TFB2_YEAST
ID TFB2_YEAST Reviewed; 513 AA.
AC Q02939; D6W3P5; P87331;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=General transcription and DNA repair factor IIH subunit TFB2;
DE Short=TFIIH subunit TFB2;
DE AltName: Full=RNA polymerase II transcription factor B 52 kDa subunit;
DE AltName: Full=RNA polymerase II transcription factor B p52 subunit;
DE AltName: Full=RNA polymerase II transcription factor B subunit 2;
GN Name=TFB2; OrderedLocusNames=YPL122C;
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 8-24 AND 110-138,
RP FUNCTION, AND IDENTIFICATION IN THE TFIIH COMPLEX.
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [3]
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 [4]
RP FUNCTION OF TFIIH IN RNA POLYMERASE II TRANSCRIPTION.
RX PubMed=7961739; DOI=10.1016/s0021-9258(18)46892-5;
RA Svejstrup J.Q., Feaver W.J., LaPointe J., Kornberg R.D.;
RT "RNA polymerase transcription factor IIH holoenzyme from yeast.";
RL J. Biol. Chem. 269:28044-28048(1994).
RN [5]
RP FUNCTION OF THE TFIIH CORE COMPLEX IN DNA REPAIR.
RX PubMed=8631896; DOI=10.1074/jbc.271.18.10821;
RA Sung P., Guzder S.N., Prakash L., Prakash S.;
RT "Reconstitution of TFIIH and requirement of its DNA helicase subunits, Rad3
RT and Rad25, in the incision step of nucleotide excision repair.";
RL J. Biol. Chem. 271:10821-10826(1996).
RN [6]
RP IDENTIFICATION IN THE TFIIH CORE COMPLEX.
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 [7]
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 [8]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 412-513, AND INTERACTION WITH
RP TFB5.
RX PubMed=19172752; DOI=10.1038/nsmb.1478;
RA Kainov D.E., Vitorino M., Cavarelli J., Poterszman A., Egly J.M.;
RT "Structural basis for group A trichothiodystrophy.";
RL Nat. Struct. Mol. Biol. 15:980-984(2008).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (6.00 ANGSTROMS) OF 447-508.
RX PubMed=26483468; DOI=10.1073/pnas.1518255112;
RA Murakami K., Tsai K.L., Kalisman N., Bushnell D.A., Asturias F.J.,
RA Kornberg R.D.;
RT "Structure of an RNA polymerase II preinitiation complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13543-13548(2015).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (15.30 ANGSTROMS).
RX PubMed=27610567; DOI=10.1016/j.cell.2016.08.050;
RA Robinson P.J., Trnka M.J., Bushnell D.A., Davis R.E., Mattei P.J.,
RA Burlingame A.L., Kornberg R.D.;
RT "Structure of a complete mediator-RNA polymerase II pre-initiation
RT complex.";
RL Cell 166:1411-1422(2016).
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 TFIIK, in RNA transcription by RNA polymerase
CC II. 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 TFIIK controls the
CC initiation of transcription. {ECO:0000269|PubMed:7961739,
CC ECO:0000269|PubMed:8631896, ECO:0000269|PubMed:9235928}.
CC -!- SUBUNIT: Component of the 7-subunit TFIIH core complex composed of
CC XPB/SSL2, XPD/RAD3, SSL1, TFB1, TFB2, TFB4 and TFB5, which is active in
CC NER. The core complex associates with the 3-subunit CTD-kinase module
CC TFIIK composed of CCL1, KIN28 and TFB3 to form the 10-subunit
CC holoenzyme (holo-TFIIH) active in transcription (PubMed:7961739,
CC PubMed:14500720, PubMed:9235928). Interacts with TFB5
CC (PubMed:19172752). {ECO:0000269|PubMed:14500720,
CC ECO:0000269|PubMed:19172752, ECO:0000269|PubMed:7961739,
CC ECO:0000269|PubMed:9235928}.
CC -!- INTERACTION:
CC Q02939; Q3E7C1: TFB5; NbExp=6; IntAct=EBI-2345544, EBI-2095127;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 8900 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TFB2 family. {ECO:0000305}.
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DR EMBL; U62804; AAB40628.1; -; Genomic_DNA.
DR EMBL; U43503; AAB68240.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11311.1; -; Genomic_DNA.
DR PIR; S62000; S62000.
DR RefSeq; NP_015203.1; NM_001183936.1.
DR PDB; 3DGP; X-ray; 1.80 A; A=435-513.
DR PDB; 3DOM; X-ray; 2.60 A; A/C=412-513.
DR PDB; 5FMF; EM; 6.00 A; W=447-508.
DR PDB; 5OQJ; EM; 4.70 A; 2=1-513.
DR PDB; 5OQM; EM; 5.80 A; 2=1-513.
DR PDB; 5SVA; EM; 15.30 A; a=1-513.
DR PDB; 6GYM; EM; 6.70 A; 2=1-513.
DR PDB; 7K01; EM; 3.90 A; 2=1-513.
DR PDB; 7K04; EM; 9.25 A; 2=1-513.
DR PDB; 7M2U; EM; 8.20 A; 2=1-513.
DR PDB; 7O4I; EM; 3.20 A; 2=1-513.
DR PDB; 7O4J; EM; 2.90 A; 2=1-513.
DR PDB; 7O4K; EM; 3.60 A; 2=1-513.
DR PDB; 7O4L; EM; 3.40 A; 2=1-513.
DR PDB; 7O72; EM; 3.40 A; 2=1-513.
DR PDB; 7O73; EM; 3.40 A; 2=1-513.
DR PDB; 7O75; EM; 3.20 A; 2=1-513.
DR PDBsum; 3DGP; -.
DR PDBsum; 3DOM; -.
DR PDBsum; 5FMF; -.
DR PDBsum; 5OQJ; -.
DR PDBsum; 5OQM; -.
DR PDBsum; 5SVA; -.
DR PDBsum; 6GYM; -.
DR PDBsum; 7K01; -.
DR PDBsum; 7K04; -.
DR PDBsum; 7M2U; -.
DR PDBsum; 7O4I; -.
DR PDBsum; 7O4J; -.
DR PDBsum; 7O4K; -.
DR PDBsum; 7O4L; -.
DR PDBsum; 7O72; -.
DR PDBsum; 7O73; -.
DR PDBsum; 7O75; -.
DR AlphaFoldDB; Q02939; -.
DR SMR; Q02939; -.
DR BioGRID; 36059; 165.
DR ComplexPortal; CPX-1659; General transcription factor complex TFIIH.
DR DIP; DIP-5783N; -.
DR IntAct; Q02939; 13.
DR MINT; Q02939; -.
DR STRING; 4932.YPL122C; -.
DR iPTMnet; Q02939; -.
DR MaxQB; Q02939; -.
DR PaxDb; Q02939; -.
DR PRIDE; Q02939; -.
DR EnsemblFungi; YPL122C_mRNA; YPL122C; YPL122C.
DR GeneID; 855981; -.
DR KEGG; sce:YPL122C; -.
DR SGD; S000006043; TFB2.
DR VEuPathDB; FungiDB:YPL122C; -.
DR eggNOG; KOG3471; Eukaryota.
DR GeneTree; ENSGT00390000014159; -.
DR HOGENOM; CLU_027280_4_0_1; -.
DR InParanoid; Q02939; -.
DR OMA; LWENERN; -.
DR BioCyc; YEAST:G3O-34021-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-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 EvolutionaryTrace; Q02939; -.
DR PRO; PR:Q02939; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q02939; protein.
DR GO; GO:0000112; C:nucleotide-excision repair factor 3 complex; IPI:SGD.
DR GO; GO:0000439; C:transcription factor TFIIH core complex; IDA:SGD.
DR GO; GO:0005675; C:transcription factor TFIIH holo complex; IDA:SGD.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
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:0006366; P:transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IDA:ComplexPortal.
DR InterPro; IPR040662; Tfb2_C.
DR InterPro; IPR004598; TFIIH_p52/Tfb2.
DR PANTHER; PTHR13152; PTHR13152; 1.
DR Pfam; PF03849; Tfb2; 1.
DR Pfam; PF18307; Tfb2_C; 1.
DR TIGRFAMs; TIGR00625; tfb2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA damage; DNA excision;
KW DNA repair; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..513
FT /note="General transcription and DNA repair factor IIH
FT subunit TFB2"
FT /id="PRO_0000119268"
FT REGION 296..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 29..38
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 59..65
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:7O72"
FT HELIX 71..83
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 118..121
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 135..151
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 177..180
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 186..192
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 196..210
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 218..230
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 245..254
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:7O4J"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 339..341
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 354..360
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:7O4J"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 380..388
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 393..402
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 406..422
FT /evidence="ECO:0007829|PDB:7O4J"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:3DGP"
FT STRAND 452..460
FT /evidence="ECO:0007829|PDB:3DGP"
FT HELIX 465..477
FT /evidence="ECO:0007829|PDB:3DGP"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:3DGP"
FT TURN 486..489
FT /evidence="ECO:0007829|PDB:3DGP"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:3DGP"
FT HELIX 495..497
FT /evidence="ECO:0007829|PDB:3DGP"
FT HELIX 498..505
FT /evidence="ECO:0007829|PDB:3DGP"
SQ SEQUENCE 513 AA; 58535 MW; 9E440B566396A95A CRC64;
MSDYSLKHSV TQYLEEIPQQ VQNRLYTSPA TCLAIYRILP PLAKFFIMAM VFNENEVPLL
DLDKWVNSNG KLQFQNAIKS MKSLHLLIPN KSSGTLMINL NPTFKISLRN ALTGGEVQNS
FGVVVEENVV SLDLLDEYSA NKWETILHFM VGTPLAKIPS EKVLNLLKHS KLMEEVNSTG
EFKITNEGFQ FLLQEINSQL WTLLLQYLKM IETSKMDLVD VLHFIFMLGA LEVGKAYKID
ALSETQRIML QDMRDYGLVF QKHSNDSIFY PTKLALMLTS DTKTIRSASN AMDSVLRQNR
EEPSVNEDGA NGKSTTDITT SDDLNKAGLK NQDIPDGSLI VETNFKIYSY SNSPLQIAVL
SLFVHLKARF VNMVLGQITR ESIRRALTNG ITADQIIAYL ETHAHPQMRR LAEEKLEKKL
ELDPNCKEPL QVLPPTVVDQ IRLWQLELDR VITYEGSLYS DFETSQEYNL LSKYAQDIGV
LLWKDDKKKK FFISKEGNSQ VLDFAKRKLK KKQ
