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{
"metadata": {
"accession": "IPR042460",
"entry_id": null,
"type": "homologous_superfamily",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"cathgene3d": {
"G3DSA:1.10.238.200": "Cullin, PONY binding domain"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR042460",
"name": "DCN1-like, PONY binding domain",
"type": "Homologous_superfamily",
"children": []
},
"name": {
"name": "DCN1-like, PONY binding domain",
"short": "DCN1-like_PONY"
},
"description": [
{
"text": "<p>This superfamily represents a domain is found in DCN1-like proteins. Proteins of the DCN family may contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes, which are multi-protein complexes required for polyubiquitination and subsequent degradation of target proteins by the 26S proteasome [[cite:PUB00021043], [cite:PUB00057468]].</p>\n\n<p>The structure of this domain is composed entirely of α helices [[cite:PUB00047735], [cite:PUB00050725]]. It has been referred to as potentiating neddylation domain (PONY) and can be found in association with an N-terminal UBA domain. The PONY domain contains a cullin-binding surface within its C-terminal region and is sufficient to promote neddylation [[cite:PUB00050725], [cite:PUB00064019]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00064019": {
"PMID": 23201271,
"ISBN": null,
"volume": "21",
"issue": "1",
"year": 2013,
"title": "Structural Conservation of Distinctive N-terminal Acetylation-Dependent Interactions across a Family of Mammalian NEDD8 Ligation Enzymes.",
"URL": null,
"raw_pages": "42-53",
"medline_journal": "Structure",
"ISO_journal": "Structure",
"authors": [
"Monda JK",
"Scott DC",
"Miller DJ",
"Lydeard J",
"King D",
"Harper JW",
"Bennett EJ",
"Schulman BA."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.str.2012.10.013"
},
"PUB00050725": {
"PMID": 18206966,
"ISBN": null,
"volume": "29",
"issue": "1",
"year": 2008,
"title": "Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation.",
"URL": null,
"raw_pages": "23-35",
"medline_journal": "Mol Cell",
"ISO_journal": "Mol. Cell",
"authors": [
"Kurz T",
"Chou YC",
"Willems AR",
"Meyer-Schaller N",
"Hecht ML",
"Tyers M",
"Peter M",
"Sicheri F."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.molcel.2007.12.012"
},
"PUB00057468": {
"PMID": 18826954,
"ISBN": null,
"volume": "283",
"issue": "48",
"year": 2008,
"title": "SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation.",
"URL": null,
"raw_pages": "33211-20",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Kim AY",
"Bommelje CC",
"Lee BE",
"Yonekawa Y",
"Choi L",
"Morris LG",
"Huang G",
"Kaufman A",
"Ryan RJ",
"Hao B",
"Ramanathan Y",
"Singh B."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M804440200"
},
"PUB00047735": {
"PMID": 17597076,
"ISBN": null,
"volume": "282",
"issue": "34",
"year": 2007,
"title": "Structural basis for the function of DCN-1 in protein Neddylation.",
"URL": null,
"raw_pages": "24490-4",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Yang X",
"Zhou J",
"Sun L",
"Wei Z",
"Gao J",
"Gong W",
"Xu RM",
"Rao Z",
"Liu Y."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.C700038200"
},
"PUB00021043": {
"PMID": 15988528,
"ISBN": null,
"volume": "435",
"issue": "7046",
"year": 2005,
"title": "The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae.",
"URL": null,
"raw_pages": "1257-61",
"medline_journal": "Nature",
"ISO_journal": "Nature",
"authors": [
"Kurz T",
"Ozlu N",
"Rudolf F",
"O'Rourke SM",
"Luke B",
"Hofmann K",
"Hyman AA",
"Bowerman B",
"Peter M."
],
"DOI_URL": "http://dx.doi.org/10.1038/nature03662"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR005176",
"name": "Potentiating neddylation domain",
"type": "domain"
},
{
"accession": "IPR014764",
"name": "Defective-in-cullin neddylation protein",
"type": "family"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 12886,
"pathways": 10,
"proteins": 12816,
"proteomes": 3211,
"sets": 0,
"structural_models": {
"alphafold": 11628,
"bfvd": 0
},
"structures": 30,
"taxa": 9240
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "3tdu",
"name": "N-terminal acetylation acts as an avidity enhancer within an interconnected multiprotein complex: Structure of a human Cul1WHB-Dcn1P-acetylated Ubc12N complex"
}
}
}
