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InterPro-Version: 108.0
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{
"metadata": {
"accession": "IPR029260",
"entry_id": null,
"type": "domain",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"cdd": {
"cd17657": "N-terminal domain pseudophosphatase domain of CDC14 family proteins"
},
"pfam": {
"PF14671": "Dual specificity protein phosphatase, N-terminal half"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR029260",
"name": "Dual specificity/tyrosine protein phosphatase, N-terminal",
"type": "Domain",
"children": []
},
"name": {
"name": "Dual specificity/tyrosine protein phosphatase, N-terminal",
"short": "DSPn"
},
"description": [
{
"text": "<p>The active core of the dual specificity protein phosphatase is made up of two globular domains both with the DSP-like fold. These domains are arranged in tandem, and are associated via an extensive interface to form a single globular whole.</p>\n\n<p>The conserved PTP signature motif (Cys-[X]5-Arg) that defines the catalytic centre of all PTP-family members is located within the C-terminal domain, DSPc ([pfam:PF00782]). Although the centre of the catalytic site is formed from DSPc, two loops from the N-terminal domain, DSPn, also contribute to the catalytic site, facilitating peptide substrate specificity [[cite:PUB00029440]].</p>",
"llm": false,
"checked": false,
"updated": false
},
{
"text": "<p>This domain represents the N-terminal half of the core (DSPn).</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00029440": {
"PMID": 12853468,
"ISBN": null,
"volume": "22",
"issue": "14",
"year": 2003,
"title": "The structure of the cell cycle protein Cdc14 reveals a proline-directed protein phosphatase.",
"URL": null,
"raw_pages": "3524-35",
"medline_journal": "EMBO J",
"ISO_journal": "EMBO J.",
"authors": [
"Gray CH",
"Good VM",
"Tonks NK",
"Barford D."
],
"DOI_URL": "http://dx.doi.org/10.1093/emboj/cdg348"
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR029021",
"name": "Protein-tyrosine phosphatase-like",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 75,
"interactions": 0,
"matches": 7757,
"pathways": 11,
"proteins": 7755,
"proteomes": 2700,
"sets": 0,
"structural_models": {
"alphafold": 6948,
"bfvd": 0
},
"structures": 8,
"taxa": 7634
},
"entry_annotations": {
"alignment:seed": 62,
"alignment:full": 5300
},
"cross_references": {
"ec": {
"displayName": "ENZYME",
"description": "ENZYME is a repository of information relative to the nomenclature of enzymes. It is primarily based on the recommendations of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB) and it describes each type of characterized enzyme for which an EC (Enzyme Commission) number has been provided.",
"rank": 19,
"accessions": [
{
"accession": "3.1.3.48",
"url": "https://enzyme.expasy.org/EC/3.1.3.48"
}
]
}
},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": null
}
}