ID TFB3_YEAST Reviewed; 321 AA. AC Q03290; D6VT84; P89104; DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 14-OCT-2015, entry version 136. DE RecName: Full=RNA polymerase II transcription factor B subunit 3; DE AltName: Full=RNA polymerase II transcription factor B 38 kDa subunit; DE AltName: Full=RNA polymerase II transcription factor B p38 subunit; GN Name=TFB3; Synonyms=RIG2; OrderedLocusNames=YDR460W; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; 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 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 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 GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., RA Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and RT now."; RL G3 (Bethesda) 4:389-398(2014). RN [6] 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 [7] 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 [8] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-258, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157 AND THR-258, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth RT phosphoproteome analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). 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. {ECO:0000269|PubMed:9235928, CC ECO:0000269|PubMed:9294030}. 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. {ECO:0000269|PubMed:11839796, CC ECO:0000269|PubMed:14500720, ECO:0000269|PubMed:9235928, CC ECO:0000269|PubMed:9294030}. CC -!- INTERACTION: CC P37366:CCL1; NbExp=4; IntAct=EBI-31406, EBI-4385; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. CC -!- MISCELLANEOUS: Present with 3050 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Contains 1 RING-type zinc finger. CC {ECO:0000255|PROSITE-ProRule:PRU00175}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB40629.1; Type=Frameshift; Positions=262; Evidence={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; U62805; AAB40629.1; ALT_FRAME; Genomic_DNA. DR EMBL; U33050; AAB64899.1; -; Genomic_DNA. DR EMBL; BK006938; DAA12294.1; -; Genomic_DNA. DR PIR; S69628; S69628. DR RefSeq; NP_010748.3; NM_001180768.3. DR ProteinModelPortal; Q03290; -. DR SMR; Q03290; 13-75. DR BioGrid; 32514; 25. DR DIP; DIP-2398N; -. DR IntAct; Q03290; 11. DR MINT; MINT-528793; -. DR MaxQB; Q03290; -. DR PaxDb; Q03290; -. DR PeptideAtlas; Q03290; -. DR EnsemblFungi; YDR460W; YDR460W; YDR460W. DR GeneID; 852071; -. DR KEGG; sce:YDR460W; -. DR EuPathDB; FungiDB:YDR460W; -. DR SGD; S000002868; TFB3. DR eggNOG; COG5220; -. DR GeneTree; ENSGT00390000002319; -. DR HOGENOM; HOG000189680; -. DR InParanoid; Q03290; -. DR KO; K10842; -. DR OMA; RIRQKQA; -. DR OrthoDB; EOG7WMCVV; -. DR BioCyc; YEAST:G3O-29988-MONOMER; -. DR Reactome; R-SCE-110302; Formation of transcription-coupled NER (TC-NER) repair complex. DR Reactome; R-SCE-110304; Dual incision reaction in TC-NER. DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex. DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-SCE-69273; Cyclin A/B1 associated events during G2/M transition. DR Reactome; R-SCE-72086; mRNA Capping. DR Reactome; R-SCE-73776; RNA Polymerase II Promoter Escape. DR Reactome; R-SCE-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening. DR Reactome; R-SCE-73935; Formation of incision complex in GG-NER. DR Reactome; R-SCE-73941; Dual incision reaction in GG-NER. DR Reactome; R-SCE-75953; RNA Polymerase II Transcription Initiation. DR Reactome; R-SCE-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance. DR Reactome; R-SCE-77075; RNA Pol II CTD phosphorylation and interaction with CE. DR NextBio; 970364; -. DR PRO; PR:Q03290; -. DR Proteomes; UP000002311; Chromosome IV. DR GO; GO:0005675; C:holo TFIIH complex; IDA:SGD. DR GO; GO:0070985; C:TFIIK complex; IDA:SGD. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:InterPro. DR GO; GO:0006289; P:nucleotide-excision repair; IMP:SGD. DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD. DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:SGD. DR Gene3D; 3.30.40.10; -; 1. DR InterPro; IPR015877; Cdk-activating_kinase_MAT1_cen. DR InterPro; IPR004575; MAT1/Tfb3. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR12683; PTHR12683; 1. DR Pfam; PF06391; MAT1; 1. DR PIRSF; PIRSF003338; MAT1_metazoa; 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. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; 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. {ECO:0000255|PROSITE- FT ProRule:PRU00175}. FT MOD_RES 157 157 Phosphoserine. FT {ECO:0000244|PubMed:18407956}. FT MOD_RES 258 258 Phosphothreonine. FT {ECO:0000244|PubMed:17330950, FT ECO:0000244|PubMed:18407956}. 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 //