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Protein

Protein BMH1

Gene

BMH1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in growth regulation.

GO - Molecular functioni

  • DNA replication origin binding Source: SGD
  • phosphoserine binding Source: SGD
  • RNA polymerase II activating transcription factor binding Source: SGD

GO - Biological processi

  • aggresome assembly Source: SGD
  • ascospore formation Source: SGD
  • DNA damage checkpoint Source: SGD
  • fungal-type cell wall chitin biosynthetic process Source: SGD
  • glycogen metabolic process Source: SGD
  • mitotic spindle orientation checkpoint Source: SGD
  • negative regulation of apoptotic process Source: SGD
  • negative regulation of transcription from RNA polymerase II promoter Source: SGD
  • negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: SGD
  • pseudohyphal growth Source: SGD
  • Ras protein signal transduction Source: SGD
  • signal transduction involved in filamentous growth Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-30336-MONOMER.
ReactomeiREACT_286478. HSF1 activation.
REACT_330550. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_333905. Regulation of HSF1-mediated heat shock response.
REACT_361610. RHO GTPases activate PKNs.

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 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER177W.
SGDiS000000979. BMH1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

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.

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. 321 interactions.
DIPiDIP-4313N.
IntActiP29311. 66 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

GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
InParanoidiP29311.
KOiK06630.
OMAiMETREDY.
OrthoDBiEOG7TXKTD.

Family and domain databases

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

        10         20         30         40         50
MSTSREDSVY LAKLAEQAER YEEMVENMKT VASSGQELSV EERNLLSVAY
60 70 80 90 100
KNVIGARRAS WRIVSSIEQK EESKEKSEHQ VELICSYRSK IETELTKISD
110 120 130 140 150
DILSVLDSHL IPSATTGESK VFYYKMKGDY HRYLAEFSSG DAREKATNAS
160 170 180 190 200
LEAYKTASEI ATTELPPTHP IRLGLALNFS VFYYEIQNSP DKACHLAKQA
210 220 230 240 250
FDDAIAELDT LSEESYKDST LIMQLLRDNL TLWTSDMSES GQAEDQQQQQ
260
QHQQQQPPAA AEGEAPK
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 (Ref. 2) Curated
Sequence conflicti263 – 2675GEAPK → VKHQSKYSDKSKEKLLKKRK KKERGCNNL in CAA50656 (PubMed:1378790).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi36930. 321 interactions.
DIPiDIP-4313N.
IntActiP29311. 66 interactions.
MINTiMINT-382223.
STRINGi4932.YER177W.

2D gel databases

COMPLUYEAST-2DPAGEP29311.
SWISS-2DPAGEP29311.

Proteomic databases

MaxQBiP29311.
PeptideAtlasiP29311.
PRIDEiP29311.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YER177W.
SGDiS000000979. BMH1.

Phylogenomic databases

GeneTreeiENSGT00760000119116.
HOGENOMiHOG000240379.
InParanoidiP29311.
KOiK06630.
OMAiMETREDY.
OrthoDBiEOG7TXKTD.

Enzyme and pathway databases

BioCyciYEAST:G3O-30336-MONOMER.
ReactomeiREACT_286478. HSF1 activation.
REACT_330550. Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex.
REACT_333905. Regulation of HSF1-mediated heat shock response.
REACT_361610. RHO GTPases activate PKNs.

Miscellaneous databases

NextBioi983392.
PROiP29311.

Family and domain databases

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 149 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.