"accession"	"counters"	"cross_references"	"description"	"entry_id"	"go_terms"	"hierarchy"	"integrated"	"is_llm"	"is_reviewed_llm"	"is_updated_llm"	"literature"	"member_databases"	"name"	"overlaps_with"	"representative_structure"	"set_info"	"source_database"	"type"	"wikipedia"
"PR01908"	"{'subfamilies': 0, 'domain_architectures': 0, 'interactions': 0, 'matches': 56686, 'pathways': 0, 'proteins': 14671, 'proteomes': 1588, 'sets': 0, 'structural_models': {'alphafold': 13514, 'bfvd': 2}, 'structures': 62, 'taxa': 5503}"	"{}"	"[{'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, 'checked': False, 'updated': False}]"	""	""	""	""	False	False	False	""	""	"{'name': 'Atypical dual specificity phosphatase family', 'short': 'ADSPHPHTASE'}"	""	""	""	"prints"	"family"	""