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RNA polymerase II subunit A C-terminal domain phosphatase SSU72Known also as: CTD phosphatase SSU72 Known abbreviations: SSU72, HSPC182, PNAS-120 Yeast homolog: not known Protein
Top 3 models:
This protein has alternative isoforms: Isoform 1:
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130 MPSSPLRVAVVCSSNQNRSMEAHNILSKRGFSVRSFGTGTHVKLPGPAPDKPNVYDFKTTYDQMYNDLLRKDKELYTQNGILHMLDRNKRIKPRPERFQNCKDLFDLILTCEERVYDQVVEDLNSREQET CQPVHVVNVDIQDNHEEATLGAFLICELCQCIQHTEDMENEIDELLQEFEEKSGRTFLHTVCFY Isoform 2:
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130 MPSSPLRVAVVCSSNQNRSMEAHNILSKRGFSVRSFGTGTHVKLPGPAPDKPNVYDFKTTYDQMYNDLLRKDKELYPSGLPFKNPPCGPPWKVLRVARAQEACHPVQCTHWLLCLCESLVSIPGARRIVH GLVPVPPMAVGVVRRTDTVWGSP Enzyme EC number: 3.1.3.16 Name: Phosphoprotein phosphatase Reaction: A phosphoprotein + H(2)O <=> a protein + phosphate Gene location: 1p36.33 Summary SSU72 is involved in the C-terminal domain of RNA polymerase II dephosphorylation, RNA processing and termination. Ssu72p was originally identified by its genetic interaction with the transcription factor TFIIB, as a mutation in Ssu72p disrupted this interaction and affected the accuracy of start site selection. It is essential for the cleavage reaction but is not required for polyadenylation. Ssu72p interacts with Pta1p, Cft2p/Ydh1p and the Rpb2p subunit of PolII. Upon binding to Pta1p, Ssu72p functions as a phosphatase with specificity for the fifth serine of the heptapeptide repeat in the CTD of PolII. In human Ssu72 has been identified as an interacting protein of the retinoblastoma tumor suppressor, Rb. Similar to its yeast homolog, hSsu72 binds directly to TFIIB and Pta1p and exhibits phosphatase activity, but its role in 3?-end processing is still unknown. hSsu72 cannot rescue a lethal mutation in Ssu72 in yeast [225]. human and yeast homologs shares 72% sequence identity. Interacts with RB1. Interacts with GTF2B and CD226. See this protein in other databases: Literature:
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