CDC37_YEAST
ID CDC37_YEAST Reviewed; 506 AA.
AC P06101; D6VSE8; Q04132;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Hsp90 co-chaperone Cdc37;
DE AltName: Full=Cell division control protein 37;
DE AltName: Full=Hsp90 chaperone protein kinase-targeting subunit;
GN Name=CDC37; Synonyms=SMO1; OrderedLocusNames=YDR168W; ORFNames=YD9489.03;
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] OF 58-506.
RX PubMed=3018676; DOI=10.1093/nar/14.16.6681;
RA Ferguson J., Ho J.-Y., Peterson T.A., Reed S.I.;
RT "Nucleotide sequence of the yeast cell division cycle start genes CDC28,
RT CDC36, CDC37, and CDC39, and a structural analysis of the predicted
RT products.";
RL Nucleic Acids Res. 14:6681-6697(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
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 INTERACTION WITH CDC28.
RX PubMed=7753858; DOI=10.1073/pnas.92.10.4651;
RA Gerber M.R., Farrell A., Deshaies R.J., Herskowitz I., Morgan D.O.;
RT "Cdc37 is required for association of the protein kinase Cdc28 with G1 and
RT mitotic cyclins.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4651-4655(1995).
RN [5]
RP INTERACTION WITH STE11.
RX PubMed=10664467; DOI=10.1016/s0014-5793(00)01134-0;
RA Abbas-Terki T., Donze O., Picard D.;
RT "The molecular chaperone Cdc37 is required for Ste11 function and
RT pheromone-induced cell cycle arrest.";
RL FEBS Lett. 467:111-116(2000).
RN [6]
RP INTERACTION WITH CDC28 AND CAK1.
RX PubMed=10629030; DOI=10.1128/mcb.20.3.749-754.2000;
RA Farrell A., Morgan D.O.;
RT "Cdc37 promotes the stability of protein kinases Cdc28 and Cak1.";
RL Mol. Cell. Biol. 20:749-754(2000).
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, INTERACTION WITH HOG1; HSP90 AND SLT2, PHOSPHORYLATION AT SER-14,
RP AND MUTAGENESIS OF SER-14.
RX PubMed=17220467; DOI=10.1128/ec.00343-06;
RA Hawle P., Horst D., Bebelman J.-P., Yang X.X., Siderius M.,
RA van der Vies S.M.;
RT "Cdc37p is required for stress-induced high-osmolarity glycerol and protein
RT kinase C mitogen-activated protein kinase pathway functionality by
RT interaction with Hog1p and Slt2p (Mpk1p).";
RL Eukaryot. Cell 6:521-532(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-17, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-17, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-17; SER-367; SER-466
RP AND SER-484, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-17; SER-367 AND
RP SER-484, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Co-chaperone that binds to numerous kinases and promotes
CC their interaction with the Hsp90 complex, resulting in stabilization
CC and promotion of their activity. Involved in both the HOG and the PKC
CC MAP kinase signaling cascade necessary for adaptation to stress
CC conditions due to high osmolarity or cell wall perturbation.
CC {ECO:0000269|PubMed:17220467}.
CC -!- SUBUNIT: Forms a complex with Hsp90. Interacts with CDC28, CAK1 HOG1,
CC SLT2 and STE11. {ECO:0000269|PubMed:10629030,
CC ECO:0000269|PubMed:10664467, ECO:0000269|PubMed:17220467,
CC ECO:0000269|PubMed:7753858}.
CC -!- INTERACTION:
CC P06101; P02829: HSP82; NbExp=3; IntAct=EBI-4266, EBI-8659;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylation at Ser-14 is required for the interactions with
CC HOG1 and SLT2 MAP kinases and is crucial for adaptation to stress
CC conditions due to high osmolarity or cell wall perturbation.
CC {ECO:0000269|PubMed:17220467}.
CC -!- MISCELLANEOUS: Present with 10200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
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DR EMBL; X04288; CAA27836.1; -; Genomic_DNA.
DR EMBL; Z47813; CAA87799.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12008.1; -; Genomic_DNA.
DR PIR; S50914; S50914.
DR RefSeq; NP_010452.1; NM_001180475.1.
DR AlphaFoldDB; P06101; -.
DR BioGRID; 32219; 733.
DR DIP; DIP-2379N; -.
DR IntAct; P06101; 10.
DR MINT; P06101; -.
DR STRING; 4932.YDR168W; -.
DR iPTMnet; P06101; -.
DR MaxQB; P06101; -.
DR PaxDb; P06101; -.
DR PRIDE; P06101; -.
DR EnsemblFungi; YDR168W_mRNA; YDR168W; YDR168W.
DR GeneID; 851746; -.
DR KEGG; sce:YDR168W; -.
DR SGD; S000002575; CDC37.
DR VEuPathDB; FungiDB:YDR168W; -.
DR eggNOG; KOG2260; Eukaryota.
DR GeneTree; ENSGT00390000013443; -.
DR HOGENOM; CLU_033261_1_0_1; -.
DR InParanoid; P06101; -.
DR OMA; YSKWDQL; -.
DR BioCyc; YEAST:G3O-29757-MON; -.
DR Reactome; R-SCE-114608; Platelet degranulation.
DR PRO; PR:P06101; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P06101; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000161; P:osmosensory signaling MAPK cascade; IPI:SGD.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IMP:SGD.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:SGD.
DR GO; GO:0030474; P:spindle pole body duplication; IMP:SGD.
DR Gene3D; 1.20.58.610; -; 1.
DR InterPro; IPR004918; Cdc37.
DR InterPro; IPR013873; Cdc37_C.
DR InterPro; IPR013874; Cdc37_Hsp90-bd.
DR InterPro; IPR038189; Cdc37_Hsp90-bd_sf.
DR InterPro; IPR013855; Cdc37_N_dom.
DR PANTHER; PTHR12800; PTHR12800; 1.
DR Pfam; PF08564; CDC37_C; 1.
DR Pfam; PF08565; CDC37_M; 1.
DR Pfam; PF03234; CDC37_N; 1.
DR SMART; SM01069; CDC37_C; 1.
DR SMART; SM01070; CDC37_M; 1.
DR SMART; SM01071; CDC37_N; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chaperone; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..506
FT /note="Hsp90 co-chaperone Cdc37"
FT /id="PRO_0000195067"
FT REGION 472..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17220467,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 14
FT /note="S->A: Leads to osmosensitivity."
FT /evidence="ECO:0000269|PubMed:17220467"
FT CONFLICT 169
FT /note="A -> D (in Ref. 1; CAA27836)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 58385 MW; 0DF0C923158A2526 CRC64;
MAIDYSKWDK IELSDDSDVE VHPNVDKKSF IKWKQQSIHE QRFKRNQDIK NLETQVDMYS
HLNKRVDRIL SNLPESSLTD LPAVTKFLNA NFDKMEKSKG ENVDPEIATY NEMVEDLFEQ
LAKDLDKEGK DSKSPSLIRD AILKHRAKID SVTVEAKKKL DELYKEKNAH ISSEDIHTGF
DSSFMNKQKG GAKPLEATPS EALSSAAESN ILNKLAKSSV PQTFIDFKDD PMKLAKETEE
FGKISINEYS KSQKFLLEHL PIISEQQKDA LMMKAFEYQL HGDDKMTLQV IHQSELMAYI
KEIYDMKKIP YLNPMELSNV INMFFEKVIF NKDKPMGKES FLRSVQEKFL HIQKRSKILQ
QEEMDESNAE GVETIQLKSL DDSTELEVNL PDFNSKDPEE MKKVKVFKTL IPEKMQEAIM
TKNLDNINKV FEDIPIEEAE KLLEVFNDID IIGIKAILEN EKDFQSLKDQ YEQDHEDATM
ENLSLNDRDG GGDNHEEVKH TADTVD
