CTDP1

CTDP1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1J2X, 1ONV, 2K7L
Identifiers
Aliases	CTDP1, CCFDN, FCP1, CTD phosphatase subunit 1
External IDs	MGI: 1926953 HomoloGene: 31254 GeneCards: CTDP1
Gene ontology Molecular function • CTD phosphatase activity • protein binding • hydrolase activity • phosphoprotein phosphatase activity Cellular component • cytoplasm • centrosome • spindle pole • DNA-directed RNA polymerase II, holoenzyme • spindle • nucleoplasm • microtubule organizing center • midbody • actin cytoskeleton • spindle midzone • cytoskeleton • nucleus Biological process • mitotic nuclear division • transcription elongation from RNA polymerase II promoter • protein dephosphorylation • exit from mitosis • transcription from RNA polymerase II promoter • cell division • negative regulation of cell growth involved in cardiac muscle cell development • dephosphorylation of RNA polymerase II C-terminal domain • positive regulation of viral transcription • cell cycle Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	9150	67655
Ensembl	n/a	ENSMUSG00000033323
UniProt	Q9Y5B0	Q7TSG2
RefSeq (mRNA)	NM_001202504 NM_004715 NM_048368 NM_001318511	NM_026295
RefSeq (protein)	NP_001189433.1 NP_004706.3 NP_430255.2	NP_080571.2
Location (UCSC)	Chr 18: 79.68 – 79.76 Mb	Chr 18: 80.41 – 80.47 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

RNA polymerase II subunit A C-terminal domain phosphatase is an enzyme that in humans is encoded by the CTDP1 gene.^[3][4][5]

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.^[5]

Interactions

CTDP1 has been shown to interact with WD repeat-containing protein 77,^[6] GTF2F1^[4] and POLR2A.^[7]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Archambault J, Chambers RS, Kobor MS, Ho Y, Cartier M, Bolotin D, Andrews B, Kane CM, Greenblatt J (Feb 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. doi:10.1073/pnas.94.26.14300. PMC 24951. PMID 9405607.
4. Archambault J, Pan G, Dahmus GK, Cartier M, Marshall N, Zhang S, Dahmus ME, Greenblatt J (Nov 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. doi:10.1074/jbc.273.42.27593. PMID 9765293.
5. "Entrez Gene: CTDP1 CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase, subunit 1".
6. Licciardo, Paolo; Amente Stefano; Ruggiero Luca; Monti Maria; Pucci Piero; Lania Luigi; Majello Barbara (Feb 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. England. 31 (3): 999–1005. doi:10.1093/nar/gkg197. PMC 149217. PMID 12560496.
7. Scully, R; Anderson S F; Chao D M; Wei W; Ye L; Young R A; Livingston D M; Parvin J D (May 1997). "BRCA1 is a component of the RNA polymerase II holoenzyme". Proc. Natl. Acad. Sci. U.S.A. UNITED STATES. 94 (11): 5605–10. doi:10.1073/pnas.94.11.5605. ISSN 0027-8424. PMC 20825. PMID 9159119.

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. doi:10.1073/pnas.94.11.5605. PMC 20825. PMID 9159119.
• 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. doi:10.1074/jbc.273.48.31726. 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. doi:10.1101/gad.13.12.1540. PMC 316795. 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. doi:10.1097/00002030-200102160-00002. 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. doi:10.1128/MCB.22.21.7543-7552.2002. PMC 135672. 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. PMC 139241. 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. doi:10.1093/nar/gkg197. PMC 149217. 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. PMC 151340. 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. PMC 151334. 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. PMC 156262. 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. PMC 514446. PMID 15302935.