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{
"metadata": {
"accession": "IPR033127",
"entry_id": null,
"type": "active_site",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"prosite": {
"PS00865": "Ubiquitin-activating enzyme active site"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR033127",
"name": "Ubiquitin-activating enzyme E1, Cys active site",
"type": "Active_site",
"children": []
},
"name": {
"name": "Ubiquitin-activating enzyme E1, Cys active site",
"short": "UBQ-activ_enz_E1_Cys_AS"
},
"description": [
{
"text": "<p>Ubiquitin-activating enzyme (E1 enzyme) [[cite:PUB00000623], [cite:PUB00005373]] activates ubiquitin by first adenylating with ATP its C-terminal glycine residue and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding an ubiquitin-E1 thiolester and free AMP. Later the ubiquitin moiety is transferred to a cysteine residue on one of the many forms of ubiquitin- conjugating enzymes (E2).</p>\n\n<p>E1 is a large monomeric protein of about 110 to 115 Kd (about 1000 residues). In yeast there are two forms (UBA1 and UBA2) [[cite:PUB00002915]], while in plants and mammals multiple forms exist including a form which is Y-linked in mouse and some other mammals and which may be involved in spermatogenesis.</p>\n\n<p>It has been shown that the last of the five cysteines that are conserved in the sequence of E1 from various species is the one that binds ubiquitin [[cite:PUB00002725]]. This entry represents a conserved region containing the active site cysteine.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00000623": {
"PMID": 1647207,
"ISBN": null,
"volume": "1089",
"issue": "2",
"year": 1991,
"title": "Genetic analysis of the ubiquitin system.",
"URL": null,
"raw_pages": "127-39",
"medline_journal": "Biochim Biophys Acta",
"ISO_journal": "Biochim. Biophys. Acta",
"authors": [
"Jentsch S",
"Seufert W",
"Hauser HP."
],
"DOI_URL": "http://dx.doi.org/10.1016/0167-4781(91)90001-3"
},
"PUB00005373": {
"PMID": 1656558,
"ISBN": null,
"volume": "16",
"issue": "7",
"year": 1991,
"title": "The ubiquitin pathway for protein degradation.",
"URL": null,
"raw_pages": "265-8",
"medline_journal": "Trends Biochem Sci",
"ISO_journal": "Trends Biochem. Sci.",
"authors": [
"Hershko A."
],
"DOI_URL": "http://dx.doi.org/10.1016/0968-0004(91)90101-Z"
},
"PUB00002915": {
"PMID": 7629121,
"ISBN": null,
"volume": "270",
"issue": "30",
"year": 1995,
"title": "An essential yeast gene encoding a homolog of ubiquitin-activating enzyme.",
"URL": null,
"raw_pages": "18099-109",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Dohmen RJ",
"Stappen R",
"McGrath JP",
"Forrova H",
"Kolarov J",
"Goffeau A",
"Varshavsky A."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.270.30.18099"
},
"PUB00002725": {
"PMID": 1634524,
"ISBN": null,
"volume": "267",
"issue": "21",
"year": 1992,
"title": "Multiple forms of ubiquitin-activating enzyme E1 from wheat. Identification of an essential cysteine by in vitro mutagenesis.",
"URL": null,
"raw_pages": "14799-803",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Hatfield PM",
"Vierstra RD."
],
"DOI_URL": "http://intl.jbc.org/cgi/reprint/267/21/14799.pdf"
}
},
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 14212,
"pathways": 53,
"proteins": 14193,
"proteomes": 3358,
"sets": 0,
"structural_models": {
"alphafold": 12556,
"bfvd": 1
},
"structures": 63,
"taxa": 9593
},
"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": "6.2.1",
"url": "https://enzyme.expasy.org/EC/6.2.1"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}
