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P29083 (T2EA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
General transcription factor IIE subunit 1
Alternative name(s):
General transcription factor IIE 56 kDa subunit
Transcription initiation factor IIE subunit alpha
Short name=TFIIE-alpha
Gene names
Name:GTF2E1
Synonyms:TF2E1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length439 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase.

Subunit structure

Tetramer of two alpha and two beta chains. Interacts with TAF6/TAFII80. Interacts with ATF7IP. Interacts with varicella-zoster virus IE63 protein. Ref.4 Ref.5 Ref.8

Subcellular location

Nucleus.

Sequence similarities

Belongs to the TFIIE alpha subunit family.

Contains 1 HTH TFE/IIEalpha-type domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GTF2E2P290842EBI-5462215,EBI-2853321
GTF2H1P3278017EBI-5462215,EBI-715539

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 439438General transcription factor IIE subunit 1
PRO_0000211222

Regions

Domain14 – 10491HTH TFE/IIEalpha-type
Zinc finger129 – 15729C4-type Potential
Compositional bias378 – 39316Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue21N-acetylalanine Ref.3 Ref.7 Ref.11
Modified residue671N6-acetyllysine Ref.9
Modified residue2681Phosphoserine Ref.6

Natural variations

Natural variant3661P → S.
Corresponds to variant rs3732401 [ dbSNP | Ensembl ].
VAR_020321

Experimental info

Sequence conflict3521S → D in CAA45068. Ref.2

Secondary structure

............................ 439
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29083 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 9234FFE3F150340B

FASTA43949,452
        10         20         30         40         50         60 
MADPDVLTEV PAALKRLAKY VIRGFYGIEH ALALDILIRN SCVKEEDMLE LLKFDRKQLR 

        70         80         90        100        110        120 
SVLNNLKGDK FIKCRMRVET AADGKTTRHN YYFINYRTLV NVVKYKLDHM RRRIETDERD 

       130        140        150        160        170        180 
STNRASFKCP VCSSTFTDLE ANQLFDPMTG TFRCTFCHTE VEEDESAMPK KDARTLLARF 

       190        200        210        220        230        240 
NEQIEPIYAL LRETEDVNLA YEILEPEPTE IPALKQSKDH AATTAGAASL AGGHHREAWA 

       250        260        270        280        290        300 
TKGPSYEDLY TQNVVINMDD QEDLHRASLE GKSAKERPIW LRESTVQGAY GSEDMKEGGI 

       310        320        330        340        350        360 
DMDAFQEREE GHAGPDDNEE VMRALLIHEK KTSSAMAGSV GAAAPVTAAN GSDSESETSE 

       370        380        390        400        410        420 
SDDDSPPRPA AVAVHKREED EEEDDEFEEV ADDPIVMVAG RPFSYSEVSQ RPELVAQMTP 

       430 
EEKEAYIAMG QRMFEDLFE 

« Hide

References

« Hide 'large scale' references
[1]"Structure and functional properties of human general transcription factor IIE."
Peterson M.G., Inostroza J., Maxon M.E., Flores O., Admon A., Reinberg D., Tjian R.
Nature 354:369-373(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"Structural motifs and potential sigma homologies in the large subunit of human general transcription factor TFIIE."
Ohkuma Y., Sumimoto H., Hoffmann A., Shimasaki S., Horikoshi M., Roeder R.G.
Nature 354:398-401(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]Bienvenut W.V.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-16; 154-170; 219-236; 243-266 AND 402-423, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[4]"Evolutionary conservation of human TATA-binding-polypeptide-associated factors TAFII31 and TAFII80 and interactions of TAFII80 with other TAFs and with general transcription factors."
Hisatake K., Ohta T., Takada R., Guermah M., Horikoshi M., Nakatani Y., Roeder R.G.
Proc. Natl. Acad. Sci. U.S.A. 92:8195-8199(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TAF6.
[5]"Varicella-zoster virus IE63 protein represses the basal transcription machinery by disorganizing the pre-initiation complex."
Di Valentin E., Bontems S., Habran L., Jolois O., Markine-Goriaynoff N., Vanderplasschen A., Sadzot-Delvaux C., Piette J.
Biol. Chem. 386:255-267(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VARICELLA-ZOSTER VIRUS IE63 PROTEIN.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated telomerase activity."
Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S., Watanabe S., Saitoh N., Ito T., Nakao M.
J. Biol. Chem. 284:5165-5174(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATF7IP.
[9]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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].
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S67859 mRNA. Translation: AAB20413.1.
X63468 mRNA. Translation: CAA45068.1.
PIRS29291.
RefSeqNP_005504.2. NM_005513.2.
UniGeneHs.445272.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VD4NMR-A113-174[»]
2JTXNMR-A336-439[»]
2RNQNMR-A378-439[»]
2RNRNMR-A378-439[»]
ProteinModelPortalP29083.
SMRP29083. Positions 113-174, 394-439.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109215. 47 interactions.
DIPDIP-717N.
IntActP29083. 3 interactions.
MINTMINT-1894058.
STRING9606.ENSP00000283875.

PTM databases

PhosphoSiteP29083.

Polymorphism databases

DMDM116242812.

Proteomic databases

PaxDbP29083.
PeptideAtlasP29083.
PRIDEP29083.

Protocols and materials databases

DNASU2960.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000283875; ENSP00000283875; ENSG00000153767.
GeneID2960.
KEGGhsa:2960.
UCSCuc003edz.4. human.

Organism-specific databases

CTD2960.
GeneCardsGC03P120461.
HGNCHGNC:4650. GTF2E1.
HPACAB009884.
HPA042437.
MIM189962. gene.
neXtProtNX_P29083.
PharmGKBPA29036.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1675.
HOGENOMHOG000007666.
HOVERGENHBG008614.
InParanoidP29083.
KOK03136.
OMALFQDMYF.
PhylomeDBP29083.
TreeFamTF313429.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP29083.
BgeeP29083.
CleanExHS_GTF2E1.
GenevestigatorP29083.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR017919. TFIIE/TFIIEa_HTH.
IPR002853. TFIIE_asu.
IPR021600. TFIIE_asu_C.
IPR024550. TFIIEa/SarR/Rpc3_HTH_dom.
IPR013083. Znf_RING/FYVE/PHD.
IPR013137. Znf_TFIIB.
[Graphical view]
PfamPF08271. TF_Zn_Ribbon. 1 hit.
PF11521. TFIIE-A_C-term. 1 hit.
PF02002. TFIIE_alpha. 1 hit.
[Graphical view]
SMARTSM00531. TFIIE. 1 hit.
[Graphical view]
PROSITEPS51344. HTH_TFE_IIE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGTF2E1. human.
EvolutionaryTraceP29083.
GeneWikiGTF2E1.
GenomeRNAi2960.
NextBio11734.
PMAP-CutDBP29083.
PROP29083.
SOURCESearch...

Entry information

Entry nameT2EA_HUMAN
AccessionPrimary (citable) accession number: P29083
Secondary accession number(s): Q16103
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 138 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM