TFB3_YEAST
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 03-AUG-2022, entry version 184.
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; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 71-85 AND 236-250,
RP 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., Bushnell D.A.,
RA 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 kinase and
RT 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 kinase
RT 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., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., 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., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and 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) and
RT 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., Dephoure N.,
RA 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 BY
RP 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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Acts as component of the general transcription and DNA repair
CC factor IIH (TFIIH or factor B), which is essential for both basal and
CC activated transcription, and is involved in nucleotide excision repair
CC (NER) of damaged DNA. TFIIH has CTD kinase and DNA-dependent ATPase
CC activity, and is essential for polymerase II transcription in vitro.
CC {ECO:0000269|PubMed:9235928, ECO:0000269|PubMed:9294030}.
CC -!- SUBUNIT: Component of the transcription factor IIH (TFIIH) holo but not
CC the TFIIH core complex. Component of a complex consisting of KIN28,
CC CCL1 and TFB3; the KIN28-CCL1 dimer is known as the TFIIK complex.
CC {ECO:0000269|PubMed:11839796, ECO:0000269|PubMed:14500720,
CC ECO:0000269|PubMed:9235928, ECO:0000269|PubMed:9294030}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 3050 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40629.1; Type=Frameshift; Evidence={ECO:0000305};
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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 PDB; 5OQJ; EM; 4.70 A; 3=1-321.
DR PDB; 5OQM; EM; 5.80 A; 3=1-321.
DR PDB; 6GYM; EM; 6.70 A; 3=1-321.
DR PDB; 6XI8; EM; 3.64 A; C=259-321.
DR PDB; 7KUE; EM; 3.50 A; C=1-321.
DR PDB; 7O4I; EM; 3.20 A; 3=1-321.
DR PDB; 7O4J; EM; 2.90 A; 3=1-321.
DR PDB; 7O4K; EM; 3.60 A; 3=1-321.
DR PDB; 7O4L; EM; 3.40 A; 3=1-321.
DR PDB; 7O72; EM; 3.40 A; 3=1-321.
DR PDB; 7O73; EM; 3.40 A; 3=1-321.
DR PDB; 7O75; EM; 3.20 A; 3=1-321.
DR PDBsum; 5OQJ; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 6GYM; -.
DR PDBsum; 6XI8; -.
DR PDBsum; 7KUE; -.
DR PDBsum; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 7O4K; -.
DR PDBsum; 7O4L; -.
DR PDBsum; 7O72; -.
DR PDBsum; 7O73; -.
DR PDBsum; 7O75; -.
DR AlphaFoldDB; Q03290; -.
DR SMR; Q03290; -.
DR BioGRID; 32514; 39.
DR ComplexPortal; CPX-1659; General transcription factor complex TFIIH.
DR ComplexPortal; CPX-1660; General transcription factor complex TFIIK.
DR DIP; DIP-2398N; -.
DR IntAct; Q03290; 16.
DR MINT; Q03290; -.
DR STRING; 4932.YDR460W; -.
DR iPTMnet; Q03290; -.
DR MaxQB; Q03290; -.
DR PaxDb; Q03290; -.
DR PRIDE; Q03290; -.
DR EnsemblFungi; YDR460W_mRNA; YDR460W; YDR460W.
DR GeneID; 852071; -.
DR KEGG; sce:YDR460W; -.
DR SGD; S000002868; TFB3.
DR VEuPathDB; FungiDB:YDR460W; -.
DR eggNOG; KOG3800; Eukaryota.
DR GeneTree; ENSGT00390000002319; -.
DR HOGENOM; CLU_048466_1_1_1; -.
DR InParanoid; Q03290; -.
DR OMA; PANCPVA; -.
DR BioCyc; YEAST:G3O-29988-MON; -.
DR Reactome; R-SCE-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SCE-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SCE-6782135; Dual incision in TC-NER.
DR Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-SCE-69231; Cyclin D associated events in G1.
DR Reactome; R-SCE-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-SCE-72086; mRNA Capping.
DR Reactome; R-SCE-73772; RNA Polymerase I Promoter Escape.
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-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
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 PRO; PR:Q03290; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03290; protein.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:SGD.
DR GO; GO:0070985; C:transcription factor TFIIK complex; IDA:SGD.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:ComplexPortal.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:SGD.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
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:SF13; PTHR12683:SF13; 1.
DR Pfam; PF06391; MAT1; 1.
DR Pfam; PF17121; zf-C3HC4_5; 1.
DR PIRSF; PIRSF003338; MAT1_metazoa; 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 3D-structure; Direct protein sequencing; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..321
FT /note="RNA polymerase II transcription factor B subunit 3"
FT /id="PRO_0000055942"
FT ZN_FING 13..60
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 258
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:7O75"
FT HELIX 40..47
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 96..99
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 103..122
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 262..265
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 280..284
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:7KUE"
FT HELIX 298..308
FT /evidence="ECO:0007829|PDB:7KUE"
FT TURN 309..312
FT /evidence="ECO:0007829|PDB:7KUE"
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
