CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021353
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 DnaJ homolog subfamily C member 5 
Protein Synonyms/Alias
 Cysteine string protein; CSP 
Gene Name
 DNAJC5 
Gene Synonyms/Alias
 CSP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
41SYRKLALKYHPDKNPubiquitination[1, 2]
46ALKYHPDKNPDNPEAubiquitination[1]
56DNPEAADKFKEINNAacetylation[3]
56DNPEAADKFKEINNAubiquitination[4, 5]
58PEAADKFKEINNAHAubiquitination[4, 5]
72AILTDATKRNIYDKYubiquitination[1, 2, 6, 7]
Reference
 [1] 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]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] 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]
 [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] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
 May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity). 
Sequence Annotation
 DOMAIN 13 82 J.
 MOD_RES 8 8 Phosphoserine.
 MOD_RES 10 10 Phosphoserine.
 MOD_RES 11 11 Phosphothreonine (By similarity).
 MOD_RES 12 12 Phosphoserine (By similarity).
 MOD_RES 15 15 Phosphoserine.
 MOD_RES 17 17 Phosphotyrosine (By similarity).
 MOD_RES 56 56 N6-acetyllysine.  
Keyword
 Acetylation; Alternative splicing; Cell membrane; Chaperone; Complete proteome; Disease mutation; Lipoprotein; Membrane; Neurodegeneration; Neuronal ceroid lipofuscinosis; Palmitate; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 198 AA 
Protein Sequence
MADQRQRSLS TSGESLYHVL GLDKNATSDD IKKSYRKLAL KYHPDKNPDN PEAADKFKEI 60
NNAHAILTDA TKRNIYDKYG SLGLYVAEQF GEENVNTYFV LSSWWAKALF VFCGLLTCCY 120
CCCCLCCCFN CCCGKCKPKA PEGEETEFYV SPEDLEAQLQ SDEREATDTP IVIQPASATE 180
TTQLTADSHP SYHTDGFN 198 
Gene Ontology
 GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:UniProtKB.
 GO:0008021; C:synaptic vesicle; IEA:Compara.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Compara.
 GO:0007269; P:neurotransmitter secretion; TAS:Reactome. 
Interpro
 IPR001623; DnaJ_domain.
 IPR018253; DnaJ_domain_CS. 
Pfam
 PF00226; DnaJ 
SMART
 SM00271; DnaJ 
PROSITE
 PS00636; DNAJ_1
 PS50076; DNAJ_2 
PRINTS
 PR00625; JDOMAIN.