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P29084 (T2EB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. 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:
Transcription initiation factor IIE subunit beta

Short name=TFIIE-beta
Alternative name(s):
General transcription factor IIE subunit 2
Gene names
Name:GTF2E2
Synonyms:TF2E2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length291 AA.
Sequence statusComplete.
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 FACT subunit SUPT16H. Interacts with ATF7IP. Ref.6 Ref.7

Subcellular location

Nucleus.

Sequence similarities

Belongs to the TFIIE beta subunit family.

Contains 1 TFIIE beta DNA-binding domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 291291Transcription initiation factor IIE subunit beta
PRO_0000211226

Regions

DNA binding66 – 14681TFIIE beta
Compositional bias26 – 3611Poly-Ser
Compositional bias37 – 426Lys-rich (basic)
Compositional bias251 – 27121Arg/Lys-rich (basic)

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9
Modified residue741N6-acetyllysine By similarity

Natural variations

Natural variant1331I → T.
Corresponds to variant rs2229299 [ dbSNP | Ensembl ].
VAR_052281
Natural variant1831K → R.
Corresponds to variant rs2978277 [ dbSNP | Ensembl ].
VAR_039003

Experimental info

Sequence conflict531Q → E in AAG39077. Ref.3

Secondary structure

................... 291
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29084 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 20F6BDFF2E06E5E7

FASTA29133,044
        10         20         30         40         50         60 
MDPSLLRERE LFKKRALSTP VVEKRSASSE SSSSSSKKKK TKVEHGGSSG SKQNSDHSNG 

        70         80         90        100        110        120 
SFNLKALSGS SGYKFGVLAK IVNYMKTRHQ RGDTHPLTLD EILDETQHLD IGLKQKQWLM 

       130        140        150        160        170        180 
TEALVNNPKI EVIDGKYAFK PKYNVRDKKA LLRLLDQHDQ RGLGGILLED IEEALPNSQK 

       190        200        210        220        230        240 
AVKALGDQIL FVNRPDKKKI LFFNDKSCQF SVDEEFQKLW RSVTVDSMDE EKIEEYLKRQ 

       250        260        270        280        290 
GISSMQESGP KKVAPIQRRK KPASQKKRRF KTHNEHLAGV LKDYSDITSS K 

« 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]"Conserved sequence motifs in the small subunit of human general transcription factor TFIIE."
Sumimoto H., Ohkuma Y., Sinn E., Kato H., Shimasaki S., Horikoshi M., Roeder R.G.
Nature 354:401-404(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]Schertzer M., Wood S.
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skin.
[6]"Functional interaction of general transcription initiation factor TFIIE with general chromatin factor SPT16/CDC68."
Kang S.-W., Kuzuhara T., Horikoshi M.
Genes Cells 5:251-263(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SUPT16H.
[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]"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].
[9]"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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S67861 mRNA. Translation: AAB20414.1.
X63469 mRNA. Translation: CAA45069.1.
AF292062 expand/collapse EMBL AC list , AF292056, AF292057, AF292058, AF292059, AF292060, AF292061 Genomic DNA. Translation: AAG39077.1.
CH471080 Genomic DNA. Translation: EAW63446.1.
CH471080 Genomic DNA. Translation: EAW63449.1.
BC030572 mRNA. Translation: AAH30572.1.
PIRS29292.
RefSeqNP_002086.1. NM_002095.4.
UniGeneHs.77100.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1D8JNMR-A66-146[»]
1D8KNMR-A66-146[»]
ProteinModelPortalP29084.
SMRP29084. Positions 66-146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109216. 30 interactions.
DIPDIP-716N.
IntActP29084. 3 interactions.
MINTMINT-1894071.
STRING9606.ENSP00000348168.

PTM databases

PhosphoSiteP29084.

Polymorphism databases

DMDM135232.

Proteomic databases

PaxDbP29084.
PeptideAtlasP29084.
PRIDEP29084.

Protocols and materials databases

DNASU2961.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355904; ENSP00000348168; ENSG00000197265.
GeneID2961.
KEGGhsa:2961.
UCSCuc003xig.3. human.

Organism-specific databases

CTD2961.
GeneCardsGC08M030429.
HGNCHGNC:4651. GTF2E2.
HPACAB009603.
HPA004816.
HPA025065.
MIM189964. gene.
neXtProtNX_P29084.
PharmGKBPA29037.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5174.
HOGENOMHOG000008149.
HOVERGENHBG009400.
InParanoidP29084.
KOK03137.
OMALGDQIIF.
OrthoDBEOG71ZP2B.
PhylomeDBP29084.
TreeFamTF105901.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressP29084.
BgeeP29084.
CleanExHS_GTF2E2.
GenevestigatorP29084.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR016656. TFIIE-bsu.
IPR003166. TFIIE_bsu_DNA-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF02186. TFIIE_beta. 1 hit.
[Graphical view]
PIRSFPIRSF016398. TFIIE-beta. 1 hit.
PROSITEPS51351. TFIIE_BETA_C. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP29084.
GeneWikiGTF2E2.
GenomeRNAi2961.
NextBio11738.
PROP29084.
SOURCESearch...

Entry information

Entry nameT2EB_HUMAN
AccessionPrimary (citable) accession number: P29084
Secondary accession number(s): D3DSV2, Q9H2B9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 139 of the entry and version 1 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 8

Human chromosome 8: entries, gene names and cross-references to MIM