Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00106
Entry Name
UniProt Accession
Theoretical PI
6.06
Molecular Weight
45745.6
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
DnaJ homolog subfamily A member 2
Protein Synonyms/Alias
Cell cycle progression restoration gene 3 protein; Dnj3; Dj3; HIRA-interacting protein 4; Renal carcinoma antigen NY-REN-14;
Gene Name
DNAJA2
Gene Synonyms/Alias
CPR3; HIRIP4;
Created Date
11-JUL-2001
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
409
Canonical
HHGPGVQCAHQ****
[1]
S-Farnesylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Kho Y, Kim SC, Jiang C, Barma D, Kwon SW, Cheng J, Jaunbergs J, Weinbaum C,Tamanoi F, Falck J, Zhao Y. A tagging-via-substrate technology for detection and proteomics of farnesylated proteins. Proc Natl Acad Sci U S A. 2004 Aug24;101(34):12479-84. Epub 2004 Aug 12.[PMID:15308774]
Functional Description
Co-chaperone of Hsc70.
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 LLQEKEHEVF QRDGNDLHMT YKIGLVEALC GFQFTFKHLD GRQIVVKYPP  300
GKVIEPGCVR VVRGEGMPQY RNPFEKGDLY IKFDVQFPEN NWINPDKLSE LEDLLPSRPE  360
VPNIIGETEE VELQEFDSTR GSGGGQRREA YNDSSDEESS SHHGPGVQCA HQ          412
FASTA
(Canonical)
>LipidDB-9606-00106|O60884
MANVADTKLYDILGVPPGASENELKKAYRKLAKEYHPDKNPNAGDKFKEISFAYEVLSNP
EKRELYDRYGEQGLREGSGGGGGMDDIFSHIFGGGLFGFMGNQSRSRNGRRRGEDMMHPL
KVSLEDLYNGKTTKLQLSKNVLCSACSGQGGKSGAVQKCSACRGRGVRIMIRQLAPGMVQ
QMQSVCSDCNGEGEVINEKDRCKKCEGKKVIKEVKILEVHVDKGMKHGQRITFTGEADQA
PGVEPGDIVLLLQEKEHEVFQRDGNDLHMTYKIGLVEALCGFQFTFKHLDGRQIVVKYPP
GKVIEPGCVRVVRGEGMPQYRNPFEKGDLYIKFDVQFPENNWINPDKLSELEDLLPSRPE
VPNIIGETEEVELQEFDSTRGSGGGQRREAYNDSSDEESSSHHGPGVQCAHQ
Gene Ontology
GO:0005829; C:cytosol; IDA:UniProt
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0005524; F:ATP binding; IEA:InterPro
GO:0051087; F:chaperone binding; IPI:UniProt
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0051082; F:unfolded protein binding; IDA:UniProt
GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc
GO:0042026; P:protein refolding; IDA:UniProt
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;