DUSP19

Dual specificity protein phosphatase 19 is an enzyme that in humans is encoded by the DUSP19 gene.[4]

DUSP19
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3S4E, 4D3P, 4D3R, 4D3Q
Identifiers
Aliases	DUSP19, DUSP17, LMWDSP3, SKRP1, TS-DSP1, dual specificity phosphatase 19
External IDs	OMIM: 611437 MGI: 1915332 HomoloGene: 41565 GeneCards: DUSP19
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q32.1 Start 183,078,559 bp[1] End 183,100,008 bp[1]
RNA expression pattern More reference expression data
Gene ontology Molecular function • phosphoprotein phosphatase activity • MAP-kinase scaffold activity • mitogen-activated protein kinase kinase kinase binding • phosphatase activity • protein kinase inhibitor activity • protein kinase activator activity • GO:0001948 protein binding • protein tyrosine phosphatase activity • hydrolase activity • protein tyrosine/serine/threonine phosphatase activity • JUN kinase phosphatase activity Cellular component • cytoplasm Biological process • negative regulation of protein kinase activity • positive regulation of JUN kinase activity • protein dephosphorylation • positive regulation of JNK cascade • negative regulation of JNK cascade • peptidyl-tyrosine dephosphorylation • negative regulation of JUN kinase activity • positive regulation of MAPK cascade • positive regulation of protein kinase activity • dephosphorylation • activation of protein kinase activity • regulation of MAP kinase activity Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	142679	68082
Ensembl	ENSG00000162999	ENSMUSG00000027001
UniProt	Q8WTR2	Q8K4T5 Q99N12
RefSeq (mRNA)	NM_001142314 NM_080876 NM_001321519	NM_024438
RefSeq (protein)	NP_001135786 NP_001308448 NP_543152	NP_077758
Location (UCSC)	Chr 2: 183.08 – 183.1 Mb	n/a
PubMed search	[2]	[3]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

DUSP19 has been shown to interact with ASK1[5] and MAP2K7.[5][6]

References

1. GRCh38: Ensembl release 89: ENSG00000162999 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Entrez Gene: DUSP19 dual specificity phosphatase 19".
5. Zama T, Aoki R, Kamimoto T, Inoue K, Ikeda Y, Hagiwara M (June 2002). "Scaffold role of a mitogen-activated protein kinase phosphatase, SKRP1, for the JNK signaling pathway". The Journal of Biological Chemistry. 277 (26): 23919–26. doi:10.1074/jbc.M200838200. PMID 11959862.
6. Zama T, Aoki R, Kamimoto T, Inoue K, Ikeda Y, Hagiwara M (June 2002). "A novel dual specificity phosphatase SKRP1 interacts with the MAPK kinase MKK7 and inactivates the JNK MAPK pathway. Implication for the precise regulation of the particular MAPK pathway". The Journal of Biological Chemistry. 277 (26): 23909–18. doi:10.1074/jbc.M200837200. PMID 11959861.

Further reading

• Cheng H, Gao Q, Jiang M, Ma Y, Ni X, Guo L, Jin W, Cao G, Ji C, Ying K, Xu W, Gu S, Ma Y, Xie Y, Mao Y (February 2003). "Molecular cloning and characterization of a novel human protein phosphatase, LMW-DSP3". The International Journal of Biochemistry & Cell Biology. 35 (2): 226–34. doi:10.1016/S1357-2725(02)00127-9. PMID 12479873.
• Zama T, Aoki R, Kamimoto T, Inoue K, Ikeda Y, Hagiwara M (June 2002). "Scaffold role of a mitogen-activated protein kinase phosphatase, SKRP1, for the JNK signaling pathway". The Journal of Biological Chemistry. 277 (26): 23919–26. doi:10.1074/jbc.M200838200. PMID 11959862.
• Zama T, Aoki R, Kamimoto T, Inoue K, Ikeda Y, Hagiwara M (June 2002). "A novel dual specificity phosphatase SKRP1 interacts with the MAPK kinase MKK7 and inactivates the JNK MAPK pathway. Implication for the precise regulation of the particular MAPK pathway". The Journal of Biological Chemistry. 277 (26): 23909–18. doi:10.1074/jbc.M200837200. PMID 11959861.

External links

• Overview of all the structural information available in the PDB for UniProt: Q8WTR2 (Human Dual specificity protein phosphatase 19 (DUSP19)) at the PDBe-KB.