background:
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. DUSP18 contains the consensus DUSP SLCterminal catalytic domain but 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:
Can dephosphorylate single and diphosphorylated synthetic MAPK peptides, with preference for the phosphotyrosine and diphosphorylated forms over phosphothreonine. In vitro, dephosphorylates p-nitrophenyl phosphate (pNPP).
Subcellular Location:
Cytoplasm. Nucleus.
Tissue Specificity:
Widely expressed with highest levels in liver, brain, ovary and testis.
Similarity:
Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.
Contains 1 tyrosine-protein phosphatase domain.
Database links:
Entrez Gene: 150290 Human
Entrez Gene: 75219 Mouse
Omim: 611446 Human
SwissProt: Q8NEJ0 Human
SwissProt: Q8VE01 Mouse
Unigene: 517544 Human
Unigene: 32588 Mouse
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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