O14776 · TCRG1_HUMAN

  • Protein
    Transcription elongation regulator 1
  • Gene
    TCERG1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

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.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentnuclear speck
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular Functionidentical protein binding
Molecular FunctionRNA binding
Molecular FunctionRNA polymerase binding
Molecular FunctionRNA polymerase II-specific DNA-binding transcription factor binding
Molecular Functiontranscription coactivator activity
Molecular Functiontranscription coregulator activity
Molecular Functiontranscription corepressor activity
Molecular Functiontranscription elongation factor activity
Molecular Functionubiquitin-like protein conjugating enzyme binding
Biological ProcessmRNA processing
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processnegative regulation of transcription elongation by RNA polymerase II
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processpositive regulation of transcription elongation by RNA polymerase II
Biological ProcessRNA splicing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Transcription elongation regulator 1
  • Alternative names
    • TATA box-binding protein-associated factor 2S
    • Transcription factor CA150

Gene names

    • Name
      TCERG1
    • Synonyms
      CA150, TAF2S

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O14776
  • Secondary accessions
    • Q2NKN2
    • Q59EA1

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis148-150Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 446-AAA-448.
Mutagenesis446-448Loss of interaction with SF1. Reduces repression of transcription by 35%. Reduces repression of transcription by 63%; when associated with 148-AAA-150.
Mutagenesis545-547No effect.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 988 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue, modified residue (large scale data), cross-link.

TypeIDPosition(s)SourceDescription
ChainPRO_00000760631-1098UniProtTranscription elongation regulator 1
Modified residue11UniProtPhosphoserine
Modified residue20UniProtOmega-N-methylarginine
Modified residue28UniProtAsymmetric dimethylarginine
Modified residue30UniProtAsymmetric dimethylarginine
Modified residue41UniProtAsymmetric dimethylarginine
Modified residue48UniProtAsymmetric dimethylarginine
Modified residue (large scale data)481PRIDEPhosphoserine
Cross-link503UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Cross-link507UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue (large scale data)591PRIDEPhosphothreonine
Cross-link608UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Modified residue638UniProtPhosphoserine
Modified residue (large scale data)638PRIDEPhosphoserine
Modified residue (large scale data)832PRIDEPhosphoserine
Modified residue (large scale data)833PRIDEPhosphoserine
Modified residue834UniProtPhosphoserine
Modified residue (large scale data)834PRIDEPhosphoserine
Modified residue (large scale data)853PRIDEPhosphoserine
Modified residue933UniProtPhosphoserine
Modified residue (large scale data)933PRIDEPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Detected in brain neurons.

Induction

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

Gene expression databases

Organism-specific databases

Interaction

Subunit

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

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY O14776BARD1 Q997282EBI-473271, EBI-473181
BINARY O14776HTT P428589EBI-473271, EBI-466029
BINARY O14776TCERG1 O147764EBI-473271, EBI-473271

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, compositional bias, domain, coiled coil, motif.

TypeIDPosition(s)Description
Region1-105Disordered
Compositional bias36-105Pro residues
Domain131-164WW 1
Coiled coil184-244
Compositional bias259-327Polar residues
Region259-348Disordered
Compositional bias328-348Pro residues
Domain429-462WW 2
Compositional bias469-484Basic and acidic residues
Region469-526Disordered
Compositional bias496-520Basic and acidic residues
Domain528-561WW 3
Coiled coil606-655
Region615-640Disordered
Compositional bias618-640Basic and acidic residues
Motif626-630Nuclear localization signal
Domain659-712FF 1
Domain725-779FF 2
Domain791-846FF 3
Coiled coil844-906
Region870-895Disordered
Domain896-952FF 4
Domain954-1010FF 5
Domain1012-1077FF 6
Region1076-1098Disordered

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.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

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.

  • Length
    1,098
  • Mass (Da)
    123,901
  • Last updated
    2007-07-24 v2
  • Checksum
    5F0A0C3A07EBF00F
MAERGGDGGESERFNPGELRMAQQQALRFRGPAPPPNAVMRGPPPLMRPPPPFGMMRGPPPPPRPPFGRPPFDPNMPPMPPPGGIPPPMGPPHLQRPPFMPPPMSSMPPPPGMMFPPGMPPVTAPGTPALPPTEEIWVENKTPDGKVYYYNARTRESAWTKPDGVKVIQQSELTPMLAAQAQVQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQVQAQVQAQVQAQAVGASTPTTSSPAPAVSTSTSSSTPSSTTSTTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSTPAPTATPVQTVPQPHPQTLPPAVPHSVPQPTTAIPAFPPVMVPPFRVPLPGMPIPLPGVAMMQIVSCPYVKTVATTKTGVLPGMAPPIVPMIHPQVAIAASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQELKEKEKLEEKIKEPIKEPSEEPLPMETEEEDPKEEPIKEIKEEPKEEEMTEEEKAAQKAKPVATAPIPGTPWCVVWTGDERVFFYNPTTRLSMWDRPDDLIGRADVDKIIQEPPHKKGMEELKKLRHPTPTMLSIQKWQFSMSAIKEEQELMEEINEDEPVKAKKRKRDDNKDIDSEKEAAMEAEIKAARERAIVPLEARMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYLLLNPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRDKYITAKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRKLIVAYVDDLDRRGPPPPPTASEPTRRSTK

O14776-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A7P0T8N8A0A7P0T8N8_HUMANTCERG11115
G3V220G3V220_HUMANTCERG11032
A0AA34QVF9A0AA34QVF9_HUMANTCERG142
A0AA34QVU1A0AA34QVU1_HUMANTCERG1674

Sequence caution

The sequence BAD93147.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for compositional bias, sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Compositional bias36-105Pro residues
Compositional bias259-327Polar residues
Sequence conflict324in Ref. 1; AAB80727
Compositional bias328-348Pro residues
Alternative sequenceVSP_026933379-399in isoform 2
Compositional bias469-484Basic and acidic residues
Compositional bias496-520Basic and acidic residues
Compositional bias618-640Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF017789
EMBL· GenBank· DDBJ
AAB80727.1
EMBL· GenBank· DDBJ
mRNA
AB209910
EMBL· GenBank· DDBJ
BAD93147.1
EMBL· GenBank· DDBJ
mRNA Different initiation
BC111727
EMBL· GenBank· DDBJ
AAI11728.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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