Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10116-01173
Entry Name
UniProt Accession
Theoretical PI
6.06
Molecular Weight
45765.59
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
DnaJ homolog subfamily A member 2
Protein Synonyms/Alias
RDJ2;
Gene Name
Dnaja2
Gene Synonyms/Alias
Created Date
11-JUL-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
409
Canonical
HHGPGVQCAHQ****
[1]
S-Farnesylation
Organism
Rattus norvegicus (Rat)
NCBI Taxa ID
10116
Reference
[1] Andres DA, Shao H, Crick DC, Finlin BS. Expression cloning of a novelfarnesylated protein, RDJ2, encoding a DnaJ protein homologue. Arch BiochemBiophys. 1997 Oct 1;346(1):113-24.[PMID:9328291]
Functional Description
Sequence Annotation
Domain: 8 70 J.
Metal binding site: 143 143 Zinc 1.
Metal binding site: 146 146 Zinc 1.
Metal binding site: 159 159 Zinc 2.
Metal binding site: 162 162 Zinc 2.
Metal binding site: 186 186 Zinc 2.
Metal binding site: 189 189 Zinc 2.
Metal binding site: 202 202 Zinc 1.
Metal binding site: 205 205 Zinc 1.
Modified residue: 39 39 N6-acetyllysine.
Modified residue: 78 78 Phosphoserine.
Modified residue: 152 152 N6-acetyllysine.
Modified residue: 409 409 Cysteine methyl ester.
Protein Length
412 AA.
Protein Sequence
(Canonical)
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
FASTA
(Canonical)
>LipidDB-10116-01173|O35824
MANVADTKLYDILGVPPGASENELKKAYRKLAKEYHPDKNPNAGDKFKEISFAYEVLSNP
EKRELYDRYGEQGLREGSGGGGGMDDIFSHIFGGGLFGFMGNQSRSRNGRRRGEDMMHPL
KVSLEDLYNGKTTKLQLSKNVLCSACSGQGGKSGAVQKCSACRGRGVRIMIRQLAPGMVQ
QMQSVCSDCNGEGEVINEKDRCKKCEGKKVIKEVKILEVHVDKGMKHGQRITFTGEADQA
PGVEPGDIVLFVQEKEHEVFQRDGNDLHMTYKIGLVEALCGFQFTFKHLDARQIVVKYPP
GKVIEPGCVRVVRGEGMPQYRNPFEKGDLYIKFDVQFPENNWINPDKLSELEDLLPSRPE
VPNVIGETEEVELQEFDSTRGSGGGQRREAYNDSSDEESSSHHGPGVQCAHQ
Gene Ontology
GO:0005829; C:cytosol; IDA:RGD
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0005634; C:nucleus; IDA:RGD
GO:0005524; F:ATP binding; IEA:InterPro
GO:0001948; F:glycoprotein binding; IPI:RGD
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
InterPro; IPR012724; DnaJ
InterPro; IPR002939; DnaJ_C
InterPro; IPR001623; DnaJ_domain
InterPro; IPR018253; DnaJ_domain_CS
InterPro; IPR008971; HSP40/DnaJ_pept-bd
InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom
Pfam
Pfam; PF01556; CTDII;
Pfam; PF00226; DnaJ;
Pfam; PF00684; DnaJ_CXXCXGXG;
SMART
SMART; SM00271; DnaJ;
PROSITE
PROSITE; PS00636; DNAJ_1;
PROSITE; PS50076; DNAJ_2;
PROSITE; PS51188; ZF_CR;
PRINTS
PRINTS; PR00625; JDOMAIN;