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Hsp90 co-chaperone Cdc37 (Cell division control protein 37) (Hsp90 chaperone protein kinase-targeting subunit)

 CDC37_YEAST             Reviewed;         506 AA.
P06101; D6VSE8; Q04132;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
23-MAY-2018, entry version 172.
RecName: Full=Hsp90 co-chaperone Cdc37;
AltName: Full=Cell division control protein 37;
AltName: Full=Hsp90 chaperone protein kinase-targeting subunit;
Name=CDC37; Synonyms=SMO1; OrderedLocusNames=YDR168W;
ORFNames=YD9489.03;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-506.
PubMed=3018676; DOI=10.1093/nar/14.16.6681;
Ferguson J., Ho J.-Y., Peterson T.A., Reed S.I.;
"Nucleotide sequence of the yeast cell division cycle start genes
CDC28, CDC36, CDC37, and CDC39, and a structural analysis of the
predicted products.";
Nucleic Acids Res. 14:6681-6697(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
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.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
INTERACTION WITH CDC28.
PubMed=7753858; DOI=10.1073/pnas.92.10.4651;
Gerber M.R., Farrell A., Deshaies R.J., Herskowitz I., Morgan D.O.;
"Cdc37 is required for association of the protein kinase Cdc28 with G1
and mitotic cyclins.";
Proc. Natl. Acad. Sci. U.S.A. 92:4651-4655(1995).
[5]
INTERACTION WITH STE11.
PubMed=10664467; DOI=10.1016/S0014-5793(00)01134-0;
Abbas-Terki T., Donze O., Picard D.;
"The molecular chaperone Cdc37 is required for Ste11 function and
pheromone-induced cell cycle arrest.";
FEBS Lett. 467:111-116(2000).
[6]
INTERACTION WITH CDC28 AND CAK1.
PubMed=10629030; DOI=10.1128/MCB.20.3.749-754.2000;
Farrell A., Morgan D.O.;
"Cdc37 promotes the stability of protein kinases Cdc28 and Cak1.";
Mol. Cell. Biol. 20:749-754(2000).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[8]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[9]
FUNCTION, INTERACTION WITH HOG1; HSP90 AND SLT2, PHOSPHORYLATION AT
SER-14, AND MUTAGENESIS OF SER-14.
PubMed=17220467; DOI=10.1128/EC.00343-06;
Hawle P., Horst D., Bebelman J.-P., Yang X.X., Siderius M.,
van der Vies S.M.;
"Cdc37p is required for stress-induced high-osmolarity glycerol and
protein kinase C mitogen-activated protein kinase pathway
functionality by interaction with Hog1p and Slt2p (Mpk1p).";
Eukaryot. Cell 6:521-532(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-17, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-17, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
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.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-17; SER-367;
SER-466 AND SER-484, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-17; SER-367 AND
SER-484, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Co-chaperone that binds to numerous kinases and promotes
their interaction with the Hsp90 complex, resulting in
stabilization and promotion of their activity. Involved in both
the HOG and the PKC MAP kinase signaling cascade necessary for
adaptation to stress conditions due to high osmolarity or cell
wall perturbation. {ECO:0000269|PubMed:17220467}.
-!- SUBUNIT: Forms a complex with Hsp90. Interacts with CDC28, CAK1
HOG1, SLT2 and STE11. {ECO:0000269|PubMed:10629030,
ECO:0000269|PubMed:10664467, ECO:0000269|PubMed:17220467,
ECO:0000269|PubMed:7753858}.
-!- INTERACTION:
P02829:HSP82; NbExp=3; IntAct=EBI-4266, EBI-8659;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
-!- PTM: Phosphorylation at Ser-14 is required for the interactions
with HOG1 and SLT2 MAP kinases and is crucial for adaptation to
stress conditions due to high osmolarity or cell wall
perturbation. {ECO:0000269|PubMed:17220467}.
-!- MISCELLANEOUS: Present with 10200 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; X04288; CAA27836.1; -; Genomic_DNA.
EMBL; Z47813; CAA87799.1; -; Genomic_DNA.
EMBL; BK006938; DAA12008.1; -; Genomic_DNA.
PIR; S50914; S50914.
RefSeq; NP_010452.1; NM_001180475.1.
ProteinModelPortal; P06101; -.
BioGrid; 32219; 731.
DIP; DIP-2379N; -.
IntAct; P06101; 10.
MINT; P06101; -.
STRING; 4932.YDR168W; -.
iPTMnet; P06101; -.
MaxQB; P06101; -.
PaxDb; P06101; -.
PRIDE; P06101; -.
EnsemblFungi; YDR168W; YDR168W; YDR168W.
GeneID; 851746; -.
KEGG; sce:YDR168W; -.
EuPathDB; FungiDB:YDR168W; -.
SGD; S000002575; CDC37.
HOGENOM; HOG000190315; -.
InParanoid; P06101; -.
KO; K09554; -.
OMA; IRWKQRD; -.
OrthoDB; EOG092C2UGT; -.
BioCyc; YEAST:G3O-29757-MONOMER; -.
PRO; PR:P06101; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
GO; GO:0051082; F:unfolded protein binding; IDA:SGD.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0000165; P:MAPK cascade; IMP:SGD.
GO; GO:0000161; P:MAPK cascade involved in osmosensory signaling pathway; IPI:SGD.
GO; GO:0006457; P:protein folding; IBA:GO_Central.
GO; GO:0050821; P:protein stabilization; IMP:SGD.
GO; GO:0051726; P:regulation of cell cycle; IMP:SGD.
GO; GO:0032872; P:regulation of stress-activated MAPK cascade; IMP:SGD.
GO; GO:0030474; P:spindle pole body duplication; IMP:SGD.
Gene3D; 1.20.58.610; -; 1.
InterPro; IPR004918; Cdc37.
InterPro; IPR013873; Cdc37_C.
InterPro; IPR013874; Cdc37_Hsp90-bd.
InterPro; IPR038189; Cdc37_Hsp90-bd_sf.
InterPro; IPR013855; Cdc37_N_dom.
PANTHER; PTHR12800; PTHR12800; 1.
Pfam; PF08564; CDC37_C; 1.
Pfam; PF08565; CDC37_M; 1.
Pfam; PF03234; CDC37_N; 1.
SMART; SM01069; CDC37_C; 1.
SMART; SM01070; CDC37_M; 1.
SMART; SM01071; CDC37_N; 1.
1: Evidence at protein level;
Cell cycle; Cell division; Chaperone; Complete proteome; Cytoplasm;
Phosphoprotein; Reference proteome.
CHAIN 1 506 Hsp90 co-chaperone Cdc37.
/FTId=PRO_0000195067.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198,
ECO:0000269|PubMed:17220467}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 367 367 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 466 466 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MUTAGEN 14 14 S->A: Leads to osmosensitivity.
{ECO:0000269|PubMed:17220467}.
CONFLICT 169 169 A -> D (in Ref. 1; CAA27836).
{ECO:0000305}.
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


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