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P29311

- BMH1_YEAST

UniProt

P29311 - BMH1_YEAST

Protein

Protein BMH1

Gene

BMH1

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 140 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Involved in growth regulation.

    GO - Molecular functioni

    1. DNA replication origin binding Source: SGD
    2. phosphoserine binding Source: SGD
    3. protein binding Source: IntAct
    4. RNA polymerase II activating transcription factor binding Source: SGD

    GO - Biological processi

    1. aggresome assembly Source: SGD
    2. ascospore formation Source: SGD
    3. DNA damage checkpoint Source: SGD
    4. fungal-type cell wall chitin biosynthetic process Source: SGD
    5. glycogen metabolic process Source: SGD
    6. negative regulation of apoptotic process Source: SGD
    7. negative regulation of transcription from RNA polymerase II promoter Source: SGD
    8. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: SGD
    9. pseudohyphal growth Source: SGD
    10. Ras protein signal transduction Source: SGD
    11. signal transduction involved in filamentous growth Source: SGD

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30336-MONOMER.
    ReactomeiREACT_205607. Regulation of HSF1-mediated heat shock response.
    REACT_209789. HSF1 activation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein BMH1
    Gene namesi
    Name:BMH1
    Ordered Locus Names:YER177W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome V

    Organism-specific databases

    SGDiS000000979. BMH1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 267266Protein BMH1PRO_0000058715Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei89 – 891Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP29311.
    PeptideAtlasiP29311.
    PRIDEiP29311.

    2D gel databases

    COMPLUYEAST-2DPAGEP29311.
    SWISS-2DPAGEP29311.

    Expressioni

    Gene expression databases

    GenevestigatoriP29311.

    Interactioni

    Subunit structurei

    Interacts with FIN1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AKT1S1Q96B363EBI-3661,EBI-720593From a different organism.
    NTH1P323566EBI-3661,EBI-19509

    Protein-protein interaction databases

    BioGridi36930. 314 interactions.
    DIPiDIP-4313N.
    IntActiP29311. 65 interactions.
    MINTiMINT-382223.
    STRINGi4932.YER177W.

    Structurei

    3D structure databases

    ProteinModelPortaliP29311.
    SMRiP29311. Positions 5-234.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 14-3-3 family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00730000110613.
    HOGENOMiHOG000240379.
    KOiK06630.
    OMAiAYQKATD.
    OrthoDBiEOG7TXKTD.

    Family and domain databases

    Gene3Di1.20.190.20. 1 hit.
    InterProiIPR000308. 14-3-3.
    IPR023409. 14-3-3_CS.
    IPR023410. 14-3-3_domain.
    [Graphical view]
    PANTHERiPTHR18860. PTHR18860. 1 hit.
    PfamiPF00244. 14-3-3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000868. 14-3-3. 1 hit.
    PRINTSiPR00305. 1433ZETA.
    SMARTiSM00101. 14_3_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48445. SSF48445. 1 hit.
    PROSITEiPS00796. 1433_1. 1 hit.
    PS00797. 1433_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P29311-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTSREDSVY LAKLAEQAER YEEMVENMKT VASSGQELSV EERNLLSVAY    50
    KNVIGARRAS WRIVSSIEQK EESKEKSEHQ VELICSYRSK IETELTKISD 100
    DILSVLDSHL IPSATTGESK VFYYKMKGDY HRYLAEFSSG DAREKATNAS 150
    LEAYKTASEI ATTELPPTHP IRLGLALNFS VFYYEIQNSP DKACHLAKQA 200
    FDDAIAELDT LSEESYKDST LIMQLLRDNL TLWTSDMSES GQAEDQQQQQ 250
    QHQQQQPPAA AEGEAPK 267
    Length:267
    Mass (Da):30,091
    Last modified:January 23, 2007 - v4
    Checksum:i0A234167E313688B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti197 – 1971A → R in CAA50656. (PubMed:1378790)Curated
    Sequence conflicti197 – 1971A → R in CAA46959. 1 PublicationCurated
    Sequence conflicti263 – 2675GEAPK → VKHQSKYSDKSKEKLLKKRK KKERGCNNL in CAA50656. (PubMed:1378790)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71664 Genomic DNA. Translation: CAA50656.1.
    X66206 Genomic DNA. Translation: CAA46959.1.
    U18922 Genomic DNA. Translation: AAB64704.1.
    BK006939 Genomic DNA. Translation: DAA07840.1.
    PIRiS30863.
    RefSeqiNP_011104.3. NM_001179067.3.

    Genome annotation databases

    EnsemblFungiiYER177W; YER177W; YER177W.
    GeneIDi856924.
    KEGGisce:YER177W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X71664 Genomic DNA. Translation: CAA50656.1 .
    X66206 Genomic DNA. Translation: CAA46959.1 .
    U18922 Genomic DNA. Translation: AAB64704.1 .
    BK006939 Genomic DNA. Translation: DAA07840.1 .
    PIRi S30863.
    RefSeqi NP_011104.3. NM_001179067.3.

    3D structure databases

    ProteinModelPortali P29311.
    SMRi P29311. Positions 5-234.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36930. 314 interactions.
    DIPi DIP-4313N.
    IntActi P29311. 65 interactions.
    MINTi MINT-382223.
    STRINGi 4932.YER177W.

    2D gel databases

    COMPLUYEAST-2DPAGE P29311.
    SWISS-2DPAGE P29311.

    Proteomic databases

    MaxQBi P29311.
    PeptideAtlasi P29311.
    PRIDEi P29311.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YER177W ; YER177W ; YER177W .
    GeneIDi 856924.
    KEGGi sce:YER177W.

    Organism-specific databases

    SGDi S000000979. BMH1.

    Phylogenomic databases

    GeneTreei ENSGT00730000110613.
    HOGENOMi HOG000240379.
    KOi K06630.
    OMAi AYQKATD.
    OrthoDBi EOG7TXKTD.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30336-MONOMER.
    Reactomei REACT_205607. Regulation of HSF1-mediated heat shock response.
    REACT_209789. HSF1 activation.

    Miscellaneous databases

    NextBioi 983392.

    Gene expression databases

    Genevestigatori P29311.

    Family and domain databases

    Gene3Di 1.20.190.20. 1 hit.
    InterProi IPR000308. 14-3-3.
    IPR023409. 14-3-3_CS.
    IPR023410. 14-3-3_domain.
    [Graphical view ]
    PANTHERi PTHR18860. PTHR18860. 1 hit.
    Pfami PF00244. 14-3-3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000868. 14-3-3. 1 hit.
    PRINTSi PR00305. 1433ZETA.
    SMARTi SM00101. 14_3_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48445. SSF48445. 1 hit.
    PROSITEi PS00796. 1433_1. 1 hit.
    PS00797. 1433_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the yeast BMH1 gene encoding a putative protein homologous to mammalian protein kinase II activators and protein kinase C inhibitors."
      van Heusden G.P., Wenzel T.J., Lagendijk E.L., de Steensma H.Y., van den Berg J.A.
      FEBS Lett. 302:145-150(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 26109 / X2180.
    2. Mulligan J.T., Dietrich F.S., Hennessey K.M., Sehl P., Komp C., Wei Y., Taylor P., Nakahara K., Roberts D., Davis R.W.
      Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
      Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
      Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT SER-2.
    6. "Self-association of the spindle pole body-related intermediate filament protein Fin1p and its phosphorylation-dependent interaction with 14-3-3 proteins in yeast."
      van Hemert M.J., Deelder A.M., Molenaar C., Steensma H.Y., van Heusden G.P.H.
      J. Biol. Chem. 278:15049-15055(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FIN1.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiBMH1_YEAST
    AccessioniPrimary (citable) accession number: P29311
    Secondary accession number(s): D3DM86, Q06854
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 140 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 158000 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3