ID PCIF1_HUMAN Reviewed; 704 AA.
AC Q9H4Z3; E1P5P1; Q54AB9; Q9NT85;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 01-MAY-2013, entry version 93.
DE RecName: Full=Phosphorylated CTD-interacting factor 1;
GN Name=PCIF1; Synonyms=C20orf67;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND INTERACTION WITH RNAPII.
RC TISSUE=Hepatoma;
RX PubMed=12565871; DOI=10.1016/S0006-291X(02)03015-2;
RA Fan H., Sakuraba K., Komuro A., Kato S., Harada F., Hirose Y.;
RT "PCIF1, a novel human WW domain-containing protein, interacts with the
RT phosphorylated RNA polymerase II.";
RL Biochem. Biophys. Res. Commun. 301:378-385(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle, and Pancreas;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 383-704.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASS
RP SPECTROMETRY.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND THR-152, AND
RP MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- FUNCTION: May play a role in transcription elongation or in
CC coupling transcription to pre-mRNA processing through its
CC association with the phosphorylated C-terminal domain (CTD) of
CC RNAPII largest subunit.
CC -!- SUBUNIT: Interacts with the phosphorylated C-terminal domain (CTD)
CC of RNAPII largest subunit.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- DOMAIN: The WW domain is sufficient for direct and specific
CC interaction with the phosphorylated CTD of RNAPII largest subunit.
CC -!- SIMILARITY: Contains 1 WW domain.
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DR EMBL; AB050014; BAC45238.1; -; mRNA.
DR EMBL; AL162458; CAC10456.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75778.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75780.1; -; Genomic_DNA.
DR EMBL; BC013365; AAH13365.1; -; mRNA.
DR EMBL; BC010005; AAH10005.1; -; mRNA.
DR EMBL; AL137473; CAB70757.2; -; mRNA.
DR IPI; IPI00942711; -.
DR RefSeq; NP_071387.1; NM_022104.3.
DR UniGene; Hs.472856; -.
DR PDB; 2JX8; NMR; -; A=40-86.
DR PDBsum; 2JX8; -.
DR ProteinModelPortal; Q9H4Z3; -.
DR IntAct; Q9H4Z3; 1.
DR MINT; MINT-4050951; -.
DR STRING; 9606.ENSP00000361486; -.
DR PhosphoSite; Q9H4Z3; -.
DR DMDM; 26392546; -.
DR PaxDb; Q9H4Z3; -.
DR PeptideAtlas; Q9H4Z3; -.
DR PRIDE; Q9H4Z3; -.
DR DNASU; 63935; -.
DR Ensembl; ENST00000372409; ENSP00000361486; ENSG00000100982.
DR GeneID; 63935; -.
DR KEGG; hsa:63935; -.
DR UCSC; uc002xqs.3; human.
DR CTD; 63935; -.
DR GeneCards; GC20P044563; -.
DR HGNC; HGNC:16200; PCIF1.
DR HPA; HPA049517; -.
DR neXtProt; NX_Q9H4Z3; -.
DR PharmGKB; PA162398977; -.
DR eggNOG; NOG80928; -.
DR HOGENOM; HOG000048178; -.
DR HOVERGEN; HBG053525; -.
DR InParanoid; Q9H4Z3; -.
DR OrthoDB; EOG4NS3B5; -.
DR PhylomeDB; Q9H4Z3; -.
DR ChiTaRS; PCIF1; human.
DR EvolutionaryTrace; Q9H4Z3; -.
DR GenomeRNAi; 63935; -.
DR NextBio; 65698; -.
DR Bgee; Q9H4Z3; -.
DR CleanEx; HS_PCIF1; -.
DR Genevestigator; Q9H4Z3; -.
DR GermOnline; ENSG00000100982; Homo sapiens.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005825; C:half bridge of spindle pole body; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
DR InterPro; IPR022035; PCIF1_WW.
DR InterPro; IPR001202; WW_dom.
DR Pfam; PF12237; PCIF1_WW; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; WW_Rsp5_WWP; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; FALSE_NEG.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 704 Phosphorylated CTD-interacting factor 1.
FT /FTId=PRO_0000076087.
FT DOMAIN 43 77 WW.
FT MOTIF 109 113 Nuclear localization signal (Potential).
FT MOTIF 669 684 Nuclear localization signal (Potential).
FT COMPBIAS 673 684 Poly-Ser.
FT MOD_RES 30 30 Phosphoserine.
FT MOD_RES 116 116 Phosphoserine.
FT MOD_RES 152 152 Phosphothreonine.
FT HELIX 42 47
FT STRAND 51 54
FT TURN 55 58
FT STRAND 59 64
FT TURN 65 68
FT STRAND 69 73
SQ SEQUENCE 704 AA; 80670 MW; 83647BC8408BA9E9 CRC64;
MANENHGSPR EEASLLSHSP GTSNQSQPCS PKPIRLVQDL PEELVHAGWE KCWSRRENRP
YYFNRFTNQS LWEMPVLGQH DVISDPLGLN ATPLPQDSSL VETPPAENKP RKRQLSEEQP
SGNGVKKPKI EIPVTPTGQS VPSSPSIPGT PTLKMWGTSP EDKQQAALLR PTEVYWDLDI
QTNAVIKHRG PSEVLPPHPE VELLRSQLIL KLRQHYRELC QQREGIEPPR ESFNRWMLER
KVVDKGSDPL LPSNCEPVVS PSMFREIMND IPIRLSRIKF REEAKRLLFK YAEAARRLIE
SRSASPDSRK VVKWNVEDTF SWLRKDHSAS KEDYMDRLEH LRRQCGPHVS AAAKDSVEGI
CSKIYHISLE YVKRIREKHL AILKENNISE EVEAPEVEPR LVYCYPVRLA VSAPPMPSVE
MHMENNVVCI RYKGEMVKVS RNYFSKLWLL YRYSCIDDSA FERFLPRVWC LLRRYQMMFG
VGLYEGTGLQ GSLPVHVFEA LHRLFGVSFE CFASPLNCYF RQYCSAFPDT DGYFGSRGPC
LDFAPLSGSF EANPPFCEEL MDAMVSHFER LLESSPEPLS FIVFIPEWRE PPTPALTRME
QSRFKRHQLI LPAFEHEYRS GSQHICKKEE MHYKAVHNTA VLFLQNDPGF AKWAPTPERL
QELSAAYRQS GRSHSSGSSS SSSSEAKDRD SGREQGPSRE PHPT
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