NCB2_YEAST
ID NCB2_YEAST Reviewed; 146 AA.
AC Q92317; D6VT30; O00064; P87340; Q04176;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Negative cofactor 2 complex subunit beta;
DE Short=NC2 complex subunit beta;
DE AltName: Full=Transcriptional repressor YDR1;
GN Name=NCB2; Synonyms=YDR1; OrderedLocusNames=YDR397C;
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], IDENTIFICATION IN THE NC2 COMPLEX, AND
RP FUNCTION OF THE NC2 COMPLEX.
RX PubMed=9023340; DOI=10.1073/pnas.94.3.820;
RA Kim S., Na J.G., Hampsey M., Reinberg D.;
RT "The Dr1/DRAP1 heterodimer is a global repressor of transcription in
RT vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:820-825(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND FUNCTION OF THE NC2 COMPLEX.
RX PubMed=8948634; DOI=10.1093/nar/24.22.4450;
RA Goppelt A.R., Meisterernst M.;
RT "Characterization of the basal inhibitor of class II transcription NC2 from
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 24:4450-4455(1996).
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 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 [5]
RP SUBUNIT, FUNCTION OF THE NC2 COMPLEX, AND INTERACTION WITH SPT15.
RX PubMed=9096360; DOI=10.1073/pnas.94.7.3145;
RA Gadbois E.L., Chao D.M., Reese J.C., Green M.R., Young R.A.;
RT "Functional antagonism between RNA polymerase II holoenzyme and global
RT negative regulator NC2 in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3145-3150(1997).
RN [6]
RP FUNCTION OF THE NC2 COMPLEX IN TRANSCRIPTIONAL ACTIVATION.
RX PubMed=12237409; DOI=10.1073/pnas.202236699;
RA Cang Y., Prelich G.;
RT "Direct stimulation of transcription by negative cofactor 2 (NC2) through
RT TATA-binding protein (TBP).";
RL Proc. Natl. Acad. Sci. U.S.A. 99:12727-12732(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(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 SER-135; SER-137 AND SER-142, AND
RP IDENTIFICATION 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-135, AND IDENTIFICATION BY
RP 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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-137 AND SER-142, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Component of the NC2 complex which represses RNA polymerase
CC II transcription through binding to SPT15/TBP and thereby inhibiting
CC the assembly of the preinitiation complex. The NC2 complex may also
CC mediate transcriptional activation from TATA-driven promoters through
CC association with SPT15/TBP. {ECO:0000269|PubMed:12237409,
CC ECO:0000269|PubMed:8948634, ECO:0000269|PubMed:9023340,
CC ECO:0000269|PubMed:9096360}.
CC -!- SUBUNIT: Component of the NC2 (negative cofactor 2) complex composed of
CC BUR6 and NCB2. The NC2 complex associates with SPT15/TBP. Interacts
CC with SPT15/TBP. {ECO:0000269|PubMed:8948634,
CC ECO:0000269|PubMed:9023340, ECO:0000269|PubMed:9096360}.
CC -!- INTERACTION:
CC Q92317; P40096: BUR6; NbExp=5; IntAct=EBI-37723, EBI-11908;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 2950 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB64838.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U91948; AAB51375.1; -; Genomic_DNA.
DR EMBL; Y09266; CAA70461.1; -; mRNA.
DR EMBL; U32274; AAB64838.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BK006938; DAA12240.1; -; Genomic_DNA.
DR PIR; S69694; S69694.
DR RefSeq; NP_010685.1; NM_001180705.1.
DR AlphaFoldDB; Q92317; -.
DR SMR; Q92317; -.
DR BioGRID; 32458; 481.
DR ComplexPortal; CPX-1662; Negative cofactor 2 complex.
DR DIP; DIP-2067N; -.
DR IntAct; Q92317; 6.
DR MINT; Q92317; -.
DR STRING; 4932.YDR397C; -.
DR iPTMnet; Q92317; -.
DR MaxQB; Q92317; -.
DR PaxDb; Q92317; -.
DR PRIDE; Q92317; -.
DR TopDownProteomics; Q92317; -.
DR EnsemblFungi; YDR397C_mRNA; YDR397C; YDR397C.
DR GeneID; 852006; -.
DR KEGG; sce:YDR397C; -.
DR SGD; S000002805; NCB2.
DR VEuPathDB; FungiDB:YDR397C; -.
DR eggNOG; KOG0871; Eukaryota.
DR GeneTree; ENSGT00550000075010; -.
DR HOGENOM; CLU_066247_11_3_1; -.
DR InParanoid; Q92317; -.
DR BioCyc; YEAST:G3O-29944-MON; -.
DR PRO; PR:Q92317; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q92317; protein.
DR GO; GO:0017054; C:negative cofactor 2 complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0140223; F:general transcription initiation factor activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0017055; P:negative regulation of RNA polymerase II transcription preinitiation complex assembly; IDA:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0061408; P:positive regulation of transcription from RNA polymerase II promoter in response to heat stress; IMP:SGD.
DR GO; GO:0045898; P:regulation of RNA polymerase II transcription preinitiation complex assembly; IMP:SGD.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IMP:SGD.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR042225; Ncb2.
DR PANTHER; PTHR46138; PTHR46138; 1.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Activator; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..146
FT /note="Negative cofactor 2 complex subunit beta"
FT /id="PRO_0000255268"
FT REGION 124..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 146 AA; 16650 MW; E04EB0D6F7E8D91D CRC64;
MAGDSDNVSL PKATVQKMIS EILDQDLMFT KDAREIIINS GIEFIMILSS MASEMADNEA
KKTIAPEHVI KALEELEYNE FIPFLEEILL NFKGSQKVKE TRDSKFKKSG LSEEELLRQQ
EELFRQSRSR LHHNSVSDPV KSEDSS
