Difference between revisions of "Phosphatase Subfamily FCP1"
From PhosphataseWiki
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| − | + | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Group_HAD|Superfamily HAD]]: [[Phosphatase_Family_FCP|Family FCP]]: [[Phosphatase_Subfamily_FCP|Subfamily FCP]] | |
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F-cell production 1 (FCP1) also called TFIIF-stimulated CTD phosphatase 1, prefers to dephosphorylate pSer2 of heptapeptide repeats at CTD of RNA polymerase II. The molecular function is mainly studied in yeast <cite>Kamenski04</cite>. | F-cell production 1 (FCP1) also called TFIIF-stimulated CTD phosphatase 1, prefers to dephosphorylate pSer2 of heptapeptide repeats at CTD of RNA polymerase II. The molecular function is mainly studied in yeast <cite>Kamenski04</cite>. | ||
| − | == | + | ===Evolution=== |
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FCP1 is conserved from yeast to human, usually one copy per genome. | FCP1 is conserved from yeast to human, usually one copy per genome. | ||
| − | == Domain | + | ===Domain Structure=== |
In additional to the catalytic domain, it has a breast cancer protein-related carboxy-terminal (BRCT) domain and a C-terminal region that binds regulatory TFIIF. | In additional to the catalytic domain, it has a breast cancer protein-related carboxy-terminal (BRCT) domain and a C-terminal region that binds regulatory TFIIF. | ||
| − | == Catalytic activity == | + | ===Catalytic activity=== |
| − | == Curation notes == | + | ===Curation notes=== |
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| + | ===Substrates and Related Kinases=== | ||
| + | See [[CTD_Phosphorylation|Phosphorylation of RNA polymerase II C-terminal domain]]. | ||
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| − | == Links == | + | ===Links=== |
[http://www.ncbi.nlm.nih.gov/gene/2221 Human FCP1] from NCBI Gene | [http://www.ncbi.nlm.nih.gov/gene/2221 Human FCP1] from NCBI Gene | ||
Revision as of 05:14, 29 December 2014
Phosphatase Classification: Superfamily HAD: Family FCP: Subfamily FCP
F-cell production 1 (FCP1) also called TFIIF-stimulated CTD phosphatase 1, prefers to dephosphorylate pSer2 of heptapeptide repeats at CTD of RNA polymerase II. The molecular function is mainly studied in yeast [1].
Evolution
FCP1 is conserved from yeast to human, usually one copy per genome.
Domain Structure
In additional to the catalytic domain, it has a breast cancer protein-related carboxy-terminal (BRCT) domain and a C-terminal region that binds regulatory TFIIF.
Catalytic activity
Curation notes
Substrates and Related Kinases
See Phosphorylation of RNA polymerase II C-terminal domain.
References
- Kamenski T, Heilmeier S, Meinhart A, and Cramer P. Structure and mechanism of RNA polymerase II CTD phosphatases. Mol Cell. 2004 Aug 13;15(3):399-407. DOI:10.1016/j.molcel.2004.06.035 |
Links
Human FCP1 from NCBI Gene
