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{
"metadata": {
"accession": "IPR053963",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF21925": "XRCC4 C-terminal region"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR053963",
"name": "XRCC4, C-terminal domain",
"type": "Domain",
"children": []
},
"name": {
"name": "XRCC4, C-terminal domain",
"short": "XRCC4_C"
},
"description": [
{
"text": "<p>This entry represents the C-terminal disordered region from the XRCC4 protein. This domain acts as an activator of the phospholipid scramblase activity of XKR4 [[cite:PUB00154390]]. Upon apoptotic stimuli, XRCC4 is cleaved by caspases, and its C-terminal fragment with an intrinsically disordered region is released into the cytoplasm. This fragment interacts directly with the Xkr4 dimer to activate it [[cite:PUB00154390]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>DNA repair protein XRCC4 is a DNA non-homologous end joining (NHEJ) core factor, required for double-strand break repair and V(D)J recombination [[cite:PUB00147236], [cite:PUB00012766]]. It acts as a scaffold protein that regulates recruitment of other proteins to DNA double-strand breaks [[cite:PUB00154391]]. XRCC4 plays a key role in the NHEJ ligation step of the broken DNA during DSB repair via direct interaction with DNA ligase IV (LIG4): the LIG4-XRCC4 subcomplex reseals the DNA breaks after the gap filling is completed [[cite:PUB00147236], [cite:PUB00012766]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00154390": {
"PMID": 33725486,
"ISBN": null,
"volume": "81",
"issue": "7",
"year": 2021,
"title": "Caspase cleavage releases a nuclear protein fragment that stimulates phospholipid scrambling at the plasma membrane.",
"URL": null,
"raw_pages": "1397-1410.e9",
"medline_journal": "Mol Cell",
"ISO_journal": "Mol Cell",
"authors": [
"Maruoka M",
"Zhang P",
"Mori H",
"Imanishi E",
"Packwood DM",
"Harada H",
"Kosako H",
"Suzuki J."
],
"DOI_URL": "https://doi.org/10.1016/j.molcel.2021.02.025"
},
"PUB00012766": {
"PMID": 12517771,
"ISBN": null,
"volume": "63",
"issue": "1",
"year": 2003,
"title": "Requirement for XRCC4 and DNA ligase IV in alignment-based gap filling for nonhomologous DNA end joining in vitro.",
"URL": null,
"raw_pages": "22-4",
"medline_journal": "Cancer Res",
"ISO_journal": "Cancer Res.",
"authors": [
"Lee JW",
"Yannone SM",
"Chen DJ",
"Povirk LF."
],
"DOI_URL": "http://cancerres.aacrjournals.org/cgi/content/abstract/63/1/22"
},
"PUB00147236": {
"PMID": 10757784,
"ISBN": null,
"volume": "20",
"issue": "9",
"year": 2000,
"title": "Ku recruits the XRCC4-ligase IV complex to DNA ends.",
"URL": null,
"raw_pages": "2996-3003",
"medline_journal": "Mol Cell Biol",
"ISO_journal": "Mol Cell Biol",
"authors": [
"Nick McElhinny SA",
"Snowden CM",
"McCarville J",
"Ramsden DA."
],
"DOI_URL": null
},
"PUB00154391": {
"PMID": 15385968,
"ISBN": null,
"volume": "23",
"issue": "19",
"year": 2004,
"title": "Xrcc4 physically links DNA end processing by polynucleotide kinase to DNA ligation by DNA ligase IV.",
"URL": null,
"raw_pages": "3874-85",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J",
"authors": [
"Koch CA",
"Agyei R",
"Galicia S",
"Metalnikov P",
"O'Donnell P",
"Starostine A",
"Weinfeld M",
"Durocher D."
],
"DOI_URL": "https://doi.org/10.1038/sj.emboj.7600375"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 10,
"interactions": 0,
"matches": 794,
"pathways": 5,
"proteins": 794,
"proteomes": 440,
"sets": 0,
"structural_models": {
"alphafold": 717,
"bfvd": 0
},
"structures": 17,
"taxa": 1560
},
"entry_annotations": {
"alignment:seed": 10,
"alignment:full": 579
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
