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While the low expression level of DUSP7 was restricted to patients with positive rheumatoid factor and anti-citrullinated protein antibodies, the altered expression of CDC25B (show CDC25B Proteins) correlated with the activity of early arthritis.
high levels of Pyst2-L detected in the active state of AML (show RUNX1 Proteins) and ALL diseases and in other types of cancer reflect an altered MAPK (show MAPK1 Proteins) signaling pathway in such malignant processes
DUSP7 is an essential regulator of multiple steps in oocyte meiosis.
Data show that Dusp7 transcripts is expressed in partially overlapping patterns that correspond to regions of active FGF signaling, suggesting combinatorial roles in negative regulation of this pathway during ear development.
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 C-terminal 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 (summary by Patterson et al., 2009
dual specificity phosphatase 7
, dual specificity protein phosphatase 7-like
, Dual specificity protein phosphatase 7
, dual specificity protein phosphatase 7
, dual specificity protein phosphatase PYST2
, dual-specificity phosphatase-7
, MAP kinase phosphatase
, dual specificity protein phosphatase MKP-X
, hypothetical protein