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O14776 (TCRG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription elongation regulator 1
Alternative name(s):
TATA box-binding protein-associated factor 2S
Transcription factor CA150
Gene names
Name:TCERG1
Synonyms:CA150, TAF2S
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1098 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.5

Subunit structure

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. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7

Subcellular location

Nucleus Ref.1 Ref.4 Ref.7.

Tissue specificity

Detected in brain neurons. Ref.6

Induction

Up-regulated in brain tissue from patients with Huntington disease. Ref.6

Domain

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 similarities

Contains 6 FF domains.

Contains 3 WW domains.

Sequence caution

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

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14776-1)

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.
Isoform 2 (identifier: O14776-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10981098Transcription elongation regulator 1
PRO_0000076063

Regions

Domain131 – 16434WW 1
Domain429 – 46234WW 2
Domain528 – 56134WW 3
Domain659 – 71254FF 1
Domain725 – 77955FF 2
Domain791 – 84656FF 3
Domain896 – 95257FF 4
Domain954 – 101057FF 5
Domain1012 – 107766FF 6
Coiled coil184 – 24461 Potential
Coiled coil606 – 65550 Potential
Coiled coil844 – 90663 Potential
Motif626 – 6305Nuclear localization signal Potential
Compositional bias32 – 132101Pro-rich
Compositional bias169 – 25890Ala/Gln-rich
Compositional bias260 – 33172Thr-rich
Compositional bias328 – 37851Pro-rich
Compositional bias454 – 51562Glu-rich
Compositional bias1083 – 10875Poly-Pro

Natural variations

Alternative sequence379 – 39921Missing in isoform 2.
VSP_026933

Experimental info

Mutagenesis148 – 1503YYY → AAA: Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 446-AAA-448.
Mutagenesis446 – 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. Ref.5
Mutagenesis545 – 5473FFY → AAA: No effect. Ref.5
Sequence conflict3241P → R in AAB80727. Ref.1

Secondary structure

................................................................................ 1098
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 24, 2007. Version 2.
Checksum: 5F0A0C3A07EBF00F

FASTA1,098123,901
        10         20         30         40         50         60 
MAERGGDGGE SERFNPGELR MAQQQALRFR GPAPPPNAVM RGPPPLMRPP PPFGMMRGPP 

        70         80         90        100        110        120 
PPPRPPFGRP PFDPNMPPMP PPGGIPPPMG PPHLQRPPFM PPPMSSMPPP PGMMFPPGMP 

       130        140        150        160        170        180 
PVTAPGTPAL PPTEEIWVEN KTPDGKVYYY NARTRESAWT KPDGVKVIQQ SELTPMLAAQ 

       190        200        210        220        230        240 
AQVQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ AQAQAQAQAQ 

       250        260        270        280        290        300 
AQVQAQVQAQ VQAQAVGAST PTTSSPAPAV STSTSSSTPS STTSTTTTAT SVAQTVSTPT 

       310        320        330        340        350        360 
TQDQTPSSAV SVATPTVSVS TPAPTATPVQ TVPQPHPQTL PPAVPHSVPQ PTTAIPAFPP 

       370        380        390        400        410        420 
VMVPPFRVPL PGMPIPLPGV AMMQIVSCPY VKTVATTKTG VLPGMAPPIV PMIHPQVAIA 

       430        440        450        460        470        480 
ASPATLAGAT AVSEWTEYKT ADGKTYYYNN RTLESTWEKP QELKEKEKLE EKIKEPIKEP 

       490        500        510        520        530        540 
SEEPLPMETE EEDPKEEPIK EIKEEPKEEE MTEEEKAAQK AKPVATAPIP GTPWCVVWTG 

       550        560        570        580        590        600 
DERVFFYNPT TRLSMWDRPD DLIGRADVDK IIQEPPHKKG MEELKKLRHP TPTMLSIQKW 

       610        620        630        640        650        660 
QFSMSAIKEE QELMEEINED EPVKAKKRKR DDNKDIDSEK EAAMEAEIKA ARERAIVPLE 

       670        680        690        700        710        720 
ARMKQFKDML LERGVSAFST WEKELHKIVF DPRYLLLNPK ERKQVFDQYV KTRAEEERRE 

       730        740        750        760        770        780 
KKNKIMQAKE DFKKMMEEAK FNPRATFSEF AAKHAKDSRF KAIEKMKDRE ALFNEFVAAA 

       790        800        810        820        830        840 
RKKEKEDSKT RGEKIKSDFF ELLSNHHLDS QSRWSKVKDK VESDPRYKAV DSSSMREDLF 

       850        860        870        880        890        900 
KQYIEKIAKN LDSEKEKELE RQARIEASLR EREREVQKAR SEQTKEIDRE REQHKREEAI 

       910        920        930        940        950        960 
QNFKALLSDM VRSSDVSWSD TRRTLRKDHR WESGSLLERE EKEKLFNEHI EALTKKKREH 

       970        980        990       1000       1010       1020 
FRQLLDETSA ITLTSTWKEV KKIIKEDPRC IKFSSSDRKK QREFEEYIRD KYITAKADFR 

      1030       1040       1050       1060       1070       1080 
TLLKETKFIT YRSKKLIQES DQHLKDVEKI LQNDKRYLVL DCVPEERRKL IVAYVDDLDR 

      1090 
RGPPPPPTAS EPTRRSTK 

« Hide

Isoform 2 [UniParc].

Checksum: D02B6E70E31F1551
Show »

FASTA1,077121,690

References

« Hide 'large scale' references
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"General structural motifs of amyloid protofilaments."
Ferguson N., Becker J., Tidow H., Tremmel S., Sharpe T.D., Krause G., Flinders J., Petrovich M., Berriman J., Oschkinat H., Fersht A.R.
Proc. Natl. Acad. Sci. U.S.A. 103:16248-16253(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF017789 mRNA. Translation: AAB80727.1.
AB209910 mRNA. Translation: BAD93147.1. Different initiation.
BC111727 mRNA. Translation: AAI11728.1.
PIRT08599.
RefSeqNP_001035095.1. NM_001040006.1.
NP_006697.2. NM_006706.3.
UniGeneHs.443465.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalO14776.
SMRO14776. Positions 126-165, 428-464, 517-579, 650-853, 895-1080.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116120. 70 interactions.
IntActO14776. 14 interactions.
MINTMINT-158391.
STRING9606.ENSP00000296702.

PTM databases

PhosphoSiteO14776.

Proteomic databases

PaxDbO14776.
PRIDEO14776.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296702; ENSP00000296702; ENSG00000113649. [O14776-1]
ENST00000394421; ENSP00000377943; ENSG00000113649. [O14776-2]
GeneID10915.
KEGGhsa:10915.
UCSCuc003lob.3. human. [O14776-1]
uc003loc.3. human. [O14776-2]

Organism-specific databases

CTD10915.
GeneCardsGC05P145807.
HGNCHGNC:15630. TCERG1.
MIM605409. gene.
neXtProtNX_O14776.
PharmGKBPA38007.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5104.
HOGENOMHOG000008544.
HOVERGENHBG062908.
InParanoidO14776.
KOK12824.
OMAQREFEDY.
OrthoDBEOG7DC24V.
PhylomeDBO14776.
TreeFamTF317748.

Enzyme and pathway databases

SignaLinkO14776.

Gene expression databases

ArrayExpressO14776.
BgeeO14776.
CleanExHS_TCERG1.
GenevestigatorO14776.

Family and domain databases

Gene3D1.10.10.440. 5 hits.
InterProIPR002713. FF_domain.
IPR001202. WW_dom.
[Graphical view]
PfamPF01846. FF. 6 hits.
PF00397. WW. 2 hits.
[Graphical view]
SMARTSM00441. FF. 6 hits.
SM00456. WW. 3 hits.
[Graphical view]
SUPFAMSSF51045. SSF51045. 3 hits.
SSF81698. SSF81698. 5 hits.
PROSITEPS51676. FF. 6 hits.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO14776.
GeneWikiTranscription_elongation_regulator_1.
GenomeRNAi10915.
NextBio41457.
PROO14776.
SOURCESearch...

Entry information

Entry nameTCRG1_HUMAN
AccessionPrimary (citable) accession number: O14776
Secondary accession number(s): Q2NKN2, Q59EA1
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: July 24, 2007
Last modified: April 16, 2014
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM