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Protein

Hsp70 nucleotide exchange factor FES1

Gene

FES1

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 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.10 Publications

GO - Molecular functioni

  1. adenyl-nucleotide exchange factor activity Source: SGD

GO - Biological processi

  1. cytoplasm-associated proteasomal ubiquitin-dependent protein catabolic process Source: SGD
  2. cytoplasmic translation Source: SGD
  3. regulation of catalytic activity Source: GOC
  4. regulation of translation Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Translation regulation

Enzyme and pathway databases

BioCyciYEAST:G3O-29063-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Hsp70 nucleotide exchange factor FES1
Alternative name(s):
Factor exchange for SSA1 protein 1
Gene namesi
Name:FES1
Ordered Locus Names:YBR101C
ORF Names:YBR0830
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome II

Organism-specific databases

CYGDiYBR101c.
EuPathDBiFungiDB:YBR101C.
SGDiS000000305. FES1.

Subcellular locationi

  1. Cytoplasm 2 Publications

GO - Cellular componenti

  1. cytosol Source: SGD
  2. cytosolic ribosome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290Hsp70 nucleotide exchange factor FES1PRO_0000202485Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38260.
PaxDbiP38260.
PeptideAtlasiP38260.

Expressioni

Gene expression databases

GenevestigatoriP38260.

Interactioni

Subunit structurei

Interacts with the Hsp70 chaperones SSA1 and SSB1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SSA1P105913EBI-21563,EBI-8591

Protein-protein interaction databases

BioGridi32805. 19 interactions.
DIPiDIP-4918N.
IntActiP38260. 14 interactions.
MINTiMINT-478258.
STRINGi4932.YBR101C.

Structurei

3D structure databases

ProteinModelPortaliP38260.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati13 – 5745ARM 1Add
BLAST
Repeati76 – 11641ARM 2Add
BLAST
Repeati120 – 16142ARM 3Add
BLAST
Repeati164 – 20542ARM 4Add
BLAST
Repeati211 – 25141ARM 5Add
BLAST
Repeati253 – 29038ARM 6Add
BLAST

Sequence similaritiesi

Belongs to the FES1 family.Curated
Contains 6 ARM repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG310365.
HOGENOMiHOG000000726.
InParanoidiP38260.
OMAiFEMLIEN.
OrthoDBiEOG776T0T.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013918. Nucleotide_exch_fac_Fes1.
[Graphical view]
PfamiPF08609. Fes1. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.

Sequencei

Sequence statusi: Complete.

P38260-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKLLQWSIA NSQGDKEAMA RAGQPDPKLL QQLFGGGGPD DPTLMKESMA
60 70 80 90 100
VIMNPEVDLE TKLVAFDNFE MLIENLDNAN NIENLKLWEP LLDVLVQTKD
110 120 130 140 150
EELRAAALSI IGTAVQNNLD SQNNFMKYDN GLRSLIEIAS DKTKPLDVRT
160 170 180 190 200
KAFYALSNLI RNHKDISEKF FKLNGLDCIA PVLSDNTAKP KLKMRAIALL
210 220 230 240 250
TAYLSSVKID ENIISVLRKD GVIESTIECL SDESNLNIID RVLSFLSHLI
260 270 280 290
SSGIKFNEQE LHKLNEGYKH IEPLKDRLNE DDYLAVKYVL
Length:290
Mass (Da):32,604
Last modified:October 1, 1994 - v1
Checksum:i4A50D069625BA500
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78993 Genomic DNA. Translation: CAA55604.1.
Z35970 Genomic DNA. Translation: CAA85056.1.
AY693000 Genomic DNA. Translation: AAT93019.1.
BK006936 Genomic DNA. Translation: DAA07220.1.
PIRiS48266.
RefSeqiNP_009659.3. NM_001178449.3.

Genome annotation databases

EnsemblFungiiYBR101C; YBR101C; YBR101C.
GeneIDi852397.
KEGGisce:YBR101C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78993 Genomic DNA. Translation: CAA55604.1.
Z35970 Genomic DNA. Translation: CAA85056.1.
AY693000 Genomic DNA. Translation: AAT93019.1.
BK006936 Genomic DNA. Translation: DAA07220.1.
PIRiS48266.
RefSeqiNP_009659.3. NM_001178449.3.

3D structure databases

ProteinModelPortaliP38260.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32805. 19 interactions.
DIPiDIP-4918N.
IntActiP38260. 14 interactions.
MINTiMINT-478258.
STRINGi4932.YBR101C.

Chemistry

ChEMBLiCHEMBL6102.

Proteomic databases

MaxQBiP38260.
PaxDbiP38260.
PeptideAtlasiP38260.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR101C; YBR101C; YBR101C.
GeneIDi852397.
KEGGisce:YBR101C.

Organism-specific databases

CYGDiYBR101c.
EuPathDBiFungiDB:YBR101C.
SGDiS000000305. FES1.

Phylogenomic databases

eggNOGiNOG310365.
HOGENOMiHOG000000726.
InParanoidiP38260.
OMAiFEMLIEN.
OrthoDBiEOG776T0T.

Enzyme and pathway databases

BioCyciYEAST:G3O-29063-MONOMER.

Miscellaneous databases

NextBioi971225.
PROiP38260.

Gene expression databases

GenevestigatoriP38260.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013918. Nucleotide_exch_fac_Fes1.
[Graphical view]
PfamiPF08609. Fes1. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. 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].

Entry informationi

Entry nameiFES1_YEAST
AccessioniPrimary (citable) accession number: P38260
Secondary accession number(s): D6VQA0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: April 29, 2015
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 13100 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: 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.