CTDP1

From Wikipedia, the free encyclopedia

CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase, subunit 1

PDB rendering based on 1onv.

Available structures: 1onv

Identifiers

Symbol(s)

CTDP1; FCP1; CCFDN

External IDs

OMIM: 604927 MGI: 1926953 HomoloGene: 31254

Gene ontology
Molecular Function:	• DNA-directed RNA polymerase activity • phosphoprotein phosphatase activity • protein binding • hydrolase activity
Cellular Component:	• intracellular • nucleus
Biological Process:	• transcription from RNA polymerase II promoter • protein amino acid dephosphorylation

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004715 (mRNA)
NP_004706 (protein)

NM_026295 (mRNA)
NP_080571 (protein)

Location

Chr 18: 75.54 - 75.62 Mb

Chr 18: 80.57 - 80.63 Mb

Pubmed search

[1]

[2]

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]

[edit] References

^ ^a ^b Entrez Gene: CTDP1 CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase, subunit 1.

[edit] 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.