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FIGURE: 1 / 4
Antibody detects endogenous levels of DUSP16 only when phosphorylated at Ser446.
Dual-specificity phosphatases 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. DUSP16 belongs to a class of DUSPs, designated MKPs, that dephosphorylate MAPK proteins ERK, JNK, and p38 with specificity distinct from that of individual MKP proteins. MKPs contain a highly conserved C-terminal catalytic domain and an N-terminal Cdc25-like domain. MAPK activation cascades mediate various physiologic processes, including cellular proliferation, apoptosis, differentiation, and stress responses.
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Protein Aliases: Dual specificity protein phosphatase 16; MAP kinase phosphatase 7; MAP kinase phosphatase-7; map kinase phosphatase-M; MAPK phosphatase-7; MGC129701; MGC129702; Mitogen-activated protein kinase phosphatase 7
Gene Aliases: 3830417M17Rik; AW558566; D6Ertd213e; DUSP16; KIAA1700; MKP-7; MKP7; Mkpm
UniProt ID: (Human) Q9BY84
Entrez Gene ID: (Human) 80824, (Mouse) 70686, (Rat) 297682
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