ID TFB3_YEAST Reviewed; 321 AA. AC Q03290; P89104; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 12-DEC-2006, entry version 46. DE RNA polymerase II transcription factor B subunit 3 (RNA polymerase II DE transcription factor B p38 subunit) (RNA polymerase II transcription DE factor B 38 kDa subunit). GN Name=TFB3; Synonyms=RIG2; OrderedLocusNames=YDR460W; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 71-85 AND RP 236-250, FUNCTION, SUBUNIT, AND INTERACTION WITH KIN28. RC STRAIN=DBY2019; RX MEDLINE=97382258; PubMed=9235928; DOI=10.1074/jbc.272.31.19319; RA Feaver W.J., Henry N.L., Wang Z., Wu X., Svejstrup J.Q., RA Bushnell D.A., Friedberg E.C., Kornberg R.D.; RT "Genes for Tfb2, Tfb3, and Tfb4 subunits of yeast transcription/repair RT factor IIH. Homology to human cyclin-dependent kinase activating RT kinase and IIH subunits."; RL J. Biol. Chem. 272:19319-19327(1997). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT. RX PubMed=9294030; DOI=10.1007/s004380050518; RA Faye G., Simon M., Valay J.G., Fesquet D., Facca C.; RT "Rig2, a RING finger protein that interacts with the Kin28/Ccl1 CTD RT kinase in yeast."; RL Mol. Gen. Genet. 255:460-466(1997). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX MEDLINE=97313263; PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., RA Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., RA Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., RA Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., RA Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., RA Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., RA Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., RA Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., RA Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., RA Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., RA Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., RA Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., RA Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., RA Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., RA Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., RA Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., RA Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., RA Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., RA Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., RA Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., RA Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., RA Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [4] RP SEQUENCE REVISION. RC STRAIN=ATCC 204508 / S288c; RA Sethuraman A., Cherry J.M.; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP IDENTIFICATION IN A COMPLEX WITH KIN28 AND CCL1. RX PubMed=11839796; DOI=10.1128/MCB.22.5.1288-1297.2002; RA Keogh M.-C., Cho E.-J., Podolny V., Buratowski S.; RT "Kin28 is found within TFIIH and a Kin28-Ccl1-Tfb3 trimer complex with RT differential sensitivities to T-loop phosphorylation."; RL Mol. Cell. Biol. 22:1288-1297(2002). RN [6] RP SUBUNIT. RX PubMed=14500720; DOI=10.1074/jbc.C300417200; RA Takagi Y., Komori H., Chang W.-H., Hudmon A., Erdjument-Bromage H., RA Tempst P., Kornberg R.D.; RT "Revised subunit structure of yeast transcription factor IIH (TFIIH) RT and reconciliation with human TFIIH."; RL J. Biol. Chem. 278:43897-43900(2003). RN [7] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-258, AND MASS RP SPECTROMETRY. RX PubMed=15665377; DOI=10.1074/mcp.M400219-MCP200; RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., RA Mann M., Jensen O.N.; RT "Quantitative phosphoproteomics applied to the yeast pheromone RT signaling pathway."; RL Mol. Cell. Proteomics 4:310-327(2005). CC -!- FUNCTION: Acts as component of the general transcription and DNA CC repair factor IIH (TFIIH or factor B), which is essential for both CC basal and activated transcription, and is involved in nucleotide CC excision repair (NER) of damaged DNA. TFIIH has CTD kinase and CC DNA-dependent ATPase activity, and is essential for polymerase II CC transcription in vitro. CC -!- SUBUNIT: Component of the transcription factor IIH (TFIIH) holo CC but not the TFIIH core complex. Component of a complex consisting CC of KIN28, CCL1 and TFB3; the KIN28-CCL1 dimer is known as the CC TFIIK complex. CC -!- INTERACTION: CC P37366:CCL1; NbExp=1; IntAct=EBI-31406, EBI-4385; CC P06839:RAD3; NbExp=1; IntAct=EBI-31406, EBI-14762; CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). CC -!- MISCELLANEOUS: Present with 3050 molecules/cell. CC -!- SIMILARITY: Contains 1 RING-type zinc finger. CC -!- CAUTION: Ref.1 (AAB40629) sequence differs from that shown due to CC a frameshift in position 262. 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; U62805; AAB40629.1; ALT_FRAME; Genomic_DNA. DR EMBL; U33050; AAB64899.1; -; Genomic_DNA. DR PIR; S69628; S69628. DR HSSP; P51948; 1G25. DR DIP; DIP:2398N; -. DR IntAct; Q03290; -. DR GermOnline; YDR460W; Saccharomyces cerevisiae. DR Ensembl; YDR460W; Saccharomyces cerevisiae. DR GenomeReviews; Z71256_GR; YDR460W. DR SGD; S000002868; TFB3. DR LinkHub; Q03290; -. DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; TAS:SGD. DR GO; GO:0005675; C:transcription factor TFIIH complex; IDA:SGD. DR GO; GO:0016251; F:general RNA polymerase II transcription fac...; TAS:SGD. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0007070; P:negative regulation of transcription from R...; TAS:SGD. DR GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwi...; TAS:SGD. DR GO; GO:0006367; P:transcription initiation from RNA polymeras...; TAS:SGD. DR InterPro; IPR004575; MAT1. DR InterPro; IPR001841; Znf_RING. DR PANTHER; PTHR12683; MAT1; 1. DR Pfam; PF06391; MAT1; 1. DR SMART; SM00184; RING; 1. DR TIGRFAMs; TIGR00570; cdk7; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. KW Complete proteome; Direct protein sequencing; Metal-binding; KW Nuclear protein; Phosphorylation; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 321 RNA polymerase II transcription factor B FT subunit 3. FT /FTId=PRO_0000055942. FT ZN_FING 13 60 RING-type. FT MOD_RES 258 258 Phosphothreonine. SQ SEQUENCE 321 AA; 38128 MW; 528D61CF25ADFAF4 CRC64; MLMDEYEENK DMCPICKTDR YLSPDVKFLV NPECYHRICE SCVDRIFSLG PAQCPYKGCD KILRKNKFKT QIFDDVEVEK EVDIRKRVFN VFNKTIDDFN GDLVEYNKYL EEVEDIIYKL DHGIDVAKTE EKLRTYEELN KQLIMNNLER SRTEIESFEQ RQKFEKEMKL KKRLLERQIE EEERMNKEWT KKEIVNRLST TTQDINETIE GVKNTVKLKK SSARRKLEEL NRVLKNNPYF NSNVNVQNSR LKDAVPFTPF NGDREAHPRF TLKGSVYNDP FIKDLEHRKE FIASGFNTNY AYERVLTEAF MGLGCVISEE L //