CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012683
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
 CDC37A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
45ERMEQFQKEKEELDRacetylation[1]
67KVAECQRKLKELEVAubiquitination[2]
69AECQRKLKELEVAEGubiquitination[2, 3]
78LEVAEGGKAELERLQacetylation[1]
101EERSWEQKLEEMRKKubiquitination[2, 4, 5]
110EEMRKKEKSMPWNVDubiquitination[3, 4, 5, 6]
121WNVDTLSKDGFSKSMubiquitination[2, 4, 5, 6]
126LSKDGFSKSMVNTKPubiquitination[3]
135MVNTKPEKTEEDSEEubiquitination[3]
154KHKTFVEKYEKQIKHacetylation[1]
157TFVEKYEKQIKHFGMubiquitination[2]
240CFRQFFTKIKTADRQacetylation[1]
260NDELEAFKERVRGRAubiquitination[3]
323MLQDAISKMDPTDAKubiquitination[3]
330KMDPTDAKYHMQRCIacetylation[1]
330KMDPTDAKYHMQRCIubiquitination[2, 4, 5, 6]
347GLWVPNSKASEAKEGubiquitination[2]
352NSKASEAKEGEEAGPubiquitination[3]
374VPKTGDEKDVSV***ubiquitination[3]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
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.
 MOD_RES 2 2 N-acetylvaline; in Hsp90 co-chaperone
 MOD_RES 13 13 Phosphoserine.
 MOD_RES 78 78 N6-acetyllysine.
 MOD_RES 154 154 N6-acetyllysine.
 MOD_RES 377 377 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Chaperone; Complete proteome; Cytoplasm; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 378 AA 
Protein Sequence
MVDYSVWDHI EVSDDEDETH PNIDTASLFR WRHQARVERM EQFQKEKEEL DRGCRECKRK 60
VAECQRKLKE LEVAEGGKAE LERLQAEAQQ LRKEERSWEQ KLEEMRKKEK SMPWNVDTLS 120
KDGFSKSMVN TKPEKTEEDS EEVREQKHKT FVEKYEKQIK HFGMLRRWDD SQKYLSDNVH 180
LVCEETANYL VIWCIDLEVE EKCALMEQVA HQTIVMQFIL ELAKSLKVDP RACFRQFFTK 240
IKTADRQYME GFNDELEAFK ERVRGRAKLR IEKAMKEYEE EERKKRLGPG GLDPVEVYES 300
LPEELQKCFD VKDVQMLQDA ISKMDPTDAK YHMQRCIDSG LWVPNSKASE AKEGEEAGPG 360
DPLLEAVPKT GDEKDVSV 378 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0043234; C:protein complex; IEA:Compara.
 GO:0032587; C:ruffle membrane; IEA:Compara.
 GO:0051082; F:unfolded protein binding; TAS:ProtInc.
 GO:0006605; P:protein targeting; TAS:ProtInc.
 GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
 GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; IMP:MGI.
 GO:0060338; P:regulation of type I interferon-mediated signaling pathway; IMP: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