P29083 (T2EA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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)

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.6 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	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW 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
Cellular component	nucleoplasm Traceable author statement. Source: Reactome
Molecular function	protein binding Inferred from physical interaction Ref.4. Source: UniProtKB 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

1

1

Removed Ref.3

Chain

2 – 439

438

General transcription factor IIE subunit 1

PRO_0000211222

Regions

Domain

14 – 104

91

HTH TFE/IIEalpha-type

Zinc finger

129 – 157

29

C4-type Potential

Compositional bias

378 – 393

16

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.3 Ref.9

Modified residue

67

1

N6-acetyllysine Ref.8

Modified residue

268

1

Phosphoserine Ref.5

Natural variations

Natural variant

366

1

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

VAR_020321

Experimental info

Sequence conflict

352

1

S → D in CAA45068. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

439

Helix Strand Turn

Details...

Beta strand

118 – 120

3

Beta strand

123 – 128

6

Beta strand

130 – 132

3

Beta strand

135 – 137

3

Helix

138 – 144

7

Turn

147 – 150

4

Beta strand

151 – 153

3

Beta strand

155 – 157

3

Beta strand

395 – 398

4

Beta strand

401 – 404

4

Helix

405 – 410

6

Helix

412 – 417

6

Helix

420 – 433

14

Sequences

	Sequence		Length	Mass (Da)
	P29083 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 9234FFE3F150340B	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

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: 1956398] [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: 1956403] [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: 7667268] [Abstract] Cited for: INTERACTION WITH TAF6.
[5]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-268, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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: 15843171] [Abstract] Cited for: INTERACTION WITH VARICELLA-ZOSTER VIRUS IE63 PROTEIN.
[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: 19106100] [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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-67, MASS SPECTROMETRY.
[9]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 21269460] [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.

SMR

P29083. Positions 113-174, 394-439.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-717N.

MINT

MINT-1894058.

STRING

P29083.

PTM databases

PhosphoSite

P29083.

Polymorphism databases

DMDM

116242812.

Proteomic databases

PeptideAtlas

P29083.

PRIDE

P29083.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000283875; ENSP00000283875; ENSG00000153767.

GeneID

2960.

KEGG

hsa:2960.

NMPDR

fig|9606.3.peg.23032.

UCSC

uc003edz.2. human.

Organism-specific databases

CTD

2960.

GeneCards

GC03P120461.

H-InvDB

HIX0030790.

HGNC

HGNC:4650. GTF2E1.

HPA

CAB009884.

MIM

189962. gene.

neXtProt

NX_P29083.

PharmGKB

PA29036.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG19332.

HOGENOM

HBG314252.

HOVERGEN

HBG008614.

InParanoid

P29083.

OMA

EDMKEGG.

PhylomeDB

P29083.

Enzyme and pathway databases

Reactome

REACT_1788. Transcription.
REACT_6185. HIV Infection.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P29083.

Bgee

P29083.

CleanEx

HS_GTF2E1.

Genevestigator

P29083.

GermOnline

ENSG00000153767. Homo sapiens.

Family and domain databases

InterPro

IPR017919. TFIIE/TFIIEa_HTH.
IPR002853. TFIIE_asu.
IPR021600. TFIIE_asu_C_met.
IPR024550. TFIIEa/SarR/Rpc3_HTH_dom.
IPR013083. Znf_RING/FYVE/PHD.
IPR013137. Znf_TFIIB.
[Graphical view]

Gene3D

G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.

KO

K03136.

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

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:	January 25, 2012
This is version 114 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.