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O14776

- TCRG1_HUMAN

UniProt

O14776 - TCRG1_HUMAN

Protein

Transcription elongation regulator 1

Gene

TCERG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (24 Jul 2007)
      Previous versions | rss
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    Functioni

    Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner. Necessary for TAT-dependent activation of the human immunodeficiency virus type 1 (HIV-1) promoter.2 Publications

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
    4. RNA polymerase II transcription corepressor activity Source: BHF-UCL
    5. transcription coactivator activity Source: ProtInc

    GO - Biological processi

    1. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    2. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    SignaLinkiO14776.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription elongation regulator 1
    Alternative name(s):
    TATA box-binding protein-associated factor 2S
    Transcription factor CA150
    Gene namesi
    Name:TCERG1
    Synonyms:CA150, TAF2S
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:15630. TCERG1.

    Subcellular locationi

    Nucleus 3 Publications

    GO - Cellular componenti

    1. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi148 – 1503YYY → AAA: Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 446-AAA-448. 1 Publication
    Mutagenesisi446 – 4483YYY → AAA: Loss of interaction with SF1. Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 148-AAA-150. 1 Publication
    Mutagenesisi545 – 5473FFY → AAA: No effect. 1 Publication

    Organism-specific databases

    PharmGKBiPA38007.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10981098Transcription elongation regulator 1PRO_0000076063Add
    BLAST

    Proteomic databases

    MaxQBiO14776.
    PaxDbiO14776.
    PRIDEiO14776.

    PTM databases

    PhosphoSiteiO14776.

    Expressioni

    Tissue specificityi

    Detected in brain neurons.1 Publication

    Inductioni

    Up-regulated in brain tissue from patients with Huntington disease.1 Publication

    Gene expression databases

    ArrayExpressiO14776.
    BgeeiO14776.
    CleanExiHS_TCERG1.
    GenevestigatoriO14776.

    Interactioni

    Subunit structurei

    Binds formin By similarity. Interacts (via the second WW domain) with TREX1 (via proline-rich region) By similarity. Binds RNA polymerase II, HD and SF1.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BARD1Q997282EBI-473271,EBI-473181
    HTTP428589EBI-473271,EBI-466029

    Protein-protein interaction databases

    BioGridi116120. 74 interactions.
    IntActiO14776. 14 interactions.
    MINTiMINT-158391.
    STRINGi9606.ENSP00000296702.

    Structurei

    Secondary structure

    1
    1098
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi429 – 43810
    Beta strandi441 – 4433
    Beta strandi446 – 45510
    Beta strandi523 – 5286
    Beta strandi530 – 5334
    Beta strandi535 – 5428
    Beta strandi544 – 5485
    Turni549 – 5524
    Turni560 – 5645
    Helixi567 – 5737
    Turni576 – 5783
    Beta strandi652 – 6565
    Helixi661 – 67212
    Beta strandi677 – 6793
    Helixi681 – 6844
    Helixi685 – 6873
    Turni688 – 6903
    Helixi692 – 6965
    Helixi699 – 73234
    Turni733 – 7353
    Helixi747 – 7537
    Turni759 – 7624
    Turni765 – 7728
    Helixi773 – 7808
    Turni782 – 7865
    Helixi787 – 7904
    Helixi792 – 80413
    Helixi814 – 8218
    Beta strandi822 – 8243
    Helixi825 – 8284
    Helixi833 – 84412
    Beta strandi888 – 8903
    Helixi895 – 91016
    Helixi918 – 9258
    Helixi929 – 9346
    Helixi939 – 96628
    Helixi977 – 9848
    Helixi988 – 9914
    Helixi997 – 102529
    Helixi1033 – 10397
    Helixi1042 – 105110
    Helixi1055 – 10584
    Turni1059 – 10624
    Helixi1064 – 107613

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DK7NMR-A520-579[»]
    2DODNMR-A651-719[»]
    2DOENMR-A784-853[»]
    2DOFNMR-A888-959[»]
    2E71NMR-A717-786[»]
    2KIQNMR-A724-782[»]
    2KISNMR-A659-724[»]
    2NNTNMR-A/B/C/D428-464[»]
    3HFHX-ray2.70A/B661-845[»]
    4FQGX-ray2.00A/B895-1081[»]
    ProteinModelPortaliO14776.
    SMRiO14776. Positions 126-165, 428-464, 517-579, 650-853, 895-1080.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14776.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini131 – 16434WW 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini429 – 46234WW 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini528 – 56134WW 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini659 – 71254FF 1Add
    BLAST
    Domaini725 – 77955FF 2Add
    BLAST
    Domaini791 – 84656FF 3Add
    BLAST
    Domaini896 – 95257FF 4Add
    BLAST
    Domaini954 – 101057FF 5Add
    BLAST
    Domaini1012 – 107766FF 6Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili184 – 24461Sequence AnalysisAdd
    BLAST
    Coiled coili606 – 65550Sequence AnalysisAdd
    BLAST
    Coiled coili844 – 90663Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi626 – 6305Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi32 – 132101Pro-richAdd
    BLAST
    Compositional biasi169 – 25890Ala/Gln-richAdd
    BLAST
    Compositional biasi260 – 33172Thr-richAdd
    BLAST
    Compositional biasi328 – 37851Pro-richAdd
    BLAST
    Compositional biasi454 – 51562Glu-richAdd
    BLAST
    Compositional biasi1083 – 10875Poly-Pro

    Domaini

    The FF domains bind the phosphorylated C-terminus of the largest subunit of RNA polymerase II, probably mediate interaction with HTATSF1 and preferentially bind peptides with the consensus sequence [DE](2-5)-[FWY]-[DE]2-5.
    The WW domains bind Pro-rich domains.

    Sequence similaritiesi

    Contains 6 FF domains.Curated
    Contains 3 WW domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiCOG5104.
    HOGENOMiHOG000008544.
    HOVERGENiHBG062908.
    InParanoidiO14776.
    KOiK12824.
    OMAiPAEEIWV.
    OrthoDBiEOG7DC24V.
    PhylomeDBiO14776.
    TreeFamiTF317748.

    Family and domain databases

    Gene3Di1.10.10.440. 5 hits.
    InterProiIPR002713. FF_domain.
    IPR001202. WW_dom.
    [Graphical view]
    PfamiPF01846. FF. 6 hits.
    PF00397. WW. 2 hits.
    [Graphical view]
    SMARTiSM00441. FF. 6 hits.
    SM00456. WW. 3 hits.
    [Graphical view]
    SUPFAMiSSF51045. SSF51045. 3 hits.
    SSF81698. SSF81698. 5 hits.
    PROSITEiPS51676. FF. 6 hits.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 3 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14776-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAERGGDGGE SERFNPGELR MAQQQALRFR GPAPPPNAVM RGPPPLMRPP     50
    PPFGMMRGPP PPPRPPFGRP PFDPNMPPMP PPGGIPPPMG PPHLQRPPFM 100
    PPPMSSMPPP PGMMFPPGMP PVTAPGTPAL PPTEEIWVEN KTPDGKVYYY 150
    NARTRESAWT KPDGVKVIQQ SELTPMLAAQ AQVQAQAQAQ AQAQAQAQAQ 200
    AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQVQAQVQAQ 250
    VQAQAVGAST PTTSSPAPAV STSTSSSTPS STTSTTTTAT SVAQTVSTPT 300
    TQDQTPSSAV SVATPTVSVS TPAPTATPVQ TVPQPHPQTL PPAVPHSVPQ 350
    PTTAIPAFPP VMVPPFRVPL PGMPIPLPGV AMMQIVSCPY VKTVATTKTG 400
    VLPGMAPPIV PMIHPQVAIA ASPATLAGAT AVSEWTEYKT ADGKTYYYNN 450
    RTLESTWEKP QELKEKEKLE EKIKEPIKEP SEEPLPMETE EEDPKEEPIK 500
    EIKEEPKEEE MTEEEKAAQK AKPVATAPIP GTPWCVVWTG DERVFFYNPT 550
    TRLSMWDRPD DLIGRADVDK IIQEPPHKKG MEELKKLRHP TPTMLSIQKW 600
    QFSMSAIKEE QELMEEINED EPVKAKKRKR DDNKDIDSEK EAAMEAEIKA 650
    ARERAIVPLE ARMKQFKDML LERGVSAFST WEKELHKIVF DPRYLLLNPK 700
    ERKQVFDQYV KTRAEEERRE KKNKIMQAKE DFKKMMEEAK FNPRATFSEF 750
    AAKHAKDSRF KAIEKMKDRE ALFNEFVAAA RKKEKEDSKT RGEKIKSDFF 800
    ELLSNHHLDS QSRWSKVKDK VESDPRYKAV DSSSMREDLF KQYIEKIAKN 850
    LDSEKEKELE RQARIEASLR EREREVQKAR SEQTKEIDRE REQHKREEAI 900
    QNFKALLSDM VRSSDVSWSD TRRTLRKDHR WESGSLLERE EKEKLFNEHI 950
    EALTKKKREH FRQLLDETSA ITLTSTWKEV KKIIKEDPRC IKFSSSDRKK 1000
    QREFEEYIRD KYITAKADFR TLLKETKFIT YRSKKLIQES DQHLKDVEKI 1050
    LQNDKRYLVL DCVPEERRKL IVAYVDDLDR RGPPPPPTAS EPTRRSTK 1098
    Length:1,098
    Mass (Da):123,901
    Last modified:July 24, 2007 - v2
    Checksum:i5F0A0C3A07EBF00F
    GO
    Isoform 2 (identifier: O14776-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         379-399: Missing.

    Show »
    Length:1,077
    Mass (Da):121,690
    Checksum:iD02B6E70E31F1551
    GO

    Sequence cautioni

    The sequence BAD93147.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti324 – 3241P → R in AAB80727. (PubMed:9315662)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei379 – 39921Missing in isoform 2. 2 PublicationsVSP_026933Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF017789 mRNA. Translation: AAB80727.1.
    AB209910 mRNA. Translation: BAD93147.1. Different initiation.
    BC111727 mRNA. Translation: AAI11728.1.
    CCDSiCCDS4282.1. [O14776-1]
    CCDS43379.1. [O14776-2]
    PIRiT08599.
    RefSeqiNP_001035095.1. NM_001040006.1. [O14776-2]
    NP_006697.2. NM_006706.3. [O14776-1]
    UniGeneiHs.443465.

    Genome annotation databases

    EnsembliENST00000296702; ENSP00000296702; ENSG00000113649. [O14776-1]
    ENST00000394421; ENSP00000377943; ENSG00000113649. [O14776-2]
    GeneIDi10915.
    KEGGihsa:10915.
    UCSCiuc003lob.3. human. [O14776-1]
    uc003loc.3. human. [O14776-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF017789 mRNA. Translation: AAB80727.1 .
    AB209910 mRNA. Translation: BAD93147.1 . Different initiation.
    BC111727 mRNA. Translation: AAI11728.1 .
    CCDSi CCDS4282.1. [O14776-1 ]
    CCDS43379.1. [O14776-2 ]
    PIRi T08599.
    RefSeqi NP_001035095.1. NM_001040006.1. [O14776-2 ]
    NP_006697.2. NM_006706.3. [O14776-1 ]
    UniGenei Hs.443465.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DK7 NMR - A 520-579 [» ]
    2DOD NMR - A 651-719 [» ]
    2DOE NMR - A 784-853 [» ]
    2DOF NMR - A 888-959 [» ]
    2E71 NMR - A 717-786 [» ]
    2KIQ NMR - A 724-782 [» ]
    2KIS NMR - A 659-724 [» ]
    2NNT NMR - A/B/C/D 428-464 [» ]
    3HFH X-ray 2.70 A/B 661-845 [» ]
    4FQG X-ray 2.00 A/B 895-1081 [» ]
    ProteinModelPortali O14776.
    SMRi O14776. Positions 126-165, 428-464, 517-579, 650-853, 895-1080.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116120. 74 interactions.
    IntActi O14776. 14 interactions.
    MINTi MINT-158391.
    STRINGi 9606.ENSP00000296702.

    PTM databases

    PhosphoSitei O14776.

    Proteomic databases

    MaxQBi O14776.
    PaxDbi O14776.
    PRIDEi O14776.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296702 ; ENSP00000296702 ; ENSG00000113649 . [O14776-1 ]
    ENST00000394421 ; ENSP00000377943 ; ENSG00000113649 . [O14776-2 ]
    GeneIDi 10915.
    KEGGi hsa:10915.
    UCSCi uc003lob.3. human. [O14776-1 ]
    uc003loc.3. human. [O14776-2 ]

    Organism-specific databases

    CTDi 10915.
    GeneCardsi GC05P145807.
    HGNCi HGNC:15630. TCERG1.
    MIMi 605409. gene.
    neXtProti NX_O14776.
    PharmGKBi PA38007.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5104.
    HOGENOMi HOG000008544.
    HOVERGENi HBG062908.
    InParanoidi O14776.
    KOi K12824.
    OMAi PAEEIWV.
    OrthoDBi EOG7DC24V.
    PhylomeDBi O14776.
    TreeFami TF317748.

    Enzyme and pathway databases

    SignaLinki O14776.

    Miscellaneous databases

    EvolutionaryTracei O14776.
    GeneWikii Transcription_elongation_regulator_1.
    GenomeRNAii 10915.
    NextBioi 41457.
    PROi O14776.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14776.
    Bgeei O14776.
    CleanExi HS_TCERG1.
    Genevestigatori O14776.

    Family and domain databases

    Gene3Di 1.10.10.440. 5 hits.
    InterProi IPR002713. FF_domain.
    IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF01846. FF. 6 hits.
    PF00397. WW. 2 hits.
    [Graphical view ]
    SMARTi SM00441. FF. 6 hits.
    SM00456. WW. 3 hits.
    [Graphical view ]
    SUPFAMi SSF51045. SSF51045. 3 hits.
    SSF81698. SSF81698. 5 hits.
    PROSITEi PS51676. FF. 6 hits.
    PS01159. WW_DOMAIN_1. 1 hit.
    PS50020. WW_DOMAIN_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription."
      Sune C., Hayashi T., Liu Y., Lane W.S., Young R.A., Garcia-Blanco M.A.
      Mol. Cell. Biol. 17:6029-6039(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 610-620; 745-753; 928-939 AND 945-955, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNA POLYMERASE II.
      Tissue: Cervix carcinoma.
    2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Aortic endothelium.
    3. "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] (ISOFORM 2).
    4. "Protein-interaction modules that organize nuclear function: FF domains of CA150 bind the phosphoCTD of RNA polymerase II."
      Carty S.M., Goldstrohm A.C., Sune C., Garcia-Blanco M.A., Greenleaf A.L.
      Proc. Natl. Acad. Sci. U.S.A. 97:9015-9020(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RNA POLYMERASE II.
    5. "The transcription elongation factor CA150 interacts with RNA polymerase II and the pre-mRNA splicing factor SF1."
      Goldstrohm A.C., Albrecht T.R., Sune C., Bedford M.T., Garcia-Blanco M.A.
      Mol. Cell. Biol. 21:7617-7628(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 148-TYR--TYR-150; 446-TYR--TYR-448 AND 545-PHE--TYR-547, INTERACTION WITH RNA POLYMERASE II AND SF1.
    6. "The Gln-Ala repeat transcriptional activator CA150 interacts with huntingtin: neuropathologic and genetic evidence for a role in Huntington's disease pathogenesis."
      Holbert S., Denghien I., Kiechle T., Rosenblatt A., Wellington C., Hayden M.R., Margolis R.L., Ross C.A., Dausset J., Ferrante R.J., Neri C.
      Proc. Natl. Acad. Sci. U.S.A. 98:1811-1816(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HD, INDUCTION, TISSUE SPECIFICITY.
    7. "FF domains of CA150 bind transcription and splicing factors through multiple weak interactions."
      Smith M.J., Kulkarni S., Pawson T.
      Mol. Cell. Biol. 24:9274-9285(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HTATSF1, SUBCELLULAR LOCATION.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: STRUCTURE BY NMR OF 428-464.
    10. "Solution structure of WW domain and FF domains in transcription elongation regulator 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 520-959.

    Entry informationi

    Entry nameiTCRG1_HUMAN
    AccessioniPrimary (citable) accession number: O14776
    Secondary accession number(s): Q2NKN2, Q59EA1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 27, 2004
    Last sequence update: July 24, 2007
    Last modified: October 1, 2014
    This is version 130 of the entry and version 2 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3