CDC37_DROME
ID CDC37_DROME Reviewed; 389 AA.
AC Q24276;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Hsp90 co-chaperone Cdc37;
DE AltName: Full=Hsp90 chaperone protein kinase-targeting subunit;
DE AltName: Full=Protein enhancer of sevenless 3B;
GN Name=Cdc37; Synonyms=E(sev)3B; ORFNames=CG12019;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RX PubMed=8020093; DOI=10.1016/0092-8674(94)90442-1;
RA Cutforth T., Rubin G.M.;
RT "Mutations in Hsp83 and cdc37 impair signaling by the sevenless receptor
RT tyrosine kinase in Drosophila.";
RL Cell 77:1027-1036(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP FUNCTION, AND INTERACTION WITH AURB.
RX PubMed=12374737; DOI=10.1093/emboj/cdf531;
RA Lange B.M.H., Rebollo E., Herold A., Gonzalez C.;
RT "Cdc37 is essential for chromosome segregation and cytokinesis in higher
RT eukaryotes.";
RL EMBO J. 21:5364-5374(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-296, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; THR-19 AND SER-355, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
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. Required for cytokinesis and
CC chromosome segregation in mitosis and male meiosis.
CC {ECO:0000269|PubMed:12374737, ECO:0000269|PubMed:8020093}.
CC -!- SUBUNIT: Forms a complex with Hsp90. Interacts with a number of kinases
CC such as Cdk1, sev and aurB. {ECO:0000269|PubMed:12374737,
CC ECO:0000269|PubMed:8020093}.
CC -!- INTERACTION:
CC Q24276; Q01071: E(spl)mdelta-HLH; NbExp=3; IntAct=EBI-167469, EBI-118907;
CC Q24276; P91656: S6k; NbExp=3; IntAct=EBI-167469, EBI-466629;
CC Q24276; Q9Y0H4: Su(dx); NbExp=3; IntAct=EBI-167469, EBI-89929;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L32839; AAA28414.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF47571.1; -; Genomic_DNA.
DR RefSeq; NP_477006.1; NM_057658.5.
DR AlphaFoldDB; Q24276; -.
DR SMR; Q24276; -.
DR BioGRID; 63764; 30.
DR DIP; DIP-20334N; -.
DR IntAct; Q24276; 27.
DR STRING; 7227.FBpp0072660; -.
DR iPTMnet; Q24276; -.
DR PaxDb; Q24276; -.
DR PRIDE; Q24276; -.
DR DNASU; 38232; -.
DR EnsemblMetazoa; FBtr0072777; FBpp0072660; FBgn0011573.
DR GeneID; 38232; -.
DR KEGG; dme:Dmel_CG12019; -.
DR CTD; 11140; -.
DR FlyBase; FBgn0011573; Cdc37.
DR VEuPathDB; VectorBase:FBgn0011573; -.
DR eggNOG; KOG2260; Eukaryota.
DR GeneTree; ENSGT00390000013443; -.
DR HOGENOM; CLU_046495_0_0_1; -.
DR InParanoid; Q24276; -.
DR OMA; IWCINLE; -.
DR OrthoDB; 786744at2759; -.
DR PhylomeDB; Q24276; -.
DR Reactome; R-DME-114608; Platelet degranulation.
DR Reactome; R-DME-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-DME-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-DME-9652282; Drug-mediated inhibition of ERBB2 signaling.
DR SignaLink; Q24276; -.
DR BioGRID-ORCS; 38232; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 38232; -.
DR PRO; PR:Q24276; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0011573; Expressed in embryonic/larval hemocyte (Drosophila) and 23 other tissues.
DR ExpressionAtlas; Q24276; baseline and differential.
DR Genevisible; Q24276; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0005158; F:insulin receptor binding; IDA:FlyBase.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0030296; F:protein tyrosine kinase activator activity; NAS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; HGI:FlyBase.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:FlyBase.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR Gene3D; 1.20.58.610; -; 1.
DR InterPro; IPR004918; Cdc37.
DR InterPro; IPR013873; Cdc37_C.
DR InterPro; IPR013874; Cdc37_Hsp90-bd.
DR InterPro; IPR038189; Cdc37_Hsp90-bd_sf.
DR InterPro; IPR013855; Cdc37_N_dom.
DR PANTHER; PTHR12800; PTHR12800; 1.
DR Pfam; PF08564; CDC37_C; 1.
DR Pfam; PF08565; CDC37_M; 1.
DR Pfam; PF03234; CDC37_N; 1.
DR SMART; SM01069; CDC37_C; 1.
DR SMART; SM01070; CDC37_M; 1.
DR SMART; SM01071; CDC37_N; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Chaperone; Chromosome partition; Cytoplasm;
KW Developmental protein; Meiosis; Mitosis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..389
FT /note="Hsp90 co-chaperone Cdc37"
FT /id="PRO_0000195063"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
SQ SEQUENCE 389 AA; 45150 MW; 33490D24D4B60BFD CRC64;
MVDYSKWKNI EISDDEDDTH PNIDTPSLFR WRHQARVERM AEMDHEKDEL KKKRQSYQAR
LMDVKERISK KDGDEEALKK ELEKIEAEGK ELDRIESEMI KKEKKTPWNV DTISKPGFEK
TVINKKAGRK PDENLSEEER EQRMKQFVKE NEKLCQQYGM LRKYDDSKRF LQEHLHLVGE
ETANYLVIWS INLEMEEKHE LMAHVAHQCI CMQYILELAK QLDVDPRACV SSFFSKIQHC
HPEYRAQFDS EIEGFKGRIQ KRAQEKIQEA IAQAEEEERK ERLGPGGLDP ADVFESLPDE
LKACFESRDV ELLQKTIAAM PVDVAKLHMK RCVDSGLWVP NAADLEGDKK EEDDSDDVAG
GEEKTDDAKS ESAAKEEPIY TGVSTEDVD
