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Q6PD62

- CTR9_HUMAN

UniProt

Q6PD62 - CTR9_HUMAN

Protein

RNA polymerase-associated protein CTR9 homolog

Gene

CTR9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both indepentently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1; it promotes leukemogenesis through association with KMT2A/MLL1-rearranged oncoproteins, such as KMT2A/MLL1-MLLT3/AF9 and KMT2A/MLL1-MLLT1/ENL. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1); UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. In case of infection by influenza A strain H3N2, PAF1C associates with viral NS1 protein, thereby regulating gene transcription. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription. Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency; this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway; may regulate DNA-association of STAT3 By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. cellular response to lipopolysaccharide Source: UniProtKB
    2. endodermal cell fate commitment Source: UniProtKB
    3. histone H2B ubiquitination Source: UniProtKB
    4. histone H3-K4 trimethylation Source: UniProtKB
    5. histone monoubiquitination Source: UniProtKB
    6. interleukin-6-mediated signaling pathway Source: UniProtKB
    7. JAK-STAT cascade Source: UniProtKB
    8. negative regulation of myeloid cell differentiation Source: UniProtKB
    9. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    10. positive regulation of histone H3-K4 methylation Source: UniProtKB
    11. positive regulation of histone H3-K79 methylation Source: UniProtKB
    12. positive regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB
    13. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    14. stem cell maintenance Source: UniProtKB
    15. transcription, DNA-templated Source: UniProtKB-KW
    16. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Biological processi

    Transcription, Transcription regulation, Wnt signaling pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA polymerase-associated protein CTR9 homolog
    Alternative name(s):
    SH2 domain-binding protein 1
    Gene namesi
    Name:CTR9
    Synonyms:KIAA0155, SH2BP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:16850. CTR9.

    Subcellular locationi

    Nucleus speckle By similarity
    Note: Found in speckles.By similarity

    GO - Cellular componenti

    1. Cdc73/Paf1 complex Source: UniProtKB
    2. nuclear speck Source: UniProtKB-SubCell
    3. transcriptionally active chromatin Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134896774.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11731173RNA polymerase-associated protein CTR9 homologPRO_0000231588Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei925 – 9251Phosphothreonine7 Publications
    Modified residuei932 – 9321Phosphoserine1 Publication
    Modified residuei941 – 9411Phosphoserine4 Publications
    Modified residuei943 – 9431Phosphoserine4 Publications
    Modified residuei970 – 9701Phosphoserine4 Publications
    Modified residuei1020 – 10201Phosphoserine2 Publications
    Modified residuei1021 – 10211Phosphoserine2 Publications
    Modified residuei1097 – 10971Phosphoserine1 Publication
    Modified residuei1102 – 11021Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ6PD62.
    PaxDbiQ6PD62.
    PRIDEiQ6PD62.

    PTM databases

    PhosphoSiteiQ6PD62.

    Miscellaneous databases

    PMAP-CutDBQ6PD62.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ6PD62.
    BgeeiQ6PD62.
    CleanExiHS_CTR9.
    GenevestigatoriQ6PD62.

    Interactioni

    Subunit structurei

    Component of the mammalian PAF1 complex, which consists of CDC73, PAF1, LEO1, CTR9, RTF1 and WDR61. Interacts with KMT2A/MLL1. Interacts with STAT3 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDC73Q6P1J915EBI-1019583,EBI-930143
    KMT2AQ031645EBI-1019583,EBI-591370
    PAF1Q8N7H522EBI-1019583,EBI-2607770
    WDR61Q9GZS39EBI-1019583,EBI-358545

    Protein-protein interaction databases

    BioGridi115004. 27 interactions.
    DIPiDIP-31693N.
    IntActiQ6PD62. 29 interactions.
    MINTiMINT-1182366.
    STRINGi9606.ENSP00000355013.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6PD62.
    SMRiQ6PD62. Positions 265-749.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati41 – 7535TPR 1Add
    BLAST
    Repeati129 – 16234TPR 2Add
    BLAST
    Repeati163 – 19634TPR 3Add
    BLAST
    Repeati198 – 23134TPR 4Add
    BLAST
    Repeati235 – 26834TPR 5Add
    BLAST
    Repeati306 – 33934TPR 6Add
    BLAST
    Repeati341 – 37434TPR 7Add
    BLAST
    Repeati412 – 44433TPR 8Add
    BLAST
    Repeati451 – 48434TPR 9Add
    BLAST
    Repeati497 – 53034TPR 10Add
    BLAST
    Repeati531 – 56434TPR 11Add
    BLAST
    Repeati566 – 59833TPR 12Add
    BLAST
    Repeati613 – 64634TPR 13Add
    BLAST
    Repeati647 – 68034TPR 14Add
    BLAST
    Repeati681 – 71434TPR 15Add
    BLAST
    Repeati717 – 75034TPR 16Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi844 – 1011168Lys-richAdd
    BLAST
    Compositional biasi904 – 9085Poly-Gly
    Compositional biasi933 – 9364Poly-Lys
    Compositional biasi956 – 9594Poly-Lys
    Compositional biasi1015 – 1172158Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 16 TPR repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, TPR repeat

    Phylogenomic databases

    eggNOGiCOG0457.
    HOGENOMiHOG000246926.
    HOVERGENiHBG081372.
    InParanoidiQ6PD62.
    KOiK15176.
    OMAiTQNDTYS.
    OrthoDBiEOG79KPDH.
    PhylomeDBiQ6PD62.
    TreeFamiTF314342.

    Family and domain databases

    Gene3Di1.25.40.10. 5 hits.
    InterProiIPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view]
    PfamiPF00515. TPR_1. 7 hits.
    PF07719. TPR_2. 1 hit.
    [Graphical view]
    SMARTiSM00028. TPR. 9 hits.
    [Graphical view]
    PROSITEiPS50005. TPR. 10 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6PD62-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE     50
    YYKQGKTEEF VKLLEAARID GNLDYRDHEK DQMTCLDTLA AYYVQQARKE 100
    KNKDNKKDLI TQATLLYTMA DKIIMYDQNH LLGRACFCLL EGDKMDQADA 150
    QFHFVLNQSP NNIPALLGKA CISFNKKDYR GALAYYKKAL RTNPGCPAEV 200
    RLGMGHCFVK LNKLEKARLA FSRALELNSK CVGALVGLAV LELNNKEADS 250
    IKNGVQLLSR AYTIDPSNPM VLNHLANHFF FKKDYSKVQH LALHAFHNTE 300
    VEAMQAESCY QLARSFHVQE DYDQAFQYYY QATQFASSSF VLPFFGLGQM 350
    YIYRGDKENA SQCFEKVLKA YPNNYETMKI LGSLYAASED QEKRDIAKGH 400
    LKKVTEQYPD DVEAWIELAQ ILEQTDIQGA LSAYGTATRI LQEKVQADVP 450
    PEILNNVGAL HFRLGNLGEA KKYFLASLDR AKAEAEHDEH YYNAISVTTS 500
    YNLARLYEAM CEFHEAEKLY KNILREHPNY VDCYLRLGAM ARDKGNFYEA 550
    SDWFKEALQI NQDHPDAWSL IGNLHLAKQE WGPGQKKFER ILKQPSTQSD 600
    TYSMLALGNV WLQTLHQPTR DREKEKRHQD RALAIYKQVL RNDAKNLYAA 650
    NGIGAVLAHK GYFREARDVF AQVREATADI SDVWLNLAHI YVEQKQYISA 700
    VQMYENCLRK FYKHQNTEVV LYLARALFKC GKLQECKQTL LKARHVAPSD 750
    TVLMFNVALV LQRLATSVLK DEKSNLKEVL NAVKELELAH RYFSYLSKVG 800
    DKMRFDLALA ATEARQCSDL LSQAQYHVAR ARKQDEEERE LRAKQEQEKE 850
    LLRQKLLKEQ EEKRLREKEE QKKLLEQRAQ YVEKTKNILM FTGETEATKE 900
    KKRGGGGGRR SKKGGEFDEF VNDDTDDDLP ISKKKKRRKG SGSEQEGEDE 950
    EGGERKKKKR RRHPKGEEGS DDDETENGPK PKKRRPPKAE KKKAPKPERL 1000
    PPSMKGKIKS KAIISSSDDS SDEDKLKIAD EGHPRNSNSN SDSDEDEQRK 1050
    KCASSESDSD ENQNKSGSEA GSPRRPRRQR SDQDSDSDQP SRKRRPSGSE 1100
    QSDNESVQSG RSHSGVSEND SRPASPSAES DHESERGSDN EGSGQGSGNE 1150
    SEPEGSNNEA SDRGSEHGSD DSD 1173
    Length:1,173
    Mass (Da):133,502
    Last modified:July 5, 2004 - v1
    Checksum:i4B5AC22A5C5573C6
    GO

    Sequence cautioni

    The sequence BAA09925.2 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63875 mRNA. Translation: BAA09925.2. Different initiation.
    CH471064 Genomic DNA. Translation: EAW68557.1.
    CH471064 Genomic DNA. Translation: EAW68558.1.
    BC058914 mRNA. Translation: AAH58914.1.
    CCDSiCCDS7805.1.
    RefSeqiNP_055448.1. NM_014633.3.
    UniGeneiHs.725151.

    Genome annotation databases

    EnsembliENST00000361367; ENSP00000355013; ENSG00000198730.
    GeneIDi9646.
    KEGGihsa:9646.
    UCSCiuc001mja.3. human.

    Polymorphism databases

    DMDMi74758318.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D63875 mRNA. Translation: BAA09925.2 . Different initiation.
    CH471064 Genomic DNA. Translation: EAW68557.1 .
    CH471064 Genomic DNA. Translation: EAW68558.1 .
    BC058914 mRNA. Translation: AAH58914.1 .
    CCDSi CCDS7805.1.
    RefSeqi NP_055448.1. NM_014633.3.
    UniGenei Hs.725151.

    3D structure databases

    ProteinModelPortali Q6PD62.
    SMRi Q6PD62. Positions 265-749.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115004. 27 interactions.
    DIPi DIP-31693N.
    IntActi Q6PD62. 29 interactions.
    MINTi MINT-1182366.
    STRINGi 9606.ENSP00000355013.

    PTM databases

    PhosphoSitei Q6PD62.

    Polymorphism databases

    DMDMi 74758318.

    Proteomic databases

    MaxQBi Q6PD62.
    PaxDbi Q6PD62.
    PRIDEi Q6PD62.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361367 ; ENSP00000355013 ; ENSG00000198730 .
    GeneIDi 9646.
    KEGGi hsa:9646.
    UCSCi uc001mja.3. human.

    Organism-specific databases

    CTDi 9646.
    GeneCardsi GC11P010772.
    HGNCi HGNC:16850. CTR9.
    MIMi 609366. gene.
    neXtProti NX_Q6PD62.
    PharmGKBi PA134896774.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0457.
    HOGENOMi HOG000246926.
    HOVERGENi HBG081372.
    InParanoidi Q6PD62.
    KOi K15176.
    OMAi TQNDTYS.
    OrthoDBi EOG79KPDH.
    PhylomeDBi Q6PD62.
    TreeFami TF314342.

    Miscellaneous databases

    ChiTaRSi CTR9. human.
    GeneWikii CTR9.
    GenomeRNAii 9646.
    NextBioi 36207.
    PMAP-CutDB Q6PD62.
    PROi Q6PD62.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6PD62.
    Bgeei Q6PD62.
    CleanExi HS_CTR9.
    Genevestigatori Q6PD62.

    Family and domain databases

    Gene3Di 1.25.40.10. 5 hits.
    InterProi IPR013026. TPR-contain_dom.
    IPR011990. TPR-like_helical.
    IPR001440. TPR_1.
    IPR013105. TPR_2.
    IPR019734. TPR_repeat.
    [Graphical view ]
    Pfami PF00515. TPR_1. 7 hits.
    PF07719. TPR_2. 1 hit.
    [Graphical view ]
    SMARTi SM00028. TPR. 9 hits.
    [Graphical view ]
    PROSITEi PS50005. TPR. 10 hits.
    PS50293. TPR_REGION. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
      DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY.
      Tissue: Bone marrow.
    2. Ohara O., Nagase T., Kikuno R., Nomura N.
      Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Uterus.
    5. "The human PAF complex coordinates transcription with events downstream of RNA synthesis."
      Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H., Batra S.K., Tempst P., Reinberg D.
      Genes Dev. 19:1668-1673(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE PAF1 COMPLEX.
    6. "Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation."
      Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D.
      Mol. Cell 20:601-611(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943 AND SER-970, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-941; SER-943; SER-1020 AND SER-1021, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-970, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: FUNCTION.
    14. "DSIF, the Paf1 complex, and Tat-SF1 have nonredundant, cooperative roles in RNA polymerase II elongation."
      Chen Y., Yamaguchi Y., Tsugeno Y., Yamamoto J., Yamada T., Nakamura M., Hisatake K., Handa H.
      Genes Dev. 23:2765-2777(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX.
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925 AND SER-932, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "The PAF complex synergizes with MLL fusion proteins at HOX loci to promote leukemogenesis."
      Muntean A.G., Tan J., Sitwala K., Huang Y., Bronstein J., Connelly J.A., Basrur V., Elenitoba-Johnson K.S., Hess J.L.
      Cancer Cell 17:609-621(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE PAF1 COMPLEX, INTERACTION WITH KMT2A.
    17. "The human PAF1 complex acts in chromatin transcription elongation both independently and cooperatively with SII/TFIIS."
      Kim J., Guermah M., Roeder R.G.
      Cell 140:491-503(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PAF1 COMPLEX, COMPOSITION OF THE PAF1 COMPLEX, FUNCTION OF THE PAF1 COMPLEX.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943 AND SER-970, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Transcriptional activators enhance polyadenylation of mRNA precursors."
      Nagaike T., Logan C., Hotta I., Rozenblatt-Rosen O., Meyerson M., Manley J.L.
      Mol. Cell 41:409-418(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, FUNCTION OF THE PAF1 COMPLEX.
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-925; SER-941; SER-943; SER-970; SER-1020; SER-1021; SER-1097 AND SER-1102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCTR9_HUMAN
    AccessioniPrimary (citable) accession number: Q6PD62
    Secondary accession number(s): D3DQV8, Q15015
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 4, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 105 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3