CTR9_HUMAN
ID CTR9_HUMAN Reviewed; 1173 AA.
AC Q6PD62; D3DQV8; Q15015;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=RNA polymerase-associated protein CTR9 homolog;
DE AltName: Full=SH2 domain-binding protein 1;
GN Name=CTR9; Synonyms=KIAA0155, SH2BP1;
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 [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R., Nomura N.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 FUNCTION, AND IDENTIFICATION IN THE PAF1 COMPLEX.
RX PubMed=16024656; DOI=10.1101/gad.1292105;
RA Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H., Batra S.K.,
RA Tempst P., Reinberg D.;
RT "The human PAF complex coordinates transcription with events downstream of
RT RNA synthesis.";
RL Genes Dev. 19:1668-1673(2005).
RN [6]
RP FUNCTION.
RX PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025;
RA Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P.,
RA Reinberg D.;
RT "Monoubiquitination of human histone H2B: the factors involved and their
RT roles in HOX gene regulation.";
RL Mol. Cell 20:601-611(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943 AND
RP SER-970, AND IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941; SER-943; SER-1020 AND
RP SER-1021, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-970, AND
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 [12]
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., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP FUNCTION.
RX PubMed=19345177; DOI=10.1016/j.stem.2009.03.009;
RA Ding L., Paszkowski-Rogacz M., Nitzsche A., Slabicki M.M., Heninger A.K.,
RA de Vries I., Kittler R., Junqueira M., Shevchenko A., Schulz H., Hubner N.,
RA Doss M.X., Sachinidis A., Hescheler J., Iacone R., Anastassiadis K.,
RA Stewart A.F., Pisabarro M.T., Caldarelli A., Poser I., Theis M.,
RA Buchholz F.;
RT "A genome-scale RNAi screen for Oct4 modulators defines a role of the Paf1
RT complex for embryonic stem cell identity.";
RL Cell Stem Cell 4:403-415(2009).
RN [14]
RP IDENTIFICATION IN THE PAF1 COMPLEX, AND FUNCTION OF THE PAF1 COMPLEX.
RX PubMed=19952111; DOI=10.1101/gad.1834709;
RA Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T., Nakamura M.,
RA Hisatake K., Handa H.;
RT "DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative roles
RT in RNA polymerase II elongation.";
RL Genes Dev. 23:2765-2777(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-932, 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 [16]
RP FUNCTION OF THE PAF1 COMPLEX, AND INTERACTION WITH KMT2A.
RX PubMed=20541477; DOI=10.1016/j.ccr.2010.04.012;
RA Muntean A.G., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly J.A.,
RA Basrur V., Elenitoba-Johnson K.S., Hess J.L.;
RT "The PAF complex synergizes with MLL fusion proteins at HOX loci to promote
RT leukemogenesis.";
RL Cancer Cell 17:609-621(2010).
RN [17]
RP IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX, AND
RP FUNCTION OF THE PAF1 COMPLEX.
RX PubMed=20178742; DOI=10.1016/j.cell.2009.12.050;
RA Kim J., Guermah M., Roeder R.G.;
RT "The human PAF1 complex acts in chromatin transcription elongation both
RT independently and cooperatively with SII/TFIIS.";
RL Cell 140:491-503(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943 AND
RP SER-970, AND 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 [19]
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 [20]
RP FUNCTION, AND FUNCTION OF THE PAF1 COMPLEX.
RX PubMed=21329879; DOI=10.1016/j.molcel.2011.01.022;
RA Nagaike T., Logan C., Hotta I., Rozenblatt-Rosen O., Meyerson M.,
RA Manley J.L.;
RT "Transcriptional activators enhance polyadenylation of mRNA precursors.";
RL Mol. Cell 41:409-418(2011).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943;
RP SER-970; SER-1020; SER-1021; SER-1097 AND SER-1102, 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-970, AND
RP 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-1087, AND
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 [24]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [25]
RP INTERACTION WITH ZIKA VIRUS FRENCH POLYNESIA 10087PF/2013 NS5; DENGUE VIRUS
RP DENV2 16681 NS5 AND DENGUE VIRUS DENV4 DOMINICA/814669/1981 NS5.
RX PubMed=30550790; DOI=10.1016/j.cell.2018.11.028;
RA Shah P.S., Link N., Jang G.M., Sharp P.P., Zhu T., Swaney D.L.,
RA Johnson J.R., Von Dollen J., Ramage H.R., Satkamp L., Newton B.,
RA Huettenhain R., Petit M.J., Baum T., Everitt A., Laufman O., Tassetto M.,
RA Shales M., Stevenson E., Iglesias G.N., Shokat L., Tripathi S.,
RA Balasubramaniam V., Webb L.G., Aguirre S., Willsey A.J., Garcia-Sastre A.,
RA Pollard K.S., Cherry S., Gamarnik A.V., Marazzi I., Taunton J.,
RA Fernandez-Sesma A., Bellen H.J., Andino R., Krogan N.J.;
RT "Comparative Flavivirus-Host Protein Interaction Mapping Reveals Mechanisms
RT of Dengue and Zika Virus Pathogenesis.";
RL Cell 175:1931-1945(2018).
CC -!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
CC functions during transcription by RNA polymerase II and is implicated
CC in regulation of development and maintenance of embryonic stem cell
CC pluripotency. PAF1C associates with RNA polymerase II through
CC interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-
CC 5'-phosphorylated forms and is involved in transcriptional elongation,
CC acting both independently and synergistically with TCEA1 and in
CC cooperation with the DSIF complex and HTATSF1. PAF1C is required for
CC transcription of Hox and Wnt target genes. PAF1C is involved in
CC hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it
CC promotes leukemogenesis through association with KMT2A/MLL1-rearranged
CC oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL.
CC PAF1C is involved in histone modifications such as ubiquitination of
CC histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C
CC recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2
CC enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of
CC 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B
CC ubiquitination is proposed to be coupled to transcription. PAF1C is
CC involved in mRNA 3' end formation probably through association with
CC cleavage and poly(A) factors. In case of infection by influenza A
CC strain H3N2, PAF1C associates with viral NS1 protein, thereby
CC regulating gene transcription. Required for mono- and trimethylation on
CC histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79'
CC (H3K4me3). Required for Hox gene transcription. Required for the
CC trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in
CC stem cell pluripotency; this function is synergistic with CXXC1
CC indicative for an involvement of the SET1 complex. Involved in
CC transcriptional regulation of IL6-responsive genes and in JAK-STAT
CC pathway; may regulate DNA-association of STAT3 (By similarity).
CC {ECO:0000250|UniProtKB:Q62018, ECO:0000269|PubMed:16024656,
CC ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:19345177,
CC ECO:0000269|PubMed:19952111, ECO:0000269|PubMed:20178742,
CC ECO:0000269|PubMed:20541477, ECO:0000269|PubMed:21329879}.
CC -!- SUBUNIT: Component of the PAF1 complex, which consists of CDC73, PAF1,
CC LEO1, CTR9, RTF1 and WDR61 (PubMed:16024656, PubMed:19952111,
CC PubMed:20178742). The PAF1 complex interacts with PHF5A (By
CC similarity). Interacts with KMT2A/MLL1 (PubMed:20541477). Interacts
CC with STAT3 (By similarity). Interacts with SETD5 (By similarity).
CC Interacts with ERCC6 (PubMed:26030138). {ECO:0000250|UniProtKB:Q62018,
CC ECO:0000269|PubMed:16024656, ECO:0000269|PubMed:19952111,
CC ECO:0000269|PubMed:20178742, ECO:0000269|PubMed:20541477,
CC ECO:0000269|PubMed:26030138}.
CC -!- SUBUNIT: (Microbial infection) The PAF1 complex interacts with Zika
CC virus French Polynesia 10087PF/2013 non-structural protein 5/NS5
CC (PubMed:30550790). The interaction with viral NS5 proteins may reduce
CC the antiviral immune response by inhibiting the recruitment of the PAF1
CC complex to interferon-stimulated genes, thus preventing their
CC transcription (PubMed:30550790). {ECO:0000269|PubMed:30550790}.
CC -!- SUBUNIT: (Microbial infection) The PAF1 complex interacts with Dengue
CC virus DENV2 16681 non-structural protein 5/NS5 (PubMed:30550790). The
CC PAF1 complex interacts with Dengue virus DENV4 Dominica/814669/1981
CC non-structural protein 5/NS5 (PubMed:30550790). The interaction with
CC viral NS5 proteins may reduce the antiviral immune response by
CC inhibiting the recruitment of the PAF1 complex to interferon-stimulated
CC genes, thus preventing their transcription (PubMed:30550790).
CC {ECO:0000269|PubMed:30550790}.
CC -!- INTERACTION:
CC Q6PD62; Q6P1J9: CDC73; NbExp=23; IntAct=EBI-1019583, EBI-930143;
CC Q6PD62; Q03164: KMT2A; NbExp=5; IntAct=EBI-1019583, EBI-591370;
CC Q6PD62; Q8N7H5: PAF1; NbExp=26; IntAct=EBI-1019583, EBI-2607770;
CC Q6PD62; Q9GZS3: WDR61; NbExp=12; IntAct=EBI-1019583, EBI-358545;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q62018}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8590280}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09925.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D63875; BAA09925.2; ALT_INIT; mRNA.
DR EMBL; CH471064; EAW68557.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68558.1; -; Genomic_DNA.
DR EMBL; BC058914; AAH58914.1; -; mRNA.
DR CCDS; CCDS7805.1; -.
DR RefSeq; NP_055448.1; NM_014633.4.
DR PDB; 5ZYQ; X-ray; 2.53 A; A=1-249.
DR PDB; 6GMH; EM; 3.10 A; Q=301-1173.
DR PDB; 6TED; EM; 3.10 A; Q=1-1173.
DR PDB; 7OOP; EM; 2.90 A; S=1-1173.
DR PDB; 7OPC; EM; 3.00 A; S=1-1173.
DR PDB; 7OPD; EM; 3.00 A; S=1-1173.
DR PDBsum; 5ZYQ; -.
DR PDBsum; 6GMH; -.
DR PDBsum; 6TED; -.
DR PDBsum; 7OOP; -.
DR PDBsum; 7OPC; -.
DR PDBsum; 7OPD; -.
DR AlphaFoldDB; Q6PD62; -.
DR SMR; Q6PD62; -.
DR BioGRID; 115004; 215.
DR CORUM; Q6PD62; -.
DR DIP; DIP-31693N; -.
DR IntAct; Q6PD62; 117.
DR MINT; Q6PD62; -.
DR STRING; 9606.ENSP00000355013; -.
DR iPTMnet; Q6PD62; -.
DR MetOSite; Q6PD62; -.
DR PhosphoSitePlus; Q6PD62; -.
DR BioMuta; CTR9; -.
DR DMDM; 74758318; -.
DR EPD; Q6PD62; -.
DR jPOST; Q6PD62; -.
DR MassIVE; Q6PD62; -.
DR MaxQB; Q6PD62; -.
DR PaxDb; Q6PD62; -.
DR PeptideAtlas; Q6PD62; -.
DR PRIDE; Q6PD62; -.
DR ProteomicsDB; 67068; -.
DR Antibodypedia; 24416; 202 antibodies from 27 providers.
DR DNASU; 9646; -.
DR Ensembl; ENST00000361367.7; ENSP00000355013.2; ENSG00000198730.9.
DR GeneID; 9646; -.
DR KEGG; hsa:9646; -.
DR MANE-Select; ENST00000361367.7; ENSP00000355013.2; NM_014633.5; NP_055448.1.
DR UCSC; uc001mja.4; human.
DR CTD; 9646; -.
DR DisGeNET; 9646; -.
DR GeneCards; CTR9; -.
DR HGNC; HGNC:16850; CTR9.
DR HPA; ENSG00000198730; Low tissue specificity.
DR MIM; 609366; gene.
DR neXtProt; NX_Q6PD62; -.
DR OpenTargets; ENSG00000198730; -.
DR PharmGKB; PA134896774; -.
DR VEuPathDB; HostDB:ENSG00000198730; -.
DR eggNOG; KOG2002; Eukaryota.
DR GeneTree; ENSGT00390000005097; -.
DR HOGENOM; CLU_006386_0_0_1; -.
DR InParanoid; Q6PD62; -.
DR OMA; MSNCIEI; -.
DR OrthoDB; 396755at2759; -.
DR PhylomeDB; Q6PD62; -.
DR TreeFam; TF314342; -.
DR PathwayCommons; Q6PD62; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR SignaLink; Q6PD62; -.
DR BioGRID-ORCS; 9646; 634 hits in 1087 CRISPR screens.
DR ChiTaRS; CTR9; human.
DR GeneWiki; CTR9; -.
DR GenomeRNAi; 9646; -.
DR Pharos; Q6PD62; Tbio.
DR PRO; PR:Q6PD62; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6PD62; protein.
DR Bgee; ENSG00000198730; Expressed in corpus epididymis and 209 other tissues.
DR ExpressionAtlas; Q6PD62; baseline and differential.
DR Genevisible; Q6PD62; HS.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
DR GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR GO; GO:0001832; P:blastocyst growth; IEA:Ensembl.
DR GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISS:UniProtKB.
DR GO; GO:0001711; P:endodermal cell fate commitment; ISS:UniProtKB.
DR GO; GO:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
DR GO; GO:0001826; P:inner cell mass cell differentiation; IEA:Ensembl.
DR GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0045638; P:negative regulation of myeloid cell differentiation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; IMP:UniProtKB.
DR GO; GO:2001162; P:positive regulation of histone H3-K79 methylation; IMP:UniProtKB.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; ISS:UniProtKB.
DR GO; GO:2000653; P:regulation of genetic imprinting; IEA:Ensembl.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0019827; P:stem cell population maintenance; IDA:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:GO_Central.
DR GO; GO:0001829; P:trophectodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR031101; Ctr9.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14027; PTHR14027; 1.
DR Pfam; PF13181; TPR_8; 3.
DR SMART; SM00028; TPR; 10.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 10.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat; Transcription; Transcription regulation; Wnt signaling pathway.
FT CHAIN 1..1173
FT /note="RNA polymerase-associated protein CTR9 homolog"
FT /id="PRO_0000231588"
FT REPEAT 41..75
FT /note="TPR 1"
FT REPEAT 129..162
FT /note="TPR 2"
FT REPEAT 163..196
FT /note="TPR 3"
FT REPEAT 198..231
FT /note="TPR 4"
FT REPEAT 235..268
FT /note="TPR 5"
FT REPEAT 306..339
FT /note="TPR 6"
FT REPEAT 341..374
FT /note="TPR 7"
FT REPEAT 412..444
FT /note="TPR 8"
FT REPEAT 451..484
FT /note="TPR 9"
FT REPEAT 497..530
FT /note="TPR 10"
FT REPEAT 531..564
FT /note="TPR 11"
FT REPEAT 566..598
FT /note="TPR 12"
FT REPEAT 613..646
FT /note="TPR 13"
FT REPEAT 647..680
FT /note="TPR 14"
FT REPEAT 681..714
FT /note="TPR 15"
FT REPEAT 717..750
FT /note="TPR 16"
FT REGION 892..1173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..983
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1005
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1058
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1101..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1140..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1156..1173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 925
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 941
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 943
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 970
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1020
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1021
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1039
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62018"
FT MOD_RES 1041
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62018"
FT MOD_RES 1043
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62018"
FT MOD_RES 1081
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62018"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62018"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1097
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:7OOP"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT HELIX 57..70
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 78..99
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT HELIX 103..121
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT HELIX 128..140
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT HELIX 145..156
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT HELIX 214..227
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:5ZYQ"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:7OOP"
FT TURN 255..258
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 269..281
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 302..318
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 322..335
FT /evidence="ECO:0007829|PDB:7OOP"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 342..352
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 357..370
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 375..382
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 391..404
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 427..443
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 451..463
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 467..483
FT /evidence="ECO:0007829|PDB:7OOP"
FT TURN 488..491
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 492..509
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 513..526
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 532..544
FT /evidence="ECO:0007829|PDB:7OOP"
FT TURN 547..549
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 550..560
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 565..575
FT /evidence="ECO:0007829|PDB:7OOP"
FT TURN 582..584
FT /evidence="ECO:0007829|PDB:6TED"
FT HELIX 585..588
FT /evidence="ECO:0007829|PDB:7OOP"
FT TURN 589..592
FT /evidence="ECO:0007829|PDB:7OOP"
FT TURN 595..597
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 601..612
FT /evidence="ECO:0007829|PDB:7OOP"
FT TURN 618..623
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 624..642
FT /evidence="ECO:0007829|PDB:7OOP"
FT STRAND 644..646
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 647..659
FT /evidence="ECO:0007829|PDB:7OOP"
FT TURN 660..662
FT /evidence="ECO:0007829|PDB:6GMH"
FT TURN 664..666
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 667..676
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 681..693
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 697..707
FT /evidence="ECO:0007829|PDB:7OOP"
FT STRAND 710..712
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 717..723
FT /evidence="ECO:0007829|PDB:7OOP"
FT STRAND 724..726
FT /evidence="ECO:0007829|PDB:7OOP"
FT TURN 731..733
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 734..746
FT /evidence="ECO:0007829|PDB:7OOP"
FT STRAND 748..750
FT /evidence="ECO:0007829|PDB:6GMH"
FT HELIX 751..766
FT /evidence="ECO:0007829|PDB:7OOP"
FT STRAND 768..771
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 776..798
FT /evidence="ECO:0007829|PDB:7OOP"
FT STRAND 803..805
FT /evidence="ECO:0007829|PDB:7OOP"
FT HELIX 810..891
FT /evidence="ECO:0007829|PDB:7OOP"
SQ SEQUENCE 1173 AA; 133502 MW; 4B5AC22A5C5573C6 CRC64;
MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE YYKQGKTEEF
VKLLEAARID GNLDYRDHEK DQMTCLDTLA AYYVQQARKE KNKDNKKDLI TQATLLYTMA
DKIIMYDQNH LLGRACFCLL EGDKMDQADA QFHFVLNQSP NNIPALLGKA CISFNKKDYR
GALAYYKKAL RTNPGCPAEV RLGMGHCFVK LNKLEKARLA FSRALELNSK CVGALVGLAV
LELNNKEADS IKNGVQLLSR AYTIDPSNPM VLNHLANHFF FKKDYSKVQH LALHAFHNTE
VEAMQAESCY QLARSFHVQE DYDQAFQYYY QATQFASSSF VLPFFGLGQM YIYRGDKENA
SQCFEKVLKA YPNNYETMKI LGSLYAASED QEKRDIAKGH LKKVTEQYPD DVEAWIELAQ
ILEQTDIQGA LSAYGTATRI LQEKVQADVP PEILNNVGAL HFRLGNLGEA KKYFLASLDR
AKAEAEHDEH YYNAISVTTS YNLARLYEAM CEFHEAEKLY KNILREHPNY VDCYLRLGAM
ARDKGNFYEA SDWFKEALQI NQDHPDAWSL IGNLHLAKQE WGPGQKKFER ILKQPSTQSD
TYSMLALGNV WLQTLHQPTR DREKEKRHQD RALAIYKQVL RNDAKNLYAA NGIGAVLAHK
GYFREARDVF AQVREATADI SDVWLNLAHI YVEQKQYISA VQMYENCLRK FYKHQNTEVV
LYLARALFKC GKLQECKQTL LKARHVAPSD TVLMFNVALV LQRLATSVLK DEKSNLKEVL
NAVKELELAH RYFSYLSKVG DKMRFDLALA ATEARQCSDL LSQAQYHVAR ARKQDEEERE
LRAKQEQEKE LLRQKLLKEQ EEKRLREKEE QKKLLEQRAQ YVEKTKNILM FTGETEATKE
KKRGGGGGRR SKKGGEFDEF VNDDTDDDLP ISKKKKRRKG SGSEQEGEDE EGGERKKKKR
RRHPKGEEGS DDDETENGPK PKKRRPPKAE KKKAPKPERL PPSMKGKIKS KAIISSSDDS
SDEDKLKIAD EGHPRNSNSN SDSDEDEQRK KCASSESDSD ENQNKSGSEA GSPRRPRRQR
SDQDSDSDQP SRKRRPSGSE QSDNESVQSG RSHSGVSEND SRPASPSAES DHESERGSDN
EGSGQGSGNE SEPEGSNNEA SDRGSEHGSD DSD
