GenomeNet

Database: UniProt
Entry: Q16543
LinkDB: Q16543
Original site: Q16543 
ID   CDC37_HUMAN             Reviewed;         378 AA.
AC   Q16543; Q53YA2;
DT   20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   31-JUL-2019, entry version 184.
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; DOI=10.1101/gad.10.12.1491;
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 AND HSP90AB1.
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   INTERACTION WITH KSR1.
RX   PubMed=10409742; DOI=10.1128/MCB.19.8.5523;
RA   Stewart S., Sundaram M., Zhang Y., Lee J., Han M., Guan K.L.;
RT   "Kinase suppressor of Ras forms a multiprotein signaling complex and
RT   modulates MEK localization.";
RL   Mol. Cell. Biol. 19:5523-5534(1999).
RN   [10]
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   [11]
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   [12]
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   [13]
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   [14]
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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND VAL-2, CLEAVAGE OF
RP   INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [17]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78 AND LYS-154, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [18]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-13, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP   SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
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   [19]
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   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT VAL-2, PHOSPHORYLATION [LARGE
RP   SCALE ANALYSIS] AT SER-13, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP   SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
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   [21]
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).
RN   [22]
RP   FUNCTION, AND INTERACTION WITH HSP90AA1.
RX   PubMed=23569206; DOI=10.1074/jbc.M112.439257;
RA   Eckl J.M., Rutz D.A., Haslbeck V., Zierer B.K., Reinstein J.,
RA   Richter K.;
RT   "Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein
RT   90) motility by interaction with N-terminal and middle domain binding
RT   sites.";
RL   J. Biol. Chem. 288:16032-16042(2013).
RN   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118 AND SER-120, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [24]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [25]
RP   INTERACTION WITH HSP90AA1; FLCN; FNIP1 AND FNIP2.
RX   PubMed=27353360; DOI=10.1038/ncomms12037;
RA   Woodford M.R., Dunn D.M., Blanden A.R., Capriotti D., Loiselle D.,
RA   Prodromou C., Panaretou B., Hughes P.F., Smith A., Ackerman W.,
RA   Haystead T.A., Loh S.N., Bourboulia D., Schmidt L.S.,
RA   Marston Linehan W., Bratslavsky G., Mollapour M.;
RT   "The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and
RT   enhance drug binding.";
RL   Nat. Commun. 7:12037-12037(2016).
RN   [26]
RP   IDENTIFICATION IN A COMPLEX WITH HSP90; HSP70; STIP1; PPP5C; PTGES3;
RP   TSC1; TSC2; AKT; CDK4; RAF1 AND NR3C1.
RX   PubMed=29127155; DOI=10.15252/embj.201796700;
RA   Woodford M.R., Sager R.A., Marris E., Dunn D.M., Blanden A.R.,
RA   Murphy R.L., Rensing N., Shapiro O., Panaretou B., Prodromou C.,
RA   Loh S.N., Gutmann D.H., Bourboulia D., Bratslavsky G., Wong M.,
RA   Mollapour M.;
RT   "Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates
RT   folding of kinase and non-kinase clients.";
RL   EMBO J. 36:3650-3665(2017).
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 (PubMed:8666233).
CC       Inhibits HSP90AA1 ATPase activity (PubMed:23569206).
CC       {ECO:0000269|PubMed:23569206, ECO:0000269|PubMed:8666233}.
CC   -!- SUBUNIT: Probably forms a complex composed of chaperones HSP90 and
CC       HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and
CC       client protein TSC2 (PubMed:29127155). Probably forms a complex
CC       composed of chaperones HSP90 and HSP70, co-chaperones CDC37,
CC       PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1;
CC       this complex does not contain co-chaperones STIP1/HOP and
CC       PTGES3/p23 (PubMed:29127155). Forms a complex with Hsp90/HSP90AB1
CC       and CDK6 (PubMed:9482106). Interacts with HSP90AA1
CC       (PubMed:23569206, PubMed:27353360). Interacts with AR, CDK4, CDK6
CC       and EIF2AK1 (PubMed:11036079, PubMed:11085988, PubMed:9150368,
CC       PubMed:9482106). Interacts with RB1 (By similarity). Interacts
CC       with KSR1 (PubMed:10409742). Interacts with FLCN, FNIP1 and FNIP2
CC       (PubMed:27353360). {ECO:0000250|UniProtKB:Q63692,
CC       ECO:0000269|PubMed:10409742, ECO:0000269|PubMed:11036079,
CC       ECO:0000269|PubMed:11085988, ECO:0000269|PubMed:23569206,
CC       ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155,
CC       ECO:0000269|PubMed:9150368, ECO:0000269|PubMed:9482106}.
CC   -!- INTERACTION:
CC       P11500:- (xeno); NbExp=3; IntAct=EBI-295634, EBI-640126;
CC       P31749:AKT1; NbExp=2; IntAct=EBI-295634, EBI-296087;
CC       Q9Y243:AKT3; NbExp=2; IntAct=EBI-295634, EBI-296115;
CC       P02649:APOE; NbExp=3; IntAct=EBI-295634, EBI-1222467;
CC       Q96GD4:AURKB; NbExp=4; IntAct=EBI-295634, EBI-624291;
CC       Q96Q40:CDK15; NbExp=2; IntAct=EBI-295634, EBI-1051975;
CC       P11802:CDK4; NbExp=11; IntAct=EBI-295634, EBI-295644;
CC       Q00534:CDK6; NbExp=3; IntAct=EBI-295634, EBI-295663;
CC       P50750:CDK9; NbExp=3; IntAct=EBI-295634, EBI-1383449;
CC       O15111:CHUK; NbExp=4; IntAct=EBI-295634, EBI-81249;
CC       Q13620:CUL4B; NbExp=2; IntAct=EBI-295634, EBI-456067;
CC       P00533:EGFR; NbExp=9; IntAct=EBI-295634, EBI-297353;
CC       P33279:EIF2AK1 (xeno); NbExp=3; IntAct=EBI-295634, EBI-640100;
CC       P04626:ERBB2; NbExp=3; IntAct=EBI-295634, EBI-641062;
CC       Q9UKT8:FBXW2; NbExp=2; IntAct=EBI-295634, EBI-914727;
CC       P16591:FER; NbExp=2; IntAct=EBI-295634, EBI-1380661;
CC       Q02790:FKBP4; NbExp=3; IntAct=EBI-295634, EBI-1047444;
CC       P07900:HSP90AA1; NbExp=14; IntAct=EBI-295634, EBI-296047;
CC       P08238:HSP90AB1; NbExp=11; IntAct=EBI-295634, EBI-352572;
CC       O14879:IFIT3; NbExp=4; IntAct=EBI-295634, EBI-745127;
CC       O14920:IKBKB; NbExp=4; IntAct=EBI-295634, EBI-81266;
CC       Q14164:IKBKE; NbExp=3; IntAct=EBI-295634, EBI-307369;
CC       Q9Y6K9:IKBKG; NbExp=6; IntAct=EBI-295634, EBI-81279;
CC       Q6VAB6:KSR2; NbExp=6; IntAct=EBI-295634, EBI-6424389;
CC       Q5S007:LRRK2; NbExp=7; IntAct=EBI-295634, EBI-5323863;
CC       Q99558:MAP3K14; NbExp=3; IntAct=EBI-295634, EBI-358011;
CC       O43318-2:MAP3K7; NbExp=5; IntAct=EBI-295634, EBI-358700;
CC       P29474:NOS3; NbExp=4; IntAct=EBI-295634, EBI-1391623;
CC       P53041:PPP5C; NbExp=5; IntAct=EBI-295634, EBI-716663;
CC       P49768:PSEN1; NbExp=3; IntAct=EBI-295634, EBI-297277;
CC       P04049:RAF1; NbExp=4; IntAct=EBI-295634, EBI-365996;
CC       Q13501:SQSTM1; NbExp=5; IntAct=EBI-295634, EBI-307104;
CC       Q15831:STK11; NbExp=3; IntAct=EBI-295634, EBI-306838;
CC       Q9Y2H1:STK38L; NbExp=6; IntAct=EBI-295634, EBI-991501;
CC       Q8N446:ZNF843; NbExp=2; IntAct=EBI-295634, EBI-6428016;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9482106}.
CC   -!- PTM: Constitutively sumoylated by UBE2I.
CC       {ECO:0000269|PubMed:17709345}.
CC   -!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/cdc37/";
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   CCDS; CCDS12237.1; -.
DR   PIR; G02313; G02313.
DR   RefSeq; NP_008996.1; NM_007065.3.
DR   PDB; 1US7; X-ray; 2.30 A; B=127-378.
DR   PDB; 2K5B; NMR; -; B=148-276.
DR   PDB; 2N5X; NMR; -; A=288-378.
DR   PDB; 2NCA; NMR; -; A=1-126.
DR   PDB; 2W0G; X-ray; 1.88 A; A=148-276.
DR   PDB; 5FWK; EM; 3.90 A; E=1-378.
DR   PDB; 5FWL; EM; 9.00 A; E=1-378.
DR   PDB; 5FWM; EM; 8.00 A; E=1-378.
DR   PDB; 5FWP; EM; 7.20 A; E=1-378.
DR   PDB; 5HPE; X-ray; 2.27 A; A=5-20.
DR   PDBsum; 1US7; -.
DR   PDBsum; 2K5B; -.
DR   PDBsum; 2N5X; -.
DR   PDBsum; 2NCA; -.
DR   PDBsum; 2W0G; -.
DR   PDBsum; 5FWK; -.
DR   PDBsum; 5FWL; -.
DR   PDBsum; 5FWM; -.
DR   PDBsum; 5FWP; -.
DR   PDBsum; 5HPE; -.
DR   SMR; Q16543; -.
DR   BioGrid; 116312; 295.
DR   ComplexPortal; CPX-3285; HSP90B-CDC37 chaperone complex.
DR   ComplexPortal; CPX-3288; HSP90A-CDC37 chaperone complex.
DR   CORUM; Q16543; -.
DR   DIP; DIP-27560N; -.
DR   IntAct; Q16543; 365.
DR   MINT; Q16543; -.
DR   STRING; 9606.ENSP00000222005; -.
DR   ChEMBL; CHEMBL1795123; -.
DR   MoonDB; Q16543; Predicted.
DR   iPTMnet; Q16543; -.
DR   PhosphoSitePlus; Q16543; -.
DR   SwissPalm; Q16543; -.
DR   BioMuta; CDC37; -.
DR   DMDM; 21542000; -.
DR   EPD; Q16543; -.
DR   jPOST; Q16543; -.
DR   MaxQB; Q16543; -.
DR   PaxDb; Q16543; -.
DR   PeptideAtlas; Q16543; -.
DR   PRIDE; Q16543; -.
DR   ProteomicsDB; 60906; -.
DR   TopDownProteomics; Q16543; -.
DR   DNASU; 11140; -.
DR   Ensembl; ENST00000222005; ENSP00000222005; ENSG00000105401.
DR   GeneID; 11140; -.
DR   KEGG; hsa:11140; -.
DR   UCSC; uc002mof.2; human.
DR   CTD; 11140; -.
DR   DisGeNET; 11140; -.
DR   GeneCards; CDC37; -.
DR   HGNC; HGNC:1735; CDC37.
DR   HPA; CAB004214; -.
DR   HPA; HPA003928; -.
DR   MIM; 605065; gene.
DR   neXtProt; NX_Q16543; -.
DR   OpenTargets; ENSG00000105401; -.
DR   PharmGKB; PA402; -.
DR   eggNOG; KOG2260; Eukaryota.
DR   eggNOG; ENOG410XTCZ; LUCA.
DR   GeneTree; ENSGT00390000013443; -.
DR   HOGENOM; HOG000018180; -.
DR   InParanoid; Q16543; -.
DR   KO; K09554; -.
DR   OrthoDB; 786744at2759; -.
DR   PhylomeDB; Q16543; -.
DR   TreeFam; TF101059; -.
DR   Reactome; R-HSA-1227986; Signaling by ERBB2.
DR   Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
DR   Reactome; R-HSA-5637810; Constitutive Signaling by EGFRvIII.
DR   Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
DR   SIGNOR; Q16543; -.
DR   ChiTaRS; CDC37; human.
DR   EvolutionaryTrace; Q16543; -.
DR   GeneWiki; CDC37; -.
DR   GenomeRNAi; 11140; -.
DR   PRO; PR:Q16543; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000105401; Expressed in 225 organ(s), highest expression level in left lobe of thyroid gland.
DR   ExpressionAtlas; Q16543; baseline and differential.
DR   Genevisible; Q16543; HS.
DR   GO; GO:0101031; C:chaperone complex; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:1990565; C:HSP90-CDC37 chaperone complex; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR   GO; GO:0031072; F:heat shock protein binding; IPI:UniProtKB.
DR   GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
DR   GO; GO:0019900; F:kinase binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR   GO; GO:0019887; F:protein kinase regulator activity; IEA:Ensembl.
DR   GO; GO:0097110; F:scaffold protein binding; IPI:UniProtKB.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
DR   GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; IEA:Ensembl.
DR   GO; GO:0010608; P:posttranscriptional regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
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   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   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                                {ECO:0000244|PubMed:19413330,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   CHAIN         2    378       Hsp90 co-chaperone Cdc37, N-terminally
FT                                processed.
FT                                /FTId=PRO_0000423197.
FT   MOD_RES       1      1       N-acetylmethionine.
FT                                {ECO:0000244|PubMed:19413330}.
FT   MOD_RES       2      2       N-acetylvaline; in Hsp90 co-chaperone
FT                                Cdc37, N-terminally processed.
FT                                {ECO:0000244|PubMed:19413330,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES      13     13       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   MOD_RES      78     78       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     118    118       Phosphothreonine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     120    120       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     154    154       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     377    377       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648}.
FT   VARIANT     360    360       G -> E (in dbSNP:rs280528).
FT                                {ECO:0000269|Ref.3}.
FT                                /FTId=VAR_022220.
FT   TURN         13     15       {ECO:0000244|PDB:2NCA}.
FT   HELIX        27     72       {ECO:0000244|PDB:2NCA}.
FT   HELIX        79    109       {ECO:0000244|PDB:2NCA}.
FT   HELIX       113    116       {ECO:0000244|PDB:2NCA}.
FT   HELIX       149    163       {ECO:0000244|PDB:2W0G}.
FT   HELIX       168    177       {ECO:0000244|PDB:2W0G}.
FT   HELIX       179    181       {ECO:0000244|PDB:2W0G}.
FT   HELIX       184    199       {ECO:0000244|PDB:2W0G}.
FT   HELIX       203    226       {ECO:0000244|PDB:2W0G}.
FT   HELIX       230    241       {ECO:0000244|PDB:2W0G}.
FT   HELIX       247    272       {ECO:0000244|PDB:2W0G}.
FT   HELIX       294    300       {ECO:0000244|PDB:1US7}.
FT   HELIX       303    310       {ECO:0000244|PDB:2N5X}.
FT   HELIX       317    321       {ECO:0000244|PDB:1US7}.
FT   STRAND      325    327       {ECO:0000244|PDB:1US7}.
FT   HELIX       328    338       {ECO:0000244|PDB:1US7}.
FT   STRAND      345    347       {ECO:0000244|PDB:2N5X}.
FT   STRAND      365    367       {ECO:0000244|PDB:2N5X}.
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
//
DBGET integrated database retrieval system