DUSP19

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. DUSP19 contains a variation of the consensus DUSP C-terminal catalytic domain, with the last serine residue replaced by alanine, and 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]

Description

Dual specificity phosphatase 19

Tissue specificity

Low tissue specificity

Subcell location

Nucleoplasm

Predicted location

Intracellular

Protein family

Enzymes
Mapped to neXtProt
Mapped to UniProt SWISS-PROT
Metabolic proteins
Predicted intracellular proteins
Protein evidence (Ezkurdia et al 2014)
Protein evidence (Kim et al 2014)

Chromosome

2 (183078559 - 183100008)

Ensembl ID

ENSG00000162999  (ver. 103.38)

Orthologs

Mouse Dusp19: ENSMUSG00000027001

UniProt

Q8WTR2

neXtProt

NX_Q8WTR2

Human splice variants
Mouse splice variants

Protein structure