MBF1_YEAST
ID MBF1_YEAST Reviewed; 151 AA.
AC O14467; D6W2Z8; Q7LGJ8; Q86ZS7;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Multiprotein-bridging factor 1;
DE AltName: Full=Suppressor of frameshift mutations protein 13;
GN Name=MBF1; Synonyms=SUF13; OrderedLocusNames=YOR298C-A;
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], INTERACTION WITH GCN4 AND TBP,
RP MUTAGENESIS OF ASP-112, AND FUNCTION.
RC STRAIN=KT130;
RX PubMed=9710580; DOI=10.1128/mcb.18.9.4971;
RA Takemaru K., Harashima S., Ueda H., Hirose S.;
RT "Yeast coactivator MBF1 mediates GCN4-dependent transcriptional
RT activation.";
RL Mol. Cell. Biol. 18:4971-4976(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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] OF 1-58.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [5]
RP PROTEIN SEQUENCE OF 76-83; 103-117 AND 138-149, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (MAY-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-151.
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 [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-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND IDENTIFICATION BY
RP 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: Transcriptional coactivator that stimulates GCN4-dependent
CC transcriptional activity by bridging the DNA-binding region of GCN4 and
CC TBP (SPT15), thereby recruiting TBP to GCN4-bound promoters.
CC {ECO:0000269|PubMed:9710580}.
CC -!- SUBUNIT: Interacts with TBP and the transcription factor GCN4.
CC {ECO:0000269|PubMed:9710580}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 47277 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the MBF1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA99527.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA99530.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB017593; BAA33217.1; -; Genomic_DNA.
DR EMBL; Z75206; CAA99527.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z75207; CAA99530.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AY260886; AAP21754.1; -; Genomic_DNA.
DR EMBL; AY692753; AAT92772.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11064.1; -; Genomic_DNA.
DR PIR; S72394; S72394.
DR RefSeq; NP_014942.4; NM_001184346.3.
DR PDB; 6ZVI; EM; 3.00 A; T=27-137.
DR PDB; 7NRD; EM; 4.36 A; Sh=26-145.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; O14467; -.
DR SMR; O14467; -.
DR BioGRID; 34687; 214.
DR DIP; DIP-8708N; -.
DR IntAct; O14467; 3.
DR MINT; O14467; -.
DR STRING; 4932.YOR298C-A; -.
DR iPTMnet; O14467; -.
DR MaxQB; O14467; -.
DR PaxDb; O14467; -.
DR PRIDE; O14467; -.
DR TopDownProteomics; O14467; -.
DR EnsemblFungi; YOR298C-A_mRNA; YOR298C-A; YOR298C-A.
DR GeneID; 854474; -.
DR KEGG; sce:YOR298C-A; -.
DR SGD; S000007253; MBF1.
DR VEuPathDB; FungiDB:YOR298C-A; -.
DR eggNOG; KOG3398; Eukaryota.
DR GeneTree; ENSGT00390000008519; -.
DR HOGENOM; CLU_112609_0_1_1; -.
DR InParanoid; O14467; -.
DR OMA; NKAHQGT; -.
DR BioCyc; YEAST:G3O-33879-MON; -.
DR PRO; PR:O14467; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; O14467; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013729; MBF1_N.
DR Pfam; PF01381; HTH_3; 1.
DR Pfam; PF08523; MBF1; 1.
DR SMART; SM00530; HTH_XRE; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..151
FT /note="Multiprotein-bridging factor 1"
FT /id="PRO_0000149814"
FT DOMAIN 85..139
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT DNA_BIND 96..115
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00257"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..119
FT /note="Essential for TBP-binding"
FT REGION 78..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MUTAGEN 112
FT /note="D->A: Reduces interaction to TBP."
FT /evidence="ECO:0000269|PubMed:9710580"
FT STRAND 29..31
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 57..60
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 79..90
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 91..93
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 96..102
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 122..132
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 151 AA; 16404 MW; E687ED8768ACD1DF CRC64;
MSDWDTNTII GSRARAGGSG PRANVARSQG QINAARRQGL VVSVDKKYGS TNTRGDNEGQ
RLTKVDRETD IVKPKKLDPN VGRAISRART DKKMSQKDLA TKINEKPTVV NDYEAARAIP
NQQVLSKLER ALGVKLRGNN IGSPLGAPKK K
