DUSP14

Chr 17

dual specificity phosphatase 14

Also known as: MKP-L, MKP6

NCBI Gene: 11072 ENSG00000276023 UniProt: O95147 OMIM: 606618

The protein is a dual-specificity phosphatase that inactivates MAP kinases (ERK, JNK, and p38) and negatively regulates T-cell receptor signaling by dephosphorylating the MAP3K7 adapter TAB1. This gene is not highly constrained against loss-of-function variants. No human diseases have been definitively associated with mutations in DUSP14 based on the provided information.

OMIM ResearchSummary from RefSeq, UniProt

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. DUSP14 contains the consensus DUSP C-terminal catalytic domain but 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]

OMIM ResearchGenerating clinical summary…

Active trials

Pubs (1 yr)

—

P/LP submissions

—

P/LP missense

—

LOEUF

Multiple*

Mechanism· predicted

Some data sources returned errors (1)