ID TF2H1_MOUSE Reviewed; 547 AA. AC Q9DBA9; O35637; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 18-OCT-2001, sequence version 2. DT 24-JAN-2024, entry version 146. 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; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Teratocarcinoma; RX PubMed=9630526; DOI=10.1016/s0378-1119(98)00197-8; RA Perez C., Auriol J., Seroz T., Egly J.-M.; RT "Genomic organization and promoter characterization of the mouse and human RT genes encoding p62 subunit of the transcription/DNA repair factor TFIIH."; RL Gene 213:73-82(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Liver; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-239, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). 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:0000250|UniProtKB:P32780}. 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:0000250|UniProtKB:P32780}. CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- SIMILARITY: Belongs to the TFB1 family. {ECO:0000305}. 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; AJ002366; CAA05340.1; -; mRNA. DR EMBL; AK005065; BAB23789.1; -; mRNA. DR CCDS; CCDS21287.1; -. DR RefSeq; NP_001278004.1; NM_001291075.1. DR RefSeq; NP_032212.3; NM_008186.4. DR AlphaFoldDB; Q9DBA9; -. DR BMRB; Q9DBA9; -. DR SMR; Q9DBA9; -. DR BioGRID; 200111; 4. DR IntAct; Q9DBA9; 3. DR STRING; 10090.ENSMUSP00000103271; -. DR iPTMnet; Q9DBA9; -. DR PhosphoSitePlus; Q9DBA9; -. DR EPD; Q9DBA9; -. DR MaxQB; Q9DBA9; -. DR PaxDb; 10090-ENSMUSP00000006774; -. DR PeptideAtlas; Q9DBA9; -. DR ProteomicsDB; 263290; -. DR Pumba; Q9DBA9; -. DR DNASU; 14884; -. DR GeneID; 14884; -. DR KEGG; mmu:14884; -. DR AGR; MGI:1277216; -. DR CTD; 2965; -. DR MGI; MGI:1277216; Gtf2h1. DR eggNOG; KOG2074; Eukaryota. DR InParanoid; Q9DBA9; -. DR OrthoDB; 810779at2759; -. DR PhylomeDB; Q9DBA9; -. DR Reactome; R-MMU-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-MMU-113418; Formation of the Early Elongation Complex. DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER. DR Reactome; R-MMU-5696400; Dual Incision in GG-NER. DR Reactome; R-MMU-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-MMU-6781823; Formation of TC-NER Pre-Incision Complex. DR Reactome; R-MMU-6782135; Dual incision in TC-NER. DR Reactome; R-MMU-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER. DR Reactome; R-MMU-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-MMU-72086; mRNA Capping. DR Reactome; R-MMU-73762; RNA Polymerase I Transcription Initiation. DR Reactome; R-MMU-73772; RNA Polymerase I Promoter Escape. DR Reactome; R-MMU-73776; RNA Polymerase II Promoter Escape. DR Reactome; R-MMU-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening. DR Reactome; R-MMU-73863; RNA Polymerase I Transcription Termination. DR Reactome; R-MMU-75953; RNA Polymerase II Transcription Initiation. DR Reactome; R-MMU-75955; RNA Polymerase II Transcription Elongation. DR Reactome; R-MMU-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance. DR Reactome; R-MMU-77075; RNA Pol II CTD phosphorylation and interaction with CE. DR BioGRID-ORCS; 14884; 21 hits in 113 CRISPR screens. DR ChiTaRS; Gtf2h1; mouse. DR PRO; PR:Q9DBA9; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q9DBA9; Protein. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0000439; C:transcription factor TFIIH core complex; ISO:MGI. DR GO; GO:0005675; C:transcription factor TFIIH holo complex; ISS:UniProtKB. DR GO; GO:0003682; F:chromatin binding; ISO:MGI. DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISO:MGI. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI. DR GO; GO:0006281; P:DNA repair; IBA:GO_Central. DR GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:0006360; P:transcription by RNA polymerase I; IBA:GO_Central. DR GO; GO:0006366; P:transcription by RNA polymerase II; ISS:UniProtKB. DR CDD; cd13229; PH_TFIIH; 1. DR Gene3D; 6.10.140.1200; -; 1. DR Gene3D; 1.10.3970.10; BSD domain; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. 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. PE 1: Evidence at protein level; KW Acetylation; DNA damage; DNA repair; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; Transcription; Transcription regulation. FT CHAIN 1..547 FT /note="General transcription factor IIH subunit 1" FT /id="PRO_0000119246" FT DOMAIN 99..154 FT /note="BSD 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00036" FT DOMAIN 179..231 FT /note="BSD 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00036" FT REGION 319..342 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 320..340 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 239 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:23806337" FT MOD_RES 338 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P32780" FT MOD_RES 356 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P32780" FT CONFLICT 137 FT /note="I -> F (in Ref. 2; BAB23789)" FT /evidence="ECO:0000305" FT CONFLICT 208 FT /note="E -> G (in Ref. 2; BAB23789)" FT /evidence="ECO:0000305" FT CONFLICT 281 FT /note="S -> G (in Ref. 2; BAB23789)" FT /evidence="ECO:0000305" FT CONFLICT 537 FT /note="T -> A (in Ref. 2; BAB23789)" FT /evidence="ECO:0000305" SQ SEQUENCE 547 AA; 61851 MW; 0167316D11F87969 CRC64; MATSSEEVLL IVKKVRQKKQ DGALYLMAER IAWAPEGKDR FTISHMYADI KCQKISPEGK AKIQLQLVLH AGDTTNFHFS NESTAVKERD AVKDLLQQLL PKFKRKANKE LEEKNRMLQE DPVLFQLYKD LVVSQVISAE EFWANRLNVN ATDSSTSSHK QDVGISAAFL ADVRPQTDGC NGLRYNLTSD IIESIFRTYP AVKMKYAETV PHNMTEKEFW TRFFQSHYFH RDRLNTGSKD LFAECAKIDE KGLKTMVSLG VKNPMLDLTS LEDKPLDEGY SISSVPSTSN SKSIKENSNA AIIKRFNHHS AMVLAAGLRK QQAQNGQNGE PSSVDGNSGD TDCFQPAVKR AKLQESIEYE DLGNNNSVKT IALNLKKSDR YYHGPTPIQS LQYATSQDII NSFQSIRQEM EAYTPKLTQV LSSSAASSTI TALSPGGALM QGGTQQAVNQ MVPNDIQSEL KHLYVAVGEL LRHFWSCFPV NTPFLEEKVV KMKSNLERFQ VTKLCPFQEK IRRQYLSTNL VSHIEEMLQT AYNKLHTWQS RRLMKKT //