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{
    "metadata": {
        "accession": "IPR038633",
        "entry_id": null,
        "type": "homologous_superfamily",
        "go_terms": null,
        "source_database": "interpro",
        "member_databases": {
            "cathgene3d": {
                "G3DSA:2.30.29.70": "Proteasomal ubiquitin receptor Rpn13/ADRM1"
            }
        },
        "integrated": null,
        "hierarchy": {
            "accession": "IPR038633",
            "name": "Proteasomal ubiquitin receptor Rpn13/ADRM1, Pru domain superfamily",
            "type": "Homologous_superfamily",
            "children": []
        },
        "name": {
            "name": "Proteasomal ubiquitin receptor Rpn13/ADRM1, Pru domain superfamily",
            "short": "Rpn13/ADRM1_Pru_sf"
        },
        "description": [
            {
                "text": "<p>This superfamily includes Rpn13 from budding yeasts and its homologue, ADRM1 from animals.</p>\n\n<p>Rpn13 is a subunit and an ubiquitin receptor of the 19S regulatory particle of the 26S proteasome lid. The 26S proteasome is a huge macromolecular protein-degradation machine consisting of a proteolytically active 20S core, in the form of four disc-like proteins, and one or two 19S regulatory particles. The regulatory particle(s) sit on the top and or bottom of the core, de-ubiquitinate the substrate peptides, unfold them and guide them into the narrow channel through the centre of the core. Rpn13 and its homologues dock onto the regulatory particle through the N-terminal region which binds Rpn2. The C-terminal part of the domain binds de-ubiquitinating enzyme Uch37/UCHL5 and enhances its isopeptidase activity. Rpn13 binds ubiquitin via a conserved amino-terminal region called the pleckstrin-like receptor for ubiquitin, termed Pru, domain [[cite:PUB00053442]]. The domain forms two contiguous anti-parallel β-sheets with a configuration similar to the pleckstrin-homology domain (PHD) fold [[cite:PUB00049233], [cite:PUB00054318]]. Rpn13's ability to bind ubiquitin and the proteasome subunit Rpn2/S1 simultaneously supports evidence of its role as a ubiquitin receptor. Finally, when complexed to di-ubiquitin, via the Pru, and Uch37 via the C-terminal part, it frees up the distal ubiquitin for de-ubiquitination by the Uch37 [[cite:PUB00049233]].</p>",
                "llm": false,
                "checked": false,
                "updated": false
            },
            {
                "text": "<p>This superfamily represents the Pru (pleckstrin-like receptor for the Ub) domain.</p>",
                "llm": false,
                "checked": false,
                "updated": false
            }
        ],
        "wikipedia": null,
        "literature": {
            "PUB00054318": {
                "PMID": 20471946,
                "ISBN": null,
                "volume": "38",
                "issue": "3",
                "year": 2010,
                "title": "Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2.",
                "URL": null,
                "raw_pages": "404-15",
                "medline_journal": "Mol Cell",
                "ISO_journal": "Mol. Cell",
                "authors": [
                    "Chen X",
                    "Lee BH",
                    "Finley D",
                    "Walters KJ."
                ],
                "DOI_URL": "http://dx.doi.org/10.1016/j.molcel.2010.04.019"
            },
            "PUB00053442": {
                "PMID": 18497817,
                "ISBN": null,
                "volume": "453",
                "issue": "7194",
                "year": 2008,
                "title": "Proteasome subunit Rpn13 is a novel ubiquitin receptor.",
                "URL": null,
                "raw_pages": "481-8",
                "medline_journal": "Nature",
                "ISO_journal": "Nature",
                "authors": [
                    "Husnjak K",
                    "Elsasser S",
                    "Zhang N",
                    "Chen X",
                    "Randles L",
                    "Shi Y",
                    "Hofmann K",
                    "Walters KJ",
                    "Finley D",
                    "Dikic I."
                ],
                "DOI_URL": "http://dx.doi.org/10.1038/nature06926"
            },
            "PUB00049233": {
                "PMID": 18497827,
                "ISBN": null,
                "volume": "453",
                "issue": "7194",
                "year": 2008,
                "title": "Ubiquitin docking at the proteasome through a novel pleckstrin-homology domain interaction.",
                "URL": null,
                "raw_pages": "548-52",
                "medline_journal": "Nature",
                "ISO_journal": "Nature",
                "authors": [
                    "Schreiner P",
                    "Chen X",
                    "Husnjak K",
                    "Randles L",
                    "Zhang N",
                    "Elsasser S",
                    "Finley D",
                    "Dikic I",
                    "Walters KJ",
                    "Groll M."
                ],
                "DOI_URL": "http://dx.doi.org/10.1038/nature06924"
            }
        },
        "set_info": null,
        "overlaps_with": [
            {
                "accession": "IPR044868",
                "name": "Rpn13/ADRM1, Pru domain",
                "type": "domain"
            },
            {
                "accession": "IPR006773",
                "name": "Proteasomal ubiquitin receptor Rpn13/ADRM1",
                "type": "family"
            }
        ],
        "counters": {
            "subfamilies": 0,
            "domain_architectures": 0,
            "interactions": 0,
            "matches": 6083,
            "pathways": 393,
            "proteins": 6062,
            "proteomes": 3139,
            "sets": 0,
            "structural_models": {
                "alphafold": 5567,
                "bfvd": 0
            },
            "structures": 42,
            "taxa": 10876
        },
        "entry_annotations": {},
        "cross_references": {},
        "is_llm": false,
        "is_reviewed_llm": false,
        "is_updated_llm": false,
        "representative_structure": {
            "accession": "5v1y",
            "name": "Crystal structure of the ternary RPN13 PRU-RPN2 (940-953)-ubiquitin complex"
        }
    }
}