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Protein

Transcription elongation regulator 1

Gene

TCERG1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • poly(A) RNA binding Source: UniProtKB
  • RNA polymerase II repressing transcription factor binding Source: BHF-UCL
  • RNA polymerase II transcription corepressor activity Source: BHF-UCL
  • transcription coactivator activity Source: ProtInc

GO - Biological processi

  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • 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

BioCyciZFISH:ENSG00000113649-MONOMER.
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
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:15630. TCERG1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi148 – 150YYY → AAA: Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 446-AAA-448. 1 Publication3
Mutagenesisi446 – 448YYY → 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 Publication3
Mutagenesisi545 – 547FFY → AAA: No effect. 1 Publication3

Organism-specific databases

DisGeNETi10915.
OpenTargetsiENSG00000113649.
PharmGKBiPA38007.

Polymorphism and mutation databases

BioMutaiTCERG1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000760631 – 1098Transcription elongation regulator 1Add BLAST1098

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei11PhosphoserineCombined sources1
Modified residuei20Omega-N-methylarginineCombined sources1
Modified residuei28Asymmetric dimethylarginineCombined sources1
Modified residuei30Asymmetric dimethylarginineCombined sources1
Modified residuei41Asymmetric dimethylarginineCombined sources1
Modified residuei48Asymmetric dimethylarginineCombined sources1
Cross-linki503Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei638PhosphoserineCombined sources1
Modified residuei834PhosphoserineCombined sources1
Modified residuei933PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO14776.
MaxQBiO14776.
PaxDbiO14776.
PeptideAtlasiO14776.
PRIDEiO14776.

PTM databases

iPTMnetiO14776.
PhosphoSitePlusiO14776.
SwissPalmiO14776.

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

BgeeiENSG00000113649.
CleanExiHS_TCERG1.
ExpressionAtlasiO14776. baseline and differential.
GenevisibleiO14776. HS.

Organism-specific databases

HPAiHPA064854.

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

GO - Molecular functioni

  • RNA polymerase II repressing transcription factor binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi116120. 84 interactors.
DIPiDIP-32504N.
IntActiO14776. 17 interactors.
MINTiMINT-158391.
STRINGi9606.ENSP00000296702.

Structurei

Secondary structure

11098
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi103 – 105Combined sources3
Beta strandi435 – 440Combined sources6
Turni441 – 443Combined sources3
Beta strandi444 – 449Combined sources6
Turni450 – 453Combined sources4
Beta strandi454 – 458Combined sources5
Turni461 – 463Combined sources3
Beta strandi523 – 528Combined sources6
Beta strandi530 – 533Combined sources4
Beta strandi535 – 542Combined sources8
Beta strandi544 – 548Combined sources5
Turni549 – 552Combined sources4
Turni560 – 564Combined sources5
Helixi567 – 573Combined sources7
Turni576 – 578Combined sources3
Beta strandi652 – 656Combined sources5
Helixi661 – 672Combined sources12
Beta strandi677 – 679Combined sources3
Helixi681 – 684Combined sources4
Helixi685 – 687Combined sources3
Turni688 – 690Combined sources3
Helixi692 – 696Combined sources5
Helixi699 – 732Combined sources34
Turni733 – 735Combined sources3
Helixi747 – 753Combined sources7
Turni759 – 762Combined sources4
Turni765 – 772Combined sources8
Helixi773 – 780Combined sources8
Turni782 – 786Combined sources5
Helixi787 – 790Combined sources4
Helixi792 – 804Combined sources13
Helixi814 – 821Combined sources8
Beta strandi822 – 824Combined sources3
Helixi825 – 828Combined sources4
Helixi833 – 844Combined sources12
Beta strandi888 – 890Combined sources3
Helixi895 – 910Combined sources16
Helixi918 – 925Combined sources8
Helixi929 – 934Combined sources6
Helixi939 – 966Combined sources28
Helixi977 – 984Combined sources8
Helixi988 – 991Combined sources4
Helixi997 – 1025Combined sources29
Helixi1033 – 1039Combined sources7
Helixi1042 – 1051Combined sources10
Helixi1055 – 1058Combined sources4
Turni1059 – 1062Combined sources4
Helixi1064 – 1076Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DK7NMR-A520-579[»]
2DODNMR-A651-719[»]
2DOENMR-A784-853[»]
2DOFNMR-A888-959[»]
2E71NMR-A717-786[»]
2KIQNMR-A724-782[»]
2KISNMR-A659-724[»]
2MW9NMR-A428-464[»]
2MWANMR-A428-464[»]
2MWBNMR-A428-464[»]
2MWDNMR-A433-460[»]
2MWENMR-A433-460[»]
2MWFNMR-A433-464[»]
2N4RNMR-A428-464[»]
2N4SNMR-A428-464[»]
2N4TNMR-A428-464[»]
2N4UNMR-A428-464[»]
2N4VNMR-A428-464[»]
2N4WNMR-A428-464[»]
2NNTNMR-A/B/C/D428-464[»]
3HFHX-ray2.70A/B661-845[»]
3Q1IX-ray1.40E99-107[»]
4FQGX-ray2.00A/B895-1081[»]
ProteinModelPortaliO14776.
SMRiO14776.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14776.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini131 – 164WW 1PROSITE-ProRule annotationAdd BLAST34
Domaini429 – 462WW 2PROSITE-ProRule annotationAdd BLAST34
Domaini528 – 561WW 3PROSITE-ProRule annotationAdd BLAST34
Domaini659 – 712FF 1Add BLAST54
Domaini725 – 779FF 2Add BLAST55
Domaini791 – 846FF 3Add BLAST56
Domaini896 – 952FF 4Add BLAST57
Domaini954 – 1010FF 5Add BLAST57
Domaini1012 – 1077FF 6Add BLAST66

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili184 – 244Sequence analysisAdd BLAST61
Coiled coili606 – 655Sequence analysisAdd BLAST50
Coiled coili844 – 906Sequence analysisAdd BLAST63

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi626 – 630Nuclear localization signalSequence analysis5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi32 – 132Pro-richAdd BLAST101
Compositional biasi169 – 258Ala/Gln-richAdd BLAST90
Compositional biasi260 – 331Thr-richAdd BLAST72
Compositional biasi328 – 378Pro-richAdd BLAST51
Compositional biasi454 – 515Glu-richAdd BLAST62
Compositional biasi1083 – 1087Poly-Pro5

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

eggNOGiKOG0155. Eukaryota.
ENOG410XPZW. LUCA.
GeneTreeiENSGT00820000127014.
HOGENOMiHOG000008544.
HOVERGENiHBG062908.
InParanoidiO14776.
KOiK12824.
OMAiNPRTTFS.
OrthoDBiEOG091G0I5O.
PhylomeDBiO14776.
TreeFamiTF317748.

Family and domain databases

Gene3Di1.10.10.440. 6 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. AlignAdd to basket

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti324P → R in AAB80727 (PubMed:9315662).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_026933379 – 399Missing in isoform 2. 2 PublicationsAdd BLAST21

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.4. human. [O14776-1]

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.
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DK7NMR-A520-579[»]
2DODNMR-A651-719[»]
2DOENMR-A784-853[»]
2DOFNMR-A888-959[»]
2E71NMR-A717-786[»]
2KIQNMR-A724-782[»]
2KISNMR-A659-724[»]
2MW9NMR-A428-464[»]
2MWANMR-A428-464[»]
2MWBNMR-A428-464[»]
2MWDNMR-A433-460[»]
2MWENMR-A433-460[»]
2MWFNMR-A433-464[»]
2N4RNMR-A428-464[»]
2N4SNMR-A428-464[»]
2N4TNMR-A428-464[»]
2N4UNMR-A428-464[»]
2N4VNMR-A428-464[»]
2N4WNMR-A428-464[»]
2NNTNMR-A/B/C/D428-464[»]
3HFHX-ray2.70A/B661-845[»]
3Q1IX-ray1.40E99-107[»]
4FQGX-ray2.00A/B895-1081[»]
ProteinModelPortaliO14776.
SMRiO14776.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116120. 84 interactors.
DIPiDIP-32504N.
IntActiO14776. 17 interactors.
MINTiMINT-158391.
STRINGi9606.ENSP00000296702.

PTM databases

iPTMnetiO14776.
PhosphoSitePlusiO14776.
SwissPalmiO14776.

Polymorphism and mutation databases

BioMutaiTCERG1.

Proteomic databases

EPDiO14776.
MaxQBiO14776.
PaxDbiO14776.
PeptideAtlasiO14776.
PRIDEiO14776.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000296702; ENSP00000296702; ENSG00000113649. [O14776-1]
ENST00000394421; ENSP00000377943; ENSG00000113649. [O14776-2]
GeneIDi10915.
KEGGihsa:10915.
UCSCiuc003lob.4. human. [O14776-1]

Organism-specific databases

CTDi10915.
DisGeNETi10915.
GeneCardsiTCERG1.
HGNCiHGNC:15630. TCERG1.
HPAiHPA064854.
MIMi605409. gene.
neXtProtiNX_O14776.
OpenTargetsiENSG00000113649.
PharmGKBiPA38007.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0155. Eukaryota.
ENOG410XPZW. LUCA.
GeneTreeiENSGT00820000127014.
HOGENOMiHOG000008544.
HOVERGENiHBG062908.
InParanoidiO14776.
KOiK12824.
OMAiNPRTTFS.
OrthoDBiEOG091G0I5O.
PhylomeDBiO14776.
TreeFamiTF317748.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000113649-MONOMER.
SignaLinkiO14776.

Miscellaneous databases

ChiTaRSiTCERG1. human.
EvolutionaryTraceiO14776.
GeneWikiiTranscription_elongation_regulator_1.
GenomeRNAii10915.
PROiO14776.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000113649.
CleanExiHS_TCERG1.
ExpressionAtlasiO14776. baseline and differential.
GenevisibleiO14776. HS.

Family and domain databases

Gene3Di1.10.10.440. 6 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]
ProtoNetiSearch...

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 30, 2016
This is version 153 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.