UniProt Accession

 CDC37_MOUSE; Q61081; Q3TGP0 

Genbank Protein ID

 U43076; AK010494; AK013255; AK145671; AK168651; BC060079 

Genbank Nucleotide ID

 AAB18761.1; BAB26984.1; BAB28749.1; BAE26580.1; BAE40508.1; AAH60079.1 

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

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
69	AECQRKLKELEVAES	ubiquitination	[1]
102	EERSWEQKLEDMRKK	acetylation	[2]
111	EDMRKKEKNMPWNVD	acetylation	[2, 3]
122	WNVDTLSKDGFSKSM	acetylation	[3]
133	SKSMVNTKPEKAEED	acetylation	[3]
254	HQYMEGFKYELEAFK	acetylation	[2, 4]
261	KYELEAFKERVRGRA	acetylation	[2]
331	KMDPTDAKYHMQRCI	acetylation	[2]
331	KMDPTDAKYHMQRCI	ubiquitination	[1]
348	GLWVPNSKSGEAKEG	ubiquitination	[1]

Reference

 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

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

Gene Ontology

 GO:0005829; C:cytosol; IDA:MGI.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0032587; C:ruffle membrane; IEA:Compara.
 GO:0051879; F:Hsp90 protein binding; IDA:MGI.
 GO:0051726; P:regulation of cell cycle; IEA:Compara.
 GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; ISO:MGI.
 GO:0060338; P:regulation of type I interferon-mediated signaling pathway; ISO:MGI. 

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