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Database: UniProt
Entry: Q9H4Z3
LinkDB: Q9H4Z3
Original site: Q9H4Z3 
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   26-NOV-2014, entry version 108.
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 IDENTIFICATION
RP   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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND THR-152, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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. {ECO:0000269|PubMed:12565871}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12565871}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12565871}.
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. {ECO:0000255|PROSITE-
CC       ProRule:PRU00224}.
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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   CCDS; CCDS13388.1; -.
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   SMR; Q9H4Z3; 40-86.
DR   BioGrid; 122003; 6.
DR   IntAct; Q9H4Z3; 3.
DR   MINT; MINT-4050951; -.
DR   STRING; 9606.ENSP00000361486; -.
DR   PhosphoSite; Q9H4Z3; -.
DR   DMDM; 26392546; -.
DR   MaxQB; Q9H4Z3; -.
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   GeneTree; ENSGT00390000016206; -.
DR   HOGENOM; HOG000048178; -.
DR   HOVERGEN; HBG053525; -.
DR   InParanoid; Q9H4Z3; -.
DR   KO; K17584; -.
DR   OMA; GFAKWEP; -.
DR   OrthoDB; EOG7TJ3H6; -.
DR   PhylomeDB; Q9H4Z3; -.
DR   TreeFam; TF350163; -.
DR   SignaLink; Q9H4Z3; -.
DR   ChiTaRS; PCIF1; human.
DR   EvolutionaryTrace; Q9H4Z3; -.
DR   GenomeRNAi; 63935; -.
DR   NextBio; 65698; -.
DR   PRO; PR:Q9H4Z3; -.
DR   Bgee; Q9H4Z3; -.
DR   CleanEx; HS_PCIF1; -.
DR   Genevestigator; Q9H4Z3; -.
DR   GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR   GO; GO:0015630; C:microtubule cytoskeleton; 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; SSF51045; 1.
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. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00224}.
FT   MOTIF       109    113       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   MOTIF       669    684       Nuclear localization signal.
FT                                {ECO:0000255}.
FT   COMPBIAS    673    684       Poly-Ser.
FT   MOD_RES      30     30       Phosphoserine.
FT                                {ECO:0000269|PubMed:18669648}.
FT   MOD_RES     116    116       Phosphoserine.
FT                                {ECO:0000269|PubMed:19690332,
FT                                ECO:0000269|PubMed:21406692}.
FT   MOD_RES     152    152       Phosphothreonine.
FT                                {ECO:0000269|PubMed:19690332}.
FT   HELIX        42     47       {ECO:0000244|PDB:2JX8}.
FT   STRAND       51     54       {ECO:0000244|PDB:2JX8}.
FT   TURN         55     58       {ECO:0000244|PDB:2JX8}.
FT   STRAND       59     64       {ECO:0000244|PDB:2JX8}.
FT   TURN         65     68       {ECO:0000244|PDB:2JX8}.
FT   STRAND       69     73       {ECO:0000244|PDB:2JX8}.
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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