CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014540
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Hsp90 co-chaperone Cdc37 
Protein Synonyms/Alias
 Hsp90 chaperone protein kinase-targeting subunit; p50Cdc37; Hsp90 co-chaperone Cdc37, N-terminally processed 
Gene Name
 Cdc37 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
155KHKTFVEKYEKQIKHacetylation[1]
158TFVEKYEKQIKHFGMacetylation[1]
161EKYEKQIKHFGMLHRacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. 
Sequence Annotation
 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 2 2 N-acetylvaline; in Hsp90 co-chaperone
 MOD_RES 13 13 Phosphoserine (By similarity).
 MOD_RES 155 155 N6-acetyllysine (By similarity).
 MOD_RES 378 378 Phosphoserine (By similarity).  
Keyword
 Acetylation; Chaperone; Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 379 AA 
Protein Sequence
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK 60
VAECQRKLKE LEVAEGGGQV ELERLRAEAQ QLRKEERSWE QKLEDMRKKE KNMPWNVDTL 120
SKDGFSKSMV NTKPEKAEED SEEAREQKHK TFVEKYEKQI KHFGMLHRWD DSQKYLSDNV 180
HLVCEETANY LVIWCIDLEV EEKCALMEQV AHQTMVMQFI LELAKSLKVD PRACFRQFFT 240
KIKTADQQYM EGFKYELEAF KERVRGRAKL RIEKAMKEYE EEERKKRLGP GGLDPVEVYE 300
SLPEELQKCF DVKDVQMLQD AISKMDPTDA KYHMQRCIDS GLWVPNSKSG EAKEGEEAGP 360
GDPLLEAVPK AGNEKDISA 379 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:RGD.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0043234; C:protein complex; IDA:RGD.
 GO:0032587; C:ruffle membrane; IDA:RGD.
 GO:0051726; P:regulation of cell cycle; IEP:RGD.
 GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; IEA:Compara.
 GO:0060338; P:regulation of type I interferon-mediated signaling pathway; IEA:Compara. 
Interpro
 IPR004918; Cdc37.
 IPR013873; Cdc37_C.
 IPR013874; Cdc37_Hsp90-bd.
 IPR013855; Cdc37_N_dom. 
Pfam
 PF08564; CDC37_C
 PF08565; CDC37_M
 PF03234; CDC37_N 
SMART
 SM01069; CDC37_C
 SM01070; CDC37_M
 SM01071; CDC37_N 
PROSITE
  
PRINTS