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dual specificity protein phosphatase 1, MAP kinase phosphatase 1 or CL100 phosphatase
Function:
- dual specificity tyrosine/serine-threonine phosphatase
- highly specific for MAP kinases
- dephosphorylates MAP kinase ERK2 on both Thr-183 & Tyr-185
- inhibits DNA synthesis induced by constitutively active p21ras [3]
protein tyrosine phosphate + H2O
protein tyrosine + phosphate
phosphoprotein + H2O a protein + phosphate
Structure:
- belongs to the protein-tyrosine phosphatase family
- non-receptor class dual specificity subfamily
- contains 1 rhodanese domain
- contains 1 tyrosine-protein phosphatase domain
Expression:
- expressed at high levels in the lung, liver placenta & pancreas
- moderate levels seen in the heart & skeletal muscle
- lower levels found in the brain & kidney
- induced by oxidative stress & heat shock
- isolated from fibroblasts exposed to oxidative stress or heat shock
- induced by mitogenic stimulation ?
Interactions
molecular events
Related
3CH134 or erp primary response gene
General
dual specificity phosphatase
mitogen activated protein kinase phosphatase
Properties
SIZE: entity length = 367 aa
MW = 39 kD
STATE: active state
MOTIF: Rhodanese {20-137}
Tyrosine-protein phosphatase {175-367}
MOTIF: cysteine residue {C258}
Database Correlations
OMIM 600714
UniProt P28562
PFAM correlations
Entrez Gene 1843
KEGG correlations
ENZYME correlations
References
- Sun H, Charles CH, Lau LF, Tonks NK.
MKP-1 (3CH134), an immediate early gene product, is a dual
specificity phosphatase that dephosphorylates MAP kinase
in vivo.
Cell. 1993 Nov 5;75(3):487-93.
PMID: 8221888
- Nebreda AR.
Inactivation of MAP kinases.
Trends Biochem Sci. 1994 Jan;19(1):1-2. Review.
PMID: 8140614
- Sun H, Tonks NK, Bar-Sagi D.
Inhibition of Ras-induced DNA synthesis by expression of the
phosphatase MKP-1.
Science. 1994 Oct 14;266(5183):285-8.
PMID: 7939666
- UniProt :accession P28562