DUSP16

From Wikipedia, the free encyclopedia

Dual specificity phosphatase 16

Identifiers

DUSP16; KIAA1700; MGC129701; MGC129702; MKP-7; MKP7

External IDs

OMIM: 607175 MGI: 1917936 HomoloGene: 15604

Gene ontology
Molecular Function:	• protein tyrosine phosphatase activity • protein binding • hydrolase activity • MAP kinase tyrosine/serine/threonine phosphatase activity
Cellular Component:	• nucleus • cytoplasm
Biological Process:	• inactivation of MAPK activity • protein amino acid dephosphorylation • MAPK export from nucleus • MAPK phosphatase export from nucleus, leptomycin B sensitive

Orthologs

Human

Mouse

n/a

Refseq

NM_030640 (mRNA)
NP_085143 (protein)

NM_181320 (mRNA)
NP_851837 (protein)

Location

Chr 12: 12.52 - 12.61 Mb

Chr 6: 134.68 - 134.76 Mb

Pubmed search

[1]

[2]

Dual specificity phosphatase 16, also known as DUSP16, is a human gene.^[1]

The activation of mitogen-activated protein kinase (MAPK) cascades transduces various extracellular signals to the nucleus to induce gene expression, cell proliferation, differentiation, cell cycle arrest, and apoptosis. For full activation of MAPKs, dual-specificity kinases phosphorylate both threonine and tyrosine residues in MAPK TXY motifs. MKPs are dual-specificity phosphatases that dephosphorylate the TXY motif, thereby negatively regulating MAPK activity.[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: DUSP16 dual specificity phosphatase 16.

[edit] Further reading

Nagase T, Kikuno R, Hattori A, et al. (2001). "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.". DNA Res. 7 (6): 347–55. PMID 11214970.
Tanoue T, Yamamoto T, Maeda R, Nishida E (2001). "A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha and beta MAPKs.". J. Biol. Chem. 276 (28): 26629–39. doi:10.1074/jbc.M101981200. PMID 11359773.
Masuda K, Shima H, Watanabe M, Kikuchi K (2001). "MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle protein.". J. Biol. Chem. 276 (42): 39002–11. doi:10.1074/jbc.M104600200. PMID 11489891.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Willoughby EA, Perkins GR, Collins MK, Whitmarsh AJ (2003). "The JNK-interacting protein-1 scaffold protein targets MAPK phosphatase-7 to dephosphorylate JNK.". J. Biol. Chem. 278 (12): 10731–6. doi:10.1074/jbc.M207324200. PMID 12524447.
Masuda K, Shima H, Katagiri C, Kikuchi K (2003). "Activation of ERK induces phosphorylation of MAPK phosphatase-7, a JNK specific phosphatase, at Ser-446.". J. Biol. Chem. 278 (34): 32448–56. doi:10.1074/jbc.M213254200. PMID 12794087.
Hoornaert I, Marynen P, Goris J, et al. (2003). "MAPK phosphatase DUSP16/MKP-7, a candidate tumor suppressor for chromosome region 12p12-13, reduces BCR-ABL-induced transformation.". Oncogene 22 (49): 7728–36. doi:10.1038/sj.onc.1207089. PMID 14586399.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Katagiri C, Masuda K, Urano T, et al. (2005). "Phosphorylation of Ser-446 determines stability of MKP-7.". J. Biol. Chem. 280 (15): 14716–22. doi:10.1074/jbc.M500200200. PMID 15689616.
Willoughby EA, Collins MK (2005). "Dynamic interaction between the dual specificity phosphatase MKP7 and the JNK3 scaffold protein beta-arrestin 2.". J. Biol. Chem. 280 (27): 25651–8. doi:10.1074/jbc.M501926200. PMID 15888437.