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Protein

General transcription factor IIH subunit 5

Gene

GTF2H5

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

Functioni

Component of the TFIIH basal transcription factor involved in nucleotide excision repair (NER) of DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. Necessary for the stability of the TFIIH complex and for the presence of normal levels of TFIIH in the cell.1 Publication

GO - Molecular functioni

  1. rDNA binding Source: Ensembl

GO - Biological processi

  1. cellular response to gamma radiation Source: Ensembl
  2. nucleotide-excision repair Source: MGI
  3. nucleotide-excision repair, preincision complex assembly Source: Ensembl
  4. regulation of transcription, DNA-templated Source: UniProtKB-KW
  5. rRNA processing Source: Ensembl
  6. transcription elongation from RNA polymerase I promoter Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
General transcription factor IIH subunit 5
Alternative name(s):
General transcription factor IIH polypeptide 5
TFB5 ortholog
TFIIH basal transcription factor complex TTD-A subunit
Gene namesi
Name:GTF2H5
Synonyms:C6orf175, TTDA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:21157. GTF2H5.

Subcellular locationi

  1. Nucleus 1 Publication

GO - Cellular componenti

  1. core TFIIH complex Source: InterPro
  2. nucleolus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Trichothiodystrophy photosensitive (TTDP)

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionTTDP is an autosomal recessive disease characterized by sulfur-deficient brittle hair and nails, ichthyosis, mental retardation, impaired sexual development, abnormal facies and cutaneous photosensitivity correlated with a nucleotide excision repair (NER) defect. Neonates with trichothiodystrophy and ichthyosis are usually born with a collodion membrane. The severity of the ichthyosis after the membrane is shed is variable, ranging from a mild to severe lamellar ichthyotic phenotype. There are no reports of skin cancer associated with TTDP.

See also OMIM:601675
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211L → P in TTDP. 1 Publication
VAR_022647

Keywords - Diseasei

Disease mutation, Ichthyosis

Organism-specific databases

MIMi601675. phenotype.
Orphaneti33364. Trichothiodystrophy.
PharmGKBiPA134962077.

Polymorphism and mutation databases

BioMutaiGTF2H5.
DMDMi67462047.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7171General transcription factor IIH subunit 5PRO_0000119256Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei69 – 691Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ6ZYL4.
PaxDbiQ6ZYL4.
PRIDEiQ6ZYL4.

PTM databases

PhosphoSiteiQ6ZYL4.

Expressioni

Gene expression databases

BgeeiQ6ZYL4.
CleanExiHS_GTF2H5.
GenevestigatoriQ6ZYL4.

Organism-specific databases

HPAiCAB037029.
CAB037042.

Interactioni

Subunit structurei

Subunit of the TFIIH basal transcription factor complex that contains ERCC2, ERCC3, GTF2H1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, MNAT1, CDK7 and CCNH.

Protein-protein interaction databases

BioGridi135676. 5 interactions.
DIPiDIP-29188N.
IntActiQ6ZYL4. 1 interaction.
STRINGi9606.ENSP00000356067.

Structurei

Secondary structure

1
71
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 114Combined sources
Helixi14 – 2512Combined sources
Turni26 – 294Combined sources
Beta strandi34 – 374Combined sources
Beta strandi39 – 457Combined sources
Helixi49 – 5911Combined sources
Turni60 – 623Combined sources
Turni65 – 706Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YDLX-ray2.30A3-71[»]
2JNJNMR-A/B1-71[»]
ProteinModelPortaliQ6ZYL4.
SMRiQ6ZYL4. Positions 1-71.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6ZYL4.

Family & Domainsi

Sequence similaritiesi

Belongs to the TFB5 family.Curated

Phylogenomic databases

eggNOGiNOG278168.
GeneTreeiENSGT00390000004028.
HOVERGENiHBG055393.
InParanoidiQ6ZYL4.
KOiK10845.
OMAiVEQIMEN.
OrthoDBiEOG7BGHPM.
PhylomeDBiQ6ZYL4.
TreeFamiTF319487.

Family and domain databases

Gene3Di3.30.70.1220. 1 hit.
InterProiIPR009400. TFIIH_TTDA/Tfb5.
[Graphical view]
PfamiPF06331. Tbf5. 1 hit.
[Graphical view]
SUPFAMiSSF142897. SSF142897. 1 hit.

Sequencei

Sequence statusi: Complete.

Q6ZYL4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVNVLKGVLI ECDPAMKQFL LYLDESNALG KKFIIQDIDD THVFVIAELV
60 70
NVLQERVGEL MDQNAFSLTQ K
Length:71
Mass (Da):8,053
Last modified:July 5, 2004 - v1
Checksum:iDBEB4D3C9BFA2C54
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211L → P in TTDP. 1 Publication
VAR_022647

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ634743 mRNA. Translation: CAG25512.1.
AL590703 Genomic DNA. Translation: CAH70241.1.
BC056906 mRNA. Translation: AAH56906.1.
BC060317 mRNA. Translation: AAH60317.1.
CCDSiCCDS5256.1.
RefSeqiNP_997001.1. NM_207118.2.
UniGeneiHs.356224.

Genome annotation databases

EnsembliENST00000607778; ENSP00000476100; ENSG00000272047.
GeneIDi404672.
KEGGihsa:404672.
UCSCiuc003qrd.3. human.

Polymorphism and mutation databases

BioMutaiGTF2H5.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ634743 mRNA. Translation: CAG25512.1.
AL590703 Genomic DNA. Translation: CAH70241.1.
BC056906 mRNA. Translation: AAH56906.1.
BC060317 mRNA. Translation: AAH60317.1.
CCDSiCCDS5256.1.
RefSeqiNP_997001.1. NM_207118.2.
UniGeneiHs.356224.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YDLX-ray2.30A3-71[»]
2JNJNMR-A/B1-71[»]
ProteinModelPortaliQ6ZYL4.
SMRiQ6ZYL4. Positions 1-71.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi135676. 5 interactions.
DIPiDIP-29188N.
IntActiQ6ZYL4. 1 interaction.
STRINGi9606.ENSP00000356067.

PTM databases

PhosphoSiteiQ6ZYL4.

Polymorphism and mutation databases

BioMutaiGTF2H5.
DMDMi67462047.

Proteomic databases

MaxQBiQ6ZYL4.
PaxDbiQ6ZYL4.
PRIDEiQ6ZYL4.

Protocols and materials databases

DNASUi404672.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000607778; ENSP00000476100; ENSG00000272047.
GeneIDi404672.
KEGGihsa:404672.
UCSCiuc003qrd.3. human.

Organism-specific databases

CTDi404672.
GeneCardsiGC06P158509.
HGNCiHGNC:21157. GTF2H5.
HPAiCAB037029.
CAB037042.
MIMi601675. phenotype.
608780. gene.
neXtProtiNX_Q6ZYL4.
Orphaneti33364. Trichothiodystrophy.
PharmGKBiPA134962077.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG278168.
GeneTreeiENSGT00390000004028.
HOVERGENiHBG055393.
InParanoidiQ6ZYL4.
KOiK10845.
OMAiVEQIMEN.
OrthoDBiEOG7BGHPM.
PhylomeDBiQ6ZYL4.
TreeFamiTF319487.

Miscellaneous databases

EvolutionaryTraceiQ6ZYL4.
GeneWikiiGTF2H5.
GenomeRNAii404672.
NextBioi107889.
PROiQ6ZYL4.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZYL4.
CleanExiHS_GTF2H5.
GenevestigatoriQ6ZYL4.

Family and domain databases

Gene3Di3.30.70.1220. 1 hit.
InterProiIPR009400. TFIIH_TTDA/Tfb5.
[Graphical view]
PfamiPF06331. Tbf5. 1 hit.
[Graphical view]
SUPFAMiSSF142897. SSF142897. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A and stabilizes TFIIH."
    Giglia-Mari G., Coin F., Ranish J.A., Hoogstraten D., Theil A., Wijgers N., Jaspers N.G.J., Raams A., Argentini M., van der Spek P.J., Botta E., Stefanini M., Egly J.-M., Aebersold R., Hoeijmakers J.H.J., Vermeulen W.
    Nat. Genet. 36:714-719(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-21, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH THE TFIIH COMPLEX.
    Tissue: Fibroblast.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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: Adrenal cortex and Liver.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  5. "Crystal structure of the human TFIIH."
    Northeast structural genomics consortium (NESG)
    Submitted (FEB-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 6-71.

Entry informationi

Entry nameiTF2H5_HUMAN
AccessioniPrimary (citable) accession number: Q6ZYL4
Secondary accession number(s): Q0P5V8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 5, 2004
Last modified: April 29, 2015
This is version 110 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, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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

External Data

Dasty 3

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 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.