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Identification
HMDB Protein ID HMDBP08901
Secondary Accession Numbers
  • 14630
Name RNA polymerase II subunit A C-terminal domain phosphatase
Synonyms
  1. TFIIF-associating CTD phosphatase
Gene Name CTDP1
Protein Type Enzyme
Biological Properties
General Function Involved in phosphoprotein phosphatase activity
Specific Function Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.
Pathways Not Available
Reactions
A phosphoprotein + Water → a protein + Phosphate details
GO Classification
Biological Process
cell division
viral reproduction
exit from mitosis
mitosis
positive regulation of viral transcription
transcription elongation from RNA polymerase II promoter
protein dephosphorylation
Cellular Component
centrosome
actin cytoskeleton
cytoplasm
nucleoplasm
midbody
spindle midzone
spindle pole
Component
cell part
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
nucleus
intracellular
Function
phosphoprotein phosphatase activity
hydrolase activity, acting on ester bonds
catalytic activity
hydrolase activity
phosphoric ester hydrolase activity
phosphatase activity
Molecular Function
CTD phosphatase activity
DNA-directed RNA polymerase activity
Cellular Location
  1. Nucleus
Gene Properties
Chromosome Location 18
Locus 18q23
SNPs CTDP1
Gene Sequence
>2886 bp
ATGGAGGTGCCGGCCGCGGGTCGCGTTCCTGCCGAGGGCGCCCCGACGGCGGCTGTGGCC
GAGGTGCGCTGCCCGGGGCCCGCGCCGCTGCGCCTGCTGGAGTGGAGGGTGGCGGCGGGC
GCGGCCGTGCGCATCGGCTCGGTGCTGGCCGTGTTCGAGGCCGCCGCCTCCGCGCAGTCC
TCCGGGGCCTCTCAGTCCCGTGTAGCCTCCGGGGGCTGCGTGCGCCCCGCGCGGCCGGAA
CGCAGGCTGAGGTCGGAGCGCGCGGGCGTGGTGCGGGAGCTGTGCGCGCAGCCGGGCCAG
GTGGTCGCCCCAGGAGCGGTTCTGGTGAGGTTGGAAGGATGCAGCCACCCGGTTGTCATG
AAAGGCCTGTGTGCTGAATGTGGCCAAGACCTCACCCAGTTGCAGAGTAAGAACGGGAAG
CAGCAGGTGCCGCTGTCCACGGCGACCGTGTCCATGGTGCACAGCGTGCCGGAGTTGATG
GTGAGCTCCGAGCAAGCTGAACAGCTGGGAAGAGAAGACCAGCAGCGACTGCACCGAAAC
CGGAAGCTGGTGCTCATGGTGGACTTGGACCAGACGTTGATTCACACAACCGAGCAGCAC
TGTCAGCAGATGTCGAATAAAGGCATCTTTCACTTCCAGCTGGGCCGGGGTGAGCCCATG
CTGCACACGCGCCTGCGTCCACACTGCAAGGACTTCCTGGAGAAGATCGCCAAGCTGTAC
GAGCTGCACGTCTTCACCTTCGGCAGCCGGCTGTACGCACACACCATCGCAGGCTTTTTA
GACCCCGAGAAGAAGCTTTTTTCTCACCGAATATTATCAAGGGATGAATGTATTGACCCA
TTTTCTAAAACGGGAAACCTTAGAAATCTCTTTCCTTGTGGAGACTCAATGGTTTGCATT
ATTGATGATCGAGAAGATGTCTGGAAGTTTGCCCCCAATCTGATAACTGTGAAGAAATAT
GTATACTTCCAGGGCACGGGTGATATGAATGCGCCCCCTGGGTCCCGAGAATCTCAGACG
AGAAAGAAAGTAAATCATTCTCGAGGCACTGAGGTCTCAGAGCCATCTCCGCCCGTGAGA
GACCCTGAGGGGGTAACGCAGGCCCCTGGAGTGGAGCCCAGCAATGGCCTGGAGAAGCCT
GCACGGGAGCTGAACGGCAGCGAGGCCGCCACCCCGCGGGACTCACCCCGCCCCGGGAAG
CCAGACGAGAGGGACATCTGGCCCCCTGCCCAGGCCCCCACCAGCAGCCAAGAGCTGGCA
GGCGCTCCTGAGCCCCAGGGATCCTGTGCGCAGGGTGGCCGGGTGGCACCGGGACAGCGG
CCTGCCCAGGGTGCCACGGGCACTGACCTGGACTTTGACTTATCCAGCGACAGCGAGAGC
AGCAGTGAGTCCGAGGGCACGAAGTCCTCCTCCTCCGCCTCTGATGGCGAAAGCGAGGGG
AAAAGAGGCCGGCAGAAGCCGAAGGCTGCCCCAGAGGGAGCCGGGGCGCTGGCACAGGGC
AGTTCCCTGGAGCCGGGGCGGCCTGCAGCACCGAGTCTCCCCGGAGAGGCCGAGCCTGGC
GCGCATGCCCCGGACAAGGAGCCTGAGCTGGGTGGGCAGGAGGAGGGCGAGCGGGATGGC
CTCTGCGGCCTGGGCAACGGCTGTGCCGACAGGAAGGAGGCGGAGACCGAGTCACAGAAC
AGCGAGCTGTCGGGGGTCACTGCGGGTGAGTCCCTGGACCAGAGCATGGAGGAGGAGGAG
GAGGAGGACACGGATGAGGATGACCACCTCATCTACCTGGAGGAGATCCTGGTCCGTGTA
CACACTGACTACTATGCCAAGTATGACCGCTACCTCAACAAGGAGATCGAGGAGGCGCCG
GACATCCGCAAGATCGTGCCGGAGCTCAAGAGCAAGGTGCTGGCAGACGTGGCCATAATT
TTCAGTGGGCTACACCCGACAAACTTCCCGATAGAGAAGACGCGGGAGCATTACCACGCC
ACGGCGCTGGGAGCGAAGATCCTCACTCGGCTGGTGCTGAGCCCCGACGCCCCTGACAGG
GCCACGCACCTGATCGCCGCGCGAGCTGGCACAGAGAAGGTGCTGCAGGCACAGGAGTGC
GGACACCTGCACGTGGTCAACCCTGACTGGCTGTGGAGCTGCCTGGAGCGCTGGGACAAG
GTGGAGGAGCAGCTCTTCCCGCTCAGGGACGATCACACCAAGGCACAGAGGGAGAACAGC
CCTGCGGCCTTTCCCGACCGGGAGGGTGTGCCCCCCACCGCCTTGTTCCACCCGATGCCG
GTTCTTCCCAAGGCCCAGCCTGGCCCCGAGGTTCGGATCTACGACTCCAACACGGGGAAG
CTCATCAGGACGGGCGCCCGGGGGCCCCCAGCACCCTCCAGCTCCCTACCCATCCGCCAG
GAGCCCTCTTCCTTCAGAGCGGTTCCGCCACCCCAGCCGCAGATGTTTGGTGAAGAGCTG
CCTGACGCTCAGGACGGAGAGCAGCCTGGCCCTTCTAGAAGAAAGCGACAGCCCAGTATG
TCTGAGACAATGCCGCTGTACACTCTTTGTAAGGAGGATTTAGAGAGTATGGACAAAGAG
GTGGACGACATCCTTGGAGAAGGCAGCGACGACAGCGACAGCGAGAAGAGGAGGCCTGAG
GAGCAGGAGGAGGAGCCCCAGCCCCGGAAGCCAGGGACCCGCAGGGAGCGGACGCTCGGG
GCACCTGCGTCCAGCGAGAGGAGCGCGGCAGGGGGCCGGGGGCCCAGAGGCCACAAGAGG
AAGCTGAATGAAGAGGACGCCGCCAGCGAGTCCAGCAGGGAGTCCAGCAACGAGGATGAG
GGCAGCAGCTCCGAGGCCGACGAGATGGCCAAGGCGCTGGAGGCGGAGCTCAACGACCTC
ATGTGA
Protein Properties
Number of Residues 961
Molecular Weight 92376.475
Theoretical pI 5.112
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>RNA polymerase II subunit A C-terminal domain phosphatase
MEVPAAGRVPAEGAPTAAVAEVRCPGPAPLRLLEWRVAAGAAVRIGSVLAVFEAAASAQS
AGASQSRVASGGCVRPARPERRLRSERAGVVRELCAQPGQVVAPGAVLVRLEGCSHPVVM
KGLCAECGQDLTQLQSKNGKQQVPLSTATVSMVHSVPELMVSSEQAEQLGREDQQRLHRN
RKLVLMVDLDQTLIHTTEQHCQQMSNKGIFHFQLGRGEPMLHTRLRPHCKDFLEKIAKLY
ELHVFTFGSRLYAHTIAGFLDPEKKLFSHRILSRDECIDPFSKTGNLRNLFPCGDSMVCI
IDDREDVWKFAPNLITVKKYVYFQGTGDMNAPPGSRESQTRKKVNHSRGTEVSEPSPPVR
DPEGVTQAPGVEPSNGLEKPARELNGSEAATPRDSPRPGKPDERDIWPPAQAPTSSQELA
GAPEPQGSCAQGGRVAPGQRPAQGATGTDLDFDLSSDSESSSESEGTKSSSSASDGESEG
KRGRQKPKAAPEGAGALAQGSSLEPGRPAAPSLPGEAEPGAHAPDKEPELGGQEEGERDG
LCGLGNGCADRKEAETESQNSELSGVTAGESLDQSMEEEEEEDTDEDDHLIYLEEILVRV
HTDYYAKYDRYLNKEIEEAPDIRKIVPELKSKVLADVAIIFSGLHPTNFPIEKTREHYHA
TALGAKILTRLVLSPDAPDRATHLIAARAGTEKVLQAQECGHLHVVNPDWLWSCLERWDK
VEEQLFPLRDDHTKAQRENSPAAFPDREGVPPTALFHPMPVLPKAQPGPEVRIYDSNTGK
LIRTGARGPPAPSSSLPIRQEPSSFRAVPPPQPQMFGEELPDAQDGEQPGPSRRKRQPSM
SETMPLYTLCKEDLESMDKEVDDILGEGSDDSDSEKRRPEEQEEEPQPRKPGTRRGADAR
APASSERSAAGGRGPRGHKRKLNEEDAASESSRESSNEDEGSSSEADEMAKALEAELNDL
M
GenBank ID Protein 67188445
UniProtKB/Swiss-Prot ID Q9Y5B0
UniProtKB/Swiss-Prot Entry Name CTDP1_HUMAN
PDB IDs
GenBank Gene ID NM_004715.3
GeneCard ID CTDP1
GenAtlas ID CTDP1
HGNC ID HGNC:2498
References
General References
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  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  5. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  6. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed:16964243 ]
  7. Archambault J, Pan G, Dahmus GK, Cartier M, Marshall N, Zhang S, Dahmus ME, Greenblatt J: FCP1, the RAP74-interacting subunit of a human protein phosphatase that dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO. J Biol Chem. 1998 Oct 16;273(42):27593-601. [PubMed:9765293 ]
  8. Cho H, Kim TK, Mancebo H, Lane WS, Flores O, Reinberg D: A protein phosphatase functions to recycle RNA polymerase II. Genes Dev. 1999 Jun 15;13(12):1540-52. [PubMed:10385623 ]
  9. Licciardo P, Amente S, Ruggiero L, Monti M, Pucci P, Lania L, Majello B: 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. 2003 Feb 1;31(3):999-1005. [PubMed:12560496 ]
  10. Friedl EM, Lane WS, Erdjument-Bromage H, Tempst P, Reinberg D: The C-terminal domain phosphatase and transcription elongation activities of FCP1 are regulated by phosphorylation. Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2328-33. Epub 2003 Feb 18. [PubMed:12591939 ]
  11. Kamada K, Roeder RG, Burley SK: 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. 2003 Mar 4;100(5):2296-9. Epub 2003 Feb 18. [PubMed:12591941 ]
  12. Varon R, Gooding R, Steglich C, Marns L, Tang H, Angelicheva D, Yong KK, Ambrugger P, Reinhold A, Morar B, Baas F, Kwa M, Tournev I, Guerguelcheva V, Kremensky I, Lochmuller H, Mullner-Eidenbock A, Merlini L, Neumann L, Burger J, Walter M, Swoboda K, Thomas PK, von Moers A, Risch N, Kalaydjieva L: Partial deficiency of the C-terminal-domain phosphatase of RNA polymerase II is associated with congenital cataracts facial dysmorphism neuropathy syndrome. Nat Genet. 2003 Oct;35(2):185-9. Epub 2003 Sep 21. [PubMed:14517542 ]