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Protein

Transcription initiation factor IIE subunit beta

Gene

GTF2E2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi66 – 146TFIIE betaPROSITE-ProRule annotationAdd BLAST81

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000074157-MONOMER.
ReactomeiR-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation factor IIE subunit beta
Short name:
TFIIE-beta
Alternative name(s):
General transcription factor IIE subunit 2
Gene namesi
Name:GTF2E2
Synonyms:TF2E2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:4651. GTF2E2.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Trichothiodystrophy 6, non-photosensitive (TTD6)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of trichothiodystrophy, a disease characterized by sulfur-deficient brittle hair and multisystem variable abnormalities. The spectrum of clinical features varies from mild disease with only hair involvement to severe disease with cutaneous, neurologic and profound developmental defects. Ichthyosis, intellectual and developmental disabilities, decreased fertility, abnormal characteristics at birth, ocular abnormalities, short stature, and infections are common manifestations. There are both photosensitive and non-photosensitive forms of the disorder. TTD6 patients do not manifest cutaneous photosensitivity. Inheritance pattern has been reported to be autosomal recessive.
See also OMIM:616943
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076893150A → P in TTD6; reduction in the levels of both TFIIE-alpha and TFIIE-beta subunits of the TFIIE complex in patient cells; reduced phosphorylation of TFIIE-alpha observed in patient cells. 1 Publication1
Natural variantiVAR_076894187D → Y in TTD6; reduction in the levels of both TFIIE-alpha and TFIIE-beta subunits of the TFIIE complex in patient cells; reduced phosphorylation of TFIIE-alpha observed in patient cells. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2961.
MIMi616943. phenotype.
OpenTargetsiENSG00000197265.
PharmGKBiPA29037.

Polymorphism and mutation databases

BioMutaiGTF2E2.
DMDMi135232.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002112261 – 291Transcription initiation factor IIE subunit betaAdd BLAST291

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei61PhosphoserineCombined sources1
Modified residuei74N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP29084.
MaxQBiP29084.
PaxDbiP29084.
PeptideAtlasiP29084.
PRIDEiP29084.

PTM databases

iPTMnetiP29084.
PhosphoSitePlusiP29084.

Expressioni

Gene expression databases

BgeeiENSG00000197265.
CleanExiHS_GTF2E2.
ExpressionAtlasiP29084. baseline and differential.
GenevisibleiP29084. HS.

Organism-specific databases

HPAiCAB009603.
HPA004816.
HPA025065.

Interactioni

Subunit structurei

Tetramer of two alpha and two beta chains. Interacts with FACT subunit SUPT16H. Interacts with ATF7IP.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GTF2E1P290834EBI-2853321,EBI-5462215
MCCP235082EBI-2853321,EBI-307531

Protein-protein interaction databases

BioGridi109216. 112 interactors.
DIPiDIP-716N.
IntActiP29084. 4 interactors.
MINTiMINT-1894071.
STRINGi9606.ENSP00000348168.

Structurei

Secondary structure

1291
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi67 – 70Combined sources4
Helixi75 – 91Combined sources17
Helixi99 – 106Combined sources8
Beta strandi109 – 111Combined sources3
Helixi113 – 120Combined sources8
Helixi123 – 126Combined sources4
Beta strandi130 – 132Combined sources3
Beta strandi134 – 139Combined sources6
Turni142 – 144Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D8JNMR-A66-146[»]
1D8KNMR-A66-146[»]
5IY6electron microscopy7.20R1-291[»]
5IY7electron microscopy8.60R1-291[»]
5IY8electron microscopy7.90R1-291[»]
5IY9electron microscopy6.30R1-291[»]
5IYAelectron microscopy5.40R1-291[»]
5IYBelectron microscopy3.90R1-291[»]
5IYCelectron microscopy3.90R1-291[»]
5IYDelectron microscopy3.90R1-291[»]
ProteinModelPortaliP29084.
SMRiP29084.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29084.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi26 – 36Poly-SerAdd BLAST11
Compositional biasi37 – 42Lys-rich (basic)6
Compositional biasi251 – 271Arg/Lys-rich (basic)Add BLAST21

Sequence similaritiesi

Belongs to the TFIIE beta subunit family.PROSITE-ProRule annotation
Contains 1 TFIIE beta DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3095. Eukaryota.
COG5174. LUCA.
GeneTreeiENSGT00390000011749.
HOGENOMiHOG000008149.
HOVERGENiHBG009400.
InParanoidiP29084.
KOiK03137.
OMAiHNNPKVE.
OrthoDBiEOG091G0HXJ.
PhylomeDBiP29084.
TreeFamiTF105901.

Family and domain databases

CDDicd07977. TFIIE_beta_winged_helix. 1 hit.
Gene3Di1.10.10.10. 1 hit.
InterProiIPR016656. TFIIE-bsu.
IPR003166. TFIIE_bsu_DNA-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02186. TFIIE_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF016398. TFIIE-beta. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51351. TFIIE_BETA_C. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29084-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPSLLRERE LFKKRALSTP VVEKRSASSE SSSSSSKKKK TKVEHGGSSG
60 70 80 90 100
SKQNSDHSNG SFNLKALSGS SGYKFGVLAK IVNYMKTRHQ RGDTHPLTLD
110 120 130 140 150
EILDETQHLD IGLKQKQWLM TEALVNNPKI EVIDGKYAFK PKYNVRDKKA
160 170 180 190 200
LLRLLDQHDQ RGLGGILLED IEEALPNSQK AVKALGDQIL FVNRPDKKKI
210 220 230 240 250
LFFNDKSCQF SVDEEFQKLW RSVTVDSMDE EKIEEYLKRQ GISSMQESGP
260 270 280 290
KKVAPIQRRK KPASQKKRRF KTHNEHLAGV LKDYSDITSS K
Length:291
Mass (Da):33,044
Last modified:December 1, 1992 - v1
Checksum:i20F6BDFF2E06E5E7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti53Q → E in AAG39077 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052281133I → T.Corresponds to variant rs2229299dbSNPEnsembl.1
Natural variantiVAR_076893150A → P in TTD6; reduction in the levels of both TFIIE-alpha and TFIIE-beta subunits of the TFIIE complex in patient cells; reduced phosphorylation of TFIIE-alpha observed in patient cells. 1 Publication1
Natural variantiVAR_039003183K → R.Corresponds to variant rs2978277dbSNPEnsembl.1
Natural variantiVAR_076894187D → Y in TTD6; reduction in the levels of both TFIIE-alpha and TFIIE-beta subunits of the TFIIE complex in patient cells; reduced phosphorylation of TFIIE-alpha observed in patient cells. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67861 mRNA. Translation: AAB20414.1.
X63469 mRNA. Translation: CAA45069.1.
AF292062
, 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.
CCDSiCCDS6078.1.
PIRiS29292.
RefSeqiNP_002086.1. NM_002095.4.
XP_016868852.1. XM_017013363.1.
XP_016868853.1. XM_017013364.1.
UniGeneiHs.77100.

Genome annotation databases

EnsembliENST00000355904; ENSP00000348168; ENSG00000197265.
GeneIDi2961.
KEGGihsa:2961.
UCSCiuc003xig.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67861 mRNA. Translation: AAB20414.1.
X63469 mRNA. Translation: CAA45069.1.
AF292062
, 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.
CCDSiCCDS6078.1.
PIRiS29292.
RefSeqiNP_002086.1. NM_002095.4.
XP_016868852.1. XM_017013363.1.
XP_016868853.1. XM_017013364.1.
UniGeneiHs.77100.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D8JNMR-A66-146[»]
1D8KNMR-A66-146[»]
5IY6electron microscopy7.20R1-291[»]
5IY7electron microscopy8.60R1-291[»]
5IY8electron microscopy7.90R1-291[»]
5IY9electron microscopy6.30R1-291[»]
5IYAelectron microscopy5.40R1-291[»]
5IYBelectron microscopy3.90R1-291[»]
5IYCelectron microscopy3.90R1-291[»]
5IYDelectron microscopy3.90R1-291[»]
ProteinModelPortaliP29084.
SMRiP29084.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109216. 112 interactors.
DIPiDIP-716N.
IntActiP29084. 4 interactors.
MINTiMINT-1894071.
STRINGi9606.ENSP00000348168.

PTM databases

iPTMnetiP29084.
PhosphoSitePlusiP29084.

Polymorphism and mutation databases

BioMutaiGTF2E2.
DMDMi135232.

Proteomic databases

EPDiP29084.
MaxQBiP29084.
PaxDbiP29084.
PeptideAtlasiP29084.
PRIDEiP29084.

Protocols and materials databases

DNASUi2961.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000355904; ENSP00000348168; ENSG00000197265.
GeneIDi2961.
KEGGihsa:2961.
UCSCiuc003xig.4. human.

Organism-specific databases

CTDi2961.
DisGeNETi2961.
GeneCardsiGTF2E2.
HGNCiHGNC:4651. GTF2E2.
HPAiCAB009603.
HPA004816.
HPA025065.
MIMi189964. gene.
616943. phenotype.
neXtProtiNX_P29084.
OpenTargetsiENSG00000197265.
PharmGKBiPA29037.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3095. Eukaryota.
COG5174. LUCA.
GeneTreeiENSGT00390000011749.
HOGENOMiHOG000008149.
HOVERGENiHBG009400.
InParanoidiP29084.
KOiK03137.
OMAiHNNPKVE.
OrthoDBiEOG091G0HXJ.
PhylomeDBiP29084.
TreeFamiTF105901.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000074157-MONOMER.
ReactomeiR-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6807505. RNA polymerase II transcribes snRNA genes.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.

Miscellaneous databases

ChiTaRSiGTF2E2. human.
EvolutionaryTraceiP29084.
GeneWikiiGTF2E2.
GenomeRNAii2961.
PROiP29084.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000197265.
CleanExiHS_GTF2E2.
ExpressionAtlasiP29084. baseline and differential.
GenevisibleiP29084. HS.

Family and domain databases

CDDicd07977. TFIIE_beta_winged_helix. 1 hit.
Gene3Di1.10.10.10. 1 hit.
InterProiIPR016656. TFIIE-bsu.
IPR003166. TFIIE_bsu_DNA-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF02186. TFIIE_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF016398. TFIIE-beta. 1 hit.
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51351. TFIIE_BETA_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiT2EB_HUMAN
AccessioniPrimary (citable) accession number: P29084
Secondary accession number(s): D3DSV2, Q9H2B9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 30, 2016
This is version 167 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.