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P29311 (BMH1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein BMH1
Gene names
Name:BMH1
Ordered Locus Names:YER177W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in growth regulation.

Subunit structure

Interacts with FIN1. Ref.6

Miscellaneous

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

Sequence similarities

Belongs to the 14-3-3 family.

Ontologies

Keywords
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage checkpoint

Inferred from mutant phenotype PubMed 14704161. Source: SGD

Ras protein signal transduction

Inferred from genetic interaction PubMed 9215628. Source: SGD

aggresome assembly

Inferred from mutant phenotype PubMed 23843611. Source: SGD

ascospore formation

Inferred from genetic interaction PubMed 9215628. Source: SGD

fungal-type cell wall chitin biosynthetic process

Inferred from genetic interaction PubMed 17559233. Source: SGD

glycogen metabolic process

Inferred from genetic interaction PubMed 9215628. Source: SGD

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 22785534. Source: SGD

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 24142105. Source: SGD

negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Inferred from physical interaction PubMed 17030612. Source: SGD

pseudohyphal growth

Inferred from genetic interaction PubMed 9215628. Source: SGD

signal transduction involved in filamentous growth

Inferred from genetic interaction PubMed 9215628. Source: SGD

   Cellular_componentnucleus

Inferred from direct assay PubMed 12167636. Source: SGD

   Molecular_functionDNA replication origin binding

Inferred from direct assay PubMed 12167636. Source: SGD

RNA polymerase II activating transcription factor binding

Inferred from direct assay PubMed 24142105. Source: SGD

phosphoserine binding

Inferred from mutant phenotype PubMed 9822578. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AKT1S1Q96B363EBI-3661,EBI-720593From a different organism.
NTH1P323566EBI-3661,EBI-19509

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 267266Protein BMH1
PRO_0000058715

Amino acid modifications

Modified residue21N-acetylserine Ref.5
Modified residue891Phosphoserine Ref.8

Experimental info

Sequence conflict1971A → R in CAA50656. Ref.1
Sequence conflict1971A → R in CAA46959. Ref.2
Sequence conflict263 – 2675GEAPK → VKHQSKYSDKSKEKLLKKRK KKERGCNNL in CAA50656. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P29311 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 0A234167E313688B

FASTA26730,091
        10         20         30         40         50         60 
MSTSREDSVY LAKLAEQAER YEEMVENMKT VASSGQELSV EERNLLSVAY KNVIGARRAS 

        70         80         90        100        110        120 
WRIVSSIEQK EESKEKSEHQ VELICSYRSK IETELTKISD DILSVLDSHL IPSATTGESK 

       130        140        150        160        170        180 
VFYYKMKGDY HRYLAEFSSG DAREKATNAS LEAYKTASEI ATTELPPTHP IRLGLALNFS 

       190        200        210        220        230        240 
VFYYEIQNSP DKACHLAKQA FDDAIAELDT LSEESYKDST LIMQLLRDNL TLWTSDMSES 

       250        260 
GQAEDQQQQQ QHQQQQPPAA AEGEAPK 

« Hide

References

« Hide 'large scale' references
[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]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X71664 Genomic DNA. Translation: CAA50656.1.
X66206 Genomic DNA. Translation: CAA46959.1.
U18922 Genomic DNA. Translation: AAB64704.1.
BK006939 Genomic DNA. Translation: DAA07840.1.
PIRS30863.
RefSeqNP_011104.3. NM_001179067.3.

3D structure databases

ProteinModelPortalP29311.
SMRP29311. Positions 5-234.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36930. 312 interactions.
DIPDIP-4313N.
IntActP29311. 64 interactions.
MINTMINT-382223.
STRING4932.YER177W.

2D gel databases

COMPLUYEAST-2DPAGEP29311.
SWISS-2DPAGEP29311.

Proteomic databases

PeptideAtlasP29311.
PRIDEP29311.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER177W; YER177W; YER177W.
GeneID856924.
KEGGsce:YER177W.

Organism-specific databases

SGDS000000979. BMH1.

Phylogenomic databases

GeneTreeENSGT00730000110613.
HOGENOMHOG000240379.
KOK06630.
OMAELSDICD.
OrthoDBEOG7TXKTD.

Enzyme and pathway databases

BioCycYEAST:G3O-30336-MONOMER.

Gene expression databases

GenevestigatorP29311.

Family and domain databases

Gene3D1.20.190.20. 1 hit.
InterProIPR000308. 14-3-3.
IPR023409. 14-3-3_CS.
IPR023410. 14-3-3_domain.
[Graphical view]
PANTHERPTHR18860. PTHR18860. 1 hit.
PfamPF00244. 14-3-3. 1 hit.
[Graphical view]
PIRSFPIRSF000868. 14-3-3. 1 hit.
PRINTSPR00305. 1433ZETA.
SMARTSM00101. 14_3_3. 1 hit.
[Graphical view]
SUPFAMSSF48445. SSF48445. 1 hit.
PROSITEPS00796. 1433_1. 1 hit.
PS00797. 1433_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio983392.

Entry information

Entry nameBMH1_YEAST
AccessionPrimary (citable) accession number: P29311
Secondary accession number(s): D3DM86, Q06854
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 136 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families