Full text data of CDC37
CDC37
(CDC37A)
[Confidence: low (only semi-automatic identification from reviews)]
Hsp90 co-chaperone Cdc37 (Hsp90 chaperone protein kinase-targeting subunit; p50Cdc37; Hsp90 co-chaperone Cdc37, N-terminally processed)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Hsp90 co-chaperone Cdc37 (Hsp90 chaperone protein kinase-targeting subunit; p50Cdc37; Hsp90 co-chaperone Cdc37, N-terminally processed)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q16543
ID CDC37_HUMAN Reviewed; 378 AA.
AC Q16543; Q53YA2;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Hsp90 co-chaperone Cdc37;
DE AltName: Full=Hsp90 chaperone protein kinase-targeting subunit;
DE AltName: Full=p50Cdc37;
DE Contains:
DE RecName: Full=Hsp90 co-chaperone Cdc37, N-terminally processed;
GN Name=CDC37; Synonyms=CDC37A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=8666233;
RA Stepanova L., Leng X., Parker S.B., Harper J.W.;
RT "Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90
RT that binds and stabilizes Cdk4.";
RL Genes Dev. 10:1491-1502(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8703009; DOI=10.1074/jbc.271.36.22030;
RA Dai K., Kobayashi R., Beach D.;
RT "Physical interaction of mammalian CDC37 with CDK4.";
RL J. Biol. Chem. 271:22030-22034(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-360.
RG NIEHS SNPs program;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH CDK4 AND CDK6.
RX PubMed=9150368; DOI=10.1038/sj.onc.1201036;
RA Lamphere L., Fiore F., Xu X., Brizuela L., Keezer S., Sardet C.,
RA Draetta G.F., Gyuris J.;
RT "Interaction between Cdc37 and Cdk4 in human cells.";
RL Oncogene 14:1999-2004(1997).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CDK6.
RX PubMed=9482106; DOI=10.1038/sj.onc.1201570;
RA Mahony D., Parry D.A., Lees E.;
RT "Active cdk6 complexes are predominantly nuclear and represent only a
RT minority of the cdk6 in T cells.";
RL Oncogene 16:603-611(1998).
RN [9]
RP CHARACTERIZATION.
RX PubMed=10858314; DOI=10.1021/bi000315r;
RA Hartson S.D., Irwin A.D., Shao J., Scroggins B.T., Volk L., Huang W.,
RA Matts R.L.;
RT "p50(cdc37) is a nonexclusive Hsp90 cohort which participates
RT intimately in Hsp90-mediated folding of immature kinase molecules.";
RL Biochemistry 39:7631-7644(2000).
RN [10]
RP INTERACTION WITH EIF2AK1.
RX PubMed=11036079; DOI=10.1074/jbc.M007583200;
RA Shao J., Grammatikakis N., Scroggins B.T., Uma S., Huang W.,
RA Chen J.-J., Hartson S.D., Matts R.L.;
RT "Hsp90 regulates p50(cdc37) function during the biogenesis of the
RT active conformation of the heme-regulated eIF2 alpha kinase.";
RL J. Biol. Chem. 276:206-214(2001).
RN [11]
RP INTERACTION WITH AR.
RX PubMed=11085988; DOI=10.1074/jbc.M007385200;
RA Rao J., Lee P., Benzeno S., Cardozo C., Albertus J., Robins D.M.,
RA Caplan A.J.;
RT "Functional interaction of human Cdc37 with the androgen receptor but
RT not with the glucocorticoid receptor.";
RL J. Biol. Chem. 276:5814-5820(2001).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP SUMOYLATION.
RX PubMed=17709345; DOI=10.1093/nar/gkm617;
RA Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R.;
RT "Ubc9 fusion-directed SUMOylation identifies constitutive and
RT inducible SUMOylation.";
RL Nucleic Acids Res. 35:E109-E109(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND VAL-2, MASS
RP SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78 AND LYS-154, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-13, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-13, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Co-chaperone that binds to numerous kinases and promotes
CC their interaction with the Hsp90 complex, resulting in
CC stabilization and promotion of their activity.
CC -!- SUBUNIT: Forms a complex with Hsp90/HSP90AB1 and CDK6. Interacts
CC with AR, CDK4, CDK6, EIF2AK1 and RB1.
CC -!- INTERACTION:
CC P11500:- (xeno); NbExp=3; IntAct=EBI-295634, EBI-640126;
CC P31749:AKT1; NbExp=2; IntAct=EBI-295634, EBI-296087;
CC P02649:APOE; NbExp=3; IntAct=EBI-295634, EBI-1222467;
CC P11802:CDK4; NbExp=6; IntAct=EBI-295634, EBI-295644;
CC Q00534:CDK6; NbExp=2; IntAct=EBI-295634, EBI-295663;
CC P33279:EIF2AK1 (xeno); NbExp=3; IntAct=EBI-295634, EBI-640100;
CC P08238:HSP90AB1; NbExp=4; IntAct=EBI-295634, EBI-352572;
CC O14879:IFIT3; NbExp=4; IntAct=EBI-295634, EBI-745127;
CC Q5S007:LRRK2; NbExp=7; IntAct=EBI-295634, EBI-5323863;
CC P29474:NOS3; NbExp=4; IntAct=EBI-295634, EBI-1391623;
CC P53041:PPP5C; NbExp=2; IntAct=EBI-295634, EBI-716663;
CC P49768:PSEN1; NbExp=3; IntAct=EBI-295634, EBI-297277;
CC Q13501:SQSTM1; NbExp=3; IntAct=EBI-295634, EBI-307104;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Constitutively sumoylated by UBE2I.
CC -!- SIMILARITY: Belongs to the CDC37 family.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc37/";
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DR EMBL; U43077; AAB63979.1; -; mRNA.
DR EMBL; U63131; AAB04798.1; -; mRNA.
DR EMBL; AY864824; AAW34362.1; -; Genomic_DNA.
DR EMBL; BT006796; AAP35442.1; -; mRNA.
DR EMBL; CH471106; EAW84101.1; -; Genomic_DNA.
DR EMBL; BC000083; AAH00083.1; -; mRNA.
DR EMBL; BC008793; AAH08793.1; -; mRNA.
DR PIR; G02313; G02313.
DR RefSeq; NP_008996.1; NM_007065.3.
DR UniGene; Hs.160958; -.
DR PDB; 1US7; X-ray; 2.30 A; B=127-378.
DR PDB; 2K5B; NMR; -; B=148-276.
DR PDB; 2W0G; X-ray; 1.88 A; A=148-276.
DR PDBsum; 1US7; -.
DR PDBsum; 2K5B; -.
DR PDBsum; 2W0G; -.
DR ProteinModelPortal; Q16543; -.
DR SMR; Q16543; 148-347.
DR DIP; DIP-27560N; -.
DR DIP; DIP-395N; -.
DR IntAct; Q16543; 133.
DR MINT; MINT-99762; -.
DR STRING; 9606.ENSP00000222005; -.
DR ChEMBL; CHEMBL1795123; -.
DR PhosphoSite; Q16543; -.
DR DMDM; 21542000; -.
DR PaxDb; Q16543; -.
DR PeptideAtlas; Q16543; -.
DR PRIDE; Q16543; -.
DR DNASU; 11140; -.
DR Ensembl; ENST00000222005; ENSP00000222005; ENSG00000105401.
DR GeneID; 11140; -.
DR KEGG; hsa:11140; -.
DR UCSC; uc002mof.1; human.
DR CTD; 11140; -.
DR GeneCards; GC19M010501; -.
DR HGNC; HGNC:1735; CDC37.
DR HPA; CAB004214; -.
DR HPA; HPA003928; -.
DR MIM; 605065; gene.
DR neXtProt; NX_Q16543; -.
DR PharmGKB; PA402; -.
DR eggNOG; NOG300020; -.
DR HOGENOM; HOG000018180; -.
DR HOVERGEN; HBG056343; -.
DR InParanoid; Q16543; -.
DR KO; K09554; -.
DR OrthoDB; EOG73805G; -.
DR PhylomeDB; Q16543; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; CDC37; human.
DR EvolutionaryTrace; Q16543; -.
DR GeneWiki; CDC37; -.
DR GenomeRNAi; 11140; -.
DR NextBio; 42344; -.
DR PRO; PR:Q16543; -.
DR ArrayExpress; Q16543; -.
DR Bgee; Q16543; -.
DR CleanEx; HS_CDC37; -.
DR Genevestigator; Q16543; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
DR GO; GO:0006605; P:protein targeting; TAS:ProtInc.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
DR GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; IMP:MGI.
DR GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; IMP:MGI.
DR InterPro; IPR004918; Cdc37.
DR InterPro; IPR013873; Cdc37_C.
DR InterPro; IPR013874; Cdc37_Hsp90-bd.
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; 2.
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 3D-structure; Acetylation; Chaperone; Complete proteome; Cytoplasm;
KW Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
FT CHAIN 1 378 Hsp90 co-chaperone Cdc37.
FT /FTId=PRO_0000195057.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 378 Hsp90 co-chaperone Cdc37, N-terminally
FT processed.
FT /FTId=PRO_0000423197.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 2 2 N-acetylvaline; in Hsp90 co-chaperone
FT Cdc37, N-terminally processed.
FT MOD_RES 13 13 Phosphoserine.
FT MOD_RES 78 78 N6-acetyllysine.
FT MOD_RES 154 154 N6-acetyllysine.
FT MOD_RES 377 377 Phosphoserine.
FT VARIANT 360 360 G -> E (in dbSNP:rs280528).
FT /FTId=VAR_022220.
FT HELIX 149 163
FT HELIX 168 177
FT HELIX 179 181
FT HELIX 184 199
FT HELIX 203 226
FT HELIX 230 241
FT HELIX 247 272
FT HELIX 294 300
FT HELIX 317 321
FT STRAND 325 327
FT HELIX 328 338
SQ SEQUENCE 378 AA; 44468 MW; 55BFEFFF3C2A5442 CRC64;
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK
VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS
KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH
LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK
IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES
LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG
DPLLEAVPKT GDEKDVSV
//
ID CDC37_HUMAN Reviewed; 378 AA.
AC Q16543; Q53YA2;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=Hsp90 co-chaperone Cdc37;
DE AltName: Full=Hsp90 chaperone protein kinase-targeting subunit;
DE AltName: Full=p50Cdc37;
DE Contains:
DE RecName: Full=Hsp90 co-chaperone Cdc37, N-terminally processed;
GN Name=CDC37; Synonyms=CDC37A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=8666233;
RA Stepanova L., Leng X., Parker S.B., Harper J.W.;
RT "Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90
RT that binds and stabilizes Cdk4.";
RL Genes Dev. 10:1491-1502(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8703009; DOI=10.1074/jbc.271.36.22030;
RA Dai K., Kobayashi R., Beach D.;
RT "Physical interaction of mammalian CDC37 with CDK4.";
RL J. Biol. Chem. 271:22030-22034(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLU-360.
RG NIEHS SNPs program;
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH CDK4 AND CDK6.
RX PubMed=9150368; DOI=10.1038/sj.onc.1201036;
RA Lamphere L., Fiore F., Xu X., Brizuela L., Keezer S., Sardet C.,
RA Draetta G.F., Gyuris J.;
RT "Interaction between Cdc37 and Cdk4 in human cells.";
RL Oncogene 14:1999-2004(1997).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CDK6.
RX PubMed=9482106; DOI=10.1038/sj.onc.1201570;
RA Mahony D., Parry D.A., Lees E.;
RT "Active cdk6 complexes are predominantly nuclear and represent only a
RT minority of the cdk6 in T cells.";
RL Oncogene 16:603-611(1998).
RN [9]
RP CHARACTERIZATION.
RX PubMed=10858314; DOI=10.1021/bi000315r;
RA Hartson S.D., Irwin A.D., Shao J., Scroggins B.T., Volk L., Huang W.,
RA Matts R.L.;
RT "p50(cdc37) is a nonexclusive Hsp90 cohort which participates
RT intimately in Hsp90-mediated folding of immature kinase molecules.";
RL Biochemistry 39:7631-7644(2000).
RN [10]
RP INTERACTION WITH EIF2AK1.
RX PubMed=11036079; DOI=10.1074/jbc.M007583200;
RA Shao J., Grammatikakis N., Scroggins B.T., Uma S., Huang W.,
RA Chen J.-J., Hartson S.D., Matts R.L.;
RT "Hsp90 regulates p50(cdc37) function during the biogenesis of the
RT active conformation of the heme-regulated eIF2 alpha kinase.";
RL J. Biol. Chem. 276:206-214(2001).
RN [11]
RP INTERACTION WITH AR.
RX PubMed=11085988; DOI=10.1074/jbc.M007385200;
RA Rao J., Lee P., Benzeno S., Cardozo C., Albertus J., Robins D.M.,
RA Caplan A.J.;
RT "Functional interaction of human Cdc37 with the androgen receptor but
RT not with the glucocorticoid receptor.";
RL J. Biol. Chem. 276:5814-5820(2001).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP SUMOYLATION.
RX PubMed=17709345; DOI=10.1093/nar/gkm617;
RA Jakobs A., Himstedt F., Funk M., Korn B., Gaestel M., Niedenthal R.;
RT "Ubc9 fusion-directed SUMOylation identifies constitutive and
RT inducible SUMOylation.";
RL Nucleic Acids Res. 35:E109-E109(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND VAL-2, MASS
RP SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78 AND LYS-154, AND MASS
RP SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-13, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-13, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Co-chaperone that binds to numerous kinases and promotes
CC their interaction with the Hsp90 complex, resulting in
CC stabilization and promotion of their activity.
CC -!- SUBUNIT: Forms a complex with Hsp90/HSP90AB1 and CDK6. Interacts
CC with AR, CDK4, CDK6, EIF2AK1 and RB1.
CC -!- INTERACTION:
CC P11500:- (xeno); NbExp=3; IntAct=EBI-295634, EBI-640126;
CC P31749:AKT1; NbExp=2; IntAct=EBI-295634, EBI-296087;
CC P02649:APOE; NbExp=3; IntAct=EBI-295634, EBI-1222467;
CC P11802:CDK4; NbExp=6; IntAct=EBI-295634, EBI-295644;
CC Q00534:CDK6; NbExp=2; IntAct=EBI-295634, EBI-295663;
CC P33279:EIF2AK1 (xeno); NbExp=3; IntAct=EBI-295634, EBI-640100;
CC P08238:HSP90AB1; NbExp=4; IntAct=EBI-295634, EBI-352572;
CC O14879:IFIT3; NbExp=4; IntAct=EBI-295634, EBI-745127;
CC Q5S007:LRRK2; NbExp=7; IntAct=EBI-295634, EBI-5323863;
CC P29474:NOS3; NbExp=4; IntAct=EBI-295634, EBI-1391623;
CC P53041:PPP5C; NbExp=2; IntAct=EBI-295634, EBI-716663;
CC P49768:PSEN1; NbExp=3; IntAct=EBI-295634, EBI-297277;
CC Q13501:SQSTM1; NbExp=3; IntAct=EBI-295634, EBI-307104;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Constitutively sumoylated by UBE2I.
CC -!- SIMILARITY: Belongs to the CDC37 family.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdc37/";
CC -----------------------------------------------------------------------
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DR EMBL; U43077; AAB63979.1; -; mRNA.
DR EMBL; U63131; AAB04798.1; -; mRNA.
DR EMBL; AY864824; AAW34362.1; -; Genomic_DNA.
DR EMBL; BT006796; AAP35442.1; -; mRNA.
DR EMBL; CH471106; EAW84101.1; -; Genomic_DNA.
DR EMBL; BC000083; AAH00083.1; -; mRNA.
DR EMBL; BC008793; AAH08793.1; -; mRNA.
DR PIR; G02313; G02313.
DR RefSeq; NP_008996.1; NM_007065.3.
DR UniGene; Hs.160958; -.
DR PDB; 1US7; X-ray; 2.30 A; B=127-378.
DR PDB; 2K5B; NMR; -; B=148-276.
DR PDB; 2W0G; X-ray; 1.88 A; A=148-276.
DR PDBsum; 1US7; -.
DR PDBsum; 2K5B; -.
DR PDBsum; 2W0G; -.
DR ProteinModelPortal; Q16543; -.
DR SMR; Q16543; 148-347.
DR DIP; DIP-27560N; -.
DR DIP; DIP-395N; -.
DR IntAct; Q16543; 133.
DR MINT; MINT-99762; -.
DR STRING; 9606.ENSP00000222005; -.
DR ChEMBL; CHEMBL1795123; -.
DR PhosphoSite; Q16543; -.
DR DMDM; 21542000; -.
DR PaxDb; Q16543; -.
DR PeptideAtlas; Q16543; -.
DR PRIDE; Q16543; -.
DR DNASU; 11140; -.
DR Ensembl; ENST00000222005; ENSP00000222005; ENSG00000105401.
DR GeneID; 11140; -.
DR KEGG; hsa:11140; -.
DR UCSC; uc002mof.1; human.
DR CTD; 11140; -.
DR GeneCards; GC19M010501; -.
DR HGNC; HGNC:1735; CDC37.
DR HPA; CAB004214; -.
DR HPA; HPA003928; -.
DR MIM; 605065; gene.
DR neXtProt; NX_Q16543; -.
DR PharmGKB; PA402; -.
DR eggNOG; NOG300020; -.
DR HOGENOM; HOG000018180; -.
DR HOVERGEN; HBG056343; -.
DR InParanoid; Q16543; -.
DR KO; K09554; -.
DR OrthoDB; EOG73805G; -.
DR PhylomeDB; Q16543; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_116125; Disease.
DR ChiTaRS; CDC37; human.
DR EvolutionaryTrace; Q16543; -.
DR GeneWiki; CDC37; -.
DR GenomeRNAi; 11140; -.
DR NextBio; 42344; -.
DR PRO; PR:Q16543; -.
DR ArrayExpress; Q16543; -.
DR Bgee; Q16543; -.
DR CleanEx; HS_CDC37; -.
DR Genevestigator; Q16543; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043234; C:protein complex; IEA:Ensembl.
DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
DR GO; GO:0006605; P:protein targeting; TAS:ProtInc.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
DR GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; IMP:MGI.
DR GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; IMP:MGI.
DR InterPro; IPR004918; Cdc37.
DR InterPro; IPR013873; Cdc37_C.
DR InterPro; IPR013874; Cdc37_Hsp90-bd.
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; 2.
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 3D-structure; Acetylation; Chaperone; Complete proteome; Cytoplasm;
KW Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
FT CHAIN 1 378 Hsp90 co-chaperone Cdc37.
FT /FTId=PRO_0000195057.
FT INIT_MET 1 1 Removed; alternate.
FT CHAIN 2 378 Hsp90 co-chaperone Cdc37, N-terminally
FT processed.
FT /FTId=PRO_0000423197.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 2 2 N-acetylvaline; in Hsp90 co-chaperone
FT Cdc37, N-terminally processed.
FT MOD_RES 13 13 Phosphoserine.
FT MOD_RES 78 78 N6-acetyllysine.
FT MOD_RES 154 154 N6-acetyllysine.
FT MOD_RES 377 377 Phosphoserine.
FT VARIANT 360 360 G -> E (in dbSNP:rs280528).
FT /FTId=VAR_022220.
FT HELIX 149 163
FT HELIX 168 177
FT HELIX 179 181
FT HELIX 184 199
FT HELIX 203 226
FT HELIX 230 241
FT HELIX 247 272
FT HELIX 294 300
FT HELIX 317 321
FT STRAND 325 327
FT HELIX 328 338
SQ SEQUENCE 378 AA; 44468 MW; 55BFEFFF3C2A5442 CRC64;
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK
VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS
KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH
LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK
IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES
LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG
DPLLEAVPKT GDEKDVSV
//
MIM
605065
*RECORD*
*FIELD* NO
605065
*FIELD* TI
*605065 CELL DIVISION CYCLE 37, S. CEREVISIAE, HOMOLOG OF; CDC37
*FIELD* TX
CLONING
read more
Cyclin-dependent kinase-4 (CDK4; 123829) is a cyclin D-dependent kinase
that controls progression through G1 phase of the mammalian cell cycle.
To identify proteins involved in CDK4 regulation, Dai et al. (1996)
analyzed CDK4 complexes from various cells by immunoprecipitation. Two
proteins coimmunoprecipitated with CDK4, one with a molecular mass of 85
kD, which was found to be HSP90 (see 140571), and the other with a
molecular mass of 44 kD. Dai et al. (1996) identified the second protein
as the human homolog of yeast CDC37. Human CDC37 contains 378 amino
acids and shares 45% and 25% amino acid identity with Drosophila and S.
cerevisiae CDC37, respectively. Mutations in yeast CDC37 cause cell
cycle arrest in G1 phase, and yeast CDC37 is required for the
association of CDC28 and cyclin and for the activation of CDC28 (Reed,
1980).
Stepanova et al. (1996) independently cloned and characterized human and
mouse CDC37 by using sequences from partial cdc37-like chicken cDNA to
amplify and screen various human and mouse cDNA libraries. The
intracellular distribution of CDC37 was largely cytoplasmic, and the
protein appeared to colocalize with cytoplasmic HSP90. CDC37 was
expressed in the same tissues during development as D-type cyclins, such
as proliferating zones of small intestine and stomach.
GENE FUNCTION
In in vitro assays, Stepanova et al. (1996) showed that CDC37 associated
most efficiently with CDK4, less with CDK6 (603368) and CDK7 (601955),
but not with CDK2 or CDK3. They determined that CDC37, CDK4, and HSP90
form a high molecular weight complex. The interactions between CDK4 and
CDC37 and those between CDK4 and D-type cyclins were found to be
mutually exclusive. Loss of association of CDC37 and CDK4 by
pharmacologic disruption of HSP90 function led to reduced stability of
newly synthesized CDK4. Stepanova et al. (1996) concluded that CDC37 and
HSP90 are important for CDK4 stability and play a positive role in cell
cycle progression.
Chen et al. (2002) identified CDC37 and HSP90 as 2 additional components
of the I-kappa-B kinase (IKK) complex. This complex also contains 2
catalytic subunits, IKK-alpha (600664) and IKK-beta (603258), and a
regulatory subunit, NEMO (300248).
Vaughan et al. (2008) stated that CDC37 is phosphorylated on ser13,
probably by casein kinase II (see 115440), and that absence of this
phosphorylation severely compromises CDC37 function. They showed that
ser13 was phosphorylated in vivo in uncomplexed CDC37, in CDC37 in a
binary complex with CDK4, and in CDC37 in a ternary complex with CDK4
and HSP90. Ser13 in the CDC37-CDK4-HSP90 complex was resistant to
nonspecific phosphatases, but it was efficiently dephosphorylated by
protein phosphatase-5 (PP5, or PPP5C; 600658), which did not
dephosphorylate uncomplexed CDC37. CDC37 and PP5 associated in HSP90
complexes in yeast and in human tumor cells, and PP5 regulated
phosphorylation of ser13 of CDC37 in vivo, directly affecting activation
of protein kinases by CDC37-HSP90. Vaughan et al. (2008) proposed that a
cyclic regulatory mechanism reverses constitutive CDC37 phosphorylation
when CDC37 is engaged in HSP90 complexes.
*FIELD* RF
1. Chen, G.; Cao, P.; Goeddel, D. V.: TNF-induced recruitment and
activation of the IKK complex require Cdc37 and Hsp90. Molec. Cell 9:
401-410, 2002.
2. Dai, K.; Kobayashi, R.; Beach, D.: Physical interaction of mammalian
CDC37 with CDK4. J. Biol. Chem. 271: 22030-22034, 1996.
3. Reed, S. I.: The selection of amber mutations in genes required
for completion of start, the controlling event of the cell division
cycle of S. cerevisiae. Genetics 95: 561-577, 1980.
4. Stepanova, L.; Leng, X.; Parker, S. B.; Harper, J. W.: Mammalian
p50(Cdc37) is a protein kinase-targeting subunit of Hsp90 that binds
and stabilizes Cdk4. Genes Dev. 10: 1491-1502, 1996.
5. Vaughan, C. K.; Mollapour, M.; Smith, J. R.; Truman, A.; Hu, B.;
Good, V. M.; Panaretou, B.; Neckers, L.; Clarke, P. A.; Workman, P.;
Piper, P. W.; Prodromou, C.; Pearl, L. H.: Hsp90-dependent activation
of protein kinases is regulated by chaperone-targeted dephosphorylation
of Cdc37. Molec. Cell 31: 886-895, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 5/29/2009
Stylianos E. Antonarakis - updated: 9/23/2002
*FIELD* CD
Yen-Pei C. Chang: 6/22/2000
*FIELD* ED
mgross: 06/02/2009
mgross: 6/2/2009
terry: 5/29/2009
mgross: 9/23/2002
carol: 6/22/2000
*RECORD*
*FIELD* NO
605065
*FIELD* TI
*605065 CELL DIVISION CYCLE 37, S. CEREVISIAE, HOMOLOG OF; CDC37
*FIELD* TX
CLONING
read more
Cyclin-dependent kinase-4 (CDK4; 123829) is a cyclin D-dependent kinase
that controls progression through G1 phase of the mammalian cell cycle.
To identify proteins involved in CDK4 regulation, Dai et al. (1996)
analyzed CDK4 complexes from various cells by immunoprecipitation. Two
proteins coimmunoprecipitated with CDK4, one with a molecular mass of 85
kD, which was found to be HSP90 (see 140571), and the other with a
molecular mass of 44 kD. Dai et al. (1996) identified the second protein
as the human homolog of yeast CDC37. Human CDC37 contains 378 amino
acids and shares 45% and 25% amino acid identity with Drosophila and S.
cerevisiae CDC37, respectively. Mutations in yeast CDC37 cause cell
cycle arrest in G1 phase, and yeast CDC37 is required for the
association of CDC28 and cyclin and for the activation of CDC28 (Reed,
1980).
Stepanova et al. (1996) independently cloned and characterized human and
mouse CDC37 by using sequences from partial cdc37-like chicken cDNA to
amplify and screen various human and mouse cDNA libraries. The
intracellular distribution of CDC37 was largely cytoplasmic, and the
protein appeared to colocalize with cytoplasmic HSP90. CDC37 was
expressed in the same tissues during development as D-type cyclins, such
as proliferating zones of small intestine and stomach.
GENE FUNCTION
In in vitro assays, Stepanova et al. (1996) showed that CDC37 associated
most efficiently with CDK4, less with CDK6 (603368) and CDK7 (601955),
but not with CDK2 or CDK3. They determined that CDC37, CDK4, and HSP90
form a high molecular weight complex. The interactions between CDK4 and
CDC37 and those between CDK4 and D-type cyclins were found to be
mutually exclusive. Loss of association of CDC37 and CDK4 by
pharmacologic disruption of HSP90 function led to reduced stability of
newly synthesized CDK4. Stepanova et al. (1996) concluded that CDC37 and
HSP90 are important for CDK4 stability and play a positive role in cell
cycle progression.
Chen et al. (2002) identified CDC37 and HSP90 as 2 additional components
of the I-kappa-B kinase (IKK) complex. This complex also contains 2
catalytic subunits, IKK-alpha (600664) and IKK-beta (603258), and a
regulatory subunit, NEMO (300248).
Vaughan et al. (2008) stated that CDC37 is phosphorylated on ser13,
probably by casein kinase II (see 115440), and that absence of this
phosphorylation severely compromises CDC37 function. They showed that
ser13 was phosphorylated in vivo in uncomplexed CDC37, in CDC37 in a
binary complex with CDK4, and in CDC37 in a ternary complex with CDK4
and HSP90. Ser13 in the CDC37-CDK4-HSP90 complex was resistant to
nonspecific phosphatases, but it was efficiently dephosphorylated by
protein phosphatase-5 (PP5, or PPP5C; 600658), which did not
dephosphorylate uncomplexed CDC37. CDC37 and PP5 associated in HSP90
complexes in yeast and in human tumor cells, and PP5 regulated
phosphorylation of ser13 of CDC37 in vivo, directly affecting activation
of protein kinases by CDC37-HSP90. Vaughan et al. (2008) proposed that a
cyclic regulatory mechanism reverses constitutive CDC37 phosphorylation
when CDC37 is engaged in HSP90 complexes.
*FIELD* RF
1. Chen, G.; Cao, P.; Goeddel, D. V.: TNF-induced recruitment and
activation of the IKK complex require Cdc37 and Hsp90. Molec. Cell 9:
401-410, 2002.
2. Dai, K.; Kobayashi, R.; Beach, D.: Physical interaction of mammalian
CDC37 with CDK4. J. Biol. Chem. 271: 22030-22034, 1996.
3. Reed, S. I.: The selection of amber mutations in genes required
for completion of start, the controlling event of the cell division
cycle of S. cerevisiae. Genetics 95: 561-577, 1980.
4. Stepanova, L.; Leng, X.; Parker, S. B.; Harper, J. W.: Mammalian
p50(Cdc37) is a protein kinase-targeting subunit of Hsp90 that binds
and stabilizes Cdk4. Genes Dev. 10: 1491-1502, 1996.
5. Vaughan, C. K.; Mollapour, M.; Smith, J. R.; Truman, A.; Hu, B.;
Good, V. M.; Panaretou, B.; Neckers, L.; Clarke, P. A.; Workman, P.;
Piper, P. W.; Prodromou, C.; Pearl, L. H.: Hsp90-dependent activation
of protein kinases is regulated by chaperone-targeted dephosphorylation
of Cdc37. Molec. Cell 31: 886-895, 2008.
*FIELD* CN
Patricia A. Hartz - updated: 5/29/2009
Stylianos E. Antonarakis - updated: 9/23/2002
*FIELD* CD
Yen-Pei C. Chang: 6/22/2000
*FIELD* ED
mgross: 06/02/2009
mgross: 6/2/2009
terry: 5/29/2009
mgross: 9/23/2002
carol: 6/22/2000