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{
"metadata": {
"accession": "PR01908",
"entry_id": null,
"type": "family",
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"source_database": "prints",
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"name": {
"name": "Atypical dual specificity phosphatase family",
"short": "ADSPHPHTASE"
},
"description": [
{
"text": "<p> Dual Specificity Phosphatases (DUSPs) are members of the superfamily of Protein Tyrosine Phosphatases (PTPs). They remove the phosphate group from both phospho-tyrosine and phospho-serine/threonine residues. Many of these proteins have been related to the MAP kinase signalling pathway and hence they are also termed MAP kinase phosphatases (MKPs). A group of DUSPs share a high degree of similarity with the MKP subgroup, but lack the N-terminal regulatory domain, which provides the substrate specificity towards the MAP kinases. These proteins form a heterogeneous group and have in common the presence of a single catalytic PTP domain. They are small-sized and have been named Low Molecular Weight-DUSPs (LMW-DUSPs) or Atypical-DUSPs. VHR was the first characterised member of this subfamily; its crystal structure is known [1281549,8650541]. </p> <p> The functions of many of the members of this group remain unknown, although some have been related to regulation of MAP kinase pathways [10224087,11971192,15796912]. VHR has also been related to the control of cell-senescence [16604064]. On the basis of sequence similarity, this family can be subdivided into two groups, for convenience termed A and B. </p>",
"llm": false,
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"updated": false
}
],
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"alphafold": 13514,
"bfvd": 2
},
"structures": 62,
"taxa": 5503
},
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"is_llm": false,
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}
}