CDC37_HUMAN
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 03-AUG-2022, entry version 200.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 that
RT 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 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 intimately in
RT 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., Chen J.-J.,
RA Hartson S.D., Matts R.L.;
RT "Hsp90 regulates p50(cdc37) function during the biogenesis of the active
RT 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 not
RT 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 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 inducible
RT SUMOylation.";
RL Nucleic Acids Res. 35:E109-E109(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY
RP 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 MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT 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., Walther T.C.,
RA 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 SCALE
RP ANALYSIS] AT SER-13, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., Buerckstuemmer T.,
RA 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 SCALE
RP ANALYSIS] AT SER-13, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT 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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT 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., Richter K.;
RT "Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90)
RT motility by interaction with N-terminal and middle domain binding 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT 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., Marston Linehan W.,
RA Bratslavsky G., Mollapour M.;
RT "The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance
RT drug binding.";
RL Nat. Commun. 7:12037-12037(2016).
RN [26]
RP IDENTIFICATION IN A COMPLEX WITH HSP90; HSP70; STIP1; PPP5C; PTGES3; TSC1;
RP 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., Murphy R.L.,
RA Rensing N., Shapiro O., Panaretou B., Prodromou C., Loh S.N., Gutmann D.H.,
RA Bourboulia D., Bratslavsky G., Wong M., Mollapour M.;
RT "Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding
RT 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 stabilization
CC and promotion of their activity (PubMed:8666233). Inhibits HSP90AA1
CC ATPase activity (PubMed:23569206). {ECO:0000269|PubMed:23569206,
CC 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, PPP5C,
CC TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex
CC does not contain co-chaperones STIP1/HOP and PTGES3/p23
CC (PubMed:29127155). Forms a complex with Hsp90/HSP90AB1 and CDK6
CC (PubMed:9482106). Interacts with HSP90AA1 (PubMed:23569206,
CC PubMed:27353360). Interacts with AR, CDK4, CDK6 and EIF2AK1
CC (PubMed:11036079, PubMed:11085988, PubMed:9150368, PubMed:9482106).
CC Interacts with RB1 (By similarity). Interacts with KSR1
CC (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 Q16543; P60709: ACTB; NbExp=3; IntAct=EBI-295634, EBI-353944;
CC Q16543; P63261: ACTG1; NbExp=3; IntAct=EBI-295634, EBI-351292;
CC Q16543; P31749: AKT1; NbExp=4; IntAct=EBI-295634, EBI-296087;
CC Q16543; Q9Y243: AKT3; NbExp=2; IntAct=EBI-295634, EBI-296115;
CC Q16543; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-295634, EBI-746752;
CC Q16543; P02649: APOE; NbExp=3; IntAct=EBI-295634, EBI-1222467;
CC Q16543; Q96GD4: AURKB; NbExp=5; IntAct=EBI-295634, EBI-624291;
CC Q16543; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-295634, EBI-10181188;
CC Q16543; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-295634, EBI-11519926;
CC Q16543; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-295634, EBI-2548012;
CC Q16543; Q9Y2F9: BTBD3; NbExp=3; IntAct=EBI-295634, EBI-311155;
CC Q16543; Q9UQM7: CAMK2A; NbExp=5; IntAct=EBI-295634, EBI-1383687;
CC Q16543; Q13554-3: CAMK2B; NbExp=3; IntAct=EBI-295634, EBI-11523526;
CC Q16543; Q13555-5: CAMK2G; NbExp=3; IntAct=EBI-295634, EBI-12020154;
CC Q16543; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-295634, EBI-3866279;
CC Q16543; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-295634, EBI-11530605;
CC Q16543; Q6NZI2: CAVIN1; NbExp=3; IntAct=EBI-295634, EBI-2559016;
CC Q16543; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-295634, EBI-11524851;
CC Q16543; Q96M89-2: CCDC138; NbExp=3; IntAct=EBI-295634, EBI-10972887;
CC Q16543; Q4G0S7: CCDC152; NbExp=3; IntAct=EBI-295634, EBI-18398007;
CC Q16543; Q7Z6B0-2: CCDC91; NbExp=3; IntAct=EBI-295634, EBI-12012082;
CC Q16543; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-295634, EBI-10175300;
CC Q16543; Q14004: CDK13; NbExp=2; IntAct=EBI-295634, EBI-968626;
CC Q16543; Q96Q40: CDK15; NbExp=2; IntAct=EBI-295634, EBI-1051975;
CC Q16543; P11802: CDK4; NbExp=14; IntAct=EBI-295634, EBI-295644;
CC Q16543; Q00534: CDK6; NbExp=3; IntAct=EBI-295634, EBI-295663;
CC Q16543; P50750: CDK9; NbExp=5; IntAct=EBI-295634, EBI-1383449;
CC Q16543; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-295634, EBI-747776;
CC Q16543; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-295634, EBI-739624;
CC Q16543; Q9UFW8: CGGBP1; NbExp=3; IntAct=EBI-295634, EBI-723153;
CC Q16543; O15111: CHUK; NbExp=5; IntAct=EBI-295634, EBI-81249;
CC Q16543; Q5HYN5: CT45A1; NbExp=3; IntAct=EBI-295634, EBI-12051833;
CC Q16543; P78358: CTAG1B; NbExp=3; IntAct=EBI-295634, EBI-1188472;
CC Q16543; Q13620: CUL4B; NbExp=2; IntAct=EBI-295634, EBI-456067;
CC Q16543; Q9NTM9: CUTC; NbExp=3; IntAct=EBI-295634, EBI-714918;
CC Q16543; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-295634, EBI-11988027;
CC Q16543; P00533: EGFR; NbExp=11; IntAct=EBI-295634, EBI-297353;
CC Q16543; P04626: ERBB2; NbExp=3; IntAct=EBI-295634, EBI-641062;
CC Q16543; Q9NWS6: FAM118A; NbExp=3; IntAct=EBI-295634, EBI-8638992;
CC Q16543; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-295634, EBI-10175124;
CC Q16543; Q969F0: FATE1; NbExp=3; IntAct=EBI-295634, EBI-743099;
CC Q16543; Q9UKT8: FBXW2; NbExp=2; IntAct=EBI-295634, EBI-914727;
CC Q16543; P16591: FER; NbExp=3; IntAct=EBI-295634, EBI-1380661;
CC Q16543; Q02790: FKBP4; NbExp=3; IntAct=EBI-295634, EBI-1047444;
CC Q16543; P06241: FYN; NbExp=4; IntAct=EBI-295634, EBI-515315;
CC Q16543; O60861-1: GAS7; NbExp=3; IntAct=EBI-295634, EBI-11745923;
CC Q16543; O95995: GAS8; NbExp=3; IntAct=EBI-295634, EBI-1052570;
CC Q16543; P14136: GFAP; NbExp=3; IntAct=EBI-295634, EBI-744302;
CC Q16543; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-295634, EBI-2548508;
CC Q16543; Q08379: GOLGA2; NbExp=3; IntAct=EBI-295634, EBI-618309;
CC Q16543; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-295634, EBI-5916454;
CC Q16543; Q96HH9: GRAMD2B; NbExp=3; IntAct=EBI-295634, EBI-2832937;
CC Q16543; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-295634, EBI-717919;
CC Q16543; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-295634, EBI-748420;
CC Q16543; O75031: HSF2BP; NbExp=3; IntAct=EBI-295634, EBI-7116203;
CC Q16543; P07900: HSP90AA1; NbExp=14; IntAct=EBI-295634, EBI-296047;
CC Q16543; P08238: HSP90AB1; NbExp=11; IntAct=EBI-295634, EBI-352572;
CC Q16543; O14879: IFIT3; NbExp=4; IntAct=EBI-295634, EBI-745127;
CC Q16543; O14920: IKBKB; NbExp=4; IntAct=EBI-295634, EBI-81266;
CC Q16543; Q14164: IKBKE; NbExp=3; IntAct=EBI-295634, EBI-307369;
CC Q16543; Q9Y6K9: IKBKG; NbExp=6; IntAct=EBI-295634, EBI-81279;
CC Q16543; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-295634, EBI-747204;
CC Q16543; O75564-2: JRK; NbExp=3; IntAct=EBI-295634, EBI-17181882;
CC Q16543; Q9H079: KATNBL1; NbExp=3; IntAct=EBI-295634, EBI-715394;
CC Q16543; Q8WZ19: KCTD13; NbExp=3; IntAct=EBI-295634, EBI-742916;
CC Q16543; Q7L273: KCTD9; NbExp=3; IntAct=EBI-295634, EBI-4397613;
CC Q16543; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-295634, EBI-14069005;
CC Q16543; O95198: KLHL2; NbExp=3; IntAct=EBI-295634, EBI-746999;
CC Q16543; O95678: KRT75; NbExp=3; IntAct=EBI-295634, EBI-2949715;
CC Q16543; Q01546: KRT76; NbExp=3; IntAct=EBI-295634, EBI-2952745;
CC Q16543; Q6VAB6: KSR2; NbExp=7; IntAct=EBI-295634, EBI-6424389;
CC Q16543; P53671: LIMK2; NbExp=2; IntAct=EBI-295634, EBI-1384350;
CC Q16543; Q03252: LMNB2; NbExp=3; IntAct=EBI-295634, EBI-2830427;
CC Q16543; Q5S007: LRRK2; NbExp=7; IntAct=EBI-295634, EBI-5323863;
CC Q16543; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-295634, EBI-1216080;
CC Q16543; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-295634, EBI-742610;
CC Q16543; Q99558: MAP3K14; NbExp=6; IntAct=EBI-295634, EBI-358011;
CC Q16543; O43318: MAP3K7; NbExp=2; IntAct=EBI-295634, EBI-358684;
CC Q16543; O43318-2: MAP3K7; NbExp=5; IntAct=EBI-295634, EBI-358700;
CC Q16543; Q99750: MDFI; NbExp=3; IntAct=EBI-295634, EBI-724076;
CC Q16543; O15344: MID1; NbExp=3; IntAct=EBI-295634, EBI-2340316;
CC Q16543; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-295634, EBI-2548751;
CC Q16543; P00540: MOS; NbExp=2; IntAct=EBI-295634, EBI-1757866;
CC Q16543; Q9BYD2: MRPL9; NbExp=3; IntAct=EBI-295634, EBI-726059;
CC Q16543; Q8N987: NECAB1; NbExp=3; IntAct=EBI-295634, EBI-11956853;
CC Q16543; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-295634, EBI-10172876;
CC Q16543; P29474: NOS3; NbExp=4; IntAct=EBI-295634, EBI-1391623;
CC Q16543; Q9NQ35: NRIP3; NbExp=3; IntAct=EBI-295634, EBI-10311735;
CC Q16543; Q9BXI3: NT5C1A; NbExp=3; IntAct=EBI-295634, EBI-10441581;
CC Q16543; P22234: PAICS; NbExp=3; IntAct=EBI-295634, EBI-712261;
CC Q16543; O76083-2: PDE9A; NbExp=3; IntAct=EBI-295634, EBI-11524542;
CC Q16543; Q8N165: PDIK1L; NbExp=3; IntAct=EBI-295634, EBI-6423298;
CC Q16543; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-295634, EBI-14066006;
CC Q16543; Q9UL42: PNMA2; NbExp=3; IntAct=EBI-295634, EBI-302355;
CC Q16543; P78424: POU6F2; NbExp=3; IntAct=EBI-295634, EBI-12029004;
CC Q16543; P53041: PPP5C; NbExp=5; IntAct=EBI-295634, EBI-716663;
CC Q16543; P31321: PRKAR1B; NbExp=3; IntAct=EBI-295634, EBI-2805516;
CC Q16543; Q99873-3: PRMT1; NbExp=3; IntAct=EBI-295634, EBI-17165527;
CC Q16543; O14744: PRMT5; NbExp=3; IntAct=EBI-295634, EBI-351098;
CC Q16543; P41219: PRPH; NbExp=3; IntAct=EBI-295634, EBI-752074;
CC Q16543; P86480: PRR20D; NbExp=3; IntAct=EBI-295634, EBI-12754095;
CC Q16543; P49768: PSEN1; NbExp=3; IntAct=EBI-295634, EBI-297277;
CC Q16543; Q96QS6: PSKH2; NbExp=3; IntAct=EBI-295634, EBI-6424813;
CC Q16543; P62333: PSMC6; NbExp=3; IntAct=EBI-295634, EBI-357669;
CC Q16543; Q13882: PTK6; NbExp=4; IntAct=EBI-295634, EBI-1383632;
CC Q16543; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-295634, EBI-14093916;
CC Q16543; P04049: RAF1; NbExp=7; IntAct=EBI-295634, EBI-365996;
CC Q16543; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-295634, EBI-14065960;
CC Q16543; Q9HAT0: ROPN1; NbExp=3; IntAct=EBI-295634, EBI-1378139;
CC Q16543; Q9UH03: SEPTIN3; NbExp=3; IntAct=EBI-295634, EBI-727037;
CC Q16543; Q13501: SQSTM1; NbExp=8; IntAct=EBI-295634, EBI-307104;
CC Q16543; P12931: SRC; NbExp=5; IntAct=EBI-295634, EBI-621482;
CC Q16543; A7MD48: SRRM4; NbExp=3; IntAct=EBI-295634, EBI-3867173;
CC Q16543; O43805: SSNA1; NbExp=3; IntAct=EBI-295634, EBI-2515299;
CC Q16543; Q15831: STK11; NbExp=4; IntAct=EBI-295634, EBI-306838;
CC Q16543; Q8WU08-2: STK32A; NbExp=3; IntAct=EBI-295634, EBI-13046508;
CC Q16543; Q9Y2H1: STK38L; NbExp=6; IntAct=EBI-295634, EBI-991501;
CC Q16543; Q16623: STX1A; NbExp=3; IntAct=EBI-295634, EBI-712466;
CC Q16543; Q6PIF2: SYCE2; NbExp=3; IntAct=EBI-295634, EBI-11958386;
CC Q16543; Q8IZU3: SYCP3; NbExp=3; IntAct=EBI-295634, EBI-7574149;
CC Q16543; P15884-3: TCF4; NbExp=3; IntAct=EBI-295634, EBI-13636688;
CC Q16543; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-295634, EBI-741515;
CC Q16543; Q9BT49: THAP7; NbExp=3; IntAct=EBI-295634, EBI-741350;
CC Q16543; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-295634, EBI-2505861;
CC Q16543; Q15025: TNIP1; NbExp=3; IntAct=EBI-295634, EBI-357849;
CC Q16543; Q12933: TRAF2; NbExp=3; IntAct=EBI-295634, EBI-355744;
CC Q16543; Q13114: TRAF3; NbExp=3; IntAct=EBI-295634, EBI-357631;
CC Q16543; O00463: TRAF5; NbExp=3; IntAct=EBI-295634, EBI-523498;
CC Q16543; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-295634, EBI-2130429;
CC Q16543; Q9BXA6: TSSK6; NbExp=2; IntAct=EBI-295634, EBI-851883;
CC Q16543; Q6PHR2: ULK3; NbExp=2; IntAct=EBI-295634, EBI-1383475;
CC Q16543; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-295634, EBI-739895;
CC Q16543; P07947: YES1; NbExp=4; IntAct=EBI-295634, EBI-515331;
CC Q16543; O96006: ZBED1; NbExp=3; IntAct=EBI-295634, EBI-740037;
CC Q16543; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-295634, EBI-3918996;
CC Q16543; Q96BR9: ZBTB8A; NbExp=3; IntAct=EBI-295634, EBI-742740;
CC Q16543; Q8N554: ZNF276; NbExp=3; IntAct=EBI-295634, EBI-750821;
CC Q16543; Q8N720: ZNF655; NbExp=3; IntAct=EBI-295634, EBI-625509;
CC Q16543; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-295634, EBI-11962574;
CC Q16543; Q8N446: ZNF843; NbExp=2; IntAct=EBI-295634, EBI-6428016;
CC Q16543; P33279: EIF2AK1; Xeno; NbExp=3; IntAct=EBI-295634, EBI-640100;
CC Q16543; P0DTC9: N; Xeno; NbExp=4; IntAct=EBI-295634, EBI-25475856;
CC Q16543; P11500; Xeno; NbExp=3; IntAct=EBI-295634, EBI-640126;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9482106}.
CC -!- PTM: Constitutively sumoylated by UBE2I. {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/";
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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 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 AlphaFoldDB; Q16543; -.
DR BMRB; Q16543; -.
DR SASBDB; Q16543; -.
DR SMR; Q16543; -.
DR BioGRID; 116312; 505.
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; 434.
DR MINT; Q16543; -.
DR STRING; 9606.ENSP00000222005; -.
DR BindingDB; Q16543; -.
DR ChEMBL; CHEMBL1795123; -.
DR MoonDB; Q16543; Predicted.
DR TCDB; 8.A.163.1.1; the hsp90/cdc37 (hsp90/cdc37) family.
DR GlyGen; Q16543; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q16543; -.
DR MetOSite; Q16543; -.
DR PhosphoSitePlus; Q16543; -.
DR SwissPalm; Q16543; -.
DR BioMuta; CDC37; -.
DR DMDM; 21542000; -.
DR EPD; Q16543; -.
DR jPOST; Q16543; -.
DR MassIVE; Q16543; -.
DR MaxQB; Q16543; -.
DR PaxDb; Q16543; -.
DR PeptideAtlas; Q16543; -.
DR PRIDE; Q16543; -.
DR ProteomicsDB; 60906; -.
DR TopDownProteomics; Q16543; -.
DR Antibodypedia; 1136; 604 antibodies from 39 providers.
DR DNASU; 11140; -.
DR Ensembl; ENST00000222005.7; ENSP00000222005.1; ENSG00000105401.9.
DR GeneID; 11140; -.
DR KEGG; hsa:11140; -.
DR MANE-Select; ENST00000222005.7; ENSP00000222005.1; NM_007065.4; NP_008996.1.
DR UCSC; uc002mof.2; human.
DR CTD; 11140; -.
DR DisGeNET; 11140; -.
DR GeneCards; CDC37; -.
DR HGNC; HGNC:1735; CDC37.
DR HPA; ENSG00000105401; Low tissue specificity.
DR MIM; 605065; gene.
DR neXtProt; NX_Q16543; -.
DR OpenTargets; ENSG00000105401; -.
DR PharmGKB; PA402; -.
DR VEuPathDB; HostDB:ENSG00000105401; -.
DR eggNOG; KOG2260; Eukaryota.
DR GeneTree; ENSGT00390000013443; -.
DR InParanoid; Q16543; -.
DR OMA; IWCINLE; -.
DR OrthoDB; 786744at2759; -.
DR PhylomeDB; Q16543; -.
DR TreeFam; TF101059; -.
DR PathwayCommons; Q16543; -.
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-5675482; Regulation of necroptotic cell death.
DR Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-HSA-9634285; Constitutive Signaling by Overexpressed ERBB2.
DR Reactome; R-HSA-9652282; Drug-mediated inhibition of ERBB2 signaling.
DR Reactome; R-HSA-9664565; Signaling by ERBB2 KD Mutants.
DR Reactome; R-HSA-9665233; Resistance of ERBB2 KD mutants to trastuzumab.
DR Reactome; R-HSA-9665244; Resistance of ERBB2 KD mutants to sapitinib.
DR Reactome; R-HSA-9665245; Resistance of ERBB2 KD mutants to tesevatinib.
DR Reactome; R-HSA-9665246; Resistance of ERBB2 KD mutants to neratinib.
DR Reactome; R-HSA-9665247; Resistance of ERBB2 KD mutants to osimertinib.
DR Reactome; R-HSA-9665249; Resistance of ERBB2 KD mutants to afatinib.
DR Reactome; R-HSA-9665250; Resistance of ERBB2 KD mutants to AEE788.
DR Reactome; R-HSA-9665251; Resistance of ERBB2 KD mutants to lapatinib.
DR Reactome; R-HSA-9665348; Signaling by ERBB2 ECD mutants.
DR Reactome; R-HSA-9665686; Signaling by ERBB2 TMD/JMD mutants.
DR Reactome; R-HSA-9665737; Drug resistance in ERBB2 TMD/JMD mutants.
DR SignaLink; Q16543; -.
DR SIGNOR; Q16543; -.
DR BioGRID-ORCS; 11140; 747 hits in 1077 CRISPR screens.
DR ChiTaRS; CDC37; human.
DR EvolutionaryTrace; Q16543; -.
DR GeneWiki; CDC37; -.
DR GenomeRNAi; 11140; -.
DR Pharos; Q16543; Tbio.
DR PRO; PR:Q16543; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q16543; protein.
DR Bgee; ENSG00000105401; Expressed in sural nerve and 197 other tissues.
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:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; IEA:Ensembl.
DR GO; GO:0010608; P:post-transcriptional 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 DisProt; DP01420; -.
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; Cytoplasm; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..378
FT /note="Hsp90 co-chaperone Cdc37"
FT /id="PRO_0000195057"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CHAIN 2..378
FT /note="Hsp90 co-chaperone Cdc37, N-terminally processed"
FT /id="PRO_0000423197"
FT REGION 123..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 2
FT /note="N-acetylvaline; in Hsp90 co-chaperone Cdc37, N-
FT terminally processed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 78
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 118
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 154
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VARIANT 360
FT /note="G -> E (in dbSNP:rs280528)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_022220"
FT TURN 13..15
FT /evidence="ECO:0007829|PDB:2NCA"
FT HELIX 27..72
FT /evidence="ECO:0007829|PDB:2NCA"
FT HELIX 79..109
FT /evidence="ECO:0007829|PDB:2NCA"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:2NCA"
FT HELIX 149..163
FT /evidence="ECO:0007829|PDB:2W0G"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:2W0G"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2W0G"
FT HELIX 184..199
FT /evidence="ECO:0007829|PDB:2W0G"
FT HELIX 203..226
FT /evidence="ECO:0007829|PDB:2W0G"
FT HELIX 230..241
FT /evidence="ECO:0007829|PDB:2W0G"
FT HELIX 247..272
FT /evidence="ECO:0007829|PDB:2W0G"
FT HELIX 294..300
FT /evidence="ECO:0007829|PDB:1US7"
FT HELIX 303..310
FT /evidence="ECO:0007829|PDB:2N5X"
FT HELIX 317..321
FT /evidence="ECO:0007829|PDB:1US7"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:1US7"
FT HELIX 328..338
FT /evidence="ECO:0007829|PDB:1US7"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:2N5X"
FT STRAND 365..367
FT /evidence="ECO:0007829|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
