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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR047560",
"entry_id": null,
"type": "domain",
"go_terms": [
{
"identifier": "GO:0008270",
"name": "zinc ion binding",
"category": {
"code": "F",
"name": "molecular_function"
}
}
],
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd20359": "Rcat domain found in cullin-9 (CUL-9) and similar proteins"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR047560",
"name": "Cullin-9, Rcat domain",
"type": "Domain",
"children": []
},
"name": {
"name": "Cullin-9, Rcat domain",
"short": "Rcat_RBR_CUL9"
},
"description": [
{
"text": "<p>This entry represents the Rcat domain of Cullin-9 and similar proteins from vertebrates. It is essential for RBR E3 ligase activity. This domain adopts the same fold as the BRcat domain and similarly coordinates two zinc atoms that are essential for its folding.</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>Cullin-9 (CUL-9), also called UbcH7-associated protein 1 (H7-AP1), p53-associated parkin-like cytoplasmic protein, or PARC, is a cytoplasmic RBR-type E3 ubiquitin-protein ligase that function as a tumour suppressor and promotes p53-dependent apoptosis. It mediates the ubiquitination and degradation of cytosolic cytochrome c to promote survival in neurons and cancer cells. It is also a critical downstream effector of the 3M complex in the maintenance of microtubules and genome integrity. Moreover, CUL-9, together with CUL-7, forms homodimers and heterodimers, as well as some atypical Cullin RING ligase complexes, which may exhibit ubiquitin ligase activity. CUL-9 contains a CPH domain (conserved in Cul7, PARC, and HERC2 proteins), a DOC (DOC1/APC10) domain, cullin homology domains linked with E3 ligase function, and a C-terminal RBR domain previously known as RING-BetweenRING-RING domain or TRIAD [two RING fingers and a DRIL (double RING finger linked)] domain. Based on current understanding of the structural biology of RBR ligases, the nomenclature of RBR has been changed to RING1-BRcat (benign-catalytic)-Rcat (required-for-catalysis) recently. The RBR domain uses an auto-inhibitory mechanism to modulate ubiquitination activity, as well as a hybrid mechanism that combines aspects from both RING and HECT E3 ligase functions to facilitate the ubiquitination reaction [[cite:PUB00075286], [cite:PUB00075287], [cite:PUB00075111], [cite:PUB00103540], [cite:PUB00103544], [cite:PUB00103542], [cite:PUB00103541], [cite:PUB00103543], [cite:PUB00103545]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00075111": {
"PMID": 24793696,
"ISBN": null,
"volume": "54",
"issue": "5",
"year": 2014,
"title": "CUL9 mediates the functions of the 3M complex and ubiquitylates survivin to maintain genome integrity.",
"URL": null,
"raw_pages": "805-19",
"medline_journal": "Mol Cell",
"ISO_journal": "Mol. Cell",
"authors": [
"Li Z",
"Pei XH",
"Yan J",
"Yan F",
"Cappell KM",
"Whitehurst AW",
"Xiong Y."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.molcel.2014.03.046"
},
"PUB00075286": {
"PMID": 12526791,
"ISBN": null,
"volume": "112",
"issue": "1",
"year": 2003,
"title": "Parc: a cytoplasmic anchor for p53.",
"URL": null,
"raw_pages": "29-40",
"medline_journal": "Cell",
"ISO_journal": "Cell",
"authors": [
"Nikolaev AY",
"Li M",
"Puskas N",
"Qin J",
"Gu W."
],
"DOI_URL": "http://dx.doi.org/10.1016/S0092-8674(02)01255-2"
},
"PUB00075287": {
"PMID": 17332328,
"ISBN": null,
"volume": "67",
"issue": "5",
"year": 2007,
"title": "PARC and CUL7 form atypical cullin RING ligase complexes.",
"URL": null,
"raw_pages": "2006-14",
"medline_journal": "Cancer Res",
"ISO_journal": "Cancer Res.",
"authors": [
"Skaar JR",
"Florens L",
"Tsutsumi T",
"Arai T",
"Tron A",
"Swanson SK",
"Washburn MP",
"DeCaprio JA."
],
"DOI_URL": "http://dx.doi.org/10.1158/0008-5472.CAN-06-3241"
},
"PUB00103540": {
"PMID": 25028717,
"ISBN": null,
"volume": "7",
"issue": "334",
"year": 2014,
"title": "The E3 ligase PARC mediates the degradation of cytosolic cytochrome c to promote survival in neurons and cancer cells.",
"URL": null,
"raw_pages": "ra67",
"medline_journal": "Sci Signal",
"ISO_journal": "Sci Signal",
"authors": [
"Gama V",
"Swahari V",
"Schafer J",
"Kole AJ",
"Evans A",
"Huang Y",
"Cliffe A",
"Golitz B",
"Sciaky N",
"Pei XH",
"Xiong Y",
"Deshmukh M."
],
"DOI_URL": null
},
"PUB00103541": {
"PMID": 21487039,
"ISBN": null,
"volume": "71",
"issue": "8",
"year": 2011,
"title": "Cytoplasmic CUL9/PARC ubiquitin ligase is a tumor suppressor and promotes p53-dependent apoptosis.",
"URL": null,
"raw_pages": "2969-77",
"medline_journal": "Cancer Res",
"ISO_journal": "Cancer Res",
"authors": [
"Pei XH",
"Bai F",
"Li Z",
"Smith MD",
"Whitewolf G",
"Jin R",
"Xiong Y."
],
"DOI_URL": null
},
"PUB00103542": {
"PMID": 21554755,
"ISBN": null,
"volume": "12",
"issue": "4",
"year": 2011,
"title": "The cullin protein family.",
"URL": null,
"raw_pages": "220",
"medline_journal": "Genome Biol",
"ISO_journal": "Genome Biol",
"authors": [
"Sarikas A",
"Hartmann T",
"Pan ZQ."
],
"DOI_URL": null
},
"PUB00103543": {
"PMID": 16875676,
"ISBN": null,
"volume": "348",
"issue": "1",
"year": 2006,
"title": "A novel p53-binding domain in CUL7.",
"URL": null,
"raw_pages": "132-8",
"medline_journal": "Biochem Biophys Res Commun",
"ISO_journal": "Biochem Biophys Res Commun",
"authors": [
"Kasper JS",
"Arai T",
"DeCaprio JA."
],
"DOI_URL": null
},
"PUB00103544": {
"PMID": 25028716,
"ISBN": null,
"volume": "7",
"issue": "334",
"year": 2014,
"title": "Killing the Killer: PARC/CUL9 promotes cell survival by destroying cytochrome C.",
"URL": null,
"raw_pages": "pe17",
"medline_journal": "Sci Signal",
"ISO_journal": "Sci Signal",
"authors": [
"Lopez J",
"Tait SW."
],
"DOI_URL": null
},
"PUB00103545": {
"PMID": 12734414,
"ISBN": null,
"volume": "2",
"issue": "3",
"year": 2003,
"title": "PARC: a potential target for cancer therapy.",
"URL": null,
"raw_pages": "169-71",
"medline_journal": "Cell Cycle",
"ISO_journal": "Cell Cycle",
"authors": [
"Nikolaev AY",
"Gu W."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 845,
"pathways": 1,
"proteins": 845,
"proteomes": 322,
"sets": 0,
"structural_models": {
"alphafold": 33,
"bfvd": 0
},
"structures": 3,
"taxa": 1205
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
