CTDP1

CTDP1
Identifiers
Aliases	CTDP1, CCFDN, FCP1, CTD phosphatase subunit 1
External IDs	OMIM: 604927; MGI: 1926953; HomoloGene: 31254; GeneCards: CTDP1; OMA:CTDP1 - orthologs
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1J2X, 1ONV, 2K7L
Enzyme activity EC # BRENDA ExPASy KEGG MetaCyc 3.1.3.16 ↗ ↗ ↗ ↗
Gene location (Human) Chr. Chromosome 18 (human) Band 18q23 Start 79,679,803 bp End 79,754,503 bp
Gene location (Mouse) Chr. Chromosome 18 (mouse) Band 18 E3|18 53.48 cM Start 80,451,174 bp End 80,512,910 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left testis right testis skin of leg oocyte granulocyte blood mucosa of transverse colon skin of abdomen secondary oocyte monocyte Top expressed in spermatid otic vesicle epiblast fetal liver hematopoietic progenitor cell hair follicle seminiferous tubule Gonadal ridge primitive streak somite Paneth cell More reference expression data BioGPS More reference expression data
Gene ontology Molecular function RNA polymerase II CTD heptapeptide repeat phosphatase activity protein binding hydrolase activity phosphoprotein phosphatase activity TFIIF-class transcription factor complex binding Tat protein binding Cellular component cytoplasm centrosome spindle pole RNA polymerase II, holoenzyme spindle microtubule organizing center midbody spindle midzone cytoskeleton nucleus nucleoplasm intracellular membrane-bounded organelle protein-containing complex actin cytoskeleton nuclear speck Biological process transcription elongation from RNA polymerase II promoter protein dephosphorylation exit from mitosis transcription by RNA polymerase II cell division negative regulation of cell growth involved in cardiac muscle cell development dephosphorylation of RNA polymerase II C-terminal domain cell cycle positive regulation by host of viral transcription positive regulation of viral transcription Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9150 67655 Ensembl ENSG00000282752 ENSG00000060069 ENSMUSG00000033323 UniProt Q9Y5B0 Q7TSG2 RefSeq (mRNA) NM_001202504 NM_004715 NM_048368 NM_001318511 NM_026295 RefSeq (protein) NP_001189433 NP_001305440 NP_004706 NP_430255 NP_080571 Location (UCSC) Chr 18: 79.68 – 79.75 Mb Chr 18: 80.45 – 80.51 Mb PubMed search
Wikidata
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RNA polymerase II subunit A C-terminal domain phosphatase is an enzyme that in humans is encoded by the CTDP1 gene.

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.

Interactions

CTDP1 has been shown to interact with WD repeat-containing protein 77, GTF2F1 and POLR2A.

External links

• Human CTDP1 genome location and CTDP1 gene details page in the UCSC Genome Browser.

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. Bibcode:1997PNAS...94.5605S. 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. S2CID 33054695.
• 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. Bibcode:2002PNAS...9916899M. 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. Bibcode:2003PNAS..100.2328F. 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. Bibcode:2003PNAS..100.2296K. 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. Bibcode:2003PNAS..100.5688N. 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. S2CID 22461437.
• Yu X, Chini CC, He M, et al. (2003). "The BRCT domain is a phospho-protein binding domain". Science. 302 (5645): 639–42. Bibcode:2003Sci...302..639Y. doi:10.1126/science.1088753. PMID 14576433. S2CID 29407635.
• 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. Bibcode:2004PNAS..10112130B. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.