Difference between revisions of "Main Page"
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===[[Dephosphorylation on unusual amino acids]]=== | ===[[Dephosphorylation on unusual amino acids]]=== | ||
Unusual evidence for phosphorylation on histidine, aspartate, cysteine, lysine, and arginine. | Unusual evidence for phosphorylation on histidine, aspartate, cysteine, lysine, and arginine. | ||
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| + | ===[[regulatory_subunits|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. | ||
Revision as of 19:22, 14 March 2014
Welcome to Phosphatase Wikepedia, 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, 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
Phosphatase Classification
Of the hundreds of phosphatases in the genome, how are they organized and classified?
Pending (the hybrid scheme of classification; alternative schemes: PTP and Ser/Thr phosphatase by substrate).
Protein Phosphatase Evolution
Where did they all come from, and how did they get to where they are today?
Topics
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.
Phosphatase-Substrate-Kinase Network
The network is based upon biological knowledge. Six types of relationship between phosphatases and kinases are recorded: 1) they work on the same substrate, 2) phosphatase dephosphorylates kinase, 3) kinase phosphorylates phosphatase, 4) binding but no reported (de)phosphorylated interaction, 5) functional relationship, but not direct interaction, and 6) no relationship.
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.
