ID TF2H4_HUMAN Reviewed; 462 AA. AC Q92759; B4DTJ5; Q76KU4; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 201. DE RecName: Full=General transcription factor IIH subunit 4; DE AltName: Full=Basic transcription factor 2 52 kDa subunit; DE Short=BTF2 p52; DE AltName: Full=General transcription factor IIH polypeptide 4; DE AltName: Full=TFIIH basal transcription factor complex p52 subunit; GN Name=GTF2H4; 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] (ISOFORM 1). RC TISSUE=Pre-B cell; RX PubMed=9118947; DOI=10.1093/emboj/16.5.1093; RA Marinoni J.-C., Roy R., Vermeulen W., Miniou P., Lutz Y., Weeda G., RA Seroz T., Molina Gomez D., Hoeijmakers J.H.J., Egly J.-M.; RT "Cloning and characterization of p52, the fifth subunit of the core of the RT transcription/DNA repair factor TFIIH."; RL EMBO J. 16:1093-1102(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Shiina S., Tamiya G., Oka A., Inoko H.; RT "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-337. RG NIEHS SNPs program; RL Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Peripheral blood leukocyte; RX PubMed=16702430; DOI=10.1534/genetics.106.057034; RA Shiina T., Ota M., Shimizu S., Katsuyama Y., Hashimoto N., Takasu M., RA Anzai T., Kulski J.K., Kikkawa E., Naruse T., Kimura N., Yanagiya K., RA Watanabe A., Hosomichi K., Kohara S., Iwamoto C., Umehara Y., Meyer A., RA Wanner V., Sano K., Macquin C., Ikeo K., Tokunaga K., Gojobori T., RA Inoko H., Bahram S.; RT "Rapid evolution of major histocompatibility complex class I genes in RT primates generates new disease alleles in humans via hitchhiking RT diversity."; RL Genetics 173:1555-1570(2006). RN [7] 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin, and Uterus; 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 [10] RP IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR. RX PubMed=9852112; DOI=10.1074/jbc.273.51.34444; RA Kershnar E., Wu S.-Y., Chiang C.-M.; RT "Immunoaffinity purification and functional characterization of human RT transcription factor IIH and RNA polymerase II from clonal cell lines that RT conditionally express epitope-tagged subunits of the multiprotein RT complexes."; RL J. Biol. Chem. 273:34444-34453(1998). RN [11] RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), AND SUBUNIT. RX PubMed=27193682; DOI=10.1038/nature17970; RA He Y., Yan C., Fang J., Inouye C., Tjian R., Ivanov I., Nogales E.; RT "Near-atomic resolution visualization of human transcription promoter RT opening."; RL Nature 533:359-365(2016). 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. {ECO:0000269|PubMed:9852112}. 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 (PubMed:9852112). Part of TBP-based Pol II pre-initiation CC complex (PIC), in which Pol II core assembles with general CC transcription factors and other specific initiation factors including CC GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1, ERCC2, ERCC3, GTF2H2, GTF2H3, CC GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and TBP; this large multi-subunit CC PIC complex mediates DNA unwinding and targets Pol II core to the CC transcription start site where the first phosphodiester bond forms CC (PubMed:27193682). {ECO:0000269|PubMed:27193682, CC ECO:0000269|PubMed:9852112}. CC -!- INTERACTION: CC Q92759; Q96JC9: EAF1; NbExp=3; IntAct=EBI-6380495, EBI-769261; CC Q92759; Q8N9N8: EIF1AD; NbExp=3; IntAct=EBI-6380495, EBI-750700; CC Q92759; Q6ZYL4: GTF2H5; NbExp=9; IntAct=EBI-6380495, EBI-6380438; CC Q92759; Q8N9Q2: SREK1IP1; NbExp=3; IntAct=EBI-6380495, EBI-10268630; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q92759-1; Sequence=Displayed; CC Name=2; CC IsoId=Q92759-2; Sequence=VSP_056835, VSP_056836, VSP_056837; CC -!- SIMILARITY: Belongs to the TFB2 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/gtf2h4/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y07595; CAA68870.1; -; mRNA. DR EMBL; BA000025; BAB63317.1; -; Genomic_DNA. DR EMBL; BT007321; AAP35985.1; -; mRNA. DR EMBL; AY124590; AAM64222.1; -; Genomic_DNA. DR EMBL; AB088103; BAC54936.1; -; Genomic_DNA. DR EMBL; AB202101; BAE78622.1; -; Genomic_DNA. DR EMBL; AB103609; BAF31271.1; -; Genomic_DNA. DR EMBL; AK300239; BAG62007.1; -; mRNA. DR EMBL; AL662870; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL669830; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL773541; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BX927194; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR759747; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CR936875; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471081; EAX03347.1; -; Genomic_DNA. DR EMBL; BC004935; AAH04935.1; -; mRNA. DR EMBL; BC016302; AAH16302.1; -; mRNA. DR CCDS; CCDS34386.1; -. [Q92759-1] DR RefSeq; NP_001508.1; NM_001517.4. [Q92759-1] DR PDB; 5IVW; EM; 10.00 A; 2=1-462. DR PDB; 5IY6; EM; 7.20 A; 2=1-462. DR PDB; 5IY7; EM; 8.60 A; 2=1-462. DR PDB; 5IY8; EM; 7.90 A; 2=1-462. DR PDB; 5IY9; EM; 6.30 A; 2=1-462. DR PDB; 5OF4; EM; 4.40 A; D=383-462. DR PDB; 6NMI; EM; 3.70 A; D=1-462. DR PDB; 6O9L; EM; 7.20 A; 2=1-462. DR PDB; 6O9M; EM; 4.40 A; 2=1-462. DR PDB; 6RO4; EM; 3.50 A; C=1-462. DR PDB; 7AD8; EM; 3.50 A; C=1-462. DR PDB; 7EGB; EM; 3.30 A; 4=1-462. DR PDB; 7EGC; EM; 3.90 A; 4=1-462. DR PDB; 7ENA; EM; 4.07 A; 4=1-462. DR PDB; 7ENC; EM; 4.13 A; 4=1-462. DR PDB; 7LBM; EM; 4.80 A; Z=1-462. DR PDB; 7NVR; EM; 4.50 A; 2=1-462. DR PDB; 7NVV; EM; 2.90 A; 2=1-462. DR PDB; 7NVW; EM; 4.30 A; 2=1-462. DR PDB; 7NVX; EM; 3.90 A; 2=1-462. DR PDB; 7NVY; EM; 7.30 A; 2=1-462. DR PDB; 7NVZ; EM; 7.20 A; 2=1-462. DR PDB; 7NW0; EM; 6.60 A; 2=1-462. DR PDB; 8BVW; EM; 4.00 A; 3=1-462. DR PDB; 8BYQ; EM; 4.10 A; 3=1-462. DR PDB; 8EBS; EM; 4.00 A; D=1-462. DR PDB; 8EBT; EM; 3.90 A; D=17-462. DR PDB; 8EBU; EM; 3.30 A; D=1-462. DR PDB; 8EBV; EM; 7.10 A; D=1-462. DR PDB; 8EBW; EM; 5.60 A; D=1-462. DR PDB; 8EBX; EM; 3.60 A; D=1-462. DR PDB; 8EBY; EM; 3.60 A; D=1-462. DR PDB; 8GXQ; EM; 5.04 A; HC=1-462. DR PDB; 8GXS; EM; 4.16 A; HC=1-462. DR PDB; 8WAK; EM; 5.47 A; 4=1-462. DR PDB; 8WAL; EM; 8.52 A; 4=1-462. DR PDB; 8WAN; EM; 6.07 A; 4=1-462. DR PDB; 8WAO; EM; 6.40 A; 4=1-462. DR PDB; 8WAP; EM; 5.85 A; 4=1-462. DR PDB; 8WAQ; EM; 6.29 A; 4=1-462. DR PDB; 8WAR; EM; 7.20 A; 4=1-462. DR PDB; 8WAS; EM; 6.13 A; 4=1-462. 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 PDBsum; 8BVW; -. DR PDBsum; 8BYQ; -. DR PDBsum; 8EBS; -. DR PDBsum; 8EBT; -. DR PDBsum; 8EBU; -. DR PDBsum; 8EBV; -. DR PDBsum; 8EBW; -. DR PDBsum; 8EBX; -. DR PDBsum; 8EBY; -. DR PDBsum; 8GXQ; -. DR PDBsum; 8GXS; -. DR PDBsum; 8WAK; -. DR PDBsum; 8WAL; -. DR PDBsum; 8WAN; -. DR PDBsum; 8WAO; -. DR PDBsum; 8WAP; -. DR PDBsum; 8WAQ; -. DR PDBsum; 8WAR; -. DR PDBsum; 8WAS; -. DR AlphaFoldDB; Q92759; -. DR EMDB; EMD-0452; -. DR EMDB; EMD-16274; -. DR EMDB; EMD-16331; -. DR EMDB; EMD-23255; -. DR EMDB; EMD-27996; -. DR EMDB; EMD-27997; -. DR EMDB; EMD-27998; -. DR EMDB; EMD-27999; -. DR EMDB; EMD-28000; -. DR EMDB; EMD-28001; -. DR EMDB; EMD-28002; -. DR EMDB; EMD-29673; -. DR EMDB; EMD-29674; -. DR EMDB; EMD-31111; -. DR EMDB; EMD-3802; -. DR SMR; Q92759; -. DR BioGRID; 109223; 107. DR ComplexPortal; CPX-2395; General transcription factor TFIIH complex. DR CORUM; Q92759; -. DR DIP; DIP-48376N; -. DR IntAct; Q92759; 19. DR MINT; Q92759; -. DR STRING; 9606.ENSP00000259895; -. DR iPTMnet; Q92759; -. DR PhosphoSitePlus; Q92759; -. DR BioMuta; GTF2H4; -. DR DMDM; 17380328; -. DR EPD; Q92759; -. DR jPOST; Q92759; -. DR MassIVE; Q92759; -. DR MaxQB; Q92759; -. DR PaxDb; 9606-ENSP00000259895; -. DR PeptideAtlas; Q92759; -. DR ProteomicsDB; 5110; -. DR ProteomicsDB; 75447; -. [Q92759-1] DR Pumba; Q92759; -. DR TopDownProteomics; Q92759-1; -. [Q92759-1] DR Antibodypedia; 48243; 208 antibodies from 26 providers. DR DNASU; 2968; -. DR Ensembl; ENST00000259895.9; ENSP00000259895.4; ENSG00000213780.11. [Q92759-1] DR Ensembl; ENST00000376316.5; ENSP00000365493.2; ENSG00000213780.11. [Q92759-1] DR Ensembl; ENST00000376326.8; ENSP00000365504.4; ENSG00000221974.11. [Q92759-1] DR Ensembl; ENST00000400450.1; ENSP00000383300.1; ENSG00000221974.11. [Q92759-1] DR Ensembl; ENST00000413314.6; ENSP00000396251.2; ENSG00000236895.10. [Q92759-1] DR Ensembl; ENST00000416773.5; ENSP00000399554.1; ENSG00000234370.10. [Q92759-1] DR Ensembl; ENST00000423881.5; ENSP00000409483.1; ENSG00000236895.10. [Q92759-1] DR Ensembl; ENST00000434226.6; ENSP00000403156.2; ENSG00000234370.10. [Q92759-1] DR Ensembl; ENST00000435498.5; ENSP00000388227.1; ENSG00000233149.10. [Q92759-1] DR Ensembl; ENST00000438348.5; ENSP00000387980.1; ENSG00000226384.10. [Q92759-1] DR Ensembl; ENST00000440824.6; ENSP00000401105.2; ENSG00000226384.10. [Q92759-1] DR Ensembl; ENST00000456968.6; ENSP00000395497.2; ENSG00000233149.10. [Q92759-1] DR GeneID; 2968; -. DR KEGG; hsa:2968; -. DR MANE-Select; ENST00000259895.9; ENSP00000259895.4; NM_001517.5; NP_001508.1. DR UCSC; uc003nsa.2; human. [Q92759-1] DR AGR; HGNC:4658; -. DR CTD; 2968; -. DR DisGeNET; 2968; -. DR GeneCards; GTF2H4; -. DR HGNC; HGNC:4658; GTF2H4. DR HPA; ENSG00000213780; Low tissue specificity. DR MIM; 601760; gene. DR neXtProt; NX_Q92759; -. DR OpenTargets; ENSG00000213780; -. DR PharmGKB; PA29044; -. DR VEuPathDB; HostDB:ENSG00000213780; -. DR eggNOG; KOG3471; Eukaryota. DR GeneTree; ENSGT00390000014159; -. DR HOGENOM; CLU_027280_4_0_1; -. DR InParanoid; Q92759; -. DR OMA; HYVMRLL; -. DR OrthoDB; 118200at2759; -. DR PhylomeDB; Q92759; -. DR TreeFam; TF300879; -. DR PathwayCommons; Q92759; -. 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; Q92759; -. DR SIGNOR; Q92759; -. DR BioGRID-ORCS; 2968; 586 hits in 1171 CRISPR screens. DR ChiTaRS; GTF2H4; human. DR GeneWiki; GTF2H4; -. DR GenomeRNAi; 2968; -. DR Pharos; Q92759; Tbio. DR PRO; PR:Q92759; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; Q92759; Protein. DR Bgee; ENSG00000213780; Expressed in right lobe of liver and 97 other cell types or tissues. DR ExpressionAtlas; Q92759; baseline and differential. DR GO; GO:0000438; C:core TFIIH complex portion of holo TFIIH complex; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. 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; IDA:UniProtKB. DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro. DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central. DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:ARUK-UCL. DR GO; GO:0006281; P:DNA repair; TAS:ProtInc. DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB. DR Gene3D; 3.30.70.2610; -; 1. DR InterPro; IPR040662; Tfb2_C. DR InterPro; IPR004598; TFIIH_p52/Tfb2. DR NCBIfam; TIGR00625; tfb2; 1. DR PANTHER; PTHR13152:SF0; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 4; 1. DR PANTHER; PTHR13152; TFIIH, POLYPEPTIDE 4; 1. DR Pfam; PF03849; Tfb2; 1. DR Pfam; PF18307; Tfb2_C; 1. DR Genevisible; Q92759; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; DNA damage; DNA repair; Nucleus; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1..462 FT /note="General transcription factor IIH subunit 4" FT /id="PRO_0000119253" FT VAR_SEQ 1..56 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056835" FT VAR_SEQ 276 FT /note="R -> V (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056836" FT VAR_SEQ 277..462 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056837" FT VARIANT 337 FT /note="R -> Q (in dbSNP:rs3218820)" FT /evidence="ECO:0000269|Ref.4" FT /id="VAR_019056" FT HELIX 19..24 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 28..34 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 38..47 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 50..58 FT /evidence="ECO:0007829|PDB:8EBU" FT TURN 59..61 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 68..72 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:7AD8" FT HELIX 80..92 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 95..100 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 106..110 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 112..122 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 146..163 FT /evidence="ECO:0007829|PDB:7NVV" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:7NVV" FT HELIX 173..180 FT /evidence="ECO:0007829|PDB:7NVV" FT TURN 181..184 FT /evidence="ECO:0007829|PDB:7NVV" FT STRAND 190..192 FT /evidence="ECO:0007829|PDB:7NVV" FT HELIX 198..205 FT /evidence="ECO:0007829|PDB:7NVV" FT HELIX 208..226 FT /evidence="ECO:0007829|PDB:7NVV" FT HELIX 230..241 FT /evidence="ECO:0007829|PDB:7NVV" FT HELIX 256..267 FT /evidence="ECO:0007829|PDB:7NVV" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:7NVV" FT STRAND 274..277 FT /evidence="ECO:0007829|PDB:7NVV" FT STRAND 279..283 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 285..288 FT /evidence="ECO:0007829|PDB:7NVV" FT STRAND 307..309 FT /evidence="ECO:0007829|PDB:7NVV" FT STRAND 313..317 FT /evidence="ECO:0007829|PDB:7NVV" FT HELIX 322..330 FT /evidence="ECO:0007829|PDB:7NVV" FT STRAND 331..338 FT /evidence="ECO:0007829|PDB:7NVV" FT STRAND 341..345 FT /evidence="ECO:0007829|PDB:7NVV" FT HELIX 348..357 FT /evidence="ECO:0007829|PDB:7NVV" FT HELIX 361..370 FT /evidence="ECO:0007829|PDB:7NVV" FT HELIX 374..378 FT /evidence="ECO:0007829|PDB:7NVV" FT STRAND 379..383 FT /evidence="ECO:0007829|PDB:7NVV" FT HELIX 385..398 FT /evidence="ECO:0007829|PDB:7NVV" FT STRAND 400..409 FT /evidence="ECO:0007829|PDB:7NVV" FT HELIX 415..428 FT /evidence="ECO:0007829|PDB:7NVV" FT STRAND 431..435 FT /evidence="ECO:0007829|PDB:7NVV" FT TURN 436..439 FT /evidence="ECO:0007829|PDB:7NVV" FT STRAND 440..443 FT /evidence="ECO:0007829|PDB:7NVV" FT HELIX 445..447 FT /evidence="ECO:0007829|PDB:7NVV" FT HELIX 448..457 FT /evidence="ECO:0007829|PDB:7NVV" SQ SEQUENCE 462 AA; 52186 MW; 5532DAD617CA743C CRC64; MESTPSRGLN RVHLQCRNLQ EFLGGLSPGV LDRLYGHPAT CLAVFRELPS LAKNWVMRML FLEQPLPQAA VALWVKKEFS KAQEESTGLL SGLRIWHTQL LPGGLQGLIL NPIFRQNLRI ALLGGGKAWS DDTSQLGPDK HARDVPSLDK YAEERWEVVL HFMVGSPSAA VSQDLAQLLS QAGLMKSTEP GEPPCITSAG FQFLLLDTPA QLWYFMLQYL QTAQSRGMDL VEILSFLFQL SFSTLGKDYS VEGMSDSLLN FLQHLREFGL VFQRKRKSRR YYPTRLAINL SSGVSGAGGT VHQPGFIVVE TNYRLYAYTE SELQIALIAL FSEMLYRFPN MVVAQVTRES VQQAIASGIT AQQIIHFLRT RAHPVMLKQT PVLPPTITDQ IRLWELERDR LRFTEGVLYN QFLSQVDFEL LLAHARELGV LVFENSAKRL MVVTPAGHSD VKRFWKRQKH SS //