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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR012108",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0000287",
"name": "magnesium ion binding",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0003875",
"name": "ADP-ribosylarginine hydrolase activity",
"category": {
"code": "F",
"name": "molecular_function"
}
},
{
"identifier": "GO:0051725",
"name": "protein de-ADP-ribosylation",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"pirsf": {
"PIRSF016939": "ADP-ribosylarginine hydrolase"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR005502",
"name": "ADP-ribosylation/Crystallin J1",
"type": "Family",
"children": [
{
"accession": "IPR012108",
"name": "ADP-ribosylarginine hydrolase",
"type": "Family",
"children": []
},
{
"accession": "IPR013479",
"name": "ADP-ribosyl-dinitrogen reductase hydrolase",
"type": "Family",
"children": []
},
{
"accession": "IPR049650",
"name": "ADP-ribosylarginine hydrolase Tri1-like",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "ADP-ribosylarginine hydrolase",
"short": "ADP-ribosylarg_hydro"
},
"description": [
{
"text": "<p>This enzyme catalyzes the reverse reaction of mono-ADP-ribosylation by removing ADP-ribose from arginine residues in ADP-ribosylated proteins. NAD:arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolases catalyse opposing arms of the putative ADP-ribosylation cycle.</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00008412": {
"PMID": 8349667,
"ISBN": null,
"volume": "268",
"issue": "24",
"year": 1993,
"title": "Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase.",
"URL": null,
"raw_pages": "17837-43",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Takada T",
"Iida K",
"Moss J."
],
"DOI_URL": "http://intl.jbc.org/cgi/content/abstract/268/24/17837"
},
"PUB00015992": {
"PMID": 10358013,
"ISBN": null,
"volume": "274",
"issue": "24",
"year": 1999,
"title": "Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases.",
"URL": null,
"raw_pages": "16736-40",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Konczalik P",
"Moss J."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.274.24.16736"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR036705",
"name": "ADP-ribosylation/Crystallin J1 superfamily",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 1328,
"pathways": 0,
"proteins": 1328,
"proteomes": 696,
"sets": 0,
"structural_models": {
"alphafold": 1250,
"bfvd": 0
},
"structures": 4,
"taxa": 2264
},
"entry_annotations": {},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "3hfw",
"name": "Crystal Structure of human ADP-ribosylhydrolase 1 (hARH1)"
}
}
}
