SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O14776

- TCRG1_HUMAN

UniProt

O14776 - TCRG1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Transcription elongation regulator 1
Gene
TCERG1, CA150, TAF2S
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. RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  2. RNA polymerase II transcription corepressor activity Source: BHF-UCL
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: IntAct
  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
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.
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 1
PRO_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 SF1.5 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

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.

Miscellaneous databases

EvolutionaryTraceiO14776.

Family & Domainsi

Domains and Repeats

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili184 – 24461 Reviewed prediction
Add
BLAST
Coiled coili606 – 65550 Reviewed prediction
Add
BLAST
Coiled coili844 – 90663 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi626 – 6305Nuclear localization signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi32 – 132101Pro-rich
Add
BLAST
Compositional biasi169 – 25890Ala/Gln-rich
Add
BLAST
Compositional biasi260 – 33172Thr-rich
Add
BLAST
Compositional biasi328 – 37851Pro-rich
Add
BLAST
Compositional biasi454 – 51562Glu-rich
Add
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.
Contains 3 WW domains.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei379 – 39921Missing in isoform 2.
VSP_026933Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti324 – 3241P → R in AAB80727. 1 Publication

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

« 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: July 9, 2014
This is version 129 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

Similar proteinsi