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{
"metadata": {
"accession": "IPR018868",
"entry_id": null,
"type": "family",
"go_terms": [
{
"identifier": "GO:0006915",
"name": "apoptotic process",
"category": {
"code": "P",
"name": "biological_process"
}
}
],
"source_database": "interpro",
"member_databases": {
"panther": {
"PTHR28540": "BCL2-ASSOCIATED AGONIST OF CELL DEATH"
},
"pfam": {
"PF10514": "Pro-apoptotic Bcl-2 protein, BAD"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR018868",
"name": "Bcl2-associated agonist of cell death",
"type": "Family",
"children": []
},
"name": {
"name": "Bcl2-associated agonist of cell death",
"short": "BAD"
},
"description": [
{
"text": "<p>BAD is a Bcl-2 homology domain 3 (BH3)-only pro-apoptotic member of the Bcl-2 protein family that is regulated by phosphorylation in response to survival factors [[cite:PUB00044167]]. Binding of BAD to mitochondria is thought to be exclusively mediated by its BH3 domain. Membrane localisation of BAD mediates membrane translocation of Bcl-XL. The C-terminal part of BAD is sufficient for membrane binding. There are two segments with differing lipid-binding preferences, LBD1 and LBD2, that are responsible for this binding: (i) LBD1 located in the proximity of the BH3 domain (amino acids 122-131) and (ii) LBD2, the putative C-terminal α-helix-5 [[cite:PUB00044168]]. Phosphorylation-regulated 14-3-3 protein binding may expose the cholesterol-preferring LBD1 and bury the LBD2, thereby mediating translocation of BAD to raft-like micro-domains [[cite:PUB00044169]].</p>",
"llm": false,
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}
],
"wikipedia": null,
"literature": {
"PUB00044167": {
"PMID": 9372935,
"ISBN": null,
"volume": "17",
"issue": "12",
"year": 1997,
"title": "Bad is a BH3 domain-containing protein that forms an inactivating dimer with Bcl-XL.",
"URL": null,
"raw_pages": "7040-6",
"medline_journal": "Mol Cell Biol",
"ISO_journal": "Mol. Cell. Biol.",
"authors": [
"Kelekar A",
"Chang BS",
"Harlan JE",
"Fesik SW",
"Thompson CB."
],
"DOI_URL": "http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=9372935"
},
"PUB00044168": {
"PMID": 16226704,
"ISBN": null,
"volume": "8",
"issue": "4",
"year": 2005,
"title": "The BAD protein integrates survival signaling by EGFR/MAPK and PI3K/Akt kinase pathways in PTEN-deficient tumor cells.",
"URL": null,
"raw_pages": "287-97",
"medline_journal": "Cancer Cell",
"ISO_journal": "Cancer Cell",
"authors": [
"She QB",
"Solit DB",
"Ye Q",
"O'Reilly KE",
"Lobo J",
"Rosen N."
],
"DOI_URL": "http://dx.doi.org/10.1016/j.ccr.2005.09.006"
},
"PUB00044169": {
"PMID": 16603546,
"ISBN": null,
"volume": "281",
"issue": "25",
"year": 2006,
"title": "Reversible membrane interaction of BAD requires two C-terminal lipid binding domains in conjunction with 14-3-3 protein binding.",
"URL": null,
"raw_pages": "17321-36",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Hekman M",
"Albert S",
"Galmiche A",
"Rennefahrt UE",
"Fueller J",
"Fischer A",
"Puehringer D",
"Wiese S",
"Rapp UR."
],
"DOI_URL": "http://dx.doi.org/10.1074/jbc.M600292200"
}
},
"set_info": null,
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"counters": {
"subfamilies": 0,
"domain_architectures": 4,
"interactions": 0,
"matches": 646,
"pathways": 11,
"proteins": 646,
"proteomes": 345,
"sets": 0,
"structural_models": {
"alphafold": 585,
"bfvd": 0
},
"structures": 6,
"taxa": 1217
},
"entry_annotations": {
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"alignment:full": 431
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "9o16",
"name": "Crystal Structure of human BCL-2 (R129L) mutant in complex with a stapled BAD BH3 peptide BAD SAHB 4.2"
}
}
}
