NCB1_YEAST
ID NCB1_YEAST Reviewed; 142 AA.
AC P40096; D3DM66;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Negative cofactor 2 complex subunit alpha;
DE Short=NC2 complex subunit alpha;
DE AltName: Full=Transcription repressor BUR6;
GN Name=BUR6; Synonyms=NCB1; OrderedLocusNames=YER159C;
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 [MRNA], FUNCTION OF THE NC2 COMPLEX, AND SUBUNIT.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP IDENTIFICATION IN THE NC2 COMPLEX, 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 [6]
RP FUNCTION OF THE NC2 COMPLEX, SUBUNIT, 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 [7]
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 [8]
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-141, 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: 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 P40096; Q92317: NCB2; NbExp=5; IntAct=EBI-11908, EBI-37723;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 5130 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NC2 alpha/DRAP1 family. {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; Y09265; CAA70460.1; -; mRNA.
DR EMBL; U18917; AAB64686.1; -; Genomic_DNA.
DR EMBL; AY693203; AAT93222.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07820.1; -; Genomic_DNA.
DR PIR; S50662; S50662.
DR RefSeq; NP_011086.3; NM_001179049.3.
DR AlphaFoldDB; P40096; -.
DR SMR; P40096; -.
DR BioGRID; 36910; 348.
DR ComplexPortal; CPX-1662; Negative cofactor 2 complex.
DR DIP; DIP-2066N; -.
DR IntAct; P40096; 4.
DR MINT; P40096; -.
DR STRING; 4932.YER159C; -.
DR iPTMnet; P40096; -.
DR MaxQB; P40096; -.
DR PaxDb; P40096; -.
DR PRIDE; P40096; -.
DR EnsemblFungi; YER159C_mRNA; YER159C; YER159C.
DR GeneID; 856904; -.
DR KEGG; sce:YER159C; -.
DR SGD; S000000961; BUR6.
DR VEuPathDB; FungiDB:YER159C; -.
DR eggNOG; KOG1659; Eukaryota.
DR GeneTree; ENSGT00390000012424; -.
DR HOGENOM; CLU_045277_9_1_1; -.
DR InParanoid; P40096; -.
DR OMA; IMKKTIM; -.
DR BioCyc; YEAST:G3O-30320-MON; -.
DR PRO; PR:P40096; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40096; protein.
DR GO; GO:0017054; C:negative cofactor 2 complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:SGD.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:SGD.
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: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:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IMP:SGD.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR027116; Bur6/Dpb3.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR PANTHER; PTHR10252:SF5; PTHR10252:SF5; 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..142
FT /note="Negative cofactor 2 complex subunit alpha"
FT /id="PRO_0000096755"
FT DOMAIN 29..137
FT /note="Histone-fold"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 142 AA; 15517 MW; 27341BD250973BA7 CRC64;
MADQVPVTTQ LPPIKPEHEV PLDAGGSPVG NMGTNSNNNN ELGDVFDRIK THFPPAKVKK
IMQTDEDIGK VSQATPVIAG RSLEFFIALL VKKSGEMARG QGTKRITAEI LKKTILNDEK
FDFLREGLCV EEGQTQPEEE SA
