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P40091 (PEA2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 PEA2
Alternative name(s):
Protein PPF2
Gene names
Name:PEA2
Synonyms:PPF2
Ordered Locus Names:YER149C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length420 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Localized to sites of polarized growth and is required for efficient mating and bipolar budding.

Miscellaneous

Present with 7820 molecules/cell in log phase SD medium.

Ontologies

Keywords
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbipolar cellular bud site selection

Inferred from mutant phenotype Ref.1. Source: SGD

budding cell apical bud growth

Inferred from mutant phenotype PubMed 10866679. Source: SGD

establishment of cell polarity

Inferred from mutant phenotype PubMed 8013906Ref.1. Source: SGD

filamentous growth

Inferred from mutant phenotype PubMed 15645503. Source: SGD

positive regulation of actin cytoskeleton reorganization

Inferred from mutant phenotype PubMed 17237521PubMed 19633059. Source: SGD

pseudohyphal growth

Inferred from mutant phenotype PubMed 9055077. Source: SGD

regulation of initiation of mating projection growth

Inferred from mutant phenotype PubMed 14734532. Source: SGD

regulation of protein localization

Inferred from mutant phenotype PubMed 10085294PubMed 11740491Ref.1. Source: SGD

regulation of termination of mating projection growth

Inferred from mutant phenotype PubMed 14734532. Source: SGD

   Cellular_componentcellular bud

Inferred from direct assay Ref.1. Source: SGD

cellular bud neck

Inferred from direct assay Ref.1. Source: SGD

cellular bud tip

Inferred from direct assay Ref.1. Source: SGD

incipient cellular bud site

Inferred from direct assay Ref.1. Source: SGD

mating projection tip

Inferred from direct assay Ref.1. Source: SGD

polarisome

Inferred from direct assay PubMed 9632790. Source: SGD

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 11087867PubMed 11743162PubMed 15020407PubMed 18719252PubMed 19841731. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FUS1P117105EBI-13106,EBI-7179
YMR124WP395233EBI-13106,EBI-27256

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 420420Protein PEA2
PRO_0000058300

Amino acid modifications

Modified residue2301Phosphoserine Ref.7 Ref.8 Ref.9

Natural variations

Natural variant901H → R in strain: CLIB 219. Ref.3
Natural variant1171M → T in strain: CLIB 630. Ref.3
Natural variant1571K → T in strain: CLIB 219. Ref.3
Natural variant1611G → S in strain: CLIB 630. Ref.3
Natural variant1651T → I in strain: CLIB 630. Ref.3
Natural variant1711D → N in strain: CLIB 630. Ref.3
Natural variant1891Q → L in strain: CLIB 382. Ref.3
Natural variant2101I → M in strain: CLIB 413 haplotype Ha2. Ref.3
Natural variant2491E → K in strain: CLIB 556. Ref.3
Natural variant2531S → R in strain: Sigma 1278B. Ref.3
Natural variant3251S → N in strain: CLIB 219. Ref.3
Natural variant3551G → S in strain: R12. Ref.3
Natural variant3841S → L in strain: CLIB 219. Ref.3
Natural variant4091L → M in strain: CLIB 410, CLIB 413 and Sigma 1278B. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P40091 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 594B9A14E71A943D

FASTA42048,165
        10         20         30         40         50         60 
MHKFDLELSR RANPLLFSAE RYEEYPLKYD ELKQYLLSQN PSHPHHNSRP YTSIDYFDYL 

        70         80         90        100        110        120 
LYRSKNDESE IDLDKKLVSE FALYYVQKEH LNSDDLNPTL NELLKLQPKS ADWYEMMLRI 

       130        140        150        160        170        180 
LESINTTGID QLTKENNNSF PNSKRARSST NMGGTDKFNK GAYHTDKADD DKNEILQELT 

       190        200        210        220        230        240 
SFLMSNSIQK GIDIKPIPLD DPVKFLKNGI NSILDTCVSL EKNTSSPPIS PNAAAIQEED 

       250        260        270        280        290        300 
SSKKLEELET AFSDLQLAHN FLTKQFENDR AEYVQDIEKL TRTNRELQDK LLNNHSNLSK 

       310        320        330        340        350        360 
TEKKLHELEQ ENKELEKANN KLNSSRHNFG MSSPASSPVT WDPSSPSSVG SPTSGSGSRS 

       370        380        390        400        410        420 
LSIMTSEFKK VLTSTQRKYE KELSDEREHR FKLERELALL KNAEANTSLA LNRDDPPDML 

« Hide

References

« Hide 'large scale' references
[1]"Pea2 protein of yeast is localized to sites of polarized growth and is required for efficient mating and bipolar budding."
Valtz N.L.M., Herskowitz I.
J. Cell Biol. 135:725-739(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A novel yeast gene necessary for pheromone-induced pointed projection formation."
Yorihuzi T., Ohsumi Y.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 26109 / X2180.
[3]"Differential evolution of the Saccharomyces cerevisiae DUP240 paralogs and implication of recombination in phylogeny."
Leh-Louis V., Wirth B., Despons L., Wain-Hobson S., Potier S., Souciet J.-L.
Nucleic Acids Res. 32:2069-2078(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-90; THR-117; THR-157; SER-161; ILE-165; ASN-171; LEU-189; MET-210; LYS-249; ARG-253; ASN-325; SER-355; LEU-384 AND MET-409.
Strain: CLIB 219, CLIB 382, CLIB 388, CLIB 410, CLIB 413, CLIB 556, CLIB 630, CLIB 95, K1, R12, R13, Sigma 1278B, YIIc12 and YIIc17.
[4]"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.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"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].
[7]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[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-230, 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-230, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y07594 Genomic DNA. Translation: CAA68869.1.
D38413 Genomic DNA. Translation: BAA07465.1.
AJ585620 Genomic DNA. Translation: CAE52140.1.
AJ585621 Genomic DNA. Translation: CAE52141.1.
AJ585622 Genomic DNA. Translation: CAE52142.1.
AJ585623 Genomic DNA. Translation: CAE52143.1.
AJ585624 Genomic DNA. Translation: CAE52144.1.
AJ585625 Genomic DNA. Translation: CAE52145.1.
AJ585626 Genomic DNA. Translation: CAE52146.1.
AJ585627 Genomic DNA. Translation: CAE52147.1.
AJ585628 Genomic DNA. Translation: CAE52148.1.
AJ585629 Genomic DNA. Translation: CAE52149.1.
AJ585630 Genomic DNA. Translation: CAE52150.1.
AJ585631 Genomic DNA. Translation: CAE52151.1.
AJ585632 Genomic DNA. Translation: CAE52152.1.
AJ585633 Genomic DNA. Translation: CAE52153.1.
AJ585634 Genomic DNA. Translation: CAE52154.1.
AJ585635 Genomic DNA. Translation: CAE52155.1.
AJ585636 Genomic DNA. Translation: CAE52156.1.
U18917 Genomic DNA. Translation: AAB64676.1.
BK006939 Genomic DNA. Translation: DAA07810.1.
PIRS50652.
RefSeqNP_011076.1. NM_001179039.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36898. 70 interactions.
DIPDIP-2463N.
IntActP40091. 7 interactions.
MINTMINT-436009.

Proteomic databases

MaxQBP40091.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER149C; YER149C; YER149C.
GeneID856892.
KEGGsce:YER149C.

Organism-specific databases

CYGDYER149c.
SGDS000000951. PEA2.

Phylogenomic databases

OrthoDBEOG72ZCQJ.

Enzyme and pathway databases

BioCycYEAST:G3O-30310-MONOMER.

Gene expression databases

GenevestigatorP40091.

Family and domain databases

ProtoNetSearch...

Other

NextBio983299.

Entry information

Entry namePEA2_YEAST
AccessionPrimary (citable) accession number: P40091
Secondary accession number(s): D3DM56 expand/collapse secondary AC list , Q70DC9, Q70DD1, Q70DD2, Q70DD3, Q70DD4, Q70DD6, Q70DD7, Q70DD8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 11, 2014
This is version 105 of the entry and version 1 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