TF2H5_MOUSE
ID TF2H5_MOUSE Reviewed; 71 AA.
AC Q8K2X8; Q8BT75;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=General transcription factor IIH subunit 5;
DE AltName: Full=General transcription factor IIH polypeptide 5;
DE AltName: Full=TFB5 ortholog {ECO:0000250|UniProtKB:Q6ZYL4};
DE AltName: Full=TFIIH basal transcription factor complex TTD-A subunit {ECO:0000250|UniProtKB:Q6ZYL4};
DE AltName: Full=TFIIH subunit p8 {ECO:0000303|PubMed:28888655};
GN Name=Gtf2h5 {ECO:0000312|MGI:MGI:107227}; Synonyms=D17Wsu155e;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [4]
RP INTERACTION WITH VSIV PROTEIN M (MICROBIAL INFECTION), AND SUBCELLULAR
RP LOCATION.
RX PubMed=28888655; DOI=10.1016/j.vetmic.2017.07.020;
RA Pan W., Song D., He W., Lu H., Lan Y., Tong J., Gao F., Zhao K.;
RT "The matrix protein of vesicular stomatitis virus inhibits host-directed
RT transcription of target genes via interaction with the TFIIH subunit p8.";
RL Vet. Microbiol. 208:82-88(2017).
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. Necessary for the stability of the TFIIH
CC complex and for the presence of normal levels of TFIIH in the cell.
CC {ECO:0000250|UniProtKB:Q6ZYL4}.
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. {ECO:0000250|UniProtKB:Q6ZYL4}.
CC -!- SUBUNIT: (Microbial infection) Interacts with the vesicular stomatitis
CC virus matrix protein/M; this interaction may lead to transcription
CC inhibition. {ECO:0000269|PubMed:28888655}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28888655}. Cytoplasm
CC {ECO:0000269|PubMed:28888655}.
CC -!- SIMILARITY: Belongs to the TFB5 family. {ECO:0000305}.
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DR EMBL; AK003547; BAC25038.1; -; mRNA.
DR EMBL; AK003579; BAC25043.1; -; mRNA.
DR EMBL; AK011281; BAC25328.1; -; mRNA.
DR EMBL; AK012257; BAC25362.1; -; mRNA.
DR EMBL; AK013225; BAC25398.1; -; mRNA.
DR EMBL; BC029238; AAH29238.1; -; mRNA.
DR CCDS; CCDS37423.1; -.
DR RefSeq; NP_852057.2; NM_181392.3.
DR RefSeq; XP_006523302.1; XM_006523239.3.
DR RefSeq; XP_006523303.1; XM_006523240.3.
DR AlphaFoldDB; Q8K2X8; -.
DR SMR; Q8K2X8; -.
DR BioGRID; 211495; 2.
DR STRING; 10090.ENSMUSP00000040355; -.
DR iPTMnet; Q8K2X8; -.
DR PhosphoSitePlus; Q8K2X8; -.
DR MaxQB; Q8K2X8; -.
DR PaxDb; Q8K2X8; -.
DR PeptideAtlas; Q8K2X8; -.
DR PRIDE; Q8K2X8; -.
DR ProteomicsDB; 262879; -.
DR Antibodypedia; 70683; 90 antibodies from 19 providers.
DR DNASU; 66467; -.
DR Ensembl; ENSMUST00000039487; ENSMUSP00000040355; ENSMUSG00000034345.
DR Ensembl; ENSMUST00000100955; ENSMUSP00000098515; ENSMUSG00000034345.
DR GeneID; 66467; -.
DR KEGG; mmu:66467; -.
DR UCSC; uc008aga.2; mouse.
DR CTD; 404672; -.
DR MGI; MGI:107227; Gtf2h5.
DR VEuPathDB; HostDB:ENSMUSG00000034345; -.
DR eggNOG; KOG3451; Eukaryota.
DR GeneTree; ENSGT00390000004028; -.
DR HOGENOM; CLU_166246_4_0_1; -.
DR InParanoid; Q8K2X8; -.
DR OMA; IMENMNP; -.
DR OrthoDB; 1591321at2759; -.
DR PhylomeDB; Q8K2X8; -.
DR TreeFam; TF319487; -.
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; 66467; 5 hits in 104 CRISPR screens.
DR ChiTaRS; Gtf2h5; mouse.
DR PRO; PR:Q8K2X8; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8K2X8; protein.
DR Bgee; ENSMUSG00000034345; Expressed in manus and 254 other tissues.
DR Genevisible; Q8K2X8; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005669; C:transcription factor TFIID complex; ISO:MGI.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; IBA:GO_Central.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IBA:GO_Central.
DR GO; GO:0071480; P:cellular response to gamma radiation; IMP:MGI.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:MGI.
DR GO; GO:0006289; P:nucleotide-excision repair; IMP:MGI.
DR GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; IMP:MGI.
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; IBA:GO_Central.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; IMP:MGI.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:InterPro.
DR Gene3D; 3.30.70.1220; -; 1.
DR InterPro; IPR035935; TFB5-like_sf.
DR InterPro; IPR009400; TFIIH_TTDA/Tfb5.
DR PANTHER; PTHR28580; PTHR28580; 1.
DR Pfam; PF06331; Tfb5; 1.
DR SMART; SM01395; Tbf5; 1.
DR SUPFAM; SSF142897; SSF142897; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; DNA damage; DNA repair; Host-virus interaction; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..71
FT /note="General transcription factor IIH subunit 5"
FT /id="PRO_0000119257"
FT MOD_RES 69
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT CONFLICT 7
FT /note="G -> R (in Ref. 1; BAC25398)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 71 AA; 8037 MW; 940B4D3C9BED9A8F CRC64;
MVNVLKGVLI ECDPAMKQFL LYLDEANALG KKFIIQDIDD THVFVIAELV NVLQERVGEL
MDQNAFSLTQ K
