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 18-SEP-2019, entry version 159. 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; OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION IN THE NC2 COMPLEX, RP AND 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 RT from 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., 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 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 [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) RT through 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., 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 SER-135; SER-137 AND RP SER-142, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 RP 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). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135; SER-137 AND RP SER-142, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 RT insights into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Component of the NC2 complex which represses RNA CC polymerase II transcription through binding to SPT15/TBP and CC thereby inhibiting the assembly of the preinitiation complex. The CC NC2 complex may also mediate transcriptional activation from TATA- CC driven promoters through association with SPT15/TBP. CC {ECO:0000269|PubMed:12237409, ECO:0000269|PubMed:8948634, CC ECO:0000269|PubMed:9023340, ECO:0000269|PubMed:9096360}. CC -!- SUBUNIT: Component of the NC2 (negative cofactor 2) complex CC composed of BUR6 and NCB2. The NC2 complex associates with CC SPT15/TBP. Interacts with SPT15/TBP. {ECO:0000269|PubMed:8948634, CC ECO:0000269|PubMed:9023340, ECO:0000269|PubMed:9096360}. CC -!- INTERACTION: CC 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 CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB64838.1; Type=Erroneous gene model prediction; 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; 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 SMR; Q92317; -. DR BioGrid; 32458; 479. 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 EuPathDB; FungiDB:YDR397C; -. DR SGD; S000002805; NCB2. DR HOGENOM; HOG000178641; -. DR InParanoid; Q92317; -. DR KO; K21751; -. DR BioCyc; YEAST:G3O-29944-MONOMER; -. DR PRO; PR:Q92317; -. DR Proteomes; UP000002311; Chromosome IV. DR GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IBA:GO_Central. 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:0001047; F:core promoter binding; IDA:SGD. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central. DR GO; GO:0003714; F:transcription corepressor activity; IDA:SGD. DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central. 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 transcriptional 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; Complete proteome; Nucleus; Phosphoprotein; KW Reference proteome; Repressor; Transcription; KW Transcription regulation. FT CHAIN 1 146 Negative cofactor 2 complex subunit beta. FT /FTId=PRO_0000255268. FT MOD_RES 135 135 Phosphoserine. FT {ECO:0000244|PubMed:17330950, FT ECO:0000244|PubMed:18407956, FT ECO:0000244|PubMed:19779198}. FT MOD_RES 137 137 Phosphoserine. FT {ECO:0000244|PubMed:17330950, FT ECO:0000244|PubMed:19779198}. FT MOD_RES 142 142 Phosphoserine. FT {ECO:0000244|PubMed:17330950, FT ECO:0000244|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 //