CTDP1_HUMAN
ID CTDP1_HUMAN Reviewed; 961 AA.
AC Q9Y5B0; A8MY97; Q7Z644; Q96BZ1; Q9Y6F5;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 3.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase;
DE EC=3.1.3.16;
DE AltName: Full=TFIIF-associating CTD phosphatase;
GN Name=CTDP1; Synonyms=FCP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Cervix carcinoma;
RX PubMed=10385623; DOI=10.1101/gad.13.12.1540;
RA Cho H., Kim T.-K., Mancebo H., Lane W.S., Flores O., Reinberg D.;
RT "A protein phosphatase functions to recycle RNA polymerase II.";
RL Genes Dev. 13:1540-1552(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 88-961 (ISOFORM 1).
RC TISSUE=Colon, Lymph, and Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 106-961 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [MRNA] OF 106-961 (ISOFORM 4), TISSUE SPECIFICITY, AND INTERACTION WITH
RP GTF2F1.
RC TISSUE=Placenta;
RX PubMed=9765293; DOI=10.1074/jbc.273.42.27593;
RA Archambault J., Pan G., Dahmus G.K., Cartier M., Marshall N., Zhang S.,
RA Dahmus M.E., Greenblatt J.;
RT "FCP1, the RAP74-interacting subunit of a human protein phosphatase that
RT dephosphorylates the carboxyl-terminal domain of RNA polymerase IIO.";
RL J. Biol. Chem. 273:27593-27601(1998).
RN [6]
RP INTERACTION WITH WDR77; SNRPB AND SNRNP70.
RX PubMed=12560496; DOI=10.1093/nar/gkg197;
RA Licciardo P., Amente S., Ruggiero L., Monti M., Pucci P., Lania L.,
RA Majello B.;
RT "The FCP1 phosphatase interacts with RNA polymerase II and with MEP50 a
RT component of the methylosome complex involved in the assembly of snRNP.";
RL Nucleic Acids Res. 31:999-1005(2003).
RN [7]
RP PHOSPHORYLATION.
RX PubMed=12591939; DOI=10.1073/pnas.2628049100;
RA Friedl E.M., Lane W.S., Erdjument-Bromage H., Tempst P., Reinberg D.;
RT "The C-terminal domain phosphatase and transcription elongation activities
RT of FCP1 are regulated by phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2328-2333(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-869, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-780, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-869 AND SER-872, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22692537; DOI=10.1038/ncomms1886;
RA Visconti R., Palazzo L., Della Monica R., Grieco D.;
RT "Fcp1-dependent dephosphorylation is required for M-phase-promoting factor
RT inactivation at mitosis exit.";
RL Nat. Commun. 3:894-894(2012).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; SER-674; SER-740 AND
RP SER-839, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 944-961 IN COMPLEX WITH GTF2F1.
RX PubMed=12591941; DOI=10.1073/pnas.262798199;
RA Kamada K., Roeder R.G., Burley S.K.;
RT "Molecular mechanism of recruitment of TFIIF-associating RNA polymerase C-
RT terminal domain phosphatase (FCP1) by transcription factor IIF.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2296-2299(2003).
RN [19]
RP INVOLVEMENT IN CCFDN.
RX PubMed=14517542; DOI=10.1038/ng1243;
RA Varon R., Gooding R., Steglich C., Marns L., Tang H., Angelicheva D.,
RA Yong K.K., Ambrugger P., Reinhold A., Morar B., Baas F., Kwa M.,
RA Tournev I., Guerguelcheva V., Kremensky I., Lochmueller H.,
RA Muellner-Eidenboeck A., Merlini L., Neumann L., Buerger J., Walter M.,
RA Swoboda K., Thomas P.K., von Moers A., Risch N., Kalaydjieva L.;
RT "Partial deficiency of the C-terminal-domain phosphatase of RNA polymerase
RT II is associated with congenital cataracts facial dysmorphism neuropathy
RT syndrome.";
RL Nat. Genet. 35:185-189(2003).
CC -!- FUNCTION: Processively dephosphorylates 'Ser-2' and 'Ser-5' of the
CC heptad repeats YSPTSPS in the C-terminal domain of the largest RNA
CC polymerase II subunit. This promotes the activity of RNA polymerase II.
CC Plays a role in the exit from mitosis by dephosphorylating crucial
CC mitotic substrates (USP44, CDC20 and WEE1) that are required for M-
CC phase-promoting factor (MPF)/CDK1 inactivation.
CC {ECO:0000269|PubMed:22692537}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Homodimer. Interacts with GTF2F1. Interacts with WDR77, SNRPB
CC and SNRNP70. {ECO:0000269|PubMed:12560496, ECO:0000269|PubMed:12591941,
CC ECO:0000269|PubMed:9765293}.
CC -!- INTERACTION:
CC Q9Y5B0; P35269: GTF2F1; NbExp=2; IntAct=EBI-2807555, EBI-457886;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22692537}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:22692537}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:22692537}. Midbody {ECO:0000269|PubMed:22692537}.
CC Note=Found at centrosomes in prometaphase, at spindle and spindle poles
CC in metaphase and at spindle midzone and midbody in anaphase and
CC telophase-G1 respectively.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y5B0-1; Sequence=Displayed;
CC Name=4;
CC IsoId=Q9Y5B0-4; Sequence=VSP_009865;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9765293}.
CC -!- PTM: Phosphorylated. In the presence of TFIIF, the phosphorylated form
CC has an increased CTD phosphatase activity. The phosphorylation is
CC required for the physical interaction with GTF2F1.
CC {ECO:0000269|PubMed:12591939}.
CC -!- DISEASE: Congenital cataracts, facial dysmorphism, and neuropathy
CC (CCFDN) [MIM:604168]: An autosomal recessive developmental disorder
CC characterized by a complex clinical phenotype with seemingly unrelated
CC features involving multiple organs and systems. Developmental
CC abnormalities include congenital cataracts and microcorneae,
CC hypomyelination of the peripheral nervous system, impaired physical
CC growth, delayed early motor and intellectual development, facial
CC dysmorphism and hypogonadism. Central nervous system involvement, with
CC cerebral and spinal cord atrophy, may be the result of disrupted
CC development with superimposed degenerative changes. Affected
CC individuals are prone to severe rhabdomyolysis after viral infections
CC and to serious complications related to general anesthesia (such as
CC pulmonary edema and epileptic seizures). {ECO:0000269|PubMed:14517542}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC64549.1; Type=Miscellaneous discrepancy; Note=Cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AF154115; AAD42088.1; -; mRNA.
DR EMBL; AC021594; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC068473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471117; EAW66631.1; -; Genomic_DNA.
DR EMBL; BC015010; AAH15010.1; -; mRNA.
DR EMBL; BC052576; AAH52576.1; -; mRNA.
DR EMBL; BC063447; AAH63447.1; -; mRNA.
DR EMBL; AF081287; AAC64549.1; ALT_SEQ; mRNA.
DR CCDS; CCDS12017.1; -. [Q9Y5B0-1]
DR CCDS; CCDS12018.1; -. [Q9Y5B0-4]
DR RefSeq; NP_001189433.1; NM_001202504.1.
DR RefSeq; NP_004706.3; NM_004715.4. [Q9Y5B0-1]
DR RefSeq; NP_430255.2; NM_048368.3. [Q9Y5B0-4]
DR PDB; 1J2X; X-ray; 2.00 A; B=944-961.
DR PDB; 1ONV; NMR; -; B=879-961.
DR PDB; 2K7L; NMR; -; B=582-600.
DR PDBsum; 1J2X; -.
DR PDBsum; 1ONV; -.
DR PDBsum; 2K7L; -.
DR AlphaFoldDB; Q9Y5B0; -.
DR BMRB; Q9Y5B0; -.
DR SMR; Q9Y5B0; -.
DR BioGRID; 114597; 181.
DR CORUM; Q9Y5B0; -.
DR DIP; DIP-41788N; -.
DR IntAct; Q9Y5B0; 16.
DR MINT; Q9Y5B0; -.
DR STRING; 9606.ENSP00000484525; -.
DR DEPOD; CTDP1; -.
DR GlyGen; Q9Y5B0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y5B0; -.
DR MetOSite; Q9Y5B0; -.
DR PhosphoSitePlus; Q9Y5B0; -.
DR BioMuta; CTDP1; -.
DR DMDM; 327478586; -.
DR EPD; Q9Y5B0; -.
DR jPOST; Q9Y5B0; -.
DR MassIVE; Q9Y5B0; -.
DR MaxQB; Q9Y5B0; -.
DR PaxDb; Q9Y5B0; -.
DR PeptideAtlas; Q9Y5B0; -.
DR PRIDE; Q9Y5B0; -.
DR ProteomicsDB; 86328; -. [Q9Y5B0-1]
DR ProteomicsDB; 86331; -. [Q9Y5B0-4]
DR Antibodypedia; 23481; 145 antibodies from 23 providers.
DR DNASU; 9150; -.
DR Ensembl; ENST00000075430.11; ENSP00000075430.7; ENSG00000060069.18. [Q9Y5B0-4]
DR Ensembl; ENST00000613122.5; ENSP00000484525.2; ENSG00000060069.18. [Q9Y5B0-1]
DR GeneID; 9150; -.
DR KEGG; hsa:9150; -.
DR MANE-Select; ENST00000613122.5; ENSP00000484525.2; NM_004715.5; NP_004706.3.
DR UCSC; uc002lnh.3; human. [Q9Y5B0-1]
DR CTD; 9150; -.
DR DisGeNET; 9150; -.
DR GeneCards; CTDP1; -.
DR GeneReviews; CTDP1; -.
DR HGNC; HGNC:2498; CTDP1.
DR HPA; ENSG00000060069; Low tissue specificity.
DR MalaCards; CTDP1; -.
DR MIM; 604168; phenotype.
DR MIM; 604927; gene.
DR neXtProt; NX_Q9Y5B0; -.
DR OpenTargets; ENSG00000060069; -.
DR Orphanet; 48431; Congenital cataracts-facial dysmorphism-neuropathy syndrome.
DR PharmGKB; PA27001; -.
DR VEuPathDB; HostDB:ENSG00000060069; -.
DR eggNOG; KOG0323; Eukaryota.
DR GeneTree; ENSGT00390000015641; -.
DR InParanoid; Q9Y5B0; -.
DR OMA; FARYETY; -.
DR OrthoDB; 683531at2759; -.
DR PhylomeDB; Q9Y5B0; -.
DR TreeFam; TF315104; -.
DR PathwayCommons; Q9Y5B0; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
DR Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-167287; HIV elongation arrest and recovery.
DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR SignaLink; Q9Y5B0; -.
DR SIGNOR; Q9Y5B0; -.
DR BioGRID-ORCS; 9150; 793 hits in 1056 CRISPR screens.
DR ChiTaRS; CTDP1; human.
DR EvolutionaryTrace; Q9Y5B0; -.
DR GeneWiki; CTDP1; -.
DR GenomeRNAi; 9150; -.
DR Pharos; Q9Y5B0; Tbio.
DR PRO; PR:Q9Y5B0; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9Y5B0; protein.
DR Bgee; ENSG00000060069; Expressed in left testis and 145 other tissues.
DR ExpressionAtlas; Q9Y5B0; baseline and differential.
DR Genevisible; Q9Y5B0; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; TAS:Reactome.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IDA:UniProtKB.
DR GO; GO:0030957; F:Tat protein binding; IPI:CAFA.
DR GO; GO:0001096; F:TFIIF-class transcription factor complex binding; IPI:CAFA.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; IDA:CAFA.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
DR DisProt; DP00177; -.
DR Gene3D; 3.40.50.1000; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR IDEAL; IID00117; -.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR015388; FCP1_C.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR011947; FCP1_euk.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR PANTHER; PTHR23081; PTHR23081; 2.
DR Pfam; PF09309; FCP1_C; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR02250; FCP1_euk; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cataract; Cell cycle;
KW Cell division; Cytoplasm; Cytoskeleton; Hydrolase; Mitosis; Neuropathy;
KW Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome.
FT CHAIN 1..961
FT /note="RNA polymerase II subunit A C-terminal domain
FT phosphatase"
FT /id="PRO_0000212564"
FT DOMAIN 178..344
FT /note="FCP1 homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00336"
FT DOMAIN 629..728
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 328..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..589
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..896
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 780
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 839
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VAR_SEQ 807..961
FT /note="AVPPPQPQMFGEELPDAQDGEQPGPSRRKRQPSMSETMPLYTLCKEDLESMD
FT KEVDDILGEGSDDSDSEKRRPEEQEEEPQPRKPGTRRERTLGAPASSERSAAGGRGPRG
FT HKRKLNEEDAASESSRESSNEDEGSSSEADEMAKALEAELNDLM -> WTTSLEKAATT
FT ATARRGGLRSRRRSPSPGSQGPAGSGRSGHLRPARGARQGAGGPEATRGS (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9765293"
FT /id="VSP_009865"
FT VARIANT 282
FT /note="S -> F (in dbSNP:rs4799078)"
FT /id="VAR_060440"
FT VARIANT 340
FT /note="T -> M (in dbSNP:rs2279103)"
FT /id="VAR_018264"
FT VARIANT 519
FT /note="P -> H (in dbSNP:rs557503)"
FT /id="VAR_060441"
FT VARIANT 755
FT /note="L -> S (in dbSNP:rs34967023)"
FT /id="VAR_032763"
FT CONFLICT 61
FT /note="S -> A (in Ref. 1; AAD42088 and 4; AAH63447)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="P -> A (in Ref. 5; AAC64549)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="F -> I (in Ref. 4; AAH52576)"
FT /evidence="ECO:0000305"
FT CONFLICT 305
FT /note="E -> K (in Ref. 1; AAD42088)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="A -> P (in Ref. 5; AAC64549)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="S -> T (in Ref. 5; AAC64549)"
FT /evidence="ECO:0000305"
FT CONFLICT 486..487
FT /note="KP -> NA (in Ref. 5; AAC64549)"
FT /evidence="ECO:0000305"
FT CONFLICT 504..505
FT /note="EP -> DA (in Ref. 5; AAC64549)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="L -> V (in Ref. 5; AAC64549)"
FT /evidence="ECO:0000305"
FT CONFLICT 656..657
FT /note="EH -> DD (in Ref. 5; AAC64549)"
FT /evidence="ECO:0000305"
FT CONFLICT 896..900
FT /note="ERTLG -> GADAR (in Ref. 1; AAD42088)"
FT /evidence="ECO:0000305"
FT HELIX 586..598
FT /evidence="ECO:0007829|PDB:2K7L"
FT HELIX 945..956
FT /evidence="ECO:0007829|PDB:1J2X"
FT TURN 957..959
FT /evidence="ECO:0007829|PDB:1J2X"
SQ SEQUENCE 961 AA; 104399 MW; 62B88FFD9CE4B157 CRC64;
MEVPAAGRVP AEGAPTAAVA EVRCPGPAPL RLLEWRVAAG AAVRIGSVLA VFEAAASAQS
SGASQSRVAS GGCVRPARPE RRLRSERAGV VRELCAQPGQ VVAPGAVLVR LEGCSHPVVM
KGLCAECGQD LTQLQSKNGK QQVPLSTATV SMVHSVPELM VSSEQAEQLG REDQQRLHRN
RKLVLMVDLD QTLIHTTEQH CQQMSNKGIF HFQLGRGEPM LHTRLRPHCK DFLEKIAKLY
ELHVFTFGSR LYAHTIAGFL DPEKKLFSHR ILSRDECIDP FSKTGNLRNL FPCGDSMVCI
IDDREDVWKF APNLITVKKY VYFQGTGDMN APPGSRESQT RKKVNHSRGT EVSEPSPPVR
DPEGVTQAPG VEPSNGLEKP ARELNGSEAA TPRDSPRPGK PDERDIWPPA QAPTSSQELA
GAPEPQGSCA QGGRVAPGQR PAQGATGTDL DFDLSSDSES SSESEGTKSS SSASDGESEG
KRGRQKPKAA PEGAGALAQG SSLEPGRPAA PSLPGEAEPG AHAPDKEPEL GGQEEGERDG
LCGLGNGCAD RKEAETESQN SELSGVTAGE SLDQSMEEEE EEDTDEDDHL IYLEEILVRV
HTDYYAKYDR YLNKEIEEAP DIRKIVPELK SKVLADVAII FSGLHPTNFP IEKTREHYHA
TALGAKILTR LVLSPDAPDR ATHLIAARAG TEKVLQAQEC GHLHVVNPDW LWSCLERWDK
VEEQLFPLRD DHTKAQRENS PAAFPDREGV PPTALFHPMP VLPKAQPGPE VRIYDSNTGK
LIRTGARGPP APSSSLPIRQ EPSSFRAVPP PQPQMFGEEL PDAQDGEQPG PSRRKRQPSM
SETMPLYTLC KEDLESMDKE VDDILGEGSD DSDSEKRRPE EQEEEPQPRK PGTRRERTLG
APASSERSAA GGRGPRGHKR KLNEEDAASE SSRESSNEDE GSSSEADEMA KALEAELNDL
M
