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{
    "metadata": {
        "accession": "PF12014",
        "entry_id": null,
        "type": "domain",
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        "source_database": "pfam",
        "member_databases": null,
        "integrated": null,
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        "name": {
            "name": "Cyclin D1 binding domain",
            "short": "Cyclin_D1_bind"
        },
        "description": [
            {
                "text": "<p>Ubiquitin-dependent proteolysis of cyclin D1 is associated with normal and tumour cell proliferation and survival. The best characterised member of this family is the SCF FBXO31 (Skp1-Cul1-Rbx1-FBXO31) ubiquitin ligase complex mediates genotoxic stress-induced cyclin D1 degradation [[cite:PUB00098610]]. FBXO31 possesses a unique substrate-binding beta barrel domain, whereas cyclin D1 binds to FBXO31 by tucking its free C-terminal carboxylate tail into an open cavity of the C-terminal FBXO31 beta-barrel. Biophysical and functional studies demonstrated that SCFFBXO31 is capable of recruiting and ubiquitinating cyclin D1 in a phosphorylation-independent manner.</p>",
                "llm": false,
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            }
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        "wikipedia": null,
        "literature": {
            "PUB00098610": {
                "PMID": 29279382,
                "ISBN": null,
                "volume": "115",
                "issue": "2",
                "year": 2018,
                "title": "Structural basis of the phosphorylation-independent recognition of cyclin D1 by the SCF<sup>FBXO31</sup> ubiquitin ligase.",
                "URL": null,
                "raw_pages": "319-324",
                "medline_journal": "Proc Natl Acad Sci U S A",
                "ISO_journal": "Proc Natl Acad Sci U S A",
                "authors": [
                    "Li Y",
                    "Jin K",
                    "Bunker E",
                    "Zhang X",
                    "Luo X",
                    "Liu X",
                    "Hao B."
                ],
                "DOI_URL": null
            }
        },
        "set_info": null,
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            "domain_architectures": 87,
            "interactions": 0,
            "matches": 5032,
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            "proteins": 5016,
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            "structural_models": {
                "alphafold": 4473,
                "bfvd": 0
            },
            "structures": 2,
            "taxa": 6206
        },
        "entry_annotations": {
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            "alignment:seed": 91,
            "alignment:full": 3341
        },
        "cross_references": {},
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": null
    }
}