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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]].<ref name="pmid9405607">{{cite journal | vauthors = Archambault J, Chambers RS, Kobor MS, Ho Y, Cartier M, Bolotin D, Andrews B, Kane CM, Greenblatt J | title = An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae | journal = Proc Natl Acad Sci U S A | volume = 94 | issue = 26 | pages = 14300–5 |date=Feb 1998 | pmid = 9405607 | pmc = 24951 | doi =10.1073/pnas.94.26.14300 }}</ref><ref name="pmid9765293">{{cite journal | vauthors = Archambault J, Pan G, Dahmus GK, Cartier M, Marshall N, Zhang S, Dahmus ME, Greenblatt J | title = FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO | journal = J Biol Chem | volume = 273 | issue = 42 | pages = 27593–601 |date=Nov 1998 | pmid = 9765293 | pmc = | doi =10.1074/jbc.273.42.27593 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: CTDP1 CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase, subunit 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9150| accessdate = }}</ref> | ||
}} | |||
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| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: CTDP1 CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase, subunit 1| url = | | summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: CTDP1 CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase, subunit 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9150| accessdate = }}</ref> | ||
}} | }} | ||
==Interactions== | |||
CTDP1 has been shown to [[Protein-protein interaction|interact]] with [[WD repeat-containing protein 77]],<ref name=pmid12560496>{{cite journal |last=Licciardo |first=Paolo |author2=Amente Stefano |author3=Ruggiero Luca |author4=Monti Maria |author5=Pucci Piero |author6=Lania Luigi |author7=Majello Barbara |date=Feb 2003 |title=The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP |journal=Nucleic Acids Res. |volume=31 |issue=3 |pages=999–1005 |publisher= |location = England| issn = | pmid = 12560496 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1093/nar/gkg197 |pmc=149217 }}</ref> [[GTF2F1]]<ref name=pmid9765293 /> and [[POLR2A]].<ref name=pmid9159119>{{cite journal |last=Scully |first=R |author2=Anderson S F |author3=Chao D M |author4=Wei W |author5=Ye L |author6=Young R A |author7=Livingston D M |author8=Parvin J D |date=May 1997 |title=BRCA1 is a component of the RNA polymerase II holoenzyme |journal=[[PNAS|Proc. Natl. Acad. Sci. U.S.A.]] |volume=94 |issue=11 |pages=5605–10 |publisher= |location = UNITED STATES| issn = 0027-8424| pmid = 9159119 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |doi=10.1073/pnas.94.11.5605 |pmc=20825 }}</ref> | |||
==References== | ==References== | ||
{{reflist| | {{reflist}} | ||
==External links== | |||
* {{UCSC gene info|CTDP1}} | |||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | | *{{cite journal | vauthors=Scully R, Anderson SF, Chao DM |title=BRCA1 is a component of the RNA polymerase II holoenzyme. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 11 |pages= 5605–10 |year= 1997 |pmid= 9159119 |doi=10.1073/pnas.94.11.5605 | pmc=20825 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Marshall NF, Dahmus GK, Dahmus ME |title=Regulation of carboxyl-terminal domain phosphatase by HIV-1 tat protein. |journal=J. Biol. Chem. |volume=273 |issue= 48 |pages= 31726–30 |year= 1998 |pmid= 9822634 |doi=10.1074/jbc.273.48.31726 }} | ||
*{{cite journal | vauthors=Cho H, Kim TK, Mancebo H |title=A protein phosphatase functions to recycle RNA polymerase II. |journal=Genes Dev. |volume=13 |issue= 12 |pages= 1540–52 |year= 1999 |pmid= 10385623 |doi=10.1101/gad.13.12.1540 | pmc=316795 |display-authors=etal}} | |||
*{{cite journal | | *{{cite journal | vauthors=Angelicheva D, Turnev I, Dye D |title=Congenital cataracts facial dysmorphism neuropathy (CCFDN) syndrome: a novel developmental disorder in Gypsies maps to 18qter. |journal=Eur. J. Hum. Genet. |volume=7 |issue= 5 |pages= 560–6 |year= 1999 |pmid= 10439962 |doi= 10.1038/sj.ejhg.5200319 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Marshall NF, Dahmus ME |title=C-terminal domain phosphatase sensitivity of RNA polymerase II in early elongation complexes on the HIV-1 and adenovirus 2 major late templates. |journal=J. Biol. Chem. |volume=275 |issue= 42 |pages= 32430–7 |year= 2000 |pmid= 10938286 |doi= 10.1074/jbc.M005898200 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Licciardo P, Napolitano G, Majello B, Lania L |title=Inhibition of Tat transactivation by the RNA polymerase II CTD-phosphatase FCP1. |journal=AIDS |volume=15 |issue= 3 |pages= 301–7 |year= 2001 |pmid= 11273209 |doi=10.1097/00002030-200102160-00002 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Bharucha DC, Zhou M, Nekhai S |title=A protein phosphatase from human T cells augments tat transactivation of the human immunodeficiency virus type 1 long-terminal repeat. |journal=Virology |volume=296 |issue= 1 |pages= 6–16 |year= 2002 |pmid= 12036313 |doi= 10.1006/viro.2002.1438 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Washington K, Ammosova T, Beullens M |title=Protein phosphatase-1 dephosphorylates the C-terminal domain of RNA polymerase-II. |journal=J. Biol. Chem. |volume=277 |issue= 43 |pages= 40442–8 |year= 2002 |pmid= 12185079 |doi= 10.1074/jbc.M205687200 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Mandal SS, Cho H, Kim S |title=FCP1, a phosphatase specific for the heptapeptide repeat of the largest subunit of RNA polymerase II, stimulates transcription elongation. |journal=Mol. Cell. Biol. |volume=22 |issue= 21 |pages= 7543–52 |year= 2002 |pmid= 12370301 |doi=10.1128/MCB.22.21.7543-7552.2002 | pmc=135672 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Strausberg RL, Feingold EA, Grouse LH |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Licciardo P, Amente S, Ruggiero L |title=The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a component of the methylosome complex involved in the assembly of snRNP. |journal=Nucleic Acids Res. |volume=31 |issue= 3 |pages= 999–1005 |year= 2003 |pmid= 12560496 |doi=10.1093/nar/gkg197 | pmc=149217 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Nguyen BD, Chen HT, Kobor MS |title=Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB. |journal=Biochemistry |volume=42 |issue= 6 |pages= 1460–9 |year= 2003 |pmid= 12578358 |doi= 10.1021/bi0265473 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Friedl EM, Lane WS, Erdjument-Bromage H |title=The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 5 |pages= 2328–33 |year= 2003 |pmid= 12591939 |doi= 10.1073/pnas.2628049100 | pmc=151340 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Kamada K, Roeder RG, Burley SK |title=Molecular mechanism of recruitment of TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 5 |pages= 2296–9 |year= 2003 |pmid= 12591941 |doi= 10.1073/pnas.262798199 | pmc=151334 }} | ||
*{{cite journal | | *{{cite journal | vauthors=Nguyen BD, Abbott KL, Potempa K |title=NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 10 |pages= 5688–93 |year= 2003 |pmid= 12732728 |doi= 10.1073/pnas.1031524100 | pmc=156262 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Varon R, Gooding R, Steglich C |title=Partial deficiency of the C-terminal-domain phosphatase of RNA polymerase II is associated with congenital cataracts facial dysmorphism neuropathy syndrome. |journal=Nat. Genet. |volume=35 |issue= 2 |pages= 185–9 |year= 2003 |pmid= 14517542 |doi= 10.1038/ng1243 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Yu X, Chini CC, He M |title=The BRCT domain is a phospho-protein binding domain. |journal=Science |volume=302 |issue= 5645 |pages= 639–42 |year= 2003 |pmid= 14576433 |doi= 10.1126/science.1088753 |display-authors=etal}} | ||
*{{cite journal | | *{{cite journal | vauthors=Beausoleil SA, Jedrychowski M, Schwartz D |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 | pmc=514446 |display-authors=etal}} | ||
}} | }} | ||
{{refend}} | {{refend}} | ||
{{PDB Gallery|geneid=9150}} | |||
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{{ | {{gene-18-stub}} | ||
Revision as of 10:09, 30 August 2017
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| External IDs | GeneCards: [1] | ||||||
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| Species | Human | Mouse | |||||
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| UniProt |
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| RefSeq (mRNA) |
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| Location (UCSC) | n/a | n/a | |||||
| PubMed search | n/a | n/a | |||||
| 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.[1][2][3]
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.[3]
Interactions
CTDP1 has been shown to interact with WD repeat-containing protein 77,[4] GTF2F1[2] and POLR2A.[5]
References
- ↑ 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.
- ↑ 2.0 2.1 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.
- ↑ 3.0 3.1 "Entrez Gene: CTDP1 CTD (carboxy-terminal domain, RNA polymerase II, polypeptide A) phosphatase, subunit 1".
- ↑ 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.
- ↑ 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.
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. 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.
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