TF2H1_MOUSE
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 03-AUG-2022, entry version 139.
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}.
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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.ENSMUSP00000006774; -.
DR iPTMnet; Q9DBA9; -.
DR PhosphoSitePlus; Q9DBA9; -.
DR EPD; Q9DBA9; -.
DR MaxQB; Q9DBA9; -.
DR PaxDb; Q9DBA9; -.
DR PeptideAtlas; Q9DBA9; -.
DR PRIDE; Q9DBA9; -.
DR ProteomicsDB; 263290; -.
DR DNASU; 14884; -.
DR GeneID; 14884; -.
DR KEGG; mmu:14884; -.
DR CTD; 2965; -.
DR MGI; MGI:1277216; Gtf2h1.
DR eggNOG; KOG2074; Eukaryota.
DR InParanoid; Q9DBA9; -.
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 108 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:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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 Gene3D; 1.10.3970.10; -; 1.
DR Gene3D; 2.30.29.30; -; 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; 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 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
