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. DUSP7 belongs to a class of DUSPs, designated MKPs, that dephosphorylate MAPK (mitogen-activated protein kinase) proteins ERK (see MIM 601795), JNK (see MIM 601158), and p38 (see MIM 600289) with specificity distinct from that of individual MKP proteins. MKPs contain a highly conserved SLCterminal catalytic domain and an N-terminal Cdc25 (see MIM 116947)-like (CH2) domain. MAPK activation cascades mediate various physiologic processes, including cellular proliferation, apoptosis, differentiation, and stress responses
Function:
Regulates the activity of the MAP kinase family in response to changes in the cellular environment. PYST2-S may act as a negative regulator of PYST2-L although it is unclear whether this is by competing for transcription, translation or activation factors.
Subcellular Location:
Cytoplasm.
Tissue Specificity:
Expressed at significantly higher levels in malignant hematopoietic cells than in corresponding non-malignant cells.
Similarity:
Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.
Contains 1 rhodanese domain.
Contains 1 tyrosine-protein phosphatase domain.
Database links:
UniProtKB/Swiss-Prot: Q16829.4
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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