Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

General transcription factor IIH subunit 2

Gene

GTF2H2

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

Functioni

Component of the core-TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. The N-terminus interacts with and regulates XPD whereas an intact C-terminus is required for a successful escape of RNAP II form the promoter.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri291 – 308C4-typeAdd BLAST18

GO - Molecular functioni

  • nucleic acid binding Source: ProtInc
  • protein N-terminus binding Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc
  • translation factor activity, RNA binding Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000145736-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-72086. mRNA Capping.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-73863. RNA Polymerase I Transcription Termination.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
General transcription factor IIH subunit 2
Alternative name(s):
Basic transcription factor 2 44 kDa subunit
Short name:
BTF2 p44
General transcription factor IIH polypeptide 2
TFIIH basal transcription factor complex p44 subunit
Gene namesi
Name:GTF2H2
Synonyms:BTF2P44
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:4656. GTF2H2.

Subcellular locationi

GO - Cellular componenti

  • core TFIIH complex Source: InterPro
  • holo TFIIH complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • transcription factor TFIID complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi291C → A: Reconstituted TFIIH complex lacks p62 and has no transcriptional activity. 1 Publication1
Mutagenesisi308C → A: Reconstituted TFIIH complex lacks p62 and has no transcriptional activity. 1 Publication1
Mutagenesisi345C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication1
Mutagenesisi360C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication1
Mutagenesisi363C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication1
Mutagenesisi376H → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication1
Mutagenesisi380H → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication1
Mutagenesisi382C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication1

Organism-specific databases

DisGeNETi2966.
728340.
730394.
OpenTargetsiENSG00000145736.
ENSG00000275045.
ENSG00000276910.
PharmGKBiPA29042.

Polymorphism and mutation databases

BioMutaiGTF2H2.
DMDMi17380326.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001192481 – 395General transcription factor IIH subunit 2Add BLAST395

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei95PhosphotyrosineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ13888.
MaxQBiQ13888.
PaxDbiQ13888.
PeptideAtlasiQ13888.
PRIDEiQ13888.

PTM databases

iPTMnetiQ13888.
PhosphoSitePlusiQ13888.

Expressioni

Tissue specificityi

Widely expressed, with higher expression in skeletal muscle.

Gene expression databases

BgeeiENSG00000145736.
CleanExiHS_GTF2H2.
ExpressionAtlasiQ13888. baseline and differential.
GenevisibleiQ13888. HS.

Interactioni

Subunit structurei

One of the 6 subunits forming the core-TFIIH basal transcription factor which associates with the CAK complex composed of CDK7, CCNH/cyclin H and MNAT1 to form the TFIIH basal transcription factor. Interacts with XPB, XPD, GTF2H1 and GTF2H3. Interacts with varicella-zoster virus IE63 protein.2 Publications

GO - Molecular functioni

  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109221. 19 interactors.
608768. 6 interactors.
DIPiDIP-786N.
IntActiQ13888. 5 interactors.
MINTiMINT-3028823.
STRINGi9606.ENSP00000274400.

Structurei

Secondary structure

1395
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi333 – 335Combined sources3
Helixi336 – 339Combined sources4
Turni346 – 349Combined sources4
Beta strandi355 – 358Combined sources4
Turni361 – 364Combined sources4
Helixi369 – 373Combined sources5
Turni374 – 378Combined sources5
Beta strandi381 – 383Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z60NMR-A328-386[»]
5IVWelectron microscopy10.0001-395[»]
5IY6electron microscopy7.2001-395[»]
5IY7electron microscopy8.6001-395[»]
5IY8electron microscopy7.9001-395[»]
5IY9electron microscopy6.3001-395[»]
ProteinModelPortaliQ13888.
SMRiQ13888.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13888.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini60 – 236VWFAPROSITE-ProRule annotationAdd BLAST177

Sequence similaritiesi

Belongs to the GTF2H2 family.Curated
Contains 1 VWFA domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri291 – 308C4-typeAdd BLAST18

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2807. Eukaryota.
COG5151. LUCA.
GeneTreeiENSGT00490000043395.
HOGENOMiHOG000159415.
HOVERGENiHBG059468.
InParanoidiQ13888.
KOiK03142.
OMAiIRMGFPH.
OrthoDBiEOG091G08ZR.
PhylomeDBiQ13888.
TreeFamiTF314037.

Family and domain databases

CDDicd01453. vWA_transcription_factor_IIH_t. 1 hit.
Gene3Di3.40.50.410. 1 hit.
InterProiIPR007198. Ssl1-like.
IPR004595. TFIIH_C1-like_dom.
IPR012170. TFIIH_SSL1/p44.
IPR002035. VWF_A.
IPR007087. Znf_C2H2.
[Graphical view]
PANTHERiPTHR12695:SF2. PTHR12695:SF2. 1 hit.
PfamiPF07975. C1_4. 1 hit.
PF04056. Ssl1. 1 hit.
[Graphical view]
PIRSFiPIRSF015919. TFIIH_SSL1. 1 hit.
SMARTiSM01047. C1_4. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
TIGRFAMsiTIGR00622. ssl1. 1 hit.
PROSITEiPS50234. VWFA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

This entry describes 1 isoform i produced by alternative splicing. AlignAdd to basket

Note: A number of isoforms may be produced. The isoforms may be also produced by incomplete gene duplication.
Isoform 1 (identifier: Q13888-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDEEPERTKR WEGGYERTWE ILKEDESGSL KATIEDILFK AKRKRVFEHH
60 70 80 90 100
GQVRLGMMRH LYVVVDGSRT MEDQDLKPNR LTCTLKLLEY FVEEYFDQNP
110 120 130 140 150
ISQIGIIVTK SKRAEKLTEL SGNPRKHITS LKKAVDMTCH GEPSLYNSLS
160 170 180 190 200
IAMQTLKHMP GHTSREVLII FSSLTTCDPS NIYDLIKTLK AAKIRVSVIG
210 220 230 240 250
LSAEVRVCTV LARETGGTYH VILDESHYKE LLTHHVSPPP ASSSSECSLI
260 270 280 290 300
RMGFPQHTIA SLSDQDAKPS FSMAHLDGNT EPGLTLGGYF CPQCRAKYCE
310 320 330 340 350
LPVECKICGL TLVSAPHLAR SYHHLFPLDA FQEIPLEEYN GERFCYGCQG
360 370 380 390
ELKDQHVYVC AVCQNVFCVD CDVFVHDSLH CCPGCIHKIP APSGV
Length:395
Mass (Da):44,419
Last modified:November 1, 1996 - v1
Checksum:i56D1BD8841288739
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti129T → S (PubMed:7552146).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_011664151I → M.1 PublicationCorresponds to variant rs200357275dbSNPEnsembl.1
Natural variantiVAR_011665236V → L.1 PublicationCorresponds to variant rs201102513dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z30094 mRNA. Translation: CAA82910.1.
AF078847 mRNA. Translation: AAD44479.1.
U21911 mRNA. Translation: AAA64502.1.
U21910 mRNA. Translation: AAA64503.1.
BC005345 mRNA. Translation: AAH05345.1.
U80017 Genomic DNA. Translation: AAC52046.1.
CCDSiCCDS34183.1. [Q13888-1]
PIRiS44454.
RefSeqiNP_001506.1. NM_001515.3. [Q13888-1]
XP_016864892.1. XM_017009403.1. [Q13888-1]
XP_016864893.1. XM_017009404.1. [Q13888-1]
XP_016864894.1. XM_017009405.1. [Q13888-1]
XP_016864895.1. XM_017009406.1. [Q13888-1]
UniGeneiHs.191356.
Hs.607501.

Genome annotation databases

EnsembliENST00000274400; ENSP00000274400; ENSG00000145736. [Q13888-1]
ENST00000330280; ENSP00000328901; ENSG00000145736. [Q13888-1]
ENST00000612581; ENSP00000480548; ENSG00000276910. [Q13888-1]
ENST00000617228; ENSP00000479262; ENSG00000275045. [Q13888-1]
ENST00000619997; ENSP00000477954; ENSG00000275045. [Q13888-1]
ENST00000628423; ENSP00000486014; ENSG00000276910. [Q13888-1]
GeneIDi2966.
KEGGihsa:2966.
UCSCiuc003kau.6. human. [Q13888-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z30094 mRNA. Translation: CAA82910.1.
AF078847 mRNA. Translation: AAD44479.1.
U21911 mRNA. Translation: AAA64502.1.
U21910 mRNA. Translation: AAA64503.1.
BC005345 mRNA. Translation: AAH05345.1.
U80017 Genomic DNA. Translation: AAC52046.1.
CCDSiCCDS34183.1. [Q13888-1]
PIRiS44454.
RefSeqiNP_001506.1. NM_001515.3. [Q13888-1]
XP_016864892.1. XM_017009403.1. [Q13888-1]
XP_016864893.1. XM_017009404.1. [Q13888-1]
XP_016864894.1. XM_017009405.1. [Q13888-1]
XP_016864895.1. XM_017009406.1. [Q13888-1]
UniGeneiHs.191356.
Hs.607501.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z60NMR-A328-386[»]
5IVWelectron microscopy10.0001-395[»]
5IY6electron microscopy7.2001-395[»]
5IY7electron microscopy8.6001-395[»]
5IY8electron microscopy7.9001-395[»]
5IY9electron microscopy6.3001-395[»]
ProteinModelPortaliQ13888.
SMRiQ13888.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109221. 19 interactors.
608768. 6 interactors.
DIPiDIP-786N.
IntActiQ13888. 5 interactors.
MINTiMINT-3028823.
STRINGi9606.ENSP00000274400.

PTM databases

iPTMnetiQ13888.
PhosphoSitePlusiQ13888.

Polymorphism and mutation databases

BioMutaiGTF2H2.
DMDMi17380326.

Proteomic databases

EPDiQ13888.
MaxQBiQ13888.
PaxDbiQ13888.
PeptideAtlasiQ13888.
PRIDEiQ13888.

Protocols and materials databases

DNASUi2966.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000274400; ENSP00000274400; ENSG00000145736. [Q13888-1]
ENST00000330280; ENSP00000328901; ENSG00000145736. [Q13888-1]
ENST00000612581; ENSP00000480548; ENSG00000276910. [Q13888-1]
ENST00000617228; ENSP00000479262; ENSG00000275045. [Q13888-1]
ENST00000619997; ENSP00000477954; ENSG00000275045. [Q13888-1]
ENST00000628423; ENSP00000486014; ENSG00000276910. [Q13888-1]
GeneIDi2966.
KEGGihsa:2966.
UCSCiuc003kau.6. human. [Q13888-1]

Organism-specific databases

CTDi2966.
728340.
DisGeNETi2966.
728340.
730394.
GeneCardsiGTF2H2.
HGNCiHGNC:4656. GTF2H2.
MIMi601748. gene.
neXtProtiNX_Q13888.
OpenTargetsiENSG00000145736.
ENSG00000275045.
ENSG00000276910.
PharmGKBiPA29042.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2807. Eukaryota.
COG5151. LUCA.
GeneTreeiENSGT00490000043395.
HOGENOMiHOG000159415.
HOVERGENiHBG059468.
InParanoidiQ13888.
KOiK03142.
OMAiIRMGFPH.
OrthoDBiEOG091G08ZR.
PhylomeDBiQ13888.
TreeFamiTF314037.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000145736-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-72086. mRNA Capping.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-73863. RNA Polymerase I Transcription Termination.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

EvolutionaryTraceiQ13888.
GeneWikiiGTF2H2.
PROiQ13888.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000145736.
CleanExiHS_GTF2H2.
ExpressionAtlasiQ13888. baseline and differential.
GenevisibleiQ13888. HS.

Family and domain databases

CDDicd01453. vWA_transcription_factor_IIH_t. 1 hit.
Gene3Di3.40.50.410. 1 hit.
InterProiIPR007198. Ssl1-like.
IPR004595. TFIIH_C1-like_dom.
IPR012170. TFIIH_SSL1/p44.
IPR002035. VWF_A.
IPR007087. Znf_C2H2.
[Graphical view]
PANTHERiPTHR12695:SF2. PTHR12695:SF2. 1 hit.
PfamiPF07975. C1_4. 1 hit.
PF04056. Ssl1. 1 hit.
[Graphical view]
PIRSFiPIRSF015919. TFIIH_SSL1. 1 hit.
SMARTiSM01047. C1_4. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF53300. SSF53300. 1 hit.
TIGRFAMsiTIGR00622. ssl1. 1 hit.
PROSITEiPS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTF2H2_HUMAN
AccessioniPrimary (citable) accession number: Q13888
Secondary accession number(s): Q15570, Q15571, Q9BS41
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 178 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 5
    Human chromosome 5: 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.