TF2H4_HUMAN
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 03-AUG-2022, entry version 192.
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).
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. {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/";
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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 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; Q92759; -.
DR SMR; Q92759; -.
DR BioGRID; 109223; 93.
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; Q92759; -.
DR PeptideAtlas; Q92759; -.
DR PRIDE; Q92759; -.
DR ProteomicsDB; 5110; -.
DR ProteomicsDB; 75447; -. [Q92759-1]
DR TopDownProteomics; Q92759-1; -. [Q92759-1]
DR Antibodypedia; 48243; 191 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 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; LWENERN; -.
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 BioGRID-ORCS; 2968; 558 hits in 1091 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 95 other tissues.
DR ExpressionAtlas; Q92759; baseline and differential.
DR Genevisible; Q92759; HS.
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:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR InterPro; IPR040662; Tfb2_C.
DR InterPro; IPR004598; TFIIH_p52/Tfb2.
DR PANTHER; PTHR13152; PTHR13152; 1.
DR Pfam; PF03849; Tfb2; 1.
DR Pfam; PF18307; Tfb2_C; 1.
DR TIGRFAMs; TIGR00625; tfb2; 1.
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:6RO4"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:7AD8"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:6RO4"
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 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
