Dual-specificity phosphatases (DUSPs) constitute a large heterogeneous subgroup of the type I cysteine-based protein-tyrosine phosphatase superfamily. DUSPs are characterized by their ability to dephosphorylate both tyrosine and serine/threonine residues. They have been implicated as major modulators of critical signaling pathways. DUSP19 contains a variation of the consensus DUSP SLCterminal catalytic domain, with the last serine residue replaced by alanine, and lacks the N-terminal CH2 domain found in the MKP (mitogen-activated protein kinase phosphatase) class of DUSPs (see MIM 600714) (summary by Patterson et al., 2009 [PubMed 19228121]).[supplied by OMIM, Dec 2009]
Function:
Has a dual specificity toward Ser/Thr and Tyr-containing proteins.
Tissue Specificity:
Expressed in the heart, lung, liver, and pancreas. The expression level in the pancreas is the highest.
Similarity:
Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.
Contains 1 tyrosine-protein phosphatase domain.
SWISS:
Q547H4
Gene ID:
142679
Database links:
Entrez Gene: 142679 Human
Entrez Gene: 13682 Mouse
Entrez Gene: 311151 Rat
Omim: 611437 Human
SwissProt: Q547H4 Human
SwissProt: Q8WTR2 Human
SwissProt: Q8K4T5 Mouse
Unigene: 132237 Human
Unigene: 306818 Mouse
Unigene: 65563 Rat
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