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{
"metadata": {
"accession": "PS51547",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "profile",
"member_databases": null,
"integrated": "IPR002420",
"hierarchy": null,
"name": {
"name": "C2 phosphatidylinositol 3-kinase (PI3K)-type domain profile",
"short": "C2_PI3K"
},
"description": [
{
"text": "<p>Phosphatidylinositol 3-kinases (PI3Ks) are lipid kinases that phosphorylate\n4,5-bisphonate (PI(4,5) P2 or PIP2) at the 3-position of the inositol ring,\nand thus generate phosphatidylinositol 3,4,5-trisphosphate (PIP3), which, in\nturns, initiates a vast array of signaling events. PI3Ks can be grouped into\nthree classes based on their domain organization. Class I PI3Ks are\nheterodimers consisting of a p110 catalytic subunit and a regulatory subunit\nof either the p85 type (associated with the class IA p110 isoforms p110alpha,\np110beta or p110delta) or the p101 type (associated with the class IB p110\nisoform p110gamma). Common to all catalytic subunits are the N-terminal\nadaptor-binding domain (ABD) that binds to p85, the Ras-\nbinding domain (RBD), the putative membrane-binding domain (C2), the helical\ndomain of unknown function, and the kinase catalytic domain.\nClass II PI3Ks lack the ABD domain and are distinguished by a carboxy terminal\nC2 domain. Class III enzymes lack the ABD and RBD domains\n[[cite:PUB00043265]][[cite:PUB00049324]][[cite:PUB00111329]][[cite:PUB00046181]].\n\nThe PI3K-type C2 domain is an eight-stranded antiparallel beta-sandwich\nconsisting of two four-stranded beta-sheets [[cite:PUB00043265]][[cite:PUB00049324]][[cite:PUB00111329]][[cite:PUB00046181]].\n\nThe profile we developed covers the entire PI3K-type C2 domain.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00046181": {
"PMID": 10580505,
"ISBN": null,
"volume": "402",
"issue": "6759",
"year": 1999,
"title": "Structural insights into phosphoinositide 3-kinase catalysis and signalling.",
"URL": null,
"raw_pages": "313-20",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Walker EH",
"Perisic O",
"Ried C",
"Stephens L",
"Williams RL."
],
"DOI_URL": "http://dx.doi.org/10.1038/46319"
},
"PUB00111329": {
"PMID": 20154668,
"ISBN": null,
"volume": "6",
"issue": "3",
"year": 2010,
"title": "The p110delta structure: mechanisms for selectivity and potency of new PI(3)K inhibitors.",
"URL": null,
"raw_pages": "244",
"medline_journal": "Nat Chem Biol",
"ISO_journal": "Nat Chem Biol",
"authors": [
"Berndt A",
"Miller S",
"Williams O",
"Le DD",
"Houseman BT",
"Pacold JI",
"Gorrec F",
"Hon WC",
"Liu Y",
"Rommel C",
"Gaillard P",
"Ruckle T",
"Schwarz MK",
"Shokat KM",
"Shaw JP",
"Williams RL."
],
"DOI_URL": null
},
"PUB00043265": {
"PMID": 17626883,
"ISBN": null,
"volume": "317",
"issue": "5835",
"year": 2007,
"title": "Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit.",
"URL": null,
"raw_pages": "239-42",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Miled N",
"Yan Y",
"Hon WC",
"Perisic O",
"Zvelebil M",
"Inbar Y",
"Schneidman-Duhovny D",
"Wolfson HJ",
"Backer JM",
"Williams RL."
],
"DOI_URL": "http://dx.doi.org/10.1126/science.1135394"
},
"PUB00049324": {
"PMID": 18079394,
"ISBN": null,
"volume": "318",
"issue": "5857",
"year": 2007,
"title": "The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations.",
"URL": null,
"raw_pages": "1744-8",
"medline_journal": "Science",
"ISO_journal": "Science",
"authors": [
"Huang CH",
"Mandelker D",
"Schmidt-Kittler O",
"Samuels Y",
"Velculescu VE",
"Kinzler KW",
"Vogelstein B",
"Gabelli SB",
"Amzel LM."
],
"DOI_URL": "http://dx.doi.org/10.1126/science.1150799"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 16009,
"pathways": 0,
"proteins": 15999,
"proteomes": 3182,
"sets": 0,
"structural_models": {
"alphafold": 11336,
"bfvd": 1
},
"structures": 328,
"taxa": 9771
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
