General transcription factor IIE subunit 1

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P29083 (T2EA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 128. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	439 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.7
Subcellular location	Nucleus.
Sequence similarities	Belongs to the TFIIE alpha subunit family. Contains 1 HTH TFE/IIEalpha-type domain.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.3

Chain

2 – 439

438

General transcription factor IIE subunit 1

PRO_0000211222

Regions

Domain

14 – 104

HTH TFE/IIEalpha-type

Zinc finger

129 – 157

C4-type Potential

Compositional bias

378 – 393

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

N-acetylalanine Ref.3

Modified residue

N6-acetyllysine Ref.8

Modified residue

268

Phosphoserine Ref.6

Natural variations

Natural variant

366

P → S.
Corresponds to variant rs3732401 [ dbSNP | Ensembl ].

VAR_020321

Experimental info

Sequence conflict

352

S → D in CAA45068. Ref.2

Secondary structure

439

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P29083 [UniParc].

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

FASTA

439

49,452

        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' referencesShow '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, 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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.
[8]	"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, MASS SPECTROMETRY.
[9]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

S67859 mRNA. Translation: AAB20413.1.
X63468 mRNA. Translation: CAA45068.1.

IPI

IPI00019977.

PIR

S29291.

RefSeq

NP_005504.2. NM_005513.2.

UniGene

Hs.445272.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1VD4	NMR	-	A	113-174	[»]
2JTX	NMR	-	A	336-439	[»]
2RNQ	NMR	-	A	378-439	[»]
2RNR	NMR	-	A	378-439	[»]

ProteinModelPortal

P29083.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-717N.

MINT

MINT-1894058.

STRING

9606.ENSP00000283875.

PTM databases

PhosphoSite

P29083.

Polymorphism databases

DMDM

116242812.

Proteomic databases

PaxDb

P29083.

PeptideAtlas

P29083.

PRIDE

P29083.

Protocols and materials databases

DNASU

2960.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000283875; ENSP00000283875; ENSG00000153767.

GeneID

2960.

KEGG

hsa:2960.

UCSC

uc003edz.4. human.

Organism-specific databases

CTD

2960.

GeneCards

GC03P120461.

HGNC

HGNC:4650. GTF2E1.

HPA

CAB009884.

MIM

189962. gene.

neXtProt

NX_P29083.

PharmGKB

PA29036.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1675.

HOGENOM

HOG000007666.

HOVERGEN

HBG008614.

InParanoid

P29083.

K03136.

OMA

QNVVISM.

PhylomeDB

P29083.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.
REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P29083.

Bgee

P29083.

CleanEx

HS_GTF2E1.

Genevestigator

P29083.

GermOnline

ENSG00000153767. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR017919. 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]

Pfam

PF08271. TF_Zn_Ribbon. 1 hit.
PF11521. TFIIE-A_C-term. 1 hit.
PF02002. TFIIE_alpha. 1 hit.
[Graphical view]

SMART

SM00531. TFIIE. 1 hit.
[Graphical view]

PROSITE

PS51344. HTH_TFE_IIE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

GTF2E1. human.

EvolutionaryTrace

P29083.

GenomeRNAi

2960.

NextBio

11734.

PMAP-CutDB

P29083.

SOURCE

Search...

Entry information

Entry name

T2EA_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents