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P38260 (FES1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 117. 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:
Hsp70 nucleotide exchange factor FES1
Alternative name(s):
Factor exchange for SSA1 protein 1
Gene names
Name:FES1
Ordered Locus Names:YBR101C
ORF Names:YBR0830
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length290 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in protein translation, propagation of [PSI+] prions, and polyamine tolerance. Functions as a nucleotide exchange factor (NEF), which accelerates the release of ADP, for the cytosolic Hsp70 chaperone SSA1 and the ribosome-associated Hsp70 chaperone SSB1. Required for fully efficient Hsp70-mediated folding of proteins. Ref.5 Ref.6 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Subunit structure

Interacts with the Hsp70 chaperones SSA1 and SSB1. Ref.6 Ref.16

Subcellular location

Cytoplasm Ref.6 Ref.7.

Miscellaneous

Present with 13100 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the FES1 family.

Contains 6 ARM repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SSA1P105913EBI-21563,EBI-8591

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 290290Hsp70 nucleotide exchange factor FES1
PRO_0000202485

Regions

Repeat13 – 5745ARM 1
Repeat76 – 11641ARM 2
Repeat120 – 16142ARM 3
Repeat164 – 20542ARM 4
Repeat211 – 25141ARM 5
Repeat253 – 29038ARM 6

Amino acid modifications

Modified residue121Phosphoserine Ref.17

Sequences

Sequence LengthMass (Da)Tools
P38260 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 4A50D069625BA500

FASTA29032,604
        10         20         30         40         50         60 
MEKLLQWSIA NSQGDKEAMA RAGQPDPKLL QQLFGGGGPD DPTLMKESMA VIMNPEVDLE 

        70         80         90        100        110        120 
TKLVAFDNFE MLIENLDNAN NIENLKLWEP LLDVLVQTKD EELRAAALSI IGTAVQNNLD 

       130        140        150        160        170        180 
SQNNFMKYDN GLRSLIEIAS DKTKPLDVRT KAFYALSNLI RNHKDISEKF FKLNGLDCIA 

       190        200        210        220        230        240 
PVLSDNTAKP KLKMRAIALL TAYLSSVKID ENIISVLRKD GVIESTIECL SDESNLNIID 

       250        260        270        280        290 
RVLSFLSHLI SSGIKFNEQE LHKLNEGYKH IEPLKDRLNE DDYLAVKYVL 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of a 70 kb region on the right arm of yeast chromosome II."
Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.
Yeast 10:1363-1381(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"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.
[4]"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.
[5]"HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor."
Kabani M., McLellan C., Raynes D.A., Guerriero V., Brodsky J.L.
FEBS Lett. 531:339-342(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p."
Kabani M., Beckerich J.-M., Brodsky J.L.
Mol. Cell. Biol. 22:4677-4689(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SSA1.
[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]"Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by factors that regulate Hsp70 substrate binding."
Jones G., Song Y., Chung S., Masison D.C.
Mol. Cell. Biol. 24:3928-3937(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Distinct but overlapping functions of Hsp70, Hsp90, and an Hsp70 nucleotide exchange factor during protein biogenesis in yeast."
Ahner A., Whyte F.M., Brodsky J.L.
Arch. Biochem. Biophys. 435:32-41(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Mechanism of polyamine tolerance in yeast: novel regulators and insights."
Porat Z., Wender N., Erez O., Kahana C.
Cell. Mol. Life Sci. 62:3106-3116(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"AGP2 encodes the major permease for high affinity polyamine import in Saccharomyces cerevisiae."
Aouida M., Leduc A., Poulin R., Ramotar D.
J. Biol. Chem. 280:24267-24276(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange."
Shomura Y., Dragovic Z., Chang H.-C., Tzvetkov N., Young J.C., Brodsky J.L., Guerriero V. Jr., Hartl F.U., Bracher A.
Mol. Cell 17:367-379(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor."
Raviol H., Sadlish H., Rodriguez F., Mayer M.P., Bukau B.
EMBO J. 25:2510-2518(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s."
Dragovic Z., Broadley S.A., Shomura Y., Bracher A., Hartl F.U.
EMBO J. 25:2519-2528(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Fes1p acts as a nucleotide exchange factor for the ribosome-associated molecular chaperone Ssb1p."
Dragovic Z., Shomura Y., Tzvetkov N., Hartl F.U., Bracher A.
Biol. Chem. 387:1593-1600(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SSB1.
[17]"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-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X78993 Genomic DNA. Translation: CAA55604.1.
Z35970 Genomic DNA. Translation: CAA85056.1.
AY693000 Genomic DNA. Translation: AAT93019.1.
BK006936 Genomic DNA. Translation: DAA07220.1.
PIRS48266.
RefSeqNP_009659.3. NM_001178449.3.

3D structure databases

ProteinModelPortalP38260.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32805. 19 interactions.
DIPDIP-4918N.
IntActP38260. 14 interactions.
MINTMINT-478258.
STRING4932.YBR101C.

Chemistry

ChEMBLCHEMBL6102.

Proteomic databases

MaxQBP38260.
PaxDbP38260.
PeptideAtlasP38260.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR101C; YBR101C; YBR101C.
GeneID852397.
KEGGsce:YBR101C.

Organism-specific databases

CYGDYBR101c.
SGDS000000305. FES1.

Phylogenomic databases

eggNOGNOG310365.
HOGENOMHOG000000726.
OMAFEMLIEN.
OrthoDBEOG776T0T.

Enzyme and pathway databases

BioCycYEAST:G3O-29063-MONOMER.

Gene expression databases

GenevestigatorP38260.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013918. Nucleotide_exch_fac_Fes1.
[Graphical view]
PfamPF08609. Fes1. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

NextBio971225.

Entry information

Entry nameFES1_YEAST
AccessionPrimary (citable) accession number: P38260
Secondary accession number(s): D6VQA0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 117 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 II

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

Yeast

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

SIMILARITY comments

Index of protein domains and families