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P39678

- MBP1_YEAST

UniProt

P39678 - MBP1_YEAST

Protein

Transcription factor MBP1

Gene

MBP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      Previous versions | rss
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    Functioni

    Binds to MCB elements (Mlu I cell cycle box) found in the promoter of most DNA synthesis genes. Transcriptional activation by MBF has an important role in the transition from G1 to S phase. It may have a dual role in that it behaves as an activator of transcription at the G1-S boundary and as a repressor during other stages of the cell cycle.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi36 – 5722H-T-H motifPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: SGD

    GO - Biological processi

    1. positive regulation of transcription involved in G1/S transition of mitotic cell cycle Source: SGD

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29472-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcription factor MBP1
    Alternative name(s):
    MBF subunit p120
    Gene namesi
    Name:MBP1
    Ordered Locus Names:YDL056W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDL056w.
    SGDiS000002214. MBP1.

    Subcellular locationi

    GO - Cellular componenti

    1. MBF transcription complex Source: SGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 833833Transcription factor MBP1PRO_0000067062Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei110 – 1101Phosphoserine2 Publications
    Modified residuei325 – 3251Phosphothreonine1 Publication
    Modified residuei326 – 3261Phosphoserine1 Publication
    Modified residuei330 – 3301Phosphoserine1 Publication
    Modified residuei827 – 8271Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP39678.
    PaxDbiP39678.

    Expressioni

    Gene expression databases

    GenevestigatoriP39678.

    Interactioni

    Subunit structurei

    Component of the transcription complex MCB-binding factor (MBF) composed of SWI6 and MBP1. Interacts with MSA1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    SWI6P099595EBI-10485,EBI-18641

    Protein-protein interaction databases

    BioGridi32002. 93 interactions.
    DIPiDIP-2391N.
    IntActiP39678. 28 interactions.
    MINTiMINT-616665.

    Structurei

    Secondary structure

    1
    833
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 106
    Beta strandi13 – 197
    Beta strandi24 – 285
    Turni29 – 313
    Beta strandi33 – 353
    Helixi36 – 427
    Helixi47 – 5711
    Turni58 – 603
    Beta strandi64 – 696
    Turni71 – 733
    Beta strandi75 – 784
    Helixi80 – 8910
    Helixi93 – 1019

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BM8X-ray1.71A4-102[»]
    1L3GNMR-A2-124[»]
    1MB1X-ray2.10A1-124[»]
    ProteinModelPortaliP39678.
    SMRiP39678. Positions 2-124, 349-547.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP39678.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 111107HTH APSES-typePROSITE-ProRule annotationAdd
    BLAST
    Repeati394 – 42330ANK 1Add
    BLAST
    Repeati512 – 54130ANK 2Add
    BLAST

    Sequence similaritiesi

    Contains 2 ANK repeats.PROSITE-ProRule annotation
    Contains 1 HTH APSES-type DNA-binding domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    GeneTreeiENSGT00530000067565.
    HOGENOMiHOG000113493.
    KOiK06647.
    OMAiTGSIMKR.
    OrthoDBiEOG7ZSJ36.

    Family and domain databases

    Gene3Di1.25.40.20. 1 hit.
    3.10.260.10. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR018004. KilA_N/APSES_HTH.
    IPR003163. Tscrpt_reg_HTH_APSES-type.
    [Graphical view]
    PfamiPF00023. Ank. 2 hits.
    PF04383. KilA-N. 1 hit.
    [Graphical view]
    SMARTiSM00248. ANK. 3 hits.
    [Graphical view]
    SUPFAMiSSF48403. SSF48403. 1 hit.
    SSF54616. SSF54616. 1 hit.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 2 hits.
    PS51299. HTH_APSES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P39678-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSNQIYSARY SGVDVYEFIH STGSIMKRKK DDWVNATHIL KAANFAKAKR    50
    TRILEKEVLK ETHEKVQGGF GKYQGTWVPL NIAKQLAEKF SVYDQLKPLF 100
    DFTQTDGSAS PPPAPKHHHA SKVDRKKAIR SASTSAIMET KRNNKKAEEN 150
    QFQSSKILGN PTAAPRKRGR PVGSTRGSRR KLGVNLQRSQ SDMGFPRPAI 200
    PNSSISTTQL PSIRSTMGPQ SPTLGILEEE RHDSRQQQPQ QNNSAQFKEI 250
    DLEDGLSSDV EPSQQLQQVF NQNTGFVPQQ QSSLIQTQQT ESMATSVSSS 300
    PSLPTSPGDF ADSNPFEERF PGGGTSPIIS MIPRYPVTSR PQTSDINDKV 350
    NKYLSKLVDY FISNEMKSNK SLPQVLLHPP PHSAPYIDAP IDPELHTAFH 400
    WACSMGNLPI AEALYEAGTS IRSTNSQGQT PLMRSSLFHN SYTRRTFPRI 450
    FQLLHETVFD IDSQSQTVIH HIVKRKSTTP SAVYYLDVVL SKIKDFSPQY 500
    RIELLLNTQD KNGDTALHIA SKNGDVVFFN TLVKMGALTT ISNKEGLTAN 550
    EIMNQQYEQM MIQNGTNQHV NSSNTDLNIH VNTNNIETKN DVNSMVIMSP 600
    VSPSDYITYP SQIATNISRN IPNVVNSMKQ MASIYNDLHE QHDNEIKSLQ 650
    KTLKSISKTK IQVSLKTLEV LKESSKDENG EAQTNDDFEI LSRLQEQNTK 700
    KLRKRLIRYK RLIKQKLEYR QTVLLNKLIE DETQATTNNT VEKDNNTLER 750
    LELAQELTML QLQRKNKLSS LVKKFEDNAK IHKYRRIIRE GTEMNIEEVD 800
    SSLDVILQTL IANNNKNKGA EQIITISNAN SHA 833
    Length:833
    Mass (Da):93,908
    Last modified:February 1, 1995 - v1
    Checksum:iBB7C35E29802BBD5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74158 Genomic DNA. Translation: CAA52271.1.
    Z74104 Genomic DNA. Translation: CAA98618.1.
    U19608 Genomic DNA. Translation: AAC49290.1.
    BK006938 Genomic DNA. Translation: DAA11800.1.
    PIRiA47528.
    RefSeqiNP_010227.1. NM_001180115.1.

    Genome annotation databases

    EnsemblFungiiYDL056W; YDL056W; YDL056W.
    GeneIDi851503.
    KEGGisce:YDL056W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X74158 Genomic DNA. Translation: CAA52271.1 .
    Z74104 Genomic DNA. Translation: CAA98618.1 .
    U19608 Genomic DNA. Translation: AAC49290.1 .
    BK006938 Genomic DNA. Translation: DAA11800.1 .
    PIRi A47528.
    RefSeqi NP_010227.1. NM_001180115.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BM8 X-ray 1.71 A 4-102 [» ]
    1L3G NMR - A 2-124 [» ]
    1MB1 X-ray 2.10 A 1-124 [» ]
    ProteinModelPortali P39678.
    SMRi P39678. Positions 2-124, 349-547.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32002. 93 interactions.
    DIPi DIP-2391N.
    IntActi P39678. 28 interactions.
    MINTi MINT-616665.

    Proteomic databases

    MaxQBi P39678.
    PaxDbi P39678.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDL056W ; YDL056W ; YDL056W .
    GeneIDi 851503.
    KEGGi sce:YDL056W.

    Organism-specific databases

    CYGDi YDL056w.
    SGDi S000002214. MBP1.

    Phylogenomic databases

    eggNOGi COG0666.
    GeneTreei ENSGT00530000067565.
    HOGENOMi HOG000113493.
    KOi K06647.
    OMAi TGSIMKR.
    OrthoDBi EOG7ZSJ36.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29472-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P39678.
    NextBioi 968852.

    Gene expression databases

    Genevestigatori P39678.

    Family and domain databases

    Gene3Di 1.25.40.20. 1 hit.
    3.10.260.10. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR018004. KilA_N/APSES_HTH.
    IPR003163. Tscrpt_reg_HTH_APSES-type.
    [Graphical view ]
    Pfami PF00023. Ank. 2 hits.
    PF04383. KilA-N. 1 hit.
    [Graphical view ]
    SMARTi SM00248. ANK. 3 hits.
    [Graphical view ]
    SUPFAMi SSF48403. SSF48403. 1 hit.
    SSF54616. SSF54616. 1 hit.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 2 hits.
    PS51299. HTH_APSES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A role for the transcription factors Mbp1 and Swi4 in progression from G1 to S phase."
      Koch C., Moll T., Neuberg M., Ahorn H., Nasmyth K.
      Science 261:1551-1557(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 372-387.
      Strain: K1107.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
      , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "Over-expression of S. cerevisiae G1 cyclins restores the viability of alg1 N-glycosylation mutants."
      Benton B.K., Plump S.D., Roos J., Lennarz W.J., Cross F.R.
      Curr. Genet. 29:106-113(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 460-833.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    7. "The SBF- and MBF-associated protein Msa1 is required for proper timing of G1-specific transcription in Saccharomyces cerevisiae."
      Ashe M., de Bruin R.A.M., Kalashnikova T., McDonald W.H., Yates J.R. III, Wittenberg C.
      J. Biol. Chem. 283:6040-6049(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MSA1.
    8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110 AND SER-827, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; THR-325; SER-326 AND SER-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "The X-ray structure of the DNA-binding domain from the Saccharomyces cerevisiae cell-cycle transcription factor Mbp1 at 2.1-A resolution."
      Taylor I.A., Treiber M.K., Olivi L., Smerdon S.J.
      J. Mol. Biol. 272:1-8(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-100.
    11. "Crystal structure of the DNA-binding domain of Mbp1, a transcription factor important in cell-cycle control of DNA synthesis."
      Xu R.M., Koch C., Liu Y., Horton J.R., Knapp D., Nasmyth K., Cheng X.
      Structure 5:349-358(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) OF 1-102.

    Entry informationi

    Entry nameiMBP1_YEAST
    AccessioniPrimary (citable) accession number: P39678
    Secondary accession number(s): D6VRU0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 152 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 521 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3