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O14776

- TCRG1_HUMAN

UniProt

O14776 - TCRG1_HUMAN

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Protein

Transcription elongation regulator 1

Gene

TCERG1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  3. RNA polymerase II transcription corepressor activity Source: BHF-UCL
  4. 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiO14776.
CleanExiHS_TCERG1.
ExpressionAtlasiO14776. baseline and differential.
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. 76 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 – 43810Combined sources
Beta strandi441 – 4433Combined sources
Beta strandi446 – 45510Combined sources
Beta strandi523 – 5286Combined sources
Beta strandi530 – 5334Combined sources
Beta strandi535 – 5428Combined sources
Beta strandi544 – 5485Combined sources
Turni549 – 5524Combined sources
Turni560 – 5645Combined sources
Helixi567 – 5737Combined sources
Turni576 – 5783Combined sources
Beta strandi652 – 6565Combined sources
Helixi661 – 67212Combined sources
Beta strandi677 – 6793Combined sources
Helixi681 – 6844Combined sources
Helixi685 – 6873Combined sources
Turni688 – 6903Combined sources
Helixi692 – 6965Combined sources
Helixi699 – 73234Combined sources
Turni733 – 7353Combined sources
Helixi747 – 7537Combined sources
Turni759 – 7624Combined sources
Turni765 – 7728Combined sources
Helixi773 – 7808Combined sources
Turni782 – 7865Combined sources
Helixi787 – 7904Combined sources
Helixi792 – 80413Combined sources
Helixi814 – 8218Combined sources
Beta strandi822 – 8243Combined sources
Helixi825 – 8284Combined sources
Helixi833 – 84412Combined sources
Beta strandi888 – 8903Combined sources
Helixi895 – 91016Combined sources
Helixi918 – 9258Combined sources
Helixi929 – 9346Combined sources
Helixi939 – 96628Combined sources
Helixi977 – 9848Combined sources
Helixi988 – 9914Combined sources
Helixi997 – 102529Combined sources
Helixi1033 – 10397Combined sources
Helixi1042 – 105110Combined sources
Helixi1055 – 10584Combined sources
Turni1059 – 10624Combined sources
Helixi1064 – 107613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00740000115182.
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

        10         20         30         40         50
MAERGGDGGE SERFNPGELR MAQQQALRFR GPAPPPNAVM RGPPPLMRPP
60 70 80 90 100
PPFGMMRGPP PPPRPPFGRP PFDPNMPPMP PPGGIPPPMG PPHLQRPPFM
110 120 130 140 150
PPPMSSMPPP PGMMFPPGMP PVTAPGTPAL PPTEEIWVEN KTPDGKVYYY
160 170 180 190 200
NARTRESAWT KPDGVKVIQQ SELTPMLAAQ AQVQAQAQAQ AQAQAQAQAQ
210 220 230 240 250
AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQVQAQVQAQ
260 270 280 290 300
VQAQAVGAST PTTSSPAPAV STSTSSSTPS STTSTTTTAT SVAQTVSTPT
310 320 330 340 350
TQDQTPSSAV SVATPTVSVS TPAPTATPVQ TVPQPHPQTL PPAVPHSVPQ
360 370 380 390 400
PTTAIPAFPP VMVPPFRVPL PGMPIPLPGV AMMQIVSCPY VKTVATTKTG
410 420 430 440 450
VLPGMAPPIV PMIHPQVAIA ASPATLAGAT AVSEWTEYKT ADGKTYYYNN
460 470 480 490 500
RTLESTWEKP QELKEKEKLE EKIKEPIKEP SEEPLPMETE EEDPKEEPIK
510 520 530 540 550
EIKEEPKEEE MTEEEKAAQK AKPVATAPIP GTPWCVVWTG DERVFFYNPT
560 570 580 590 600
TRLSMWDRPD DLIGRADVDK IIQEPPHKKG MEELKKLRHP TPTMLSIQKW
610 620 630 640 650
QFSMSAIKEE QELMEEINED EPVKAKKRKR DDNKDIDSEK EAAMEAEIKA
660 670 680 690 700
ARERAIVPLE ARMKQFKDML LERGVSAFST WEKELHKIVF DPRYLLLNPK
710 720 730 740 750
ERKQVFDQYV KTRAEEERRE KKNKIMQAKE DFKKMMEEAK FNPRATFSEF
760 770 780 790 800
AAKHAKDSRF KAIEKMKDRE ALFNEFVAAA RKKEKEDSKT RGEKIKSDFF
810 820 830 840 850
ELLSNHHLDS QSRWSKVKDK VESDPRYKAV DSSSMREDLF KQYIEKIAKN
860 870 880 890 900
LDSEKEKELE RQARIEASLR EREREVQKAR SEQTKEIDRE REQHKREEAI
910 920 930 940 950
QNFKALLSDM VRSSDVSWSD TRRTLRKDHR WESGSLLERE EKEKLFNEHI
960 970 980 990 1000
EALTKKKREH FRQLLDETSA ITLTSTWKEV KKIIKEDPRC IKFSSSDRKK
1010 1020 1030 1040 1050
QREFEEYIRD KYITAKADFR TLLKETKFIT YRSKKLIQES DQHLKDVEKI
1060 1070 1080 1090
LQNDKRYLVL DCVPEERRKL IVAYVDDLDR RGPPPPPTAS EPTRRSTK
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 76 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.
GeneTreei ENSGT00740000115182.
HOGENOMi HOG000008544.
HOVERGENi HBG062908.
InParanoidi O14776.
KOi K12824.
OMAi PAEEIWV.
OrthoDBi EOG7DC24V.
PhylomeDBi O14776.
TreeFami TF317748.

Enzyme and pathway databases

SignaLinki O14776.

Miscellaneous databases

ChiTaRSi TCERG1. human.
EvolutionaryTracei O14776.
GeneWikii Transcription_elongation_regulator_1.
GenomeRNAii 10915.
NextBioi 41457.
PROi O14776.
SOURCEi Search...

Gene expression databases

Bgeei O14776.
CleanExi HS_TCERG1.
ExpressionAtlasi O14776. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 132 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