 840, "end_pos": 842, "annotation": "n_glycosylation_sequon" }, { "start_pos": 948, "end_pos": 950, "annotation": "n_glycosylation_sequon" } ], "ptm_annotation": [ { "annotation": "Autophosphorylation on Ser-1039 results in the almost complete inactivation of the lipid kinase activity.", "evidence": [ { "database": "UniProtKB", "id": "O00329", "url": "https://www.uniprot.org/uniprot/O00329" }, { "database": "PubMed", "id": "10064595", "url": "https://glygen.org/publication/PubMed/10064595" } ] } ], "interactions": [], "reactions": [ { "id": "12709", "name": "", "equation": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+)", "summary": "", "cellular_location": "", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O88763-1", "A0A0G2K344-1", "O70173-1", "Q8NEB9-1", "P48736-1", "O00750-1", "P42336-1", "O00443-1", "O00329-1", "O75747-1", "P42337-1", "Q61194-1", "Q6PF93-1", "O35904-1", "Q9JHG7-1", "O70167-1", "P22543-1", "P54673-1", "P54674-1", "P54675-1", "P54676-1", "Q7K3H0-1", "Q9W1M7-1" ], "evidence": [ { "id": "12709", "database": "Rhea", "url": "https://www.rhea-db.org/rhea/12709" } ] }, { "id": "21292", "name": "", "equation": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+)", "summary": "", "cellular_location": "", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "A0A0G2K344-1", "Q9Z1L0-1", "Q99NI4-1", "A0A8I5Y949-1", "D3ZFJ0-1", "P42336-1", "Q8NFU5-1", "P48736-1", "P42338-1", "O00329-1", "O00443-1", "O35904-1", "Q7TT16-1", "P42337-1", "Q8BTI9-1", "Q9JHG7-1", "Q61194-1", "P07250-1" ], "evidence": [ { "id": "21292", "database": "Rhea", "url": "https://www.rhea-db.org/rhea/21292" } ] }, { "id": "43396", "name": "", "equation": "1-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phospho-1D-myo-inositol 4,5-bisphosphate + ATP = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-(1D-myo-inositol 3,4,5-triphosphate) + ADP + H(+)", "summary": "", "cellular_location": "", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "Q99NI4-1", "Q9Z1L0-1", "A0A0G2K344-1", "Q8NFU5-1", "P42336-1", "P42338-1", "O00329-1", "P42337-1", "Q8BTI9-1", "Q7TT16-1", "O35904-1" ], "evidence": [ { "id": "43396", "database": "Rhea", "url": "https://www.rhea-db.org/rhea/43396" } ] }, { "id": "R-HSA-1676048", "name": "PI(4,5)P2 is phosphorylated to PI(3,4,5)P3 by PIK3C[1] at the plasma membrane", "equation": "", "summary": "At the plasma membrane, phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunits form complexes with regulatory subunits. These complexes phosphorylate phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2) to phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) (Stephens et al. 1997). The PI(4,5)P2 3-kinase complexes involved are: PI(4,5)P2 3-kinase catalytic subunit alpha isoform (PIK3CA) bound to PI 3-kinase regulatory subunit alpha/beta/gamma (PIK3R1/2/3); beta (PIK3CB) bound to PIK3R1/2/3; delta (PIK3CD) bound to PIK3R1/2/3; and gamma (PIK3CG) bound to PI 3-kinase regulatory subunit 5 (PIK3R5) or 6 (PIK3R6).

The following lists the above proteins with their corresponding literature references: PIK3CA:PIK3R1, PIK3CA:PIK3R2, PIK3CA:PIK3R3 (Dey et al. 1998, Vanhaesebroeck et al. 1997, Meier et al. 2004); PIK3CB:PIK3R1, PIK3CB:PIK3R2, PIK3CB:PIK3R3 (Meier et al. 2004); PIK3CD:PIK3R1, PIK3CD:PIK3R2, PIK3CD:PIK3R3 (Vanhaesebroeck et al. 1997, Meier et al. 2004); and PIK3CG:PIK3R5, PIK3CG:PIK3R6 (Voigt et al. 2006, Suire et al. 2005, Stoyanov et al. 1995).", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P42336-1", "P48736-1", "P42338-1", "O00329-1" ], "evidence": [ { "id": "R-HSA-1676048", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1676048" } ] }, { "id": "R-HSA-1676109", "name": "PI4P is phosphorylated to PI(3,4)P2 by PI3K3C[2] at the plasma membrane", "equation": "", "summary": "At the plasma membrane, phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) 3-kinase catalytic subunits form complexes with regulatory subunits. These complexes along with phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunits alpha (PIK3C2A), beta (PIK3C2B), and gamma (PIK3C2G) phosphorylate phosphatidylinositol 4-phosphate (PI4P) to phosphatidylinositol 3,4-bisphosphate (PI(3,4)P2). The PI(4,5)P2 3-kinase complexes involved are: PI(4,5)P2 3-kinase catalytic subunit alpha isoform (PIK3CA) bound to PI 3-kinase regulatory subunit alpha/beta/gamma (PIK3R1/2/3); beta (PIK3CB) bound to PIK3R1/2/3; delta (PIK3CD) bound to PIK3R1/2/3; and gamma (PIK3CG) bound to PI 3-kinase regulatory subunit 5 (PIK3R5) or 6 (PIK3R6).

The following lists the above proteins with their corresponding literature references: PIK3C2A (Arcaro et al. 2000); PIK3C2B (Arcaro et al. 2000, Arcaro et al. 1998); PIK3C2G (Misawa et al. 1998, Ono et al. 1998); PIK3CA:PIK3R1, PIK3CA:PIK3R2, PIK3CA:PIK3R3 (Vanhaesebroeck et al. 1997); PIK3CB:PIK3R1, PIK3CB:PIK3R2, PIK3CB:PIK3R3 (Meier et al. 2004, Guo et al. 1997); PIK3CD:PIK3R1, PIK3CD:PIK3R2, PIK3CD:PIK3R3 (Vanhaesebroeck et al. 1997); and PIK3CG:PIK3R5, PIK3CG:PIK3R6 (Suire et al. 2005, Stoyanov et al. 1995).", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P42336-1", "O00443-1", "O75747-1", "P48736-1", "P42338-1", "O00329-1", "O00750-1" ], "evidence": [ { "id": "R-HSA-1676109", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-1676109" } ] }, { "id": "R-HSA-2045911", "name": "BCAP Signalosome phosphorylates PI(4,5)P2 forming PI(3,4,5)P3", "equation": "", "summary": "PI3K generates phosphoinositol-3,4,5-trisphosphate (PIP3) from PIP2 after activation of the BCR (Gold et al. 1992, Chantry et al. 1997). Experiments in mice indicate that PI3K associated with BCAP is partly responsible for the activity (Aiba et al. 2008). (PI3K associated with CD19 is also partly responsible (Aiba et al. 2008).)", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O00329-1" ], "evidence": [ { "id": "R-HSA-2045911", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2045911" } ] }, { "id": "R-HSA-2076220", "name": "CD19 Signalosome phosphorylates PI(4,5)P2 forming PI(3,4,5)P3", "equation": "", "summary": "PI3K generates phosphoinositol-3,4,5-trisphosphate (PIP3) from PIP2 after activation of the BCR (Gold et al. 1992). Experiments in mice indicate that PI3K associated with CD19 is partly responsible for the activity (Buhl et al. 1997, Otero et al. 2001, Aiba et al. 2008). (PI3K associated with BCAP is also partly responsible (Aiba et al. 2008).)", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O00329-1" ], "evidence": [ { "id": "R-HSA-2076220", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-2076220" } ] }, { "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-508247", "name": "Gab2 binds the p85 subunit of Class 1A PI3 kinases", "equation": "", "summary": "Shc promotes Gab2 tyrosine phosphorylation via Grb2 (Gu et al. 2000). This promotes binding of Gab2 to p85alpha, a component of Class 1A PI3Ks (Gu et al. 1998). JAK1 may also be involved in PI3K recruitment (Migone et al. 1998). Binding of p85 activates PI3K kinase activity, with consequent effects on many processes including Akt activation. This is one of two mechanisms described for the recruitment of PI3K to the IL-3/IL-5/GM-CSF receptors, the other is mediated by Serine-585 phosphorylation of the common beta chain.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P52333-1", "P42336-1", "O60674-1", "P42338-1", "O00329-1", "P23458-1" ], "evidence": [ { "id": "R-HSA-508247", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-508247" } ] }, { "id": "R-HSA-879917", "name": "CBL, GRB2, FYN and PI3K p85 subunit are constitutively associated", "equation": "", "summary": "Cbl is constitutively associated with Grb2 in resting hematopoietic cells (Anderson et al. 1997, Odai et al. 1995, Park et al. 1998, Panchamoorthy et al. 1996). Both the SH2 and SH3 domains of Grb2 are involved. Cbl has 2 distinct C-terminal domains, proximal and distal. The proximal domain binds Grb2 in resting and stimulated cells, and in stimulated cells also binds Shc. The distal domain can bind the adaptor protein CRKL.

; Tyrosine phosphorylation of Cbl in response to IL-3 releases the SH3 domain of Grb2 which then is free to bind other molecules (Park et al. 1998).
Cbl also associates with Fyn (Anderson et al. 1997) and the related kinases Hck and Lyn (Hunter et al. 1999). Binding studies indicate that this binding is independent of the phosphorylation state of Cbl; The association of Fyn with Cbl has been described as constitutive (Hunter et al. 1999).

; Cbl further associates with the p85 subunit of PI3K (Hartley et al. 1995, Anderson et al. 1997, Hunter et al. 1997), this is also described as constitutive and is mediated by the SH3 domain of p85 (Hunter et al. 1997).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P42336-1", "P06241-1", "P22681-1", "P07947-1", "P07948-1", "P08631-1", "P43405-1", "P42338-1", "O00329-1" ], "evidence": [ { "id": "R-HSA-879917", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-879917" } ] }, { "id": "R-HSA-8854905", "name": "p-5Y-GAB in the RET-GRB2-GAB complexes binds p85-PI3K", "equation": "", "summary": "Following recruitment and phosphorylation of GAB1 or GAB2 to the RET complex, it binds the p85 subunit of p85-containing PI3 kinase (p85-PI3K), resulting in its activation (Murakami et al. 1999, Hayashi et al. 2000, Besset et al. 2000). p85-PI3K consists of a p85 adaptor subunit, which contains one Src homology 3 (SH3) and two Src homology 2 (SH2) domains, and a p110 subunit that has catalytic activity (Kapeller & Cantley 1994). These subunits are tightly associated (Carpenter et al. 1990). Though p85-PI3K can be phosphorylated, it is binding of the p85 SH2 domains that activates the enzyme (Rordorf-Nikolic et al. 1995).

GAB2 has three tyrosine residues, Y452, Y476 and Y584, which are involved in p85-PI3K binding (Crouin et al. 2001, Maus et al. 2009). GAB1 also becomes tyrosine phosphorylated and directly associates with p85 when transducing signals from receptor tyrosine kinases to p85 (Holgado-Madruga et al. 1997, Mattoon et al. 2004). There are three potential binding sites for p85 on GAB1 (Y447, Y472, and Y589) (Holgado-Madruga et al. 1997). Phosphorylation at these sites in GAB1 is represented in this reaction as a likely prerequisite for p85 binding, but this is not experimentally confirmed, hence this reaction is displayed as an uncertain event.", "cellular_location": "cytosol, extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P07949-1", "P42336-1", "P42338-1", "O00329-1" ], "evidence": [ { "id": "R-HSA-8854905", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-8854905" } ] }, { "id": "R-HSA-9012657", "name": "EPO:phospho-EPOR:phospho-JAK2:LYN:phospho-IRS2 binds PI3K", "equation": "", "summary": "Phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) binds phosphorylated IRS2 associated with the phosphorylated EPOR (Bouscary et al. 2003).", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P42336-1", "O60674-1", "P48736-1", "P07948-1", "P42338-1", "O00329-1" ], "evidence": [ { "id": "R-HSA-9012657", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9012657" } ] }, { "id": "R-HSA-9021627", "name": "EPOR-associated PI3K phosphorylates PIP2 to PIP3", "equation": "", "summary": "Phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) associated with EPOR phosphorylates phosphatidylinositol 4,5-bisphosphate to yield phosphatidyl 3,4,5-trisphosphate (Kubota et al. 2001, Schmidt et al. 2004). PI3K binds the phosphorylated EPOR directly or indirectly via phosphorylated IRS2 or phosphorylated GAB1 (Bouscary et al. 2003).", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P42336-1", "O60674-1", "P48736-1", "P07948-1", "P42338-1", "O00329-1" ], "evidence": [ { "id": "R-HSA-9021627", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9021627" } ] }, { "id": "R-HSA-9027275", "name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2:phospho-GAB1 binds PI3K", "equation": "", "summary": "Phosphorylated GAB1 in a complex with EPOR binds the p85 subunit of phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) (Lecoq-Lafon et al. 1999, Wickrema et al. 1999, Bouscary et al. 2003).", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P42336-1", "O60674-1", "P48736-1", "P07948-1", "P42338-1", "O00329-1" ], "evidence": [ { "id": "R-HSA-9027275", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027275" } ] }, { "id": "R-HSA-9027280", "name": "EPO:phospho-EPOR:phospho-JAK2:LYN:IRS2 binds PI3K", "equation": "", "summary": "Phosphatidylinositol 4,5-bisphosphate 3-kinase (PI3K) can directly bind phosphotyrosine-479 in the cytosolic domain of EPOR (Kubota et al. 2001, Bouscary et al. 2003, and inferred from mouse homologs).", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P42336-1", "O60674-1", "P48736-1", "P07948-1", "P42338-1", "O00329-1" ], "evidence": [ { "id": "R-HSA-9027280", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9027280" } ] }, { "id": "R-HSA-912627", "name": "CBL ubiquitinates PI3K", "equation": "", "summary": "Cbl is an E3 ubiquitin-protein ligase that negatively regulates signaling pathways by targeting proteins for ubiquitination and proteasomal degradation (Rao et al. 2002). Cbl-B targets PI3K for ubiquitination and degradation in T cells (Fang et al. 2000). Similarly, Cbl activation by tyrosine phosphorylation increases PI3K ubiquitination and proteasomal degradation (Dufour et al. 2008).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P42336-1", "P06241-1", "P22681-1", "P07947-1", "P07948-1", "P08631-1", "P43405-1", "P42338-1", "O00329-1" ], "evidence": [ { "id": "R-HSA-912627", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912627" } ] }, { "id": "R-HSA-912629", "name": "CBL is tyrosine phosphorylated", "equation": "", "summary": "Cbl is tyrosine phosphorylated following stimulation with IL-3 (Anderson et al. 1997) and GM-CSF (Odai et al. 1995). Cbl may be phosphorylated prior to this IL-3 stimulated tyrosyl phosphorylation (Park et al. 1998). The kinase responsible for Cbl phosphorylation may be dependent on cell type; Fyn is demonstrated to have the ability to phosphorylate Cbl (Hunter et al. 1999), other candidates include Hck, Lyn (Hunter et al. 1999) and Syk (Park et al. 1998).

; Tyrosines 700, 731 and 774 are the major sites of Cbl phosphorylation by non-receptor protein tyrosine kinases, with none showing any particular specificity for sites (Tsygankov et al. 2001). Fyn was observed to be constitutively associated with Cbl in lysates of several different cell types including the interleukin-3-dependent murine myeloid cell line 32Dcl3, and the prolactin-dependent rat thymoma cell line Nb2. Cbl phosphorylation at Y731 is postulated to provide an additional interaction between Cbl and the SH2 domain of p85-PI3K (Hunter et al. 1999). Cbl-p85 association increases in activated cells (Panchamoorthy et al. 1996). Expression of a Cbl Y731F mutant which abolishes binding of Cbl to p85 markedly increased levels of p85-PI3K (Dufour et al. 2008). Cbl-p85 binding negatively regulates PI3K activity (Fang et al. 2001); Cbl phosphorylation increased PI3K ubiquitination and proteasome degradation (Dufour et al. 2008). Cbl association with members of the Crk family is mediated by phosphorylation of Y700 and Y774 (Andoniou et al. 1996), binding with Vav is mediated by Y770 (Marengere et al 1997).", "cellular_location": "cytosol", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P42336-1", "P06241-1", "P22681-1", "P07947-1", "P07948-1", "P08631-1", "P43405-1", "P42338-1", "O00329-1" ], "evidence": [ { "id": "R-HSA-912629", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-912629" } ] }, { "id": "R-HSA-914182", "name": "14-3-3 zeta binding allows recruitment of PI3K", "equation": "", "summary": "Immunoprecipitation and kinase activity experiments demonstrated that Ser-585 phosphorylation of the common beta chain (Bc) was required for activation of PI3K activity in response to IL-3 and co-precipitation of Bc, 14-3-3 zeta and the p85 subunit of Class 1A PI3 kinases (Guthridge et al. 2000). Subsequent experiments confirmed that Ser-585 phosphorylation and PI3K activation are required to promote cell survival in response to GM-CSF, but not for proliferation responses, and that this mechanism is independent of Bc tyrosine phosphorylation (Guthridge et al. 2004). This is one of two mechanisms described for the recruitment of PI3K to the IL-3/IL-5/GM-CSF receptors; the other involves Bc tyrosine-593 phosphorylation-mediated recruitment of SHC1, GRB2 and GAB2.", "cellular_location": "cytosol, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P42336-1", "O60674-1", "P42338-1", "O00329-1" ], "evidence": [ { "id": "R-HSA-914182", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-914182" } ] }, { "id": "R-HSA-9606160", "name": "p-PIK3AP1 (p-BCAP) binds PIK3CD:PIK3R1 (PI3K delta)", "equation": "", "summary": "Phosphorylated PIK3AP1 (BCAP) binds the p85 subunit of phosphoinositide 3-kinase (PI3K) (inferred from chicken homologs). PIK3AP1 is phosphorylated by LYN in response to activation of CD19.", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O00329-1" ], "evidence": [ { "id": "R-HSA-9606160", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9606160" } ] }, { "id": "R-HSA-9606887", "name": "p-CD19:VAV binds PI3K and GRB2", "equation": "", "summary": "Phosphorylated CD19 binds PI3K (Roifman and Ke 1993, Chalupny et al. 1993, Uckun et al. 1993, Weng et al. 1994, Brooks et al. 2000, Brooks et al. 2004) and can bind PLC-gamma2 (PLCG2), which competes with VAV1 for the binding to phosphotyrosine-391 on CD19 (Brooks et al. 2000, Brooks et al. 2004). GRB2 appears to bind phosphotyrosine-330 on CD19 (Brooks et al. 2004).", "cellular_location": "plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "O00329-1" ], "evidence": [ { "id": "R-HSA-9606887", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-9606887" } ] } ], "reaction_participants": [], "reaction_enzymes": [ { "uniprot_ac": "A0A0G2K344", "gene_name": "Pik3ca", "activity": [ { "ec_number": "2.7.11.1", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "A0A0G2K344", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/A0A0G2K344" } ] }, { "ec_number": "2.7.1.153", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+).", "evidence": [ { "id": "A0A0G2K344", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/A0A0G2K344" } ] }, { "ec_number": "2.7.1.137", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+).", "evidence": [ { "id": "A0A0G2K344", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/A0A0G2K344" } ] }, { "ec_number": "2.7.1.137", "activity": "", "evidence": [ { "id": "A0A0G2K344", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/A0A0G2K344" } ] }, { "ec_number": "2.7.1.153", "activity": "", "evidence": [ { "id": "A0A0G2K344", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/A0A0G2K344" } ] } ] }, { "uniprot_ac": "A0A8I5Y949", "gene_name": "Pik3cd", "activity": [ { "ec_number": "2.7.1.153", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+).", "evidence": [ { "id": "A0A8I5Y949", 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"id": "P08581", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08581" } ] } ] }, { "uniprot_ac": "P08631", "gene_name": "HCK", "activity": [ { "ec_number": "2.7.10.2", "activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].", "evidence": [ { "id": "P08631", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08631" } ] }, { "ec_number": "2.7.10.2", "activity": "", "evidence": [ { "id": "P08631", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P08631" } ] } ] }, { "uniprot_ac": "P09619", "gene_name": "PDGFRB", "activity": [ { "ec_number": "2.7.10.1", "activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].", "evidence": [ { "id": "P09619", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09619" } ] }, { "ec_number": "2.7.10.1", "activity": "", "evidence": [ { "id": "P09619", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P09619" } ] } ] }, { 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L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].", "evidence": [ { "id": "P16234", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P16234" } ] }, { "ec_number": "2.7.10.1", "activity": "", "evidence": [ { "id": "P16234", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P16234" } ] } ] }, { "uniprot_ac": "P22455", "gene_name": "FGFR4", "activity": [ { "ec_number": "2.7.10.1", "activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].", "evidence": [ { "id": "P22455", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P22455" } ] }, { "ec_number": "2.7.10.1", "activity": "", "evidence": [ { "id": "P22455", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P22455" } ] } ] }, { "uniprot_ac": "P22543", "gene_name": "VPS34", "activity": [ { "ec_number": "2.7.1.137", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+).", "evidence": [ { "id": "P22543", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P22543" } ] }, { "ec_number": "2.7.1.137", "activity": "", "evidence": [ { "id": "P22543", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P22543" } ] } ] }, { "uniprot_ac": "P22681", "gene_name": "CBL", "activity": [ { "ec_number": "2.3.2.27", "activity": "S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.", "evidence": [ { "id": "P22681", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P22681" } ] }, { "ec_number": "2.3.2.27", "activity": "", "evidence": [ { "id": "P22681", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P22681" } ] } ] }, { "uniprot_ac": "P23458", "gene_name": "JAK1", "activity": [ { "ec_number": "2.7.10.2", "activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].", "evidence": [ { "id": "P23458", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P23458" } ] }, { "ec_number": "2.7.10.2", "activity": "", "evidence": [ { "id": "P23458", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P23458" } ] } ] }, { "uniprot_ac": "P36888", "gene_name": "FLT3", "activity": [ { "ec_number": "2.7.10.1", "activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].", "evidence": [ { "id": "P36888", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P36888" } ] }, { "ec_number": "2.7.10.1", "activity": "", "evidence": [ { "id": "P36888", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P36888" } ] } ] }, { "uniprot_ac": "P42336", "gene_name": "PIK3CA", "activity": [ { "ec_number": "2.7.1.153", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+).", "evidence": [ { "id": "P42336", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42336" } ] }, { "ec_number": "2.7.1.153", "activity": "", "evidence": [ { "id": "P42336", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42336" } ] }, { "ec_number": "2.7.11.1", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "P42336", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42336" } ] }, { "ec_number": "2.7.1.137", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+).", "evidence": [ { "id": "P42336", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42336" } ] }, { "ec_number": "2.7.1.137", "activity": "", "evidence": [ { "id": "P42336", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42336" } ] } ] }, { "uniprot_ac": "P42337", "gene_name": "Pik3ca", "activity": [ { "ec_number": "2.7.11.1", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "P42337", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42337" } ] }, { "ec_number": "2.7.1.153", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+).", "evidence": [ { "id": "P42337", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42337" } ] }, { "ec_number": "2.7.1.137", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+).", "evidence": [ { "id": "P42337", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42337" } ] }, { "ec_number": "2.7.1.153", "activity": "", "evidence": [ { "id": "P42337", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42337" } ] }, { "ec_number": "2.7.1.137", "activity": "", "evidence": [ { "id": "P42337", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42337" } ] } ] }, { "uniprot_ac": "P42338", "gene_name": "PIK3CB", "activity": [ { "ec_number": "2.7.11.1", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "P42338", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42338" } ] }, { "ec_number": "2.7.1.153", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+).", "evidence": [ { "id": "P42338", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42338" } ] }, { "ec_number": "2.7.1.153", "activity": "", "evidence": [ { "id": "P42338", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42338" } ] }, { "ec_number": "2.7.1.137", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+).", "evidence": [ { "id": "P42338", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42338" } ] }, { "ec_number": "2.7.1.137", "activity": "", "evidence": [ { "id": "P42338", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P42338" } ] } ] }, { "uniprot_ac": "P43405", "gene_name": "SYK", "activity": [ { "ec_number": "2.7.10.2", "activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].", "evidence": [ { "id": "P43405", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P43405" } ] }, { "ec_number": "2.7.10.2", "activity": "", "evidence": [ { "id": "P43405", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P43405" } ] } ] }, { "uniprot_ac": "P48736", "gene_name": "PIK3CG", "activity": [ { "ec_number": "2.7.11.1", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "P48736", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P48736" } ] }, { "ec_number": "2.7.1.153", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4,5-trisphosphate) + ADP + H(+).", "evidence": [ { "id": "P48736", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P48736" } ] }, { "ec_number": "2.7.1.137", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+).", "evidence": [ { "id": "P48736", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P48736" } ] }, { "ec_number": "2.7.1.154", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + ADP + H(+).", "evidence": [ { "id": "P48736", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P48736" } ] }, { "ec_number": "2.7.1.153", "activity": "", "evidence": [ { "id": "P48736", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P48736" } ] }, { "ec_number": "2.7.1.137", "activity": "", "evidence": [ { "id": "P48736", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P48736" } ] }, { "ec_number": "2.7.1.154", "activity": "", "evidence": [ { "id": "P48736", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P48736" } ] } ] }, { "uniprot_ac": "P51617", "gene_name": "IRAK1", "activity": [ { "ec_number": "2.7.11.1", "activity": "ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].", "evidence": [ { "id": "P51617", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P51617" } ] }, { "ec_number": "2.7.11.1", "activity": "", "evidence": [ { "id": "P51617", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P51617" } ] } ] }, { "uniprot_ac": "P52333", "gene_name": "JAK3", "activity": [ { "ec_number": "2.7.10.2", "activity": "ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein].", "evidence": [ { "id": "P52333", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P52333" } ] }, { "ec_number": "2.7.10.2", "activity": "", "evidence": [ { "id": "P52333", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P52333" } ] } ] }, { "uniprot_ac": "P54673", "gene_name": "pikA", "activity": [ { "ec_number": "2.7.1.137", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+).", "evidence": [ { "id": "P54673", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P54673" } ] }, { "ec_number": "2.7.1.137", "activity": "", "evidence": [ { "id": "P54673", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P54673" } ] } ] }, { "uniprot_ac": "P54674", "gene_name": "pikB", "activity": [ { "ec_number": "2.7.1.137", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+).", "evidence": [ { "id": "P54674", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P54674" } ] }, { "ec_number": "2.7.1.137", "activity": "", "evidence": [ { "id": "P54674", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P54674" } ] } ] }, { "uniprot_ac": "P54675", "gene_name": "pikC", "activity": [ { "ec_number": "2.7.1.137", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+).", "evidence": [ { "id": "P54675", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P54675" } ] }, { "ec_number": "2.7.1.137", "activity": "", "evidence": [ { "id": "P54675", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P54675" } ] } ] }, { "uniprot_ac": "P54676", "gene_name": "pikE", "activity": [ { "ec_number": "2.7.1.137", "activity": "a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + ADP + H(+).", "evidence": [ { "id": "P54676", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P54676" } ] }, { "ec_number": "2.7.1.137", "activity": "", "evidence": [ { "id": "P54676", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P54676" } ] } ] }, { "uniprot_ac": "P63000", "gene_name": "RAC1", "activity": [ { "ec_number": "3.6.5.2", "activity": "GTP + H2O = GDP + H(+) + phosphate.", "evidence": [ { "id": "P63000", "database": "UniProtKB", "url": "https://www.uniprot.org/uniprot/P63000" } ] }, { "ec_number": "3.6.5.2", "activity": "", "evidence": [ { "id": "P63000", "database": "UniProtKB", "url": 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