TF2H5_HUMAN
ID TF2H5_HUMAN Reviewed; 71 AA.
AC Q6ZYL4; Q0P5V8;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=General transcription factor IIH subunit 5;
DE AltName: Full=General transcription factor IIH polypeptide 5;
DE AltName: Full=TFB5 ortholog {ECO:0000303|PubMed:15220921};
DE AltName: Full=TFIIH basal transcription factor complex TTD-A subunit {ECO:0000303|PubMed:15220921};
DE AltName: Full=TFIIH subunit p8 {ECO:0000305|PubMed:15220921};
GN Name=GTF2H5 {ECO:0000312|HGNC:HGNC:21157}; Synonyms=C6orf175, TTDA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT TTD3 PRO-21, IDENTIFICATION BY MASS
RP SPECTROMETRY, SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH THE TFIIH
RP COMPLEX, AND INVOLVEMENT IN TTD3.
RC TISSUE=Fibroblast;
RX PubMed=15220921; DOI=10.1038/ng1387;
RA Giglia-Mari G., Coin F., Ranish J.A., Hoogstraten D., Theil A., Wijgers N.,
RA Jaspers N.G.J., Raams A., Argentini M., van der Spek P.J., Botta E.,
RA Stefanini M., Egly J.-M., Aebersold R., Hoeijmakers J.H.J., Vermeulen W.;
RT "A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome
RT trichothiodystrophy group A and stabilizes TFIIH.";
RL Nat. Genet. 36:714-719(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal cortex, and Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 6-71.
RG Northeast structural genomics consortium (NESG);
RT "Crystal structure of the human TFIIH.";
RL Submitted (FEB-2005) to the PDB data bank.
CC -!- FUNCTION: Component of the general transcription and DNA repair factor
CC IIH (TFIIH) core complex, which is involved in general and
CC transcription-coupled nucleotide excision repair (NER) of damaged DNA
CC and, when complexed to CAK, in RNA transcription by RNA polymerase II.
CC In NER, TFIIH acts by opening DNA around the lesion to allow the
CC excision of the damaged oligonucleotide and its replacement by a new
CC DNA fragment. In transcription, TFIIH has an essential role in
CC transcription initiation. When the pre-initiation complex (PIC) has
CC been established, TFIIH is required for promoter opening and promoter
CC escape. Phosphorylation of the C-terminal tail (CTD) of the largest
CC subunit of RNA polymerase II by the kinase module CAK controls the
CC initiation of transcription. Necessary for the stability of the TFIIH
CC complex and for the presence of normal levels of TFIIH in the cell.
CC {ECO:0000269|PubMed:15220921}.
CC -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2, GTF2H3, GTF2H4 and GTF2H5, which
CC is active in NER. The core complex associates with the 3-subunit CDK-
CC activating kinase (CAK) module composed of CCNH/cyclin H, CDK7 and
CC MNAT1 to form the 10-subunit holoenzyme (holo-TFIIH) active in
CC transcription. {ECO:0000269|PubMed:15220921}.
CC -!- INTERACTION:
CC Q6ZYL4; O95994: AGR2; NbExp=3; IntAct=EBI-6380438, EBI-712648;
CC Q6ZYL4; Q8N6D5: ANKRD29; NbExp=3; IntAct=EBI-6380438, EBI-17439331;
CC Q6ZYL4; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-6380438, EBI-742054;
CC Q6ZYL4; P19447: ERCC3; NbExp=4; IntAct=EBI-6380438, EBI-1183307;
CC Q6ZYL4; O15499: GSC2; NbExp=3; IntAct=EBI-6380438, EBI-19954058;
CC Q6ZYL4; Q13888: GTF2H2; NbExp=4; IntAct=EBI-6380438, EBI-1565170;
CC Q6ZYL4; Q92759: GTF2H4; NbExp=9; IntAct=EBI-6380438, EBI-6380495;
CC Q6ZYL4; Q0VD86: INCA1; NbExp=3; IntAct=EBI-6380438, EBI-6509505;
CC Q6ZYL4; Q9NPE2: NGRN; NbExp=3; IntAct=EBI-6380438, EBI-2683432;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15220921}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8K2X8}.
CC -!- DISEASE: Trichothiodystrophy 3, photosensitive (TTD3) [MIM:616395]: A
CC form of trichothiodystrophy, an autosomal recessive disease
CC characterized by sulfur-deficient brittle hair and multisystem variable
CC abnormalities. The spectrum of clinical features varies from mild
CC disease with only hair involvement to severe disease with cutaneous,
CC neurologic and profound developmental defects. Ichthyosis, intellectual
CC and developmental disabilities, decreased fertility, abnormal
CC characteristics at birth, ocular abnormalities, short stature, and
CC infections are common manifestations. There are both photosensitive and
CC non-photosensitive forms of the disorder.
CC {ECO:0000269|PubMed:15220921}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TFB5 family. {ECO:0000305}.
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DR EMBL; AJ634743; CAG25512.1; -; mRNA.
DR EMBL; AL590703; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC056906; AAH56906.1; -; mRNA.
DR EMBL; BC060317; AAH60317.1; -; mRNA.
DR CCDS; CCDS5256.1; -.
DR RefSeq; NP_997001.1; NM_207118.2.
DR PDB; 1YDL; X-ray; 2.30 A; A=3-71.
DR PDB; 2JNJ; NMR; -; A/B=1-71.
DR PDB; 5IVW; EM; 10.00 A; 1=1-71.
DR PDB; 5IY6; EM; 7.20 A; 1=1-71.
DR PDB; 5IY7; EM; 8.60 A; 1=1-71.
DR PDB; 5IY8; EM; 7.90 A; 1=1-71.
DR PDB; 5IY9; EM; 6.30 A; 1=1-71.
DR PDB; 5OF4; EM; 4.40 A; G=1-71.
DR PDB; 6NMI; EM; 3.70 A; G=1-71.
DR PDB; 6O9L; EM; 7.20 A; 5=1-71.
DR PDB; 6O9M; EM; 4.40 A; 5=1-71.
DR PDB; 6RO4; EM; 3.50 A; F=1-71.
DR PDB; 7AD8; EM; 3.50 A; F=1-71.
DR PDB; 7EGB; EM; 3.30 A; 5=1-71.
DR PDB; 7EGC; EM; 3.90 A; 5=1-71.
DR PDB; 7ENA; EM; 4.07 A; 5=1-71.
DR PDB; 7ENC; EM; 4.13 A; 5=1-71.
DR PDB; 7LBM; EM; 4.80 A; c=1-71.
DR PDB; 7NVR; EM; 4.50 A; 5=1-71.
DR PDB; 7NVV; EM; 2.90 A; 5=1-71.
DR PDB; 7NVW; EM; 4.30 A; 5=1-71.
DR PDB; 7NVX; EM; 3.90 A; 5=1-71.
DR PDB; 7NVY; EM; 7.30 A; 5=1-71.
DR PDB; 7NVZ; EM; 7.20 A; 5=1-71.
DR PDB; 7NW0; EM; 6.60 A; 5=1-71.
DR PDBsum; 1YDL; -.
DR PDBsum; 2JNJ; -.
DR PDBsum; 5IVW; -.
DR PDBsum; 5IY6; -.
DR PDBsum; 5IY7; -.
DR PDBsum; 5IY8; -.
DR PDBsum; 5IY9; -.
DR PDBsum; 5OF4; -.
DR PDBsum; 6NMI; -.
DR PDBsum; 6O9L; -.
DR PDBsum; 6O9M; -.
DR PDBsum; 6RO4; -.
DR PDBsum; 7AD8; -.
DR PDBsum; 7EGB; -.
DR PDBsum; 7EGC; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR PDBsum; 7NVV; -.
DR PDBsum; 7NVW; -.
DR PDBsum; 7NVX; -.
DR PDBsum; 7NVY; -.
DR PDBsum; 7NVZ; -.
DR PDBsum; 7NW0; -.
DR AlphaFoldDB; Q6ZYL4; -.
DR SMR; Q6ZYL4; -.
DR BioGRID; 135676; 29.
DR CORUM; Q6ZYL4; -.
DR DIP; DIP-29188N; -.
DR IntAct; Q6ZYL4; 24.
DR MINT; Q6ZYL4; -.
DR STRING; 9606.ENSP00000476100; -.
DR iPTMnet; Q6ZYL4; -.
DR MetOSite; Q6ZYL4; -.
DR PhosphoSitePlus; Q6ZYL4; -.
DR BioMuta; GTF2H5; -.
DR DMDM; 67462047; -.
DR EPD; Q6ZYL4; -.
DR jPOST; Q6ZYL4; -.
DR MassIVE; Q6ZYL4; -.
DR MaxQB; Q6ZYL4; -.
DR PaxDb; Q6ZYL4; -.
DR PeptideAtlas; Q6ZYL4; -.
DR PRIDE; Q6ZYL4; -.
DR ProteomicsDB; 68501; -.
DR TopDownProteomics; Q6ZYL4; -.
DR Antibodypedia; 70683; 90 antibodies from 19 providers.
DR DNASU; 404672; -.
DR Ensembl; ENST00000607778.2; ENSP00000476100.1; ENSG00000272047.4.
DR Ensembl; ENST00000689809.1; ENSP00000510752.1; ENSG00000272047.4.
DR Ensembl; ENST00000691867.1; ENSP00000510706.1; ENSG00000272047.4.
DR GeneID; 404672; -.
DR KEGG; hsa:404672; -.
DR MANE-Select; ENST00000607778.2; ENSP00000476100.1; NM_207118.3; NP_997001.1.
DR UCSC; uc003qrd.4; human.
DR CTD; 404672; -.
DR DisGeNET; 404672; -.
DR GeneCards; GTF2H5; -.
DR HGNC; HGNC:21157; GTF2H5.
DR HPA; ENSG00000272047; Low tissue specificity.
DR MalaCards; GTF2H5; -.
DR MIM; 608780; gene.
DR MIM; 616395; phenotype.
DR neXtProt; NX_Q6ZYL4; -.
DR OpenTargets; ENSG00000272047; -.
DR Orphanet; 33364; Trichothiodystrophy.
DR PharmGKB; PA134962077; -.
DR VEuPathDB; HostDB:ENSG00000272047; -.
DR eggNOG; KOG3451; Eukaryota.
DR GeneTree; ENSGT00390000004028; -.
DR HOGENOM; CLU_166246_4_0_1; -.
DR InParanoid; Q6ZYL4; -.
DR OMA; IMENMNP; -.
DR OrthoDB; 1591321at2759; -.
DR PhylomeDB; Q6ZYL4; -.
DR TreeFam; TF319487; -.
DR PathwayCommons; Q6ZYL4; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-72086; mRNA Capping.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR SignaLink; Q6ZYL4; -.
DR BioGRID-ORCS; 404672; 69 hits in 1093 CRISPR screens.
DR ChiTaRS; GTF2H5; human.
DR EvolutionaryTrace; Q6ZYL4; -.
DR GeneWiki; GTF2H5; -.
DR GenomeRNAi; 404672; -.
DR Pharos; Q6ZYL4; Tbio.
DR PRO; PR:Q6ZYL4; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q6ZYL4; protein.
DR Bgee; ENSG00000272047; Expressed in renal medulla and 217 other tissues.
DR ExpressionAtlas; Q6ZYL4; baseline and differential.
DR Genevisible; Q6ZYL4; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005669; C:transcription factor TFIID complex; IDA:UniProtKB.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; IBA:GO_Central.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IBA:GO_Central.
DR GO; GO:0071480; P:cellular response to gamma radiation; IEA:Ensembl.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:Ensembl.
DR GO; GO:0006289; P:nucleotide-excision repair; IMP:MGI.
DR GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; IBA:GO_Central.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IEA:Ensembl.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:InterPro.
DR Gene3D; 3.30.70.1220; -; 1.
DR InterPro; IPR035935; TFB5-like_sf.
DR InterPro; IPR009400; TFIIH_TTDA/Tfb5.
DR PANTHER; PTHR28580; PTHR28580; 1.
DR Pfam; PF06331; Tfb5; 1.
DR SMART; SM01395; Tbf5; 1.
DR SUPFAM; SSF142897; SSF142897; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disease variant; DNA damage; DNA repair;
KW Ichthyosis; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..71
FT /note="General transcription factor IIH subunit 5"
FT /id="PRO_0000119256"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VARIANT 21
FT /note="L -> P (in TTD3; dbSNP:rs121434365)"
FT /evidence="ECO:0000269|PubMed:15220921"
FT /id="VAR_022647"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:1YDL"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1YDL"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:1YDL"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1YDL"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1YDL"
FT HELIX 49..59
FT /evidence="ECO:0007829|PDB:1YDL"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2JNJ"
FT TURN 65..70
FT /evidence="ECO:0007829|PDB:1YDL"
SQ SEQUENCE 71 AA; 8053 MW; DBEB4D3C9BFA2C54 CRC64;
MVNVLKGVLI ECDPAMKQFL LYLDESNALG KKFIIQDIDD THVFVIAELV NVLQERVGEL
MDQNAFSLTQ K
