Difference between revisions of "Phosphatase Subfamily DSP1"
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[[Phosphatase classification|Phosphatase Classification]]: Superfamily [[Phosphatase_Superfamily_CC1|CC1]]: Family [[Phosphatase_Family_DSP|DSP]]: [[Phosphatase_Subfamily_DSP1|Subfamily DSP1]] | [[Phosphatase classification|Phosphatase Classification]]: Superfamily [[Phosphatase_Superfamily_CC1|CC1]]: Family [[Phosphatase_Family_DSP|DSP]]: [[Phosphatase_Subfamily_DSP1|Subfamily DSP1]] | ||
| − | This is a stub!! Excuse the mess. | + | This is a stub!! Excuse the mess. DSP1 is a nuclear subfamily of MAP Kinase phosphatases (MKPs), also known as the Group A DSPs. They are dual-specificity phosphatases, which act on Erk, p38, and Jnk MAP Kinases. |
| + | ===Evolution=== | ||
| + | The subfamily is found in animals, plants, amoeba, and some basal eukaryotes, but is absent from ecdysozoa (nematodes and arthropods), most fungi and monosiga (unpublished data, [http://resdev.gene.com/gOrtholog/view/cluster/MC0008107/overview DUSP1], [http://resdev.gene.com/gOrtholog/view/cluster/MC0013833/overview DUSP2], [http://resdev.gene.com/gOrtholog/view/cluster/MC0006670/overview DUSP4], [http://resdev.gene.com/gOrtholog/view/cluster/MC0008873/overview DUSP5]). Human members are DUSP1, DUSP2, DUSP4 and DUSP5. | ||
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| + | ===Domain Structure=== | ||
| + | DSP1 has an inactive Rhodanese domain, followed by a CC1-fold phosphatase domain. | ||
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| + | ===Functions==== | ||
Revision as of 01:05, 28 December 2014
Phosphatase Classification: Superfamily CC1: Family DSP: Subfamily DSP1
This is a stub!! Excuse the mess. DSP1 is a nuclear subfamily of MAP Kinase phosphatases (MKPs), also known as the Group A DSPs. They are dual-specificity phosphatases, which act on Erk, p38, and Jnk MAP Kinases.
Evolution
The subfamily is found in animals, plants, amoeba, and some basal eukaryotes, but is absent from ecdysozoa (nematodes and arthropods), most fungi and monosiga (unpublished data, DUSP1, DUSP2, DUSP4, DUSP5). Human members are DUSP1, DUSP2, DUSP4 and DUSP5.
Domain Structure
DSP1 has an inactive Rhodanese domain, followed by a CC1-fold phosphatase domain.
