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=== [[phosphatase classification|Protein phosphatase classification]]=== | === [[phosphatase classification|Protein phosphatase classification]]=== | ||
| − | Of the hundreds of phosphatases in the genome, how are they organized and classified? | + | Of the hundreds of phosphatases in the genome, how are they organized and classified? How did they evolved? |
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==Topics== | ==Topics== | ||
Revision as of 19:38, 9 September 2015
Welcome to Phosphatase Wiki, a resource for of phosphatases and phosphatase signaling. This is a pilot project for sharing and publication of discoveries that do not fit into traditional publications or haven't yet been polished for publication. Initial content is mostly from the Manning lab at Salk (moved to Genentech in 2012), but we welcome anyone who would like to contribute. Like other wiki's, just go to the login page to request an account.
Introduction to Phosphatases
Protein phosphatase classification
Of the hundreds of phosphatases in the genome, how are they organized and classified? How did they evolved?
Topics
Catalytically inactive phosphatases (pseudophosphatases)
Dephosphorylation on unusual amino acids
Unusual evidence for phosphorylation on histidine, aspartate, cysteine, lysine, and arginine.
Regulatory subunits
Some phosphatases, particularly PPPs, consist of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits.
Phosphorylation of RNA polymerase II C-terminal domain
The C-terminal domain of RNA polymerase II's largest subunit undergoes dynamic phosphorylation during transcription, and the different phosphorylation patterns that predominate at each stage of transcription recruit the appropriate set of mRNA-processing and histone-modifying factors. This complex phosphorylation patterns are regulated by quite a few phosphatases and kinases.
