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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR050168",
"entry_id": null,
"type": "family",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"panther": {
"PTHR23077": "AAA ATPase domain-containing protein"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR050168",
"name": "AAA ATPase domain-containing protein",
"type": "Family",
"children": []
},
"name": {
"name": "AAA ATPase domain-containing protein",
"short": "AAA_ATPase_domain"
},
"description": [
{
"text": "<p>This family of proteins is characterized by the presence of AAA ATPase domains, suggesting a role in various cellular processes that require ATP hydrolysis. Members are involved in critical functions such as cell division, growth, protein degradation, vesicle fusion, and organelle biogenesis. They participate in the unfolding of substrate proteins, disassembly of protein complexes, and the regulation of proteasomal degradation pathways. Some proteins in this family are implicated in the endoplasmic reticulum-associated degradation (ERAD) process, ribosome biogenesis, and the response to endoplasmic reticulum stress. They also contribute to the maintenance of protein quality control by mediating the extraction and degradation of misfolded or damaged proteins. Additionally, these proteins play roles in the formation and reassembly of the Golgi apparatus during mitosis, DNA damage response, and autophagy.</p>",
"llm": true,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": null,
"set_info": null,
"overlaps_with": null,
"counters": {
"subfamilies": 0,
"domain_architectures": 0,
"interactions": 0,
"matches": 49774,
"pathways": 98,
"proteins": 49774,
"proteomes": 10097,
"sets": 0,
"structural_models": {
"alphafold": 40879,
"bfvd": 2
},
"structures": 194,
"taxa": 23489
},
"entry_annotations": {},
"cross_references": {},
"is_llm": true,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "6g2z",
"name": "Crystal structure of the p97 D2 domain in a helical split-washer conformation"
}
}
}