FES1_YEAST
ID FES1_YEAST Reviewed; 290 AA.
AC P38260; D6VQA0;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Hsp70 nucleotide exchange factor FES1;
DE AltName: Full=Factor exchange for SSA1 protein 1;
GN Name=FES1; OrderedLocusNames=YBR101C; ORFNames=YBR0830;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7900426; DOI=10.1002/yea.320101014;
RA Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL Yeast 10:1363-1381(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=12417338; DOI=10.1016/s0014-5793(02)03570-6;
RA Kabani M., McLellan C., Raynes D.A., Guerriero V., Brodsky J.L.;
RT "HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70
RT nucleotide exchange factor.";
RL FEBS Lett. 531:339-342(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SSA1.
RX PubMed=12052876; DOI=10.1128/mcb.22.13.4677-4689.2002;
RA Kabani M., Beckerich J.-M., Brodsky J.L.;
RT "Nucleotide exchange factor for the yeast Hsp70 molecular chaperone
RT Ssa1p.";
RL Mol. Cell. Biol. 22:4677-4689(2002).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP FUNCTION.
RX PubMed=15082786; DOI=10.1128/mcb.24.9.3928-3937.2004;
RA Jones G., Song Y., Chung S., Masison D.C.;
RT "Propagation of Saccharomyces cerevisiae [PSI+] prion is impaired by
RT factors that regulate Hsp70 substrate binding.";
RL Mol. Cell. Biol. 24:3928-3937(2004).
RN [10]
RP FUNCTION.
RX PubMed=15680904; DOI=10.1016/j.abb.2004.11.005;
RA Ahner A., Whyte F.M., Brodsky J.L.;
RT "Distinct but overlapping functions of Hsp70, Hsp90, and an Hsp70
RT nucleotide exchange factor during protein biogenesis in yeast.";
RL Arch. Biochem. Biophys. 435:32-41(2005).
RN [11]
RP FUNCTION.
RX PubMed=16374585; DOI=10.1007/s00018-005-5341-7;
RA Porat Z., Wender N., Erez O., Kahana C.;
RT "Mechanism of polyamine tolerance in yeast: novel regulators and
RT insights.";
RL Cell. Mol. Life Sci. 62:3106-3116(2005).
RN [12]
RP FUNCTION.
RX PubMed=15855155; DOI=10.1074/jbc.m503071200;
RA Aouida M., Leduc A., Poulin R., Ramotar D.;
RT "AGP2 encodes the major permease for high affinity polyamine import in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:24267-24276(2005).
RN [13]
RP FUNCTION.
RX PubMed=15694338; DOI=10.1016/j.molcel.2004.12.023;
RA Shomura Y., Dragovic Z., Chang H.-C., Tzvetkov N., Young J.C.,
RA Brodsky J.L., Guerriero V. Jr., Hartl F.U., Bracher A.;
RT "Regulation of Hsp70 function by HspBP1: structural analysis reveals an
RT alternate mechanism for Hsp70 nucleotide exchange.";
RL Mol. Cell 17:367-379(2005).
RN [14]
RP FUNCTION.
RX PubMed=16688211; DOI=10.1038/sj.emboj.7601139;
RA Raviol H., Sadlish H., Rodriguez F., Mayer M.P., Bukau B.;
RT "Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70
RT nucleotide exchange factor.";
RL EMBO J. 25:2510-2518(2006).
RN [15]
RP FUNCTION.
RX PubMed=16688212; DOI=10.1038/sj.emboj.7601138;
RA Dragovic Z., Broadley S.A., Shomura Y., Bracher A., Hartl F.U.;
RT "Molecular chaperones of the Hsp110 family act as nucleotide exchange
RT factors of Hsp70s.";
RL EMBO J. 25:2519-2528(2006).
RN [16]
RP FUNCTION, AND INTERACTION WITH SSB1.
RX PubMed=17132105; DOI=10.1515/bc.2006.198;
RA Dragovic Z., Shomura Y., Tzvetkov N., Hartl F.U., Bracher A.;
RT "Fes1p acts as a nucleotide exchange factor for the ribosome-associated
RT molecular chaperone Ssb1p.";
RL Biol. Chem. 387:1593-1600(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Involved in protein translation, propagation of [PSI+]
CC prions, and polyamine tolerance. Functions as a nucleotide exchange
CC factor (NEF), which accelerates the release of ADP, for the cytosolic
CC Hsp70 chaperone SSA1 and the ribosome-associated Hsp70 chaperone SSB1.
CC Required for fully efficient Hsp70-mediated folding of proteins.
CC {ECO:0000269|PubMed:12052876, ECO:0000269|PubMed:12417338,
CC ECO:0000269|PubMed:15082786, ECO:0000269|PubMed:15680904,
CC ECO:0000269|PubMed:15694338, ECO:0000269|PubMed:15855155,
CC ECO:0000269|PubMed:16374585, ECO:0000269|PubMed:16688211,
CC ECO:0000269|PubMed:16688212, ECO:0000269|PubMed:17132105}.
CC -!- SUBUNIT: Interacts with the Hsp70 chaperones SSA1 and SSB1.
CC {ECO:0000269|PubMed:12052876, ECO:0000269|PubMed:17132105}.
CC -!- INTERACTION:
CC P38260; P10591: SSA1; NbExp=3; IntAct=EBI-21563, EBI-8591;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12052876,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 13100 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the FES1 family. {ECO:0000305}.
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DR EMBL; X78993; CAA55604.1; -; Genomic_DNA.
DR EMBL; Z35970; CAA85056.1; -; Genomic_DNA.
DR EMBL; AY693000; AAT93019.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07220.1; -; Genomic_DNA.
DR PIR; S48266; S48266.
DR RefSeq; NP_009659.3; NM_001178449.3.
DR AlphaFoldDB; P38260; -.
DR SMR; P38260; -.
DR BioGRID; 32805; 108.
DR DIP; DIP-4918N; -.
DR IntAct; P38260; 25.
DR MINT; P38260; -.
DR STRING; 4932.YBR101C; -.
DR ChEMBL; CHEMBL6102; -.
DR iPTMnet; P38260; -.
DR MaxQB; P38260; -.
DR PaxDb; P38260; -.
DR PRIDE; P38260; -.
DR EnsemblFungi; YBR101C_mRNA; YBR101C; YBR101C.
DR GeneID; 852397; -.
DR KEGG; sce:YBR101C; -.
DR SGD; S000000305; FES1.
DR VEuPathDB; FungiDB:YBR101C; -.
DR eggNOG; KOG2160; Eukaryota.
DR GeneTree; ENSGT00940000153909; -.
DR HOGENOM; CLU_046722_1_0_1; -.
DR InParanoid; P38260; -.
DR OMA; LHWSIAN; -.
DR BioCyc; YEAST:G3O-29063-MON; -.
DR PRO; PR:P38260; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38260; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0071629; P:cytoplasm protein quality control by the ubiquitin-proteasome system; IDA:SGD.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR013918; Nucleotide_exch_fac_Fes1.
DR Pfam; PF08609; Fes1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat;
KW Translation regulation.
FT CHAIN 1..290
FT /note="Hsp70 nucleotide exchange factor FES1"
FT /id="PRO_0000202485"
FT REPEAT 13..57
FT /note="ARM 1"
FT REPEAT 76..116
FT /note="ARM 2"
FT REPEAT 120..161
FT /note="ARM 3"
FT REPEAT 164..205
FT /note="ARM 4"
FT REPEAT 211..251
FT /note="ARM 5"
FT REPEAT 253..290
FT /note="ARM 6"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 290 AA; 32604 MW; 4A50D069625BA500 CRC64;
MEKLLQWSIA NSQGDKEAMA RAGQPDPKLL QQLFGGGGPD DPTLMKESMA VIMNPEVDLE
TKLVAFDNFE MLIENLDNAN NIENLKLWEP LLDVLVQTKD EELRAAALSI IGTAVQNNLD
SQNNFMKYDN GLRSLIEIAS DKTKPLDVRT KAFYALSNLI RNHKDISEKF FKLNGLDCIA
PVLSDNTAKP KLKMRAIALL TAYLSSVKID ENIISVLRKD GVIESTIECL SDESNLNIID
RVLSFLSHLI SSGIKFNEQE LHKLNEGYKH IEPLKDRLNE DDYLAVKYVL
