DUSP16 Proteins

Protein Information

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.

Synonyms

3830417M17Rik; AW558566; D6Ertd213e; dual specificity phosphatase 16; dual specificity protein phosphatase 16; DUSP16; KIAA1700; MAP kinase phosphatase 7; MAP kinase phosphatase-7; map kinase phosphatase-M; MAPK phosphatase-7; MGC129701; MGC129702; mitogen-activated protein kinase phosphatase 7; Mkp7; MKP-7; Mkpm