GTF2H5

Protein-coding gene in the species Homo sapiens

GTF2H5

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
1YDL, 2JNJ, 5IY8, 5IY6, 5IY7, 5IVW, 5IY9

Identifiers

Aliases

GTF2H5, C6orf175, TFB5, TFIIH, TGF2H5, TTD, TTD-A, TTDA, bA120J8.2, TTD3, general transcription factor IIH subunit 5

External IDs

OMIM: 608780; MGI: 107227; HomoloGene: 45635; GeneCards: GTF2H5; OMA:GTF2H5 - orthologs

Gene location (Human)

Chr.	Chromosome 6 (human)^[1]

Band	6q25.3	Start	158,168,350 bp^[1]
Band	6q25.3	End	158,199,344 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 17 (mouse)^[2]

Band	17 A1\|17 3.7 cM	Start	6,130,061 bp^[2]
Band	17 A1\|17 3.7 cM	End	6,136,792 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

renal medulla

superior surface of tongue

saphenous vein

vena cava

pericardium

trigeminal ganglion

mucosa of pharynx

pons

body of tongue

external globus pallidus

Top expressed in

hand

endocardial cushion

morula

otic vesicle

otolith organ

hair follicle

utricle

atrioventricular valve

medial ganglionic eminence

abdominal wall

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	rDNA binding protein binding
Cellular component	nucleoplasm nucleolus transcription factor TFIIH core complex nucleus transcription factor TFIID complex transcription factor TFIIH holo complex
Biological process	termination of RNA polymerase I transcription regulation of transcription, DNA-templated transcription initiation from RNA polymerase I promoter transcription elongation from RNA polymerase II promoter 7-methylguanosine mRNA capping transcription by RNA polymerase II transcription, DNA-templated cellular response to DNA damage stimulus global genome nucleotide-excision repair cellular response to gamma radiation rRNA processing transcription-coupled nucleotide-excision repair transcription initiation from RNA polymerase II promoter nucleotide-excision repair, DNA incision nucleotide-excision repair, preincision complex assembly nucleotide-excision repair nucleotide-excision repair, DNA incision, 5'-to lesion DNA repair nucleotide-excision repair, preincision complex stabilization transcription elongation from RNA polymerase I promoter phosphorylation of RNA polymerase II C-terminal domain nucleotide-excision repair, DNA duplex unwinding nucleotide-excision repair, DNA incision, 3'-to lesion
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


404672


66467

Ensembl


ENSG00000272047


ENSMUSG00000034345

UniProt


Q6ZYL4


Q8K2X8

RefSeq (mRNA)


NM_207118


NM_181392 NM_001357804

RefSeq (protein)


NP_997001


NP_852057 NP_001344733

Location (UCSC)

Chr 6: 158.17 – 158.2 Mb

Chr 17: 6.13 – 6.14 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

General transcription factor IIH subunit 5 is a protein that in humans is encoded by the GTF2H5 gene.^[5]^[6]

Function

The GTF2H5(TTDA) gene encodes a small (71 amino acid) protein that stabilizes the multi-subunit transcription repair factor IIH(TFIIH). TFIIH plays a key role in a major DNA repair process, nucleotide excision repair (NER), by opening the DNA double helix after the initial recognition of damage in one strand. This step is followed by excision of the damaged region to generate a single-strand gap, and then repair synthesis, using the undamaged strand as template, to accurately fill in the gap. Disruption of the GTF2H5(TTDA) gene in a knockout mouse-model completely inactivates NER.^[7] In humans, mutation in any one of four genes can give rise to the trichothiodystrophy phenotype. These genes are TTDN1, XPB, XPD and GTF2H5(TTDA).^[7]

Interactions

GTF2H5 has been shown to interact with GTF2H2^[5]^[8] and XPB.^[5]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000272047 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000034345 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b ^c Giglia-Mari G, Coin F, Ranish JA, Hoogstraten D, Theil A, Wijgers N, Jaspers NG, Raams A, Argentini M, van der Spek PJ, Botta E, Stefanini M, Egly JM, Aebersold R, Hoeijmakers JH, Vermeulen W (June 2004). "A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A". Nat. Genet. 36 (7): 714–9. doi:10.1038/ng1387. PMID 15220921.
^ "Entrez Gene: GTF2H5 general transcription factor IIH, polypeptide 5".
^ ^a ^b Theil AF, Hoeijmakers JH, Vermeulen W (2014). "TTDA: big impact of a small protein". Exp. Cell Res. 329 (1): 61–8. doi:10.1016/j.yexcr.2014.07.008. PMID 25016283.
^ Vermeulen W, Bergmann E, Auriol J, Rademakers S, Frit P, Appeldoorn E, Hoeijmakers JH, Egly JM (November 2000). "Sublimiting concentration of TFIIH transcription/DNA repair factor causes TTD-A trichothiodystrophy disorder". Nat. Genet. 26 (3): 307–13. doi:10.1038/81603. PMID 11062469. S2CID 25233797.

Vermeulen W, Bergmann E, Auriol J, Rademakers S, Frit P, Appeldoorn E, Hoeijmakers JH, Egly JM (2000). "Sublimiting concentration of TFIIH transcription/DNA repair factor causes TTD-A trichothiodystrophy disorder". Nat. Genet. 26 (3): 307–13. doi:10.1038/81603. PMID 11062469. S2CID 25233797.
Coin F, Proietti De Santis L, Nardo T, Zlobinskaya O, Stefanini M, Egly JM (2006). "p8/TTD-A as a repair-specific TFIIH subunit". Mol. Cell. 21 (2): 215–26. doi:10.1016/j.molcel.2005.10.024. PMID 16427011.
Giglia-Mari G, Miquel C, Theil AF, Mari PO, Hoogstraten D, Ng JM, Dinant C, Hoeijmakers JH, Vermeulen W (2006). "Dynamic interaction of TTDA with TFIIH is stabilized by nucleotide excision repair in living cells". PLOS Biol. 4 (6): e156. doi:10.1371/journal.pbio.0040156. PMC 1457016. PMID 16669699.
Vitorino M, Coin F, Zlobinskaya O, Atkinson RA, Moras D, Egly JM, Poterszman A, Kieffer B (2007). "Solution structure and self-association properties of the p8 TFIIH subunit responsible for trichothiodystrophy". J. Mol. Biol. 368 (2): 473–80. doi:10.1016/j.jmb.2007.02.020. PMID 17350038.