CDC37_RAT
ID CDC37_RAT Reviewed; 379 AA.
AC Q63692; Q8CH95;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 03-AUG-2022, entry version 146.
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8534368; DOI=10.1089/dna.1995.14.1017;
RA Ozaki T., Irie K., Sakiyama S.;
RT "Molecular cloning and cell cycle-dependent expression of a novel gene that
RT is homologous to cdc37.";
RL DNA Cell Biol. 14:1017-1023(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Miyata Y.;
RT "Coding region of rat Cdc37, a kinase-associated HSP90 co-chaperone.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [4]
RP INTERACTION WITH RB1.
RX PubMed=8945638; DOI=10.1089/dna.1996.15.975;
RA Ozaki T., Sakiyama S.;
RT "Interaction of rat Cdc37-related protein with retinoblastoma gene
RT product.";
RL DNA Cell Biol. 15:975-979(1996).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Inhibits HSP90AA1 ATPase activity.
CC {ECO:0000250|UniProtKB:Q16543}.
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 (By similarity). Probably forms a complex composed
CC of chaperones HSP90 and HSP70, co-chaperones CDC37, PPP5C, TSC1 and
CC client protein TSC2, CDK4, AKT, RAF1 and NR3C1; this complex does not
CC contain co-chaperones STIP1/HOP and PTGES3/p23 (By similarity). Forms a
CC complex with Hsp90/HSP90AB1 and CDK6 (By similarity). Interacts with
CC HSP90AA1 (By similarity). Interacts with AR, CDK4, CDK6 and EIF2AK1 (By
CC similarity). Interacts with RB1 (PubMed:8945638). Interacts with KSR1
CC (By similarity). Interacts with FLCN, FNIP1 and FNIP2 (By similarity).
CC {ECO:0000250|UniProtKB:Q16543, ECO:0000269|PubMed:8945638}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16543}.
CC -!- PTM: Constitutively sumoylated by UBE2I.
CC {ECO:0000250|UniProtKB:Q16543}.
CC -!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
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DR EMBL; D26564; BAA05618.1; -; mRNA.
DR EMBL; AB097113; BAC54286.1; -; mRNA.
DR EMBL; BC061720; AAH61720.1; -; mRNA.
DR RefSeq; NP_446195.1; NM_053743.1.
DR AlphaFoldDB; Q63692; -.
DR SMR; Q63692; -.
DR BioGRID; 250380; 6.
DR IntAct; Q63692; 4.
DR MINT; Q63692; -.
DR STRING; 10116.ENSRNOP00000051248; -.
DR iPTMnet; Q63692; -.
DR PhosphoSitePlus; Q63692; -.
DR jPOST; Q63692; -.
DR PaxDb; Q63692; -.
DR PRIDE; Q63692; -.
DR GeneID; 114562; -.
DR KEGG; rno:114562; -.
DR UCSC; RGD:71006; rat.
DR CTD; 11140; -.
DR RGD; 71006; Cdc37.
DR eggNOG; KOG2260; Eukaryota.
DR InParanoid; Q63692; -.
DR OrthoDB; 786744at2759; -.
DR PhylomeDB; Q63692; -.
DR Reactome; R-RNO-1227986; Signaling by ERBB2.
DR Reactome; R-RNO-5675482; Regulation of necroptotic cell death.
DR Reactome; R-RNO-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-RNO-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-RNO-9652282; Drug-mediated inhibition of ERBB2 signaling.
DR PRO; PR:Q63692; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q63692; RN.
DR GO; GO:0101031; C:chaperone complex; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:1990565; C:HSP90-CDC37 chaperone complex; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0032587; C:ruffle membrane; IDA:RGD.
DR GO; GO:0051087; F:chaperone binding; IPI:RGD.
DR GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
DR GO; GO:0051879; F:Hsp90 protein binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:RGD.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
DR GO; GO:0043422; F:protein kinase B binding; IPI:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISO:RGD.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IEP:RGD.
DR GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; ISO:RGD.
DR GO; GO:0045859; P:regulation of protein kinase activity; ISO:RGD.
DR GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; ISO:RGD.
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 Acetylation; Chaperone; Cytoplasm; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..379
FT /note="Hsp90 co-chaperone Cdc37"
FT /id="PRO_0000423199"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT CHAIN 2..379
FT /note="Hsp90 co-chaperone Cdc37, N-terminally processed"
FT /id="PRO_0000195059"
FT REGION 123..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT MOD_RES 2
FT /note="N-acetylvaline; in Hsp90 co-chaperone Cdc37, N-
FT terminally processed"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT MOD_RES 155
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT MOD_RES 378
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16543"
FT CONFLICT 64
FT /note="C -> F (in Ref. 1; BAA05618)"
FT /evidence="ECO:0000305"
FT CONFLICT 98..107
FT /note="SWEQKLEDMR -> TGSRSWRTCG (in Ref. 1; BAA05618)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="N -> F (in Ref. 1; BAA05618)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 44510 MW; 52D1314C88824CE1 CRC64;
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK
VAECQRKLKE LEVAEGGGQV ELERLRAEAQ QLRKEERSWE QKLEDMRKKE KNMPWNVDTL
SKDGFSKSMV NTKPEKAEED SEEAREQKHK TFVEKYEKQI KHFGMLHRWD DSQKYLSDNV
HLVCEETANY LVIWCIDLEV EEKCALMEQV AHQTMVMQFI LELAKSLKVD PRACFRQFFT
KIKTADQQYM EGFKYELEAF KERVRGRAKL RIEKAMKEYE EEERKKRLGP GGLDPVEVYE
SLPEELQKCF DVKDVQMLQD AISKMDPTDA KYHMQRCIDS GLWVPNSKSG EAKEGEEAGP
GDPLLEAVPK AGNEKDISA
