TF2H1_HUMAN
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 03-AUG-2022, entry version 199.
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=2; 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/";
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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; 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 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; 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 AlphaFoldDB; P32780; -.
DR BMRB; P32780; -.
DR SMR; P32780; -.
DR BioGRID; 109220; 84.
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; P32780; -.
DR PeptideAtlas; P32780; -.
DR PRIDE; P32780; -.
DR ProteomicsDB; 3810; -.
DR ProteomicsDB; 54882; -. [P32780-1]
DR Antibodypedia; 3302; 333 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 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; ENVPAKM; -.
DR OrthoDB; 946128at2759; -.
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; 589 hits in 1096 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 103 other tissues.
DR ExpressionAtlas; P32780; baseline and differential.
DR Genevisible; P32780; HS.
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:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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 Gene3D; 2.30.29.30; -; 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; PTHR12856; 1.
DR Pfam; PF03909; BSD; 1.
DR Pfam; PF08567; PH_TFIIH; 1.
DR SMART; SM00751; BSD; 2.
DR SUPFAM; SSF140383; SSF140383; 2.
DR PROSITE; PS50858; BSD; 2.
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 122..132
FT /evidence="ECO:0007829|PDB:2DII"
FT TURN 133..135
FT /evidence="ECO:0007829|PDB:2DII"
FT HELIX 139..146
FT /evidence="ECO:0007829|PDB:2DII"
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 400..410
FT /evidence="ECO:0007829|PDB:7AD8"
FT STRAND 418..421
FT /evidence="ECO:0007829|PDB:7AD8"
FT HELIX 424..433
FT /evidence="ECO:0007829|PDB:7AD8"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:7AD8"
FT HELIX 457..478
FT /evidence="ECO:0007829|PDB:7AD8"
FT HELIX 486..504
FT /evidence="ECO:0007829|PDB:7AD8"
FT TURN 505..508
FT /evidence="ECO:0007829|PDB:7AD8"
FT HELIX 509..513
FT /evidence="ECO:0007829|PDB:7AD8"
FT HELIX 523..546
FT /evidence="ECO:0007829|PDB:7AD8"
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
