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{
"metadata": {
"accession": "IPR004861",
"entry_id": null,
"type": "family",
"go_terms": null,
"source_database": "interpro",
"member_databases": {
"pfam": {
"PF03162": "Tyrosine phosphatase family"
}
},
"integrated": null,
"hierarchy": {
"accession": "IPR004861",
"name": "Atypical dual-specificity phosphatase Siw14-like",
"type": "Family",
"children": [
{
"accession": "IPR020428",
"name": "Atypical dual-specificity phosphatase Siw14-like, plant and fungi",
"type": "Family",
"children": []
}
]
},
"name": {
"name": "Atypical dual-specificity phosphatase Siw14-like",
"short": "Siw14-like"
},
"description": [
{
"text": "<p>This group of atypical dual-specificity phosphatases are predominantly from fungi, plants and bacteria. This entry includes budding yeast Siw14 (also known as Oca3) and related proteins. Siw14 is a inositol pyrophosphate phosphatase that modulates inositol pyrophosphate metabolism by dephosphorylating the IP7 isoform 5PP-IP5to IP6 [[cite:PUB00088170]]. This entry also includes budding yeast Oca1/2/4/6 and Arabidopsis DSP1/2/3/4/5. All DSPs tested (AtPFA-DSP1, -2, -3, and -5) displayed phosphatase activity toward PI(3,5)P2, with AtPFA-DSP2 showing a higher activity [[cite:PUB00088172]]. Oca1/2/4/6 are putative phosphatases associated with the caffeine-sensitivity stress pathway in S. cerevisiae [[cite:PUB00088172]]. It also includes dual specificity protein phosphatase TpbA that regulates diverse phenotypes in P.aeruginosa via regulation of the concentration of cellular c-di-GMP [[cite:PUB00078743]]. This phosphatase acts by dephosphorylating the membrane-anchored diguanylate cyclase TpbB at tyrosine and serine/threonine sites, leading to inactivation of TpbB and reduced c-di-GMP production [[cite:PUB00078743], [cite:PUB00151104]].</p>",
"llm": false,
"checked": false,
"updated": false
}
],
"wikipedia": null,
"literature": {
"PUB00088170": {
"PMID": 26828065,
"ISBN": null,
"volume": "291",
"issue": "13",
"year": 2016,
"title": "A Novel Inositol Pyrophosphate Phosphatase in Saccharomyces cerevisiae: Siw14 PROTEIN SELECTIVELY CLEAVES THE β-PHOSPHATE FROM 5-DIPHOSPHOINOSITOL PENTAKISPHOSPHATE (5PP-IP5).",
"URL": null,
"raw_pages": "6772-83",
"medline_journal": "J Biol Chem",
"ISO_journal": "J. Biol. Chem.",
"authors": [
"Steidle EA",
"Chong LS",
"Wu M",
"Crooke E",
"Fiedler D",
"Resnick AC",
"Rolfes RJ."
],
"DOI_URL": "https://doi.org/10.1074/jbc.M116.714907"
},
"PUB00088172": {
"PMID": 21409566,
"ISBN": null,
"volume": "285",
"issue": "4",
"year": 2011,
"title": "Phylogenetic and genetic linkage between novel atypical dual-specificity phosphatases from non-metazoan organisms.",
"URL": null,
"raw_pages": "341-54",
"medline_journal": "Mol Genet Genomics",
"ISO_journal": "Mol. Genet. Genomics",
"authors": [
"Roma-Mateo C",
"Sacristan-Reviriego A",
"Beresford NJ",
"Caparros-Martin JA",
"Culianez-Macia FA",
"Martin H",
"Molina M",
"Tabernero L",
"Pulido R."
],
"DOI_URL": "https://doi.org/10.1007/s00438-011-0611-6"
},
"PUB00078743": {
"PMID": 19543378,
"ISBN": null,
"volume": "5",
"issue": "6",
"year": 2009,
"title": "Connecting quorum sensing, c-di-GMP, pel polysaccharide, and biofilm formation in Pseudomonas aeruginosa through tyrosine phosphatase TpbA (PA3885).",
"URL": null,
"raw_pages": "e1000483",
"medline_journal": "PLoS Pathog",
"ISO_journal": "PLoS Pathog.",
"authors": [
"Ueda A",
"Wood TK."
],
"DOI_URL": "http://dx.doi.org/10.1371/journal.ppat.1000483"
},
"PUB00151104": {
"PMID": 20946878,
"ISBN": null,
"volume": "402",
"issue": "2",
"year": 2010,
"title": "Tyrosine phosphatase TpbA controls rugose colony formation in Pseudomonas aeruginosa by dephosphorylating diguanylate cyclase TpbB.",
"URL": null,
"raw_pages": "351-5",
"medline_journal": "Biochem Biophys Res Commun",
"ISO_journal": "Biochem Biophys Res Commun",
"authors": [
"Pu M",
"Wood TK."
],
"DOI_URL": null
}
},
"set_info": null,
"overlaps_with": [
{
"accession": "IPR029021",
"name": "Protein-tyrosine phosphatase-like",
"type": "homologous_superfamily"
}
],
"counters": {
"subfamilies": 0,
"domain_architectures": 87,
"interactions": 0,
"matches": 7101,
"pathways": 0,
"proteins": 6895,
"proteomes": 1974,
"sets": 0,
"structural_models": {
"alphafold": 6070,
"bfvd": 1
},
"structures": 17,
"taxa": 4798
},
"entry_annotations": {
"alignment:seed": 8,
"alignment:full": 4180
},
"cross_references": {},
"is_llm": false,
"is_reviewed_llm": false,
"is_updated_llm": false,
"representative_structure": {
"accession": "7mod",
"name": "Crystal Structure of Arabidopsis thaliana Plant and Fungi Atypical Dual Specificity Phosphatase 1(AtPFA-DSP1 ) Cys150Ser in Complex with Phosphate in Conformation A (Pi(A))"
}
}
}
