CBF1_YEAST
ID CBF1_YEAST Reviewed; 351 AA.
AC P17106; D6VWN1; P17623; Q6Q5N1;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Centromere-binding protein 1;
DE Short=CBP-1;
DE AltName: Full=Centromere promoter factor 1;
DE AltName: Full=Centromere-binding factor 1;
GN Name=CBF1; Synonyms=CEP1, CP1, CPF1; OrderedLocusNames=YJR060W;
GN ORFNames=J1730;
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 214-231, AND
RP SUBCELLULAR LOCATION.
RX PubMed=2185892; DOI=10.1016/0092-8674(90)90525-j;
RA Cai M., Davis R.W.;
RT "Yeast centromere binding protein CBF1, of the helix-loop-helix protein
RT family, is required for chromosome stability and methionine prototrophy.";
RL Cell 61:437-446(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 44827 / SKQ2N;
RX PubMed=2249662; DOI=10.1002/j.1460-2075.1990.tb07623.x;
RA Mellor J., Jiang W., Funk M., Rathjen J., Barnes C.A., Hinz T.,
RA Hegemann J.H., Philippsen P.;
RT "CPF1, a yeast protein which functions in centromeres and promoters.";
RL EMBO J. 9:4017-4026(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2188087; DOI=10.1128/mcb.10.6.2458-2467.1990;
RA Baker R.E., Masison D.C.;
RT "Isolation of the gene encoding the Saccharomyces cerevisiae centromere-
RT binding protein CP1.";
RL Mol. Cell. Biol. 10:2458-2467(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8840504;
RX DOI=10.1002/(sici)1097-0061(199607)12:9<869::aid-yea964>3.0.co;2-1;
RA Huang M.-E., Manus V., Chuat J.-C., Galibert F.;
RT "Analysis of a 62 kb DNA sequence of chromosome X reveals 36 open reading
RT frames and a gene cluster with a counterpart on chromosome XI.";
RL Yeast 12:869-875(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [6]
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 [7]
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 [8]
RP FUNCTION.
RX PubMed=1549123; DOI=10.1128/mcb.12.4.1719-1727.1992;
RA Thomas D., Jacquemin I., Surdin-Kerjan Y.;
RT "MET4, a leucine zipper protein, and centromere-binding factor 1 are both
RT required for transcriptional activation of sulfur metabolism in
RT Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 12:1719-1727(1992).
RN [9]
RP FUNCTION, AND INTERACTION WITH MET4.
RX PubMed=8665859; DOI=10.1002/j.1460-2075.1996.tb00609.x;
RA Kuras L., Cherest H., Surdin-Kerjan Y., Thomas D.;
RT "A heteromeric complex containing the centromere binding factor 1 and two
RT basic leucine zipper factors, Met4 and Met28, mediates the transcription
RT activation of yeast sulfur metabolism.";
RL EMBO J. 15:2519-2529(1996).
RN [10]
RP SUBUNIT.
RX PubMed=9171357; DOI=10.1093/emboj/16.9.2441;
RA Kuras L., Barbey R., Thomas D.;
RT "Assembly of a bZIP-bHLH transcription activation complex: formation of the
RT yeast Cbf1-Met4-Met28 complex is regulated through Met28 stimulation of
RT Cbf1 DNA binding.";
RL EMBO J. 16:2441-2451(1997).
RN [11]
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 [12]
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 [13]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-48 AND SER-84, 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).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-48 AND THR-138, 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).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Required for chromosome stability and methionine prototrophy.
CC It is involved in chromosomal segregation. Binds to a highly conserved
CC DNA sequence (5'-RTCACRTG-3'), called CDEI, found in centromeres and in
CC several promoters. DNA-binding activity is enhanced by MET28. Required
CC as an auxiliary factor for transcriptional activation of sulfur
CC metabolism together with MET4 and MET28. {ECO:0000269|PubMed:1549123,
CC ECO:0000269|PubMed:8665859}.
CC -!- SUBUNIT: Binds DNA as a dimer. Associates with MET4 to form a
CC heteromeric complex which also includes MET28.
CC {ECO:0000269|PubMed:9171357}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC Mitochondrion {ECO:0000269|PubMed:14576278}. Chromosome, centromere
CC {ECO:0000269|PubMed:2185892}.
CC -!- MISCELLANEOUS: Present with 6890 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M33620; AAA34490.1; -; Genomic_DNA.
DR EMBL; X52137; CAA36382.1; -; Genomic_DNA.
DR EMBL; M34070; AAA34524.1; -; Genomic_DNA.
DR EMBL; L47993; AAB39286.1; -; Genomic_DNA.
DR EMBL; Z49560; CAA89588.1; -; Genomic_DNA.
DR EMBL; AY557919; AAS56245.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08847.1; -; Genomic_DNA.
DR PIR; S57079; JSBYP1.
DR RefSeq; NP_012594.1; NM_001181718.1.
DR AlphaFoldDB; P17106; -.
DR SMR; P17106; -.
DR BioGRID; 33817; 554.
DR ComplexPortal; CPX-1016; CBF1-MET4-MET28 sulfur metabolism transcription factor complex.
DR DIP; DIP-2239N; -.
DR IntAct; P17106; 4.
DR MINT; P17106; -.
DR STRING; 4932.YJR060W; -.
DR iPTMnet; P17106; -.
DR MaxQB; P17106; -.
DR PaxDb; P17106; -.
DR PRIDE; P17106; -.
DR EnsemblFungi; YJR060W_mRNA; YJR060W; YJR060W.
DR GeneID; 853523; -.
DR KEGG; sce:YJR060W; -.
DR SGD; S000003821; CBF1.
DR VEuPathDB; FungiDB:YJR060W; -.
DR eggNOG; KOG1318; Eukaryota.
DR HOGENOM; CLU_046871_0_0_1; -.
DR InParanoid; P17106; -.
DR BioCyc; YEAST:G3O-31693-MON; -.
DR PRO; PR:P17106; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P17106; protein.
DR GO; GO:0089713; C:Cbf1-Met4-Met28 complex; IDA:SGD.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:SGD.
DR GO; GO:0000776; C:kinetochore; IPI:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0019237; F:centromeric DNA binding; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0098781; P:ncRNA transcription; IMP:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0042762; P:regulation of sulfur metabolic process; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:SGD.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Centromere; Chromosome; Direct protein sequencing;
KW DNA-binding; Mitochondrion; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..351
FT /note="Centromere-binding protein 1"
FT /id="PRO_0000127161"
FT DOMAIN 222..270
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 134..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 45
FT /note="Phosphoserine; by ATM or ATR"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 138
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 144
FT /note="V -> F (in Ref. 2; CAA36382)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="M -> T (in Ref. 7; AAS56245)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="C -> R (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 39388 MW; 068F7FA578CB90FC CRC64;
MNSLANNNKL STEDEEIHSA RKRGYNEEQN YSEARKKQRD QGLLSQESND GNIDSALLSE
GATLKGTQSQ YESGLTSNKD EKGSDDEDAS VAEAAVAATV NYTDLIQGQE DSSDAHTSNQ
TNANGEHKDS LNGERAITPS NEGVKPNTSL EGMTSSPMES TQQSKNDMLI PLAEHDRGPE
HQQDDEDNDD ADIDLKKDIS MQPGRRGRKP TTLATTDEWK KQRKDSHKEV ERRRRENINT
AINVLSDLLP VRESSKAAIL ACAAEYIQKL KETDEANIEK WTLQKLLSEQ NASQLASANE
KLQEELGNAY KEIEYMKRVL RKEGIEYEDM HTHKKQENER KSTRSDNPHE A
