TF2H3_HUMAN
ID TF2H3_HUMAN Reviewed; 308 AA.
AC Q13889; B2R819; B4DNZ6; Q7L0G0; Q96AT7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=General transcription factor IIH subunit 3;
DE AltName: Full=Basic transcription factor 2 34 kDa subunit;
DE Short=BTF2 p34 {ECO:0000303|PubMed:8194529};
DE AltName: Full=General transcription factor IIH polypeptide 3;
DE AltName: Full=TFIIH basal transcription factor complex p34 subunit {ECO:0000303|PubMed:8194529};
GN Name=GTF2H3;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RG NIEHS SNPs program;
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Eye, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-305 (ISOFORM 1), AND PROTEIN SEQUENCE OF
RP 57-68; 78-97; 107-112; 127-132 AND 239-251 (ISOFORMS 1/2).
RX PubMed=8194529; DOI=10.1002/j.1460-2075.1994.tb06523.x;
RA Humbert S., van Vuuren H.A., Lutz Y., Hoeijmakers J.H.J., Egly J.-M.,
RA Moncollin V.;
RT "p44 and p34 subunits of the BTF2/TFIIH transcription factor have
RT homologies with SSL1, a yeast protein involved in DNA repair.";
RL EMBO J. 13:2393-2398(1994).
RN [7]
RP IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
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 [8] {ECO:0007744|PDB:5IVW, ECO:0007744|PDB:5IY6, ECO:0007744|PDB:5IY7, ECO:0007744|PDB:5IY8, ECO:0007744|PDB:5IY9}
RP STRUCTURE BY ELECTRON MICROSCOPY (6.30 ANGSTROMS), SUBUNIT, SUBCELLULAR
RP LOCATION, AND FUNCTION.
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: Part of a TFIID-containing RNA polymerase II pre-initiation
CC complex that is composed of TBP and at least GTF2A1, GTF2A2, GTF2E1,
CC GTF2E2, GTF2F1, GTF2H2, GTF2H3, GTF2H4, GTF2H5, GTF2B, TCEA1, ERCC2,
CC ERCC3, TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10,
CC TAF11, TAF12 and TAF13 (PubMed:27193682). Component of the 7-subunit
CC TFIIH core complex composed of XPB/ERCC3, XPD/ERCC2, GTF2H1, GTF2H2,
CC GTF2H3, GTF2H4 and GTF2H5, which is active in NER. The core complex
CC associates with the 3-subunit CDK-activating kinase (CAK) module
CC composed of CCNH/cyclin H, CDK7 and MNAT1 to form the 10-subunit
CC holoenzyme (holo-TFIIH) active in transcription (PubMed:9852112).
CC Interacts with RARA; the interaction requires prior phosphorylation of
CC RARA on 'Ser-369' which then enhances interaction of RARA with CDK7 (By
CC similarity). {ECO:0000250|UniProtKB:Q8VD76,
CC ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:9852112}.
CC -!- INTERACTION:
CC Q13889; Q6P1K8: GTF2H2C_2; NbExp=5; IntAct=EBI-6380459, EBI-8469755;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:27193682,
CC ECO:0000269|PubMed:9852112}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q13889-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13889-2; Sequence=VSP_055153;
CC -!- SIMILARITY: Belongs to the TFB4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA82909.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/gtf2h3/";
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DR EMBL; AK298128; BAG60408.1; -; mRNA.
DR EMBL; AK313200; BAG36016.1; -; mRNA.
DR EMBL; AF548661; AAN40702.1; -; Genomic_DNA.
DR EMBL; AC117503; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW98426.1; -; Genomic_DNA.
DR EMBL; BC039726; AAH39726.1; -; mRNA.
DR EMBL; BC047868; AAH47868.2; -; mRNA.
DR EMBL; BC065250; AAH65250.1; -; mRNA.
DR EMBL; Z30093; CAA82909.1; ALT_FRAME; mRNA.
DR CCDS; CCDS61275.1; -. [Q13889-2]
DR CCDS; CCDS9252.1; -. [Q13889-1]
DR PIR; S44455; S44455.
DR RefSeq; NP_001258795.1; NM_001271866.1.
DR RefSeq; NP_001258796.1; NM_001271867.1. [Q13889-2]
DR RefSeq; NP_001258797.1; NM_001271868.1.
DR RefSeq; NP_001507.2; NM_001516.4. [Q13889-1]
DR PDB; 5IVW; EM; 10.00 A; 3=1-308.
DR PDB; 5IY6; EM; 7.20 A; 3=1-308.
DR PDB; 5IY7; EM; 8.60 A; 3=1-308.
DR PDB; 5IY8; EM; 7.90 A; 3=1-308.
DR PDB; 5IY9; EM; 6.30 A; 3=1-308.
DR PDB; 5O85; X-ray; 3.40 A; A/C=1-308.
DR PDB; 5OF4; EM; 4.40 A; F=1-308.
DR PDB; 6NMI; EM; 3.70 A; F=1-308.
DR PDB; 6O9L; EM; 7.20 A; 4=1-308.
DR PDB; 6O9M; EM; 4.40 A; 4=1-308.
DR PDB; 6RO4; EM; 3.50 A; E=1-308.
DR PDB; 7AD8; EM; 3.50 A; E=1-308.
DR PDB; 7EGB; EM; 3.30 A; 3=1-308.
DR PDB; 7EGC; EM; 3.90 A; 3=1-308.
DR PDB; 7ENA; EM; 4.07 A; 3=1-308.
DR PDB; 7ENC; EM; 4.13 A; 3=1-308.
DR PDB; 7LBM; EM; 4.80 A; b=1-308.
DR PDB; 7NVR; EM; 4.50 A; 4=1-308.
DR PDB; 7NVW; EM; 4.30 A; 4=1-308.
DR PDB; 7NVX; EM; 3.90 A; 4=1-308.
DR PDB; 7NVY; EM; 7.30 A; 4=1-308.
DR PDB; 7NVZ; EM; 7.20 A; 4=1-308.
DR PDB; 7NW0; EM; 6.60 A; 4=1-308.
DR PDBsum; 5IVW; -.
DR PDBsum; 5IY6; -.
DR PDBsum; 5IY7; -.
DR PDBsum; 5IY8; -.
DR PDBsum; 5IY9; -.
DR PDBsum; 5O85; -.
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; 7NVW; -.
DR PDBsum; 7NVX; -.
DR PDBsum; 7NVY; -.
DR PDBsum; 7NVZ; -.
DR PDBsum; 7NW0; -.
DR AlphaFoldDB; Q13889; -.
DR SMR; Q13889; -.
DR BioGRID; 109222; 42.
DR CORUM; Q13889; -.
DR DIP; DIP-787N; -.
DR IntAct; Q13889; 27.
DR MINT; Q13889; -.
DR STRING; 9606.ENSP00000445162; -.
DR iPTMnet; Q13889; -.
DR PhosphoSitePlus; Q13889; -.
DR BioMuta; GTF2H3; -.
DR DMDM; 50403772; -.
DR EPD; Q13889; -.
DR jPOST; Q13889; -.
DR MassIVE; Q13889; -.
DR MaxQB; Q13889; -.
DR PaxDb; Q13889; -.
DR PeptideAtlas; Q13889; -.
DR PRIDE; Q13889; -.
DR ProteomicsDB; 59717; -. [Q13889-1]
DR Antibodypedia; 19294; 130 antibodies from 25 providers.
DR DNASU; 2967; -.
DR Ensembl; ENST00000228955.11; ENSP00000228955.7; ENSG00000111358.14. [Q13889-2]
DR Ensembl; ENST00000543341.7; ENSP00000445162.1; ENSG00000111358.14. [Q13889-1]
DR GeneID; 2967; -.
DR KEGG; hsa:2967; -.
DR MANE-Select; ENST00000543341.7; ENSP00000445162.1; NM_001516.5; NP_001507.2.
DR UCSC; uc001ufo.3; human. [Q13889-1]
DR CTD; 2967; -.
DR DisGeNET; 2967; -.
DR GeneCards; GTF2H3; -.
DR HGNC; HGNC:4657; GTF2H3.
DR HPA; ENSG00000111358; Low tissue specificity.
DR MIM; 601750; gene.
DR neXtProt; NX_Q13889; -.
DR OpenTargets; ENSG00000111358; -.
DR PharmGKB; PA29043; -.
DR VEuPathDB; HostDB:ENSG00000111358; -.
DR eggNOG; KOG2487; Eukaryota.
DR GeneTree; ENSGT00390000013143; -.
DR HOGENOM; CLU_040211_1_0_1; -.
DR InParanoid; Q13889; -.
DR OMA; CFCHRKV; -.
DR OrthoDB; 1220881at2759; -.
DR PhylomeDB; Q13889; -.
DR TreeFam; TF314336; -.
DR PathwayCommons; Q13889; -.
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; Q13889; -.
DR BioGRID-ORCS; 2967; 428 hits in 1065 CRISPR screens.
DR ChiTaRS; GTF2H3; human.
DR GenomeRNAi; 2967; -.
DR Pharos; Q13889; Tbio.
DR PRO; PR:Q13889; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q13889; protein.
DR Bgee; ENSG00000111358; Expressed in endothelial cell and 208 other tissues.
DR ExpressionAtlas; Q13889; baseline and differential.
DR Genevisible; Q13889; HS.
DR GO; GO:0000438; C:core TFIIH complex portion of holo TFIIH complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0097550; C:transcription preinitiation complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
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 Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR004600; TFIIH_Tfb4/GTF2H3.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR12831; PTHR12831; 1.
DR Pfam; PF03850; Tfb4; 1.
DR TIGRFAMs; TIGR00627; tfb4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing; DNA damage;
KW DNA repair; Metal-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..308
FT /note="General transcription factor IIH subunit 3"
FT /id="PRO_0000119251"
FT ZN_FING 268..285
FT /note="C4-type"
FT VAR_SEQ 1..41
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055153"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:5O85"
FT HELIX 19..27
FT /evidence="ECO:0007829|PDB:5O85"
FT HELIX 34..51
FT /evidence="ECO:0007829|PDB:5O85"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:5O85"
FT STRAND 67..71
FT /evidence="ECO:0007829|PDB:5O85"
FT HELIX 106..120
FT /evidence="ECO:0007829|PDB:5O85"
FT HELIX 133..150
FT /evidence="ECO:0007829|PDB:5O85"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:5O85"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:6RO4"
FT HELIX 174..186
FT /evidence="ECO:0007829|PDB:5O85"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:5O85"
FT HELIX 201..210
FT /evidence="ECO:0007829|PDB:5O85"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:5O85"
FT HELIX 220..222
FT /evidence="ECO:0007829|PDB:5O85"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:5O85"
FT HELIX 235..240
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:6RO4"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:6RO4"
SQ SEQUENCE 308 AA; 34378 MW; E739E2176CD6BAA5 CRC64;
MVSDEDELNL LVIVVDANPI WWGKQALKES QFTLSKCIDA VMVLGNSHLF MNRSNKLAVI
ASHIQESRFL YPGKNGRLGD FFGDPGNPPE FNPSGSKDGK YELLTSANEV IVEEIKDLMT
KSDIKGQHTE TLLAGSLAKA LCYIHRMNKE VKDNQEMKSR ILVIKAAEDS ALQYMNFMNV
IFAAQKQNIL IDACVLDSDS GLLQQACDIT GGLYLKVPQM PSLLQYLLWV FLPDQDQRSQ
LILPPPVHVD YRAACFCHRN LIEIGYVCSV CLSIFCNFSP ICTTCETAFK ISLPPVLKAK
KKKLKVSA
