MBP1_YEAST
ID MBP1_YEAST Reviewed; 833 AA.
AC P39678; D6VRU0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Transcription factor MBP1;
DE AltName: Full=MBF subunit p120;
GN Name=MBP1; OrderedLocusNames=YDL056W;
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], AND PROTEIN SEQUENCE OF 372-387.
RC STRAIN=K1107;
RX PubMed=8372350; DOI=10.1126/science.8372350;
RA Koch C., Moll T., Neuberg M., Ahorn H., Nasmyth K.;
RT "A role for the transcription factors Mbp1 and Swi4 in progression from G1
RT to S phase.";
RL Science 261:1551-1557(1993).
RN [2]
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 [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 460-833.
RX PubMed=8821656; DOI=10.1007/bf02221573;
RA Benton B.K., Plump S.D., Roos J., Lennarz W.J., Cross F.R.;
RT "Over-expression of S. cerevisiae G1 cyclins restores the viability of alg1
RT N-glycosylation mutants.";
RL Curr. Genet. 29:106-113(1996).
RN [5]
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 [6]
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 [7]
RP INTERACTION WITH MSA1.
RX PubMed=18160399; DOI=10.1074/jbc.m708248200;
RA Ashe M., de Bruin R.A.M., Kalashnikova T., McDonald W.H., Yates J.R. III,
RA Wittenberg C.;
RT "The SBF- and MBF-associated protein Msa1 is required for proper timing of
RT G1-specific transcription in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 283:6040-6049(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-827, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; THR-325; SER-326 AND
RP SER-330, AND 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 [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-100.
RX PubMed=9299332; DOI=10.1006/jmbi.1997.1229;
RA Taylor I.A., Treiber M.K., Olivi L., Smerdon S.J.;
RT "The X-ray structure of the DNA-binding domain from the Saccharomyces
RT cerevisiae cell-cycle transcription factor Mbp1 at 2.1-A resolution.";
RL J. Mol. Biol. 272:1-8(1997).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 1-102.
RX PubMed=9083114; DOI=10.1016/s0969-2126(97)00192-5;
RA Xu R.M., Koch C., Liu Y., Horton J.R., Knapp D., Nasmyth K., Cheng X.;
RT "Crystal structure of the DNA-binding domain of Mbp1, a transcription
RT factor important in cell-cycle control of DNA synthesis.";
RL Structure 5:349-358(1997).
CC -!- FUNCTION: Binds to MCB elements (Mlu I cell cycle box) found in the
CC promoter of most DNA synthesis genes. Transcriptional activation by MBF
CC has an important role in the transition from G1 to S phase. It may have
CC a dual role in that it behaves as an activator of transcription at the
CC G1-S boundary and as a repressor during other stages of the cell cycle.
CC -!- SUBUNIT: Component of the transcription complex MCB-binding factor
CC (MBF) composed of SWI6 and MBP1. Interacts with MSA1.
CC {ECO:0000269|PubMed:18160399}.
CC -!- INTERACTION:
CC P39678; P09959: SWI6; NbExp=4; IntAct=EBI-10485, EBI-18641;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- MISCELLANEOUS: Present with 521 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X74158; CAA52271.1; -; Genomic_DNA.
DR EMBL; Z74104; CAA98618.1; -; Genomic_DNA.
DR EMBL; U19608; AAC49290.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11800.1; -; Genomic_DNA.
DR PIR; A47528; A47528.
DR RefSeq; NP_010227.1; NM_001180115.1.
DR PDB; 1BM8; X-ray; 1.71 A; A=4-102.
DR PDB; 1L3G; NMR; -; A=2-124.
DR PDB; 1MB1; X-ray; 2.10 A; A=1-124.
DR PDBsum; 1BM8; -.
DR PDBsum; 1L3G; -.
DR PDBsum; 1MB1; -.
DR AlphaFoldDB; P39678; -.
DR BMRB; P39678; -.
DR SMR; P39678; -.
DR BioGRID; 32002; 162.
DR ComplexPortal; CPX-950; MBP transcription complex.
DR DIP; DIP-2391N; -.
DR IntAct; P39678; 29.
DR MINT; P39678; -.
DR STRING; 4932.YDL056W; -.
DR iPTMnet; P39678; -.
DR MaxQB; P39678; -.
DR PaxDb; P39678; -.
DR PRIDE; P39678; -.
DR EnsemblFungi; YDL056W_mRNA; YDL056W; YDL056W.
DR GeneID; 851503; -.
DR KEGG; sce:YDL056W; -.
DR SGD; S000002214; MBP1.
DR VEuPathDB; FungiDB:YDL056W; -.
DR eggNOG; KOG4177; Eukaryota.
DR HOGENOM; CLU_009666_3_0_1; -.
DR InParanoid; P39678; -.
DR OMA; QRNARKC; -.
DR BioCyc; YEAST:G3O-29472-MON; -.
DR EvolutionaryTrace; P39678; -.
DR PRO; PR:P39678; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P39678; protein.
DR GO; GO:0030907; C:MBF transcription complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0033309; C:SBF transcription complex; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:SGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0071931; P:positive regulation of transcription involved in G1/S transition of mitotic cell cycle; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.10.260.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR036887; HTH_APSES_sf.
DR InterPro; IPR018004; KilA_N/APSES_HTH.
DR InterPro; IPR029793; Mbp1/Res1/Res2.
DR InterPro; IPR003163; Tscrpt_reg_HTH_APSES-type.
DR PANTHER; PTHR43828:SF1; PTHR43828:SF1; 1.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF04383; KilA-N; 1.
DR SMART; SM00248; ANK; 3.
DR SMART; SM01252; KilA-N; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF54616; SSF54616; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS51299; HTH_APSES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; ANK repeat; Direct protein sequencing;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..833
FT /note="Transcription factor MBP1"
FT /id="PRO_0000067062"
FT DOMAIN 5..111
FT /note="HTH APSES-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REPEAT 394..423
FT /note="ANK 1"
FT REPEAT 512..541
FT /note="ANK 2"
FT DNA_BIND 36..57
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00630"
FT REGION 104..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 325
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 827
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:1BM8"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:1BM8"
FT STRAND 24..28
FT /evidence="ECO:0007829|PDB:1BM8"
FT TURN 29..31
FT /evidence="ECO:0007829|PDB:1BM8"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1L3G"
FT HELIX 36..42
FT /evidence="ECO:0007829|PDB:1BM8"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:1BM8"
FT TURN 58..60
FT /evidence="ECO:0007829|PDB:1BM8"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1BM8"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1MB1"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:1BM8"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:1BM8"
FT HELIX 93..101
FT /evidence="ECO:0007829|PDB:1BM8"
SQ SEQUENCE 833 AA; 93908 MW; BB7C35E29802BBD5 CRC64;
MSNQIYSARY SGVDVYEFIH STGSIMKRKK DDWVNATHIL KAANFAKAKR TRILEKEVLK
ETHEKVQGGF GKYQGTWVPL NIAKQLAEKF SVYDQLKPLF DFTQTDGSAS PPPAPKHHHA
SKVDRKKAIR SASTSAIMET KRNNKKAEEN QFQSSKILGN PTAAPRKRGR PVGSTRGSRR
KLGVNLQRSQ SDMGFPRPAI PNSSISTTQL PSIRSTMGPQ SPTLGILEEE RHDSRQQQPQ
QNNSAQFKEI DLEDGLSSDV EPSQQLQQVF NQNTGFVPQQ QSSLIQTQQT ESMATSVSSS
PSLPTSPGDF ADSNPFEERF PGGGTSPIIS MIPRYPVTSR PQTSDINDKV NKYLSKLVDY
FISNEMKSNK SLPQVLLHPP PHSAPYIDAP IDPELHTAFH WACSMGNLPI AEALYEAGTS
IRSTNSQGQT PLMRSSLFHN SYTRRTFPRI FQLLHETVFD IDSQSQTVIH HIVKRKSTTP
SAVYYLDVVL SKIKDFSPQY RIELLLNTQD KNGDTALHIA SKNGDVVFFN TLVKMGALTT
ISNKEGLTAN EIMNQQYEQM MIQNGTNQHV NSSNTDLNIH VNTNNIETKN DVNSMVIMSP
VSPSDYITYP SQIATNISRN IPNVVNSMKQ MASIYNDLHE QHDNEIKSLQ KTLKSISKTK
IQVSLKTLEV LKESSKDENG EAQTNDDFEI LSRLQEQNTK KLRKRLIRYK RLIKQKLEYR
QTVLLNKLIE DETQATTNNT VEKDNNTLER LELAQELTML QLQRKNKLSS LVKKFEDNAK
IHKYRRIIRE GTEMNIEEVD SSLDVILQTL IANNNKNKGA EQIITISNAN SHA
