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Q13888 (TF2H2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 151. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GTF2H2
Synonyms:BTF2P44
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.6 Ref.8

Subcellular location

Nucleus.

Tissue specificity

Widely expressed, with higher expression in skeletal muscle.

Sequence similarities

Belongs to the GTF2H2 family.

Contains 1 VWFA domain.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Traceable author statement. Source: Reactome

ATP catabolic process

Inferred from direct assay Ref.6. Source: GOC

DNA repair

Traceable author statement. Source: Reactome

G-protein coupled receptor internalization

Inferred from mutant phenotype PubMed 15775968. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

nucleotide-excision repair

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA damage removal

Traceable author statement. Source: Reactome

positive regulation of viral transcription

Traceable author statement. Source: Reactome

protein phosphorylation

Inferred from direct assay Ref.6. Source: GOC

response to UV

Traceable author statement Ref.1. Source: ProtInc

termination of RNA polymerase I transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.6. Source: UniProtKB

transcription initiation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

translation

Traceable author statement Ref.1. Source: GOC

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcore TFIIH complex

Inferred from electronic annotation. Source: InterPro

holo TFIIH complex

Inferred from direct assay Ref.6. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

   Molecular_functionnucleic acid binding

Traceable author statement Ref.1. Source: ProtInc

protein N-terminus binding

Inferred from physical interaction PubMed 8652557. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Non-traceable author statement Ref.1. Source: ProtInc

translation factor activity, nucleic acid binding

Traceable author statement Ref.1. Source: ProtInc

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms may be produced. The isoforms may be also produced by incomplete gene duplication.
Isoform 1 (identifier: Q13888-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 395395General transcription factor IIH subunit 2
PRO_0000119248

Regions

Domain60 – 236177VWFA
Zinc finger291 – 30818C4-type

Amino acid modifications

Modified residue951Phosphotyrosine By similarity

Natural variations

Natural variant1511I → M. Ref.10
VAR_011664
Natural variant2361V → L. Ref.10
VAR_011665

Experimental info

Mutagenesis2911C → A: Reconstituted TFIIH complex lacks p62 and has no transcriptional activity. Ref.7
Mutagenesis3081C → A: Reconstituted TFIIH complex lacks p62 and has no transcriptional activity. Ref.7
Mutagenesis3451C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. Ref.7
Mutagenesis3601C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. Ref.7
Mutagenesis3631C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. Ref.7
Mutagenesis3761H → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. Ref.7
Mutagenesis3801H → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. Ref.7
Mutagenesis3821C → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. Ref.7
Sequence conflict1291T → S Ref.4

Secondary structure

............... 395
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 56D1BD8841288739

FASTA39544,419
        10         20         30         40         50         60 
MDEEPERTKR WEGGYERTWE ILKEDESGSL KATIEDILFK AKRKRVFEHH GQVRLGMMRH 

        70         80         90        100        110        120 
LYVVVDGSRT MEDQDLKPNR LTCTLKLLEY FVEEYFDQNP ISQIGIIVTK SKRAEKLTEL 

       130        140        150        160        170        180 
SGNPRKHITS LKKAVDMTCH GEPSLYNSLS IAMQTLKHMP GHTSREVLII FSSLTTCDPS 

       190        200        210        220        230        240 
NIYDLIKTLK AAKIRVSVIG LSAEVRVCTV LARETGGTYH VILDESHYKE LLTHHVSPPP 

       250        260        270        280        290        300 
ASSSSECSLI RMGFPQHTIA SLSDQDAKPS FSMAHLDGNT EPGLTLGGYF CPQCRAKYCE 

       310        320        330        340        350        360 
LPVECKICGL TLVSAPHLAR SYHHLFPLDA FQEIPLEEYN GERFCYGCQG ELKDQHVYVC 

       370        380        390 
AVCQNVFCVD CDVFVHDSLH CCPGCIHKIP APSGV 

« Hide

References

« Hide 'large scale' references
[1]"p44 and p34 subunits of the BTF2/TFIIH transcription factor have homologies with SSL1, a yeast protein involved in DNA repair."
Humbert S., van Vuuren H.A., Lutz Y., Hoeijmakers J.H.J., Egly J.-M., Moncollin V.
EMBO J. 13:2393-2398(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-40; 46-54; 60-68; 117-125 AND 214-229.
[2]Zhang Q., Huang Q., Song H., Peng J., Fu G., Mao M., Dai M., Mao Y., Zhou J., Chen Z., Chen J.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pituitary tumor.
[3]"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.
[4]"A provisional transcript map of the spinal muscular atrophy (SMA) critical region."
van der Steege G., Draaijers T.G., Grootscholten P.M., Osinga J., Anzevino R., Velona I., Den Dunnen J.T., Scheffer H., Brahe C., van Ommen G.J.B., Buys C.H.C.M.
Eur. J. Hum. Genet. 3:87-95(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-130 AND 327-395.
Tissue: Pre-B cell.
[5]"Sequence of a 131-kb region of 5q13.1 containing the spinal muscular atrophy candidate genes SMN and NAIP."
Chen Q., Baird S.D., Mahadevan M., Besner-Johnston A., Farahani R., Xuan J.-Y., Kang X., Lefebvre C., Ikeda J.-E., Korneluk R.G., MacKenzie A.E.
Genomics 48:121-127(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 253-395.
Tissue: Brain.
[6]"Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes."
Kershnar E., Wu S.-Y., Chiang C.-M.
J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.
[7]"A role of the C-terminal part of p44 in the promoter escape activity of transcription factor IIH."
Tremeau-Bravard A., Perez C., Egly J.-M.
J. Biol. Chem. 276:27693-27697(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-291; CYS-308; CYS-345; CYS-360; CYS-363; HIS-376; HIS-380 AND CYS-382.
[8]"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.
[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].
[10]"A multicopy transcription-repair gene, BTF2p44, maps to the SMA region and demonstrates SMA associated deletions."
Carter T.A., Bonnemann C.G., Wang C.H., Obici S., Parano E., Bonaldo M.F., Ross B.M., Penchaszadeh G.K., Mackenzie A.E., Soares M.B., Kunkel L.M., Gilliam T.C.
Hum. Mol. Genet. 6:229-236(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MET-151 AND LEU-236.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS44454.
RefSeqNP_001506.1. NM_001515.3.
XP_005248541.1. XM_005248484.1.
XP_005276841.1. XM_005276784.1.
XP_005276843.1. XM_005276786.2.
UniGeneHs.191356.
Hs.422901.
Hs.607501.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Z60NMR-A328-386[»]
ProteinModelPortalQ13888.
SMRQ13888. Positions 328-386.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109221. 15 interactions.
DIPDIP-786N.
IntActQ13888. 4 interactions.
MINTMINT-3028823.
STRING9606.ENSP00000274400.

PTM databases

PhosphoSiteQ13888.

Polymorphism databases

DMDM17380326.

Proteomic databases

PaxDbQ13888.
PRIDEQ13888.

Protocols and materials databases

DNASU2966.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000274400; ENSP00000274400; ENSG00000145736. [Q13888-1]
ENST00000330280; ENSP00000328901; ENSG00000145736. [Q13888-1]
ENST00000573143; ENSP00000458297; ENSG00000262169. [Q13888-1]
ENST00000575673; ENSP00000459636; ENSG00000262169. [Q13888-1]
GeneID2966.
728340.
KEGGhsa:2966.
hsa:728340.
UCSCuc003kau.4. human. [Q13888-1]

Organism-specific databases

CTD2966.
728340.
GeneCardsGC05M070366.
HGNCHGNC:4656. GTF2H2.
MIM601748. gene.
neXtProtNX_Q13888.
PharmGKBPA29042.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5151.
HOGENOMHOG000159415.
HOVERGENHBG059468.
InParanoidQ13888.
KOK03142.
OMANCPGCES.
PhylomeDBQ13888.
TreeFamTF314037.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_216. DNA Repair.
REACT_71. Gene Expression.

Gene expression databases

BgeeQ13888.
CleanExHS_GTF2H2.
GenevestigatorQ13888.

Family and domain databases

Gene3D3.40.50.410. 1 hit.
InterProIPR007198. Ssl1-like.
IPR004595. TFIIH_C1-like_dom.
IPR012170. TFIIH_SSL1/p44.
IPR002035. VWF_A.
IPR007087. Znf_C2H2.
[Graphical view]
PANTHERPTHR12695. PTHR12695. 1 hit.
PfamPF07975. C1_4. 1 hit.
PF04056. Ssl1. 1 hit.
[Graphical view]
PIRSFPIRSF015919. TFIIH_SSL1. 1 hit.
SMARTSM01047. C1_4. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF53300. SSF53300. 1 hit.
TIGRFAMsTIGR00622. ssl1. 1 hit.
PROSITEPS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13888.
GeneWikiGTF2H2.
NextBio11756.
PROQ13888.
SOURCESearch...

Entry information

Entry nameTF2H2_HUMAN
AccessionPrimary (citable) accession number: Q13888
Secondary accession number(s): Q15570, Q15571, Q9BS41
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 151 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 5

Human chromosome 5: entries, gene names and cross-references to MIM