DUSP16

This gene encodes a mitogen-activated protein kinase phosphatase that is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. The encoded protein specifically regulates the c-Jun amino-terminal kinase (JNK) and extracellular signal-regulated kinase (ERK) pathways.[provided by RefSeq, May 2010]

Full Name

Dual Specificity Phosphatase 16

Research Area

Dual specificity protein phosphatase involved in the inactivation of MAP kinases. Dephosphorylates MAPK10 bound to ARRB2.

Biological Process

Dephosphorylation Source: UniProtKB
Inactivation of MAPK activity Source: GO_Central
MAPK export from nucleus Source: UniProtKB
MAPK phosphatase export from nucleus, leptomycin B sensitive Source: UniProtKB
Peptidyl-threonine dephosphorylation Source: GO_Central
Peptidyl-tyrosine dephosphorylation Source: GO_Central
Protein dephosphorylation Source: GO_Central

Cellular Location

Nucleus; Cytoplasm; Cytoplasmic vesicle. After dissociation upon AGTR stimulation, re-associates with ARRB2 on endocytic vesicles.

PTM

Phosphorylated at Ser-446 by MAPK1/ERK2, which prevents its degradation, and thereby stabilizes it and blocks JNK MAPK activity.
(Microbial infection) Acetylated at Lys-55 by the M.tuberculosis Eis protein; this leads to the inhibition of JNK-dependent autophagy, phagosome maturation, and ROS (reactive oxygen species) generation for enhanced intracellular survival of M.tuberculosis.