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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR034663",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0004697",
"name": "diacylglycerol-dependent serine/threonine kinase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0006468",
"name": "protein phosphorylation",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd05615": "Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR034663",
"name": "Classical Protein Kinase C alpha, catalytic domain",
"type": "Domain",
"children": []
},
"name": {
"name": "Classical Protein Kinase C alpha, catalytic domain",
"short": "cPKC_alpha"
},
"description": [
{
"text": "<p>Protein kinases C (PKCs) constitute a family of Ser/Thr kinases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain [[cite:PUB00043770], [cite:PUB00083979]]. Conventional PKCs (cPKCs) have functional C1A and C1B domains, and a C2 domain. PKCs undergo three phosphorylations in order to take mature forms [[cite:PUB00083977], [cite:PUB00083978]]. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine for activation. There are three conventional PKC isoenzymes (alpha, beta, and gamma).</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility [[cite:PUB00083976], [cite:PUB00083975]]. It plays a role in the signalling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumours [[cite:PUB00083963], [cite:PUB00083968], [cite:PUB00083971], [cite:PUB00083972]]. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion [[cite:PUB00083981]].</p>",
"llm": false,
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}
],
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"literature": {
"PUB00083963": {
"PMID": 16424642,
"ISBN": null,
"volume": "115",
"issue": "1-2",
"year": 2006,
"title": "The role of protein kinase C-alpha in hematologic malignancies.",
"URL": null,
"raw_pages": "1-8",
"medline_journal": "Acta Haematol",
"ISO_journal": "Acta Haematol.",
"authors": [
"Lahn M",
"Sundell K",
"Kohler G."
],
"DOI_URL": "http://dx.doi.org/10.1159/000089458"
},
"PUB00083968": {
"PMID": 15057036,
"ISBN": null,
"volume": "14",
"issue": "2",
"year": 2004,
"title": "The role of protein kinase C-alpha (PKC-alpha) in melanoma.",
"URL": null,
"raw_pages": "85-9",
"medline_journal": "Melanoma Res",
"ISO_journal": "Melanoma Res.",
"authors": [
"Lahn MM",
"Sundell KL."
],
"DOI_URL": "http://dx.doi.org/10.1097/00008390-200404000-00002"
},
"PUB00083981": {
"PMID": 16407820,
"ISBN": null,
"volume": "25",
"issue": "23",
"year": 2006,
"title": "Upregulation and activation of PKC alpha by ErbB2 through Src promotes breast cancer cell invasion that can be blocked by combined treatment with PKC alpha and Src inhibitors.",
"URL": null,
"raw_pages": "3286-95",
"medline_journal": "Oncogene",
"ISO_journal": "Oncogene",
"authors": [
"Tan M",
"Li P",
"Sun M",
"Yin G",
"Yu D."
],
"DOI_URL": "http://dx.doi.org/10.1038/sj.onc.1209361"
},
"PUB00043770": {
"PMID": 12495431,
"ISBN": null,
"volume": "370",
"issue": "Pt 2",
"year": 2003,
"title": "Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm.",
"URL": null,
"raw_pages": "361-71",
"medline_journal": "Biochem J",
"ISO_journal": "Biochem. J.",
"authors": [
"Newton AC."
],
"DOI_URL": "http://dx.doi.org/10.1042/BJ20021626"
},
"PUB00083975": {
"PMID": 17603037,
"ISBN": null,
"volume": "85",
"issue": "2",
"year": 2007,
"title": "Protein kinase C alpha and epsilon differentially modulate hepatocyte growth factor-induced epithelial proliferation and migration.",
"URL": null,
"raw_pages": "289-97",
"medline_journal": "Exp Eye Res",
"ISO_journal": "Exp. Eye Res.",
"authors": [
"Sharma GD",
"Kakazu A",
"Bazan HE."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.exer.2007.05.004"
},
"PUB00083977": {
"PMID": 8749392,
"ISBN": null,
"volume": "5",
"issue": "12",
"year": 1995,
"title": "Protein kinase C is regulated in vivo by three functionally distinct phosphorylations.",
"URL": null,
"raw_pages": "1394-1403",
"medline_journal": "Curr Biol",
"ISO_journal": "Curr. Biol.",
"authors": [
"Keranen LM",
"Dutil EM",
"Newton AC."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0960-9822(95)00277-6"
},
"PUB00083976": {
"PMID": 17588800,
"ISBN": null,
"volume": "39",
"issue": "10",
"year": 2007,
"title": "Protein kinase C-alpha antagonizes apoptosis induction by histone deacetylase inhibitors in multidrug resistant leukaemia cells.",
"URL": null,
"raw_pages": "1877-85",
"medline_journal": "Int J Biochem Cell Biol",
"ISO_journal": "Int. J. Biochem. Cell Biol.",
"authors": [
"Castro-Galache MD",
"Menendez-Gutierrez MP",
"Carrasco Garcia E",
"Garcia-Morales P",
"Martinez-Lacaci I",
"Saceda M",
"Ferragut JA."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.biocel.2007.05.007"
},
"PUB00083979": {
"PMID": 24766842,
"ISBN": null,
"volume": "21",
"issue": "4",
"year": 2014,
"title": "Ready, set, go! How protein kinase C manages dynamic signaling.",
"URL": null,
"raw_pages": "433-4",
"medline_journal": "Chem Biol",
"ISO_journal": "Chem. Biol.",
"authors": [
"Stahelin RV."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.chembiol.2014.04.003"
},
"PUB00083978": {
"PMID": 19934406,
"ISBN": null,
"volume": "298",
"issue": "3",
"year": 2010,
"title": "Protein kinase C: poised to signal.",
"URL": null,
"raw_pages": "E395-402",
"medline_journal": "Am J Physiol Endocrinol Metab",
"ISO_journal": "Am. J. Physiol. Endocrinol. Metab.",
"authors": [
"Newton AC."
],
"DOI_URL": "http://dx.doi.org/10.1152/ajpendo.00477.2009"
},
"PUB00083971": {
"PMID": 14687784,
"ISBN": null,
"volume": "40",
"issue": "1",
"year": 2004,
"title": "The role of protein kinase C-alpha (PKC-alpha) in malignancies of the gastrointestinal tract.",
"URL": null,
"raw_pages": "10-20",
"medline_journal": "Eur J Cancer",
"ISO_journal": "Eur. J. Cancer",
"authors": [
"Lahn M",
"Paterson BM",
"Sundell K",
"Ma D."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.ejca.2003.08.020"
},
"PUB00083972": {
"PMID": 17548205,
"ISBN": null,
"volume": "55",
"issue": "6",
"year": 2007,
"title": "Classical PKC isoforms in cancer.",
"URL": null,
"raw_pages": "477-86",
"medline_journal": "Pharmacol Res",
"ISO_journal": "Pharmacol. Res.",
"authors": [
"Martiny-Baron G",
"Fabbro D."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.phrs.2007.04.001"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR011009",
"name": "Protein kinase-like domain superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 618,
"pathways": 52,
"proteins": 618,
"proteomes": 435,
"sets": 0,
"structural_models": {
"alphafold": 582,
"bfvd": 0
},
"structures": 4,
"taxa": 1339
},
"entry_annotations": {},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "2.7.11.13",
"url": "https://enzyme.expasy.org/EC/2.7.11.13"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
