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Q02969 (PEX25_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisomal membrane protein PEX25
Alternative name(s):
Peroxin-25
Gene names
Name:PEX25
Ordered Locus Names:YPL112C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for regulation of peroxisome size and maintenance. Has a role in the import of peroxisomal matrix proteins. Imports RHO1 into the peroxisome. Also promotes peroxisome division and biogenesis. Ref.4 Ref.5 Ref.6 Ref.9 Ref.14

Subunit structure

Homooligomer. Interacts with PEX27 and PEX34. Ref.4 Ref.6 Ref.14

Subcellular location

Peroxisome membrane; Single-pass membrane protein Ref.4 Ref.5 Ref.7 Ref.9.

Miscellaneous

Present with 2420 molecules/cell in log phase SD medium.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394Peroxisomal membrane protein PEX25
PRO_0000270568

Regions

Topological domain1 – 366366Cytoplasmic Potential
Transmembrane367 – 38317Helical; Potential
Topological domain384 – 39411Lumenal Potential

Amino acid modifications

Modified residue581Phosphoserine Ref.11
Modified residue631Phosphoserine Ref.11
Modified residue2891Phosphoserine Ref.10 Ref.12

Experimental info

Sequence conflict81D → N in AAT92840. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q02969 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: A453AF4B5E41DB68

FASTA39444,911
        10         20         30         40         50         60 
MSQFGTTDIV SGSETPPYSG ASYQDAQDDN THPHSSDAGA EKFSAGSGSE SHTESSRSDD 

        70         80         90        100        110        120 
EDSQAKTKMV DNITILKYIL DSLSGRDKLA KIIKYALDIL KLFIEKSKRN LTVLDPSVLT 

       130        140        150        160        170        180 
YYTKILKNLT VKVALRHPIT VIKVLLLSLL RNFDKKIDFI SQQLSTFRYI LRFGGTPFRV 

       190        200        210        220        230        240 
CSFLGKFNKT RKCNFQIDQI KKIWFNEASL REFLDLYYGI FDELDLLYKL KIWTNKSFYS 

       250        260        270        280        290        300 
FVSRQESLAW QYDILLSLKD HWLNLQSLQK RQLELEVQLK VQNNALLLSP ILMHQAHKDD 

       310        320        330        340        350        360 
GSQSPIRKQL LNDLNVNNDA EVLIHKQLKA IKDEKTLVYL DIARLSFDCM ANTSDILNLK 

       370        380        390 
TPKGTYAVLS LGSGLTGLVK LWITTKRSLC SSKD 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. expand/collapse author list , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Conserved function of pex11p and the novel pex25p and pex27p in peroxisome biogenesis."
Rottensteiner H., Stein K., Sonnenhol E., Erdmann R.
Mol. Biol. Cell 14:4316-4328(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 56-70 AND 337-354, FUNCTION, SUBUNIT, INTERACTION WITH PEX27, SUBCELLULAR LOCATION.
Strain: ATCC 201389 / BY4742.
[5]"Transcriptome profiling to identify genes involved in peroxisome assembly and function."
Smith J.J., Marelli M., Christmas R.H., Vizeacoumar F.J., Dilworth D.J., Ideker T., Galitski T., Dimitrov K., Rachubinski R.A., Aitchison J.D.
J. Cell Biol. 158:259-271(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Pex11-related proteins in peroxisome dynamics: a role for the novel peroxin Pex27p in controlling peroxisome size and number in Saccharomyces cerevisiae."
Tam Y.Y.C., Torres-Guzman J.C., Vizeacoumar F.J., Smith J.J., Marelli M., Aitchison J.D., Rachubinski R.A.
Mol. Biol. Cell 14:4089-4102(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT, INTERACTION WITH PEX27.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"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].
[9]"Quantitative mass spectrometry reveals a role for the GTPase Rho1p in actin organization on the peroxisome membrane."
Marelli M., Smith J.J., Jung S., Yi E., Nesvizhskii A.I., Christmas R.H., Saleem R.A., Tam Y.Y.C., Fagarasanu A., Goodlett D.R., Aebersold R., Rachubinski R.A., Aitchison J.D.
J. Cell Biol. 167:1099-1112(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"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-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[11]"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-58 AND SER-63, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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].
[14]"The peroxin Pex34p functions with the Pex11 family of peroxisomal divisional proteins to regulate the peroxisome population in yeast."
Tower R.J., Fagarasanu A., Aitchison J.D., Rachubinski R.A.
Mol. Biol. Cell 22:1727-1738(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PEX34.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U43503 Genomic DNA. Translation: AAB68249.1.
AY692821 Genomic DNA. Translation: AAT92840.1.
BK006949 Genomic DNA. Translation: DAA11321.1.
PIRS62009.
RefSeqNP_015213.1. NM_001183926.1.

3D structure databases

ProteinModelPortalQ02969.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36068. 25 interactions.
DIPDIP-5292N.
IntActQ02969. 5 interactions.
MINTMINT-504153.
STRING4932.YPL112C.

Protein family/group databases

TCDB3.A.20.1.5. the peroxisomal protein importer (ppi) family.

Proteomic databases

PaxDbQ02969.
PeptideAtlasQ02969.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL112C; YPL112C; YPL112C.
GeneID855991.
KEGGsce:YPL112C.

Organism-specific databases

CYGDYPL112c.
SGDS000006033. PEX25.

Phylogenomic databases

eggNOGNOG40921.
HOGENOMHOG000066022.
OMAYGIMDEL.
OrthoDBEOG7PCJS4.

Enzyme and pathway databases

BioCycYEAST:G3O-34013-MONOMER.

Gene expression databases

GenevestigatorQ02969.

Family and domain databases

InterProIPR008733. PEX11.
[Graphical view]
PfamPF05648. PEX11. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio980843.

Entry information

Entry namePEX25_YEAST
AccessionPrimary (citable) accession number: Q02969
Secondary accession number(s): D6W3Q5, Q6B2A9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 95 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 XVI

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

Yeast

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