CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000627
UniProt Accession
Genbank Protein ID
 U95727 
Genbank Nucleotide ID
Protein Name
 DnaJ homolog subfamily A member 2 
Protein Synonyms/Alias
 RDJ2 
Gene Name
 Dnaja2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
25GASENELKKAYRKLAacetylation[1]
62EVLSNPEKRELYDRYubiquitination[2]
326QYRNPFEKGDLYIKFacetylation[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]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113
Functional Description
  
Sequence Annotation
 DOMAIN 8 70 J.
 REPEAT 143 150 CXXCXGXG motif.
 REPEAT 159 166 CXXCXGXG motif.
 REPEAT 186 193 CXXCXGXG motif.
 REPEAT 202 209 CXXCXGXG motif.
 ZN_FING 130 214 CR-type.
 METAL 143 143 Zinc 1 (By similarity).
 METAL 146 146 Zinc 1 (By similarity).
 METAL 159 159 Zinc 2 (By similarity).
 METAL 162 162 Zinc 2 (By similarity).
 METAL 186 186 Zinc 2 (By similarity).
 METAL 189 189 Zinc 2 (By similarity).
 METAL 202 202 Zinc 1 (By similarity).
 METAL 205 205 Zinc 1 (By similarity).
 MOD_RES 78 78 Phosphoserine (By similarity).
 MOD_RES 409 409 Cysteine methyl ester (By similarity).
 LIPID 409 409 S-farnesyl cysteine (By similarity).  
Keyword
 Chaperone; Complete proteome; Lipoprotein; Membrane; Metal-binding; Methylation; Phosphoprotein; Prenylation; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 412 AA 
Protein Sequence
MANVADTKLY DILGVPPGAS ENELKKAYRK LAKEYHPDKN PNAGDKFKEI SFAYEVLSNP 60
EKRELYDRYG EQGLREGSGG GGGMDDIFSH IFGGGLFGFM GNQSRSRNGR RRGEDMMHPL 120
KVSLEDLYNG KTTKLQLSKN VLCSACSGQG GKSGAVQKCS ACRGRGVRIM IRQLAPGMVQ 180
QMQSVCSDCN GEGEVINEKD RCKKCEGKKV IKEVKILEVH VDKGMKHGQR ITFTGEADQA 240
PGVEPGDIVL FVQEKEHEVF QRDGNDLHMT YKIGLVEALC GFQFTFKHLD ARQIVVKYPP 300
GKVIEPGCVR VVRGEGMPQY RNPFEKGDLY IKFDVQFPEN NWINPDKLSE LEDLLPSRPE 360
VPNVIGETEE VELQEFDSTR GSGGGQRREA YNDSSDEESS SHHGPGVQCA HQ 412 
Gene Ontology
 GO:0005829; C:cytosol; IDA:RGD.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:RGD.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0018885; P:carbon tetrachloride metabolic process; IEP:RGD.
 GO:0006457; P:protein folding; IEA:InterPro.
 GO:0009408; P:response to heat; IEA:InterPro. 
Interpro
 IPR012724; DnaJ.
 IPR002939; DnaJ_C.
 IPR001623; DnaJ_domain.
 IPR018253; DnaJ_domain_CS.
 IPR008971; HSP40/DnaJ_pept-bd.
 IPR001305; HSP_DnaJ_Cys-rich_dom. 
Pfam
 PF00226; DnaJ
 PF01556; DnaJ_C
 PF00684; DnaJ_CXXCXGXG 
SMART
 SM00271; DnaJ 
PROSITE
 PS00636; DNAJ_1
 PS50076; DNAJ_2
 PS51188; ZF_CR 
PRINTS
 PR00625; JDOMAIN.