ID TF2H1_HUMAN Reviewed; 548 AA. AC P32780; B3KXE0; D3DQY2; Q6I9Y7; Q9H5K5; Q9NQD9; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 27-MAR-2024, entry version 208. DE RecName: Full=General transcription factor IIH subunit 1; DE AltName: Full=Basic transcription factor 2 62 kDa subunit; DE Short=BTF2 p62; DE AltName: Full=General transcription factor IIH polypeptide 1; DE AltName: Full=TFIIH basal transcription factor complex p62 subunit; GN Name=GTF2H1; Synonyms=BTF2; 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). RX PubMed=1529339; DOI=10.1126/science.1529339; RA Fischer L., Gerard M., Chalut C., Lutz Y., Humbert S., Kanno M., RA Chambon P., Egly J.-M.; RT "Cloning of the 62-kilodalton component of basic transcription factor RT BTF2."; RL Science 257:1392-1395(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Hippocampus, and Liver; 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-234; PHE-285 AND RP VAL-517. RG NIEHS SNPs program; RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 [8] RP NUCLEOTIDE SEQUENCE OF 521-548. RA Critcher R., Palin A.H., Zhang J., Chin S.F., Gayther S.A., Li L., RA Cohen S.N., Caldas C., Farr C.J.; RT "An aphidicolin-sensitive fragile site (FRA11C) lies within 100 kb of the RT putative tumour suppressor gene TSG101 on both human and mouse RT chromosomes."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [9] 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 [10] RP INTERACTION WITH PUF60. RX PubMed=10882074; DOI=10.1016/s1097-2765(00)80428-1; RA Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M., Levens D.; RT "The FBP interacting repressor targets TFIIH to inhibit activated RT transcription."; RL Mol. Cell 5:331-341(2000). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339 AND SER-357, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] RP INTERACTION WITH RIFT VALLEY FEVER VIRUS NSS (MICROBIAL INFECTION). RX PubMed=25918396; DOI=10.1073/pnas.1503688112; RA Cyr N., de la Fuente C., Lecoq L., Guendel I., Chabot P.R., Kehn-Hall K., RA Omichinski J.G.; RT "A OmegaXaV motif in the Rift Valley fever virus NSs protein is essential RT for degrading p62, forming nuclear filaments and virulence."; RL Proc. Natl. Acad. Sci. U.S.A. 112:6021-6026(2015). RN [15] RP STRUCTURE BY NMR OF 103-155. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the BSD domain of human TFIIH basal transcription RT factor complex p62 subunit."; RL Submitted (SEP-2006) 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. {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. Interacts with PUF60. {ECO:0000269|PubMed:10882074, CC ECO:0000269|PubMed:9852112}. CC -!- SUBUNIT: (Microbial infection) interacts with Rift valley fever virus CC NSs (via OmegaXaV motif). {ECO:0000269|PubMed:25918396}. CC -!- INTERACTION: CC P32780; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-715539, EBI-11522760; CC P32780; Q96JC9: EAF1; NbExp=3; IntAct=EBI-715539, EBI-769261; CC P32780; Q14192: FHL2; NbExp=3; IntAct=EBI-715539, EBI-701903; CC P32780; P29083: GTF2E1; NbExp=21; IntAct=EBI-715539, EBI-5462215; CC P32780; Q13888: GTF2H2; NbExp=5; IntAct=EBI-715539, EBI-1565170; CC P32780; Q13351: KLF1; NbExp=2; IntAct=EBI-715539, EBI-8284732; CC P32780; P13473-2: LAMP2; NbExp=3; IntAct=EBI-715539, EBI-21591415; CC P32780; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-715539, EBI-5280197; CC P32780; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-715539, EBI-2623095; CC P32780; P04637: TP53; NbExp=12; IntAct=EBI-715539, EBI-366083; CC P32780; Q01831: XPC; NbExp=3; IntAct=EBI-715539, EBI-372610; CC P32780; Q01831-1: XPC; NbExp=3; IntAct=EBI-715539, EBI-15950383; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P32780-1; Sequence=Displayed; CC Name=2; CC IsoId=P32780-2; Sequence=VSP_056562; CC -!- SIMILARITY: Belongs to the TFB1 family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/gtf2h1/"; 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; M95809; AAA58399.1; -; mRNA. DR EMBL; AK027003; BAB15621.1; -; mRNA. DR EMBL; AK127204; BAG54452.1; -; mRNA. DR EMBL; AY163770; AAN46740.1; -; Genomic_DNA. DR EMBL; CR457368; CAG33649.1; -; mRNA. DR EMBL; AC084117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471064; EAW68399.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68400.1; -; Genomic_DNA. DR EMBL; CH471064; EAW68401.1; -; Genomic_DNA. DR EMBL; BC000365; AAH00365.1; -; mRNA. DR EMBL; BC004452; AAH04452.1; -; mRNA. DR EMBL; AJ131959; CAC00685.1; -; Genomic_DNA. DR CCDS; CCDS7838.1; -. [P32780-1] DR PIR; S27958; S27958. DR RefSeq; NP_001135779.1; NM_001142307.1. [P32780-1] DR RefSeq; NP_005307.1; NM_005316.3. [P32780-1] DR RefSeq; XP_006718271.1; XM_006718208.3. [P32780-1] DR PDB; 1PFJ; NMR; -; A=1-108. DR PDB; 2DII; NMR; -; A=103-150. DR PDB; 2RNR; NMR; -; B=1-108. DR PDB; 2RUK; NMR; -; B=1-108. DR PDB; 2RVB; NMR; -; B=1-108. DR PDB; 5GOW; NMR; -; B=1-108. DR PDB; 5XV8; NMR; -; B=2-108. DR PDB; 6NMI; EM; 3.70 A; C=1-539. DR PDB; 6O9L; EM; 7.20 A; 1=1-548. DR PDB; 6O9M; EM; 4.40 A; 1=1-548. DR PDB; 7AD8; EM; 3.50 A; I=1-548. DR PDB; 7BUL; NMR; -; A=1-158. DR PDB; 7DTI; NMR; -; B=1-108. DR PDB; 7EGB; EM; 3.30 A; 1=1-548. DR PDB; 7EGC; EM; 3.90 A; 1=1-548. DR PDB; 7ENA; EM; 4.07 A; 1=1-548. DR PDB; 7ENC; EM; 4.13 A; 1=1-548. DR PDB; 7LBM; EM; 4.80 A; Y=1-548. DR PDB; 7NVR; EM; 4.50 A; 1=1-548. DR PDB; 7NVW; EM; 4.30 A; 1=1-548. DR PDB; 7NVX; EM; 3.90 A; 1=1-548. DR PDB; 7NVY; EM; 7.30 A; 1=1-548. DR PDB; 7NVZ; EM; 7.20 A; 1=1-548. DR PDB; 7NW0; EM; 6.60 A; 1=1-548. DR PDB; 8BVW; EM; 4.00 A; 2=1-548. DR PDB; 8BYQ; EM; 4.10 A; 2=1-548. DR PDB; 8EBS; EM; 4.00 A; C=1-548. DR PDB; 8EBT; EM; 3.90 A; C=111-548. DR PDB; 8EBU; EM; 3.30 A; C=1-548. DR PDB; 8EBV; EM; 7.10 A; C=1-548. DR PDB; 8EBW; EM; 5.60 A; C=1-548. DR PDB; 8EBX; EM; 3.60 A; C=1-548. DR PDB; 8EBY; EM; 3.60 A; C=1-548. DR PDB; 8GXQ; EM; 5.04 A; HB=1-548. DR PDB; 8GXS; EM; 4.16 A; HB=1-548. DR PDB; 8WAK; EM; 5.47 A; 1=1-548. DR PDB; 8WAL; EM; 8.52 A; 1=1-548. DR PDB; 8WAN; EM; 6.07 A; 1=1-548. DR PDB; 8WAO; EM; 6.40 A; 1=1-548. DR PDB; 8WAP; EM; 5.85 A; 1=1-548. DR PDB; 8WAQ; EM; 6.29 A; 1=1-548. DR PDB; 8WAR; EM; 7.20 A; 1=1-548. DR PDB; 8WAS; EM; 6.13 A; 1=1-548. DR PDBsum; 1PFJ; -. DR PDBsum; 2DII; -. DR PDBsum; 2RNR; -. DR PDBsum; 2RUK; -. DR PDBsum; 2RVB; -. DR PDBsum; 5GOW; -. DR PDBsum; 5XV8; -. DR PDBsum; 6NMI; -. DR PDBsum; 6O9L; -. DR PDBsum; 6O9M; -. DR PDBsum; 7AD8; -. DR PDBsum; 7BUL; -. DR PDBsum; 7DTI; -. DR PDBsum; 7EGB; -. DR PDBsum; 7EGC; -. DR PDBsum; 7ENA; -. DR PDBsum; 7ENC; -. DR PDBsum; 7LBM; -. DR PDBsum; 7NVR; -. 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; P32780; -. DR BMRB; P32780; -. DR EMDB; EMD-0452; -. DR EMDB; EMD-12610; -. DR EMDB; EMD-12615; -. DR EMDB; EMD-12616; -. DR EMDB; EMD-12617; -. DR EMDB; EMD-12618; -. DR EMDB; EMD-12619; -. 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-31112; -. DR EMDB; EMD-31204; -. DR EMDB; EMD-31207; -. DR EMDB; EMD-34359; -. DR EMDB; EMD-34360; -. DR SMR; P32780; -. DR BioGRID; 109220; 98. DR ComplexPortal; CPX-2395; General transcription factor TFIIH complex. DR CORUM; P32780; -. DR DIP; DIP-708N; -. DR IntAct; P32780; 42. DR MINT; P32780; -. DR STRING; 9606.ENSP00000265963; -. DR GlyGen; P32780; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P32780; -. DR PhosphoSitePlus; P32780; -. DR BioMuta; GTF2H1; -. DR DMDM; 416727; -. DR EPD; P32780; -. DR jPOST; P32780; -. DR MassIVE; P32780; -. DR MaxQB; P32780; -. DR PaxDb; 9606-ENSP00000265963; -. DR PeptideAtlas; P32780; -. DR ProteomicsDB; 3810; -. DR ProteomicsDB; 54882; -. [P32780-1] DR Pumba; P32780; -. DR Antibodypedia; 3302; 375 antibodies from 32 providers. DR DNASU; 2965; -. DR Ensembl; ENST00000265963.9; ENSP00000265963.4; ENSG00000110768.12. [P32780-1] DR Ensembl; ENST00000453096.6; ENSP00000393638.2; ENSG00000110768.12. [P32780-1] DR Ensembl; ENST00000534641.5; ENSP00000435375.1; ENSG00000110768.12. [P32780-2] DR Ensembl; ENST00000672527.1; ENSP00000500852.1; ENSG00000288114.1. [P32780-1] DR Ensembl; ENST00000672827.1; ENSP00000500178.1; ENSG00000288114.1. [P32780-1] DR Ensembl; ENST00000672845.1; ENSP00000500357.1; ENSG00000288114.1. [P32780-2] DR GeneID; 2965; -. DR KEGG; hsa:2965; -. DR MANE-Select; ENST00000265963.9; ENSP00000265963.4; NM_005316.4; NP_005307.1. DR UCSC; uc001moh.3; human. [P32780-1] DR AGR; HGNC:4655; -. DR CTD; 2965; -. DR DisGeNET; 2965; -. DR GeneCards; GTF2H1; -. DR HGNC; HGNC:4655; GTF2H1. DR HPA; ENSG00000110768; Low tissue specificity. DR MIM; 189972; gene. DR neXtProt; NX_P32780; -. DR OpenTargets; ENSG00000110768; -. DR PharmGKB; PA29041; -. DR VEuPathDB; HostDB:ENSG00000110768; -. DR eggNOG; KOG2074; Eukaryota. DR GeneTree; ENSGT00390000015066; -. DR HOGENOM; CLU_037467_0_0_1; -. DR InParanoid; P32780; -. DR OMA; EEFWSQH; -. DR OrthoDB; 810779at2759; -. DR PhylomeDB; P32780; -. DR TreeFam; TF314689; -. DR PathwayCommons; P32780; -. 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; P32780; -. DR SIGNOR; P32780; -. DR BioGRID-ORCS; 2965; 621 hits in 1176 CRISPR screens. DR ChiTaRS; GTF2H1; human. DR EvolutionaryTrace; P32780; -. DR GeneWiki; GTF2H1; -. DR GenomeRNAi; 2965; -. DR Pharos; P32780; Tbio. DR PRO; PR:P32780; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P32780; Protein. DR Bgee; ENSG00000110768; Expressed in calcaneal tendon and 105 other cell types or tissues. DR ExpressionAtlas; P32780; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0000439; C:transcription factor TFIIH core complex; IDA:UniProtKB. DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IPI:UniProtKB. DR GO; GO:0006281; P:DNA repair; IBA:GO_Central. DR GO; GO:0009755; P:hormone-mediated signaling pathway; NAS:UniProtKB. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc. DR GO; GO:0006360; P:transcription by RNA polymerase I; IBA:GO_Central. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB. DR CDD; cd13229; PH_TFIIH; 1. DR Gene3D; 6.10.140.1200; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR IDEAL; IID00549; -. DR InterPro; IPR005607; BSD_dom. DR InterPro; IPR035925; BSD_dom_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR027079; Tfb1/GTF2H1. DR InterPro; IPR013876; TFIIH_BTF_p62_N. DR PANTHER; PTHR12856:SF0; GENERAL TRANSCRIPTION FACTOR IIH SUBUNIT 1; 1. DR PANTHER; PTHR12856; TRANSCRIPTION INITIATION FACTOR IIH-RELATED; 1. DR Pfam; PF03909; BSD; 1. DR Pfam; PF08567; PH_TFIIH; 1. DR SMART; SM00751; BSD; 2. DR SUPFAM; SSF140383; BSD domain-like; 2. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50858; BSD; 2. DR Genevisible; P32780; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; DNA damage; DNA repair; KW Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome; KW Repeat; Transcription; Transcription regulation. FT CHAIN 1..548 FT /note="General transcription factor IIH subunit 1" FT /id="PRO_0000119245" FT DOMAIN 99..154 FT /note="BSD 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00036" FT DOMAIN 180..232 FT /note="BSD 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00036" FT REGION 321..340 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 322..340 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 240 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9DBA9" FT MOD_RES 339 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 357 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..116 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056562" FT VARIANT 234 FT /note="R -> W (in dbSNP:rs4150603)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_014345" FT VARIANT 285 FT /note="S -> F (in dbSNP:rs4150636)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_014346" FT VARIANT 517 FT /note="L -> V (in dbSNP:rs4150665)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_014347" FT CONFLICT 292 FT /note="S -> P (in Ref. 2; BAB15621)" FT /evidence="ECO:0000305" FT CONFLICT 385 FT /note="G -> A (in Ref. 2; BAB15621)" FT /evidence="ECO:0000305" FT STRAND 3..5 FT /evidence="ECO:0007829|PDB:1PFJ" FT STRAND 8..13 FT /evidence="ECO:0007829|PDB:1PFJ" FT STRAND 14..17 FT /evidence="ECO:0007829|PDB:2RVB" FT STRAND 23..27 FT /evidence="ECO:0007829|PDB:1PFJ" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:1PFJ" FT STRAND 36..40 FT /evidence="ECO:0007829|PDB:1PFJ" FT STRAND 42..46 FT /evidence="ECO:0007829|PDB:1PFJ" FT TURN 47..49 FT /evidence="ECO:0007829|PDB:1PFJ" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:1PFJ" FT STRAND 58..62 FT /evidence="ECO:0007829|PDB:1PFJ" FT STRAND 64..68 FT /evidence="ECO:0007829|PDB:1PFJ" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:1PFJ" FT STRAND 74..78 FT /evidence="ECO:0007829|PDB:1PFJ" FT TURN 82..84 FT /evidence="ECO:0007829|PDB:2RNR" FT HELIX 87..103 FT /evidence="ECO:0007829|PDB:1PFJ" FT HELIX 109..120 FT /evidence="ECO:0007829|PDB:2DII" FT HELIX 124..132 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 139..146 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 152..155 FT /evidence="ECO:0007829|PDB:7BUL" FT HELIX 297..301 FT /evidence="ECO:0007829|PDB:7AD8" FT TURN 302..311 FT /evidence="ECO:0007829|PDB:7AD8" FT HELIX 313..321 FT /evidence="ECO:0007829|PDB:7AD8" FT STRAND 322..324 FT /evidence="ECO:0007829|PDB:7AD8" FT TURN 328..332 FT /evidence="ECO:0007829|PDB:7AD8" FT HELIX 333..342 FT /evidence="ECO:0007829|PDB:7AD8" FT STRAND 345..348 FT /evidence="ECO:0007829|PDB:7AD8" FT HELIX 399..412 FT /evidence="ECO:0007829|PDB:8EBU" FT STRAND 418..421 FT /evidence="ECO:0007829|PDB:7AD8" FT HELIX 424..434 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 441..444 FT /evidence="ECO:0007829|PDB:7AD8" FT STRAND 445..448 FT /evidence="ECO:0007829|PDB:8EBU" FT TURN 449..451 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 455..478 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 484..515 FT /evidence="ECO:0007829|PDB:8EBU" FT HELIX 521..546 FT /evidence="ECO:0007829|PDB:8EBU" SQ SEQUENCE 548 AA; 62032 MW; 8F0FCEBBB1FC9C1D CRC64; MATSSEEVLL IVKKVRQKKQ DGALYLMAER IAWAPEGKDR FTISHMYADI KCQKISPEGK AKIQLQLVLH AGDTTNFHFS NESTAVKERD AVKDLLQQLL PKFKRKANKE LEEKNRMLQE DPVLFQLYKD LVVSQVISAE EFWANRLNVN ATDSSSTSNH KQDVGISAAF LADVRPQTDG CNGLRYNLTS DIIESIFRTY PAVKMKYAEN VPHNMTEKEF WTRFFQSHYF HRDRLNTGSK DLFAECAKID EKGLKTMVSL GVKNPLLDLT ALEDKPLDEG YGISSVPSAS NSKSIKENSN AAIIKRFNHH SAMVLAAGLR KQEAQNEQTS EPSNMDGNSG DADCFQPAVK RAKLQESIEY EDLGKNNSVK TIALNLKKSD RYYHGPTPIQ SLQYATSQDI INSFQSIRQE MEAYTPKLTQ VLSSSAASST ITALSPGGAL MQGGTQQAIN QMVPNDIQSE LKHLYVAVGE LLRHFWSCFP VNTPFLEEKV VKMKSNLERF QVTKLCPFQE KIRRQYLSTN LVSHIEEMLQ TAYNKLHTWQ SRRLMKKT //