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Hsp90 co-chaperone Cdc37 (Hsp90 chaperone protein kinase-targeting subunit) (p50Cdc37) [Cleaved into: Hsp90 co-chaperone Cdc37, N-terminally processed]

 CDC37_RAT               Reviewed;         379 AA.
Q63692; Q8CH95;
20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
20-JUN-2003, sequence version 2.
20-JUN-2018, entry version 132.
RecName: Full=Hsp90 co-chaperone Cdc37;
AltName: Full=Hsp90 chaperone protein kinase-targeting subunit;
AltName: Full=p50Cdc37;
Contains:
RecName: Full=Hsp90 co-chaperone Cdc37, N-terminally processed;
Name=Cdc37;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8534368; DOI=10.1089/dna.1995.14.1017;
Ozaki T., Irie K., Sakiyama S.;
"Molecular cloning and cell cycle-dependent expression of a novel gene
that is homologous to cdc37.";
DNA Cell Biol. 14:1017-1023(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Miyata Y.;
"Coding region of rat Cdc37, a kinase-associated HSP90 co-chaperone.";
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH RB1.
PubMed=8945638; DOI=10.1089/dna.1996.15.975;
Ozaki T., Sakiyama S.;
"Interaction of rat Cdc37-related protein with retinoblastoma gene
product.";
DNA Cell Biol. 15:975-979(1996).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Co-chaperone that binds to numerous kinases and promotes
their interaction with the Hsp90 complex, resulting in
stabilization and promotion of their activity. Inhibits HSP90AA1
ATPase activity. {ECO:0000250|UniProtKB:Q16543}.
-!- SUBUNIT: Probably forms a complex composed of chaperones HSP90 and
HSP70, co-chaperones STIP1/HOP, CDC37, PPP5C, PTGES3/p23, TSC1 and
client protein TSC2 (By similarity). Probably forms a complex
composed of chaperones HSP90 and HSP70, co-chaperones CDC37,
PPP5C, TSC1 and client protein TSC2, CDK4, AKT, RAF1 and NR3C1;
this complex does not contain co-chaperones STIP1/HOP and
PTGES3/p23 (By similarity). Forms a complex with Hsp90/HSP90AB1
and CDK6 (By similarity). Interacts with HSP90AA1 (By similarity).
Interacts with AR, CDK4, CDK6 and EIF2AK1 (By similarity).
Interacts with RB1 (PubMed:8945638). Interacts with KSR1 (By
similarity). Interacts with FLCN, FNIP1 and FNIP2 (By similarity).
{ECO:0000250|UniProtKB:Q16543, ECO:0000269|PubMed:8945638}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16543}.
-!- PTM: Constitutively sumoylated by UBE2I.
{ECO:0000250|UniProtKB:Q16543}.
-!- SIMILARITY: Belongs to the CDC37 family. {ECO:0000305}.
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EMBL; D26564; BAA05618.1; -; mRNA.
EMBL; AB097113; BAC54286.1; -; mRNA.
EMBL; BC061720; AAH61720.1; -; mRNA.
RefSeq; NP_446195.1; NM_053743.1.
UniGene; Rn.17982; -.
ProteinModelPortal; Q63692; -.
SMR; Q63692; -.
BioGrid; 250380; 4.
IntAct; Q63692; 2.
MINT; Q63692; -.
STRING; 10116.ENSRNOP00000051248; -.
iPTMnet; Q63692; -.
PhosphoSitePlus; Q63692; -.
PaxDb; Q63692; -.
PRIDE; Q63692; -.
GeneID; 114562; -.
KEGG; rno:114562; -.
UCSC; RGD:71006; rat.
CTD; 11140; -.
RGD; 71006; Cdc37.
eggNOG; KOG2260; Eukaryota.
eggNOG; ENOG410XTCZ; LUCA.
HOGENOM; HOG000018180; -.
HOVERGEN; HBG056343; -.
InParanoid; Q63692; -.
KO; K09554; -.
OrthoDB; EOG091G0HL8; -.
PhylomeDB; Q63692; -.
PRO; PR:Q63692; -.
Proteomes; UP000002494; Unplaced.
Genevisible; Q63692; RN.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0032587; C:ruffle membrane; IDA:RGD.
GO; GO:0051087; F:chaperone binding; IPI:RGD.
GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
GO; GO:0031435; F:mitogen-activated protein kinase kinase kinase binding; IPI:RGD.
GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
GO; GO:0043422; F:protein kinase B binding; IPI:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
GO; GO:0006457; P:protein folding; IBA:GO_Central.
GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
GO; GO:0051726; P:regulation of cell cycle; IEP:RGD.
Gene3D; 1.20.58.610; -; 1.
InterPro; IPR004918; Cdc37.
InterPro; IPR013873; Cdc37_C.
InterPro; IPR013874; Cdc37_Hsp90-bd.
InterPro; IPR038189; Cdc37_Hsp90-bd_sf.
InterPro; IPR013855; Cdc37_N_dom.
PANTHER; PTHR12800; PTHR12800; 1.
Pfam; PF08564; CDC37_C; 1.
Pfam; PF08565; CDC37_M; 1.
Pfam; PF03234; CDC37_N; 1.
SMART; SM01069; CDC37_C; 1.
SMART; SM01070; CDC37_M; 1.
SMART; SM01071; CDC37_N; 1.
1: Evidence at protein level;
Acetylation; Chaperone; Complete proteome; Cytoplasm; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 379 Hsp90 co-chaperone Cdc37.
/FTId=PRO_0000423199.
INIT_MET 1 1 Removed; alternate.
{ECO:0000250|UniProtKB:Q16543}.
CHAIN 2 379 Hsp90 co-chaperone Cdc37, N-terminally
processed.
/FTId=PRO_0000195059.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:Q16543}.
MOD_RES 2 2 N-acetylvaline; in Hsp90 co-chaperone
Cdc37, N-terminally processed.
{ECO:0000250|UniProtKB:Q16543}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 119 119 Phosphothreonine.
{ECO:0000250|UniProtKB:Q16543}.
MOD_RES 121 121 Phosphoserine.
{ECO:0000250|UniProtKB:Q16543}.
MOD_RES 155 155 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q16543}.
MOD_RES 378 378 Phosphoserine.
{ECO:0000250|UniProtKB:Q16543}.
CONFLICT 64 64 C -> F (in Ref. 1; BAA05618).
{ECO:0000305}.
CONFLICT 98 107 SWEQKLEDMR -> TGSRSWRTCG (in Ref. 1;
BAA05618). {ECO:0000305}.
CONFLICT 373 373 N -> F (in Ref. 1; BAA05618).
{ECO:0000305}.
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


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