CTDP1

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CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase, subunit 1
PDB rendering based on 1onv.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols CTDP1 ; FCP1; CCFDN
External IDs Template:OMIM5 Template:MGI HomoloGene31254
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase, subunit 1, also known as CTDP1, is a human gene.[1]

This gene encodes a protein which interacts with the carboxy-terminus of transcription initiation factor TFIIF, a transcription factor which regulates elongation as well as initiation by RNA polymerase II. The protein may also represent a component of an RNA polymerase II holoenzyme complex. Alternative splicing of this gene results in two transcript variants encoding 2 different isoforms.[1]

References

  1. 1.0 1.1 "Entrez Gene: CTDP1 CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase, subunit 1".

Further reading

  • Scully R, Anderson SF, Chao DM; et al. (1997). "BRCA1 is a component of the RNA polymerase II holoenzyme". Proc. Natl. Acad. Sci. U.S.A. 94 (11): 5605–10. PMID 9159119.
  • Archambault J, Chambers RS, Kobor MS; et al. (1998). "An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae". Proc. Natl. Acad. Sci. U.S.A. 94 (26): 14300–5. PMID 9405607.
  • Archambault J, Pan G, Dahmus GK; et al. (1998). "FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO". J. Biol. Chem. 273 (42): 27593–601. PMID 9765293.
  • Marshall NF, Dahmus GK, Dahmus ME (1998). "Regulation of carboxyl-terminal domain phosphatase by HIV-1 tat protein". J. Biol. Chem. 273 (48): 31726–30. PMID 9822634.
  • Cho H, Kim TK, Mancebo H; et al. (1999). "A protein phosphatase functions to recycle RNA polymerase II". Genes Dev. 13 (12): 1540–52. PMID 10385623.
  • Angelicheva D, Turnev I, Dye D; et al. (1999). "Congenital cataracts facial dysmorphism neuropathy (CCFDN) syndrome: a novel developmental disorder in Gypsies maps to 18qter". Eur. J. Hum. Genet. 7 (5): 560–6. doi:10.1038/sj.ejhg.5200319. PMID 10439962.
  • Marshall NF, Dahmus ME (2000). "C-terminal domain phosphatase sensitivity of RNA polymerase II in early elongation complexes on the HIV-1 and adenovirus 2 major late templates". J. Biol. Chem. 275 (42): 32430–7. doi:10.1074/jbc.M005898200. PMID 10938286.
  • Licciardo P, Napolitano G, Majello B, Lania L (2001). "Inhibition of Tat transactivation by the RNA polymerase II CTD-phosphatase FCP1". AIDS. 15 (3): 301–7. PMID 11273209.
  • Bharucha DC, Zhou M, Nekhai S; et al. (2002). "A protein phosphatase from human T cells augments tat transactivation of the human immunodeficiency virus type 1 long-terminal repeat". Virology. 296 (1): 6–16. doi:10.1006/viro.2002.1438. PMID 12036313.
  • Washington K, Ammosova T, Beullens M; et al. (2002). "Protein phosphatase-1 dephosphorylates the C-terminal domain of RNA polymerase-II". J. Biol. Chem. 277 (43): 40442–8. doi:10.1074/jbc.M205687200. PMID 12185079.
  • Mandal SS, Cho H, Kim S; et al. (2002). "FCP1, a phosphatase specific for the heptapeptide repeat of the largest subunit of RNA polymerase II, stimulates transcription elongation". Mol. Cell. Biol. 22 (21): 7543–52. PMID 12370301.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Licciardo P, Amente S, Ruggiero L; et al. (2003). "The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP". Nucleic Acids Res. 31 (3): 999–1005. PMID 12560496.
  • Nguyen BD, Chen HT, Kobor MS; et al. (2003). "Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB". Biochemistry. 42 (6): 1460–9. doi:10.1021/bi0265473. PMID 12578358.
  • Friedl EM, Lane WS, Erdjument-Bromage H; et al. (2003). "The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation". Proc. Natl. Acad. Sci. U.S.A. 100 (5): 2328–33. doi:10.1073/pnas.2628049100. PMID 12591939.
  • Kamada K, Roeder RG, Burley SK (2003). "Molecular mechanism of recruitment of TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF". Proc. Natl. Acad. Sci. U.S.A. 100 (5): 2296–9. doi:10.1073/pnas.262798199. PMID 12591941.
  • Nguyen BD, Abbott KL, Potempa K; et al. (2003). "NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1". Proc. Natl. Acad. Sci. U.S.A. 100 (10): 5688–93. doi:10.1073/pnas.1031524100. PMID 12732728.
  • Varon R, Gooding R, Steglich C; et al. (2003). "Partial deficiency of the C-terminal-domain phosphatase of RNA polymerase II is associated with congenital cataracts facial dysmorphism neuropathy syndrome". Nat. Genet. 35 (2): 185–9. doi:10.1038/ng1243. PMID 14517542.
  • Yu X, Chini CC, He M; et al. (2003). "The BRCT domain is a phospho-protein binding domain". Science. 302 (5645): 639–42. doi:10.1126/science.1088753. PMID 14576433.
  • Beausoleil SA, Jedrychowski M, Schwartz D; et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMID 15302935.

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