Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00553
Entry Name
UniProt Accession
Theoretical PI
6.65
Molecular Weight
44868.18
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
DnaJ homolog subfamily A member 1
Protein Synonyms/Alias
DnaJ protein homolog 2; HSDJ; Heat shock 40 kDa protein 4; Heat shock protein J2; HSJ-2; Human DnaJ protein 2; hDj-2;
Gene Name
DNAJA1
Gene Synonyms/Alias
DNAJ2; HDJ2; HSJ2; HSPF4;
Created Date
01-JUL-1993
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
394
Canonical
HPRGGVQCQTS****
[1]
S-Farnesylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Kanazawa M, Terada K, Kato S, Mori M. HSDJ, a human homolog of DnaJ, isfarnesylated and is involved in protein import into mitochondria. J Biochem. 1997May;121(5):890-5.[PMID:9192730]
Functional Description
Co-chaperone for HSPA8/Hsc70 (PubMed:10816573). Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (PubMed:24318877). Plays a role in protein transport into mitochondria via its role as co- chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis (PubMed:14752510). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (PubMed:24512202).
Sequence Annotation
Domain: 6 68 J.
Metal binding site: 134 134 Zinc 1.
Metal binding site: 137 137 Zinc 1.
Metal binding site: 150 150 Zinc 2.
Metal binding site: 153 153 Zinc 2.
Metal binding site: 177 177 Zinc 2.
Metal binding site: 180 180 Zinc 2.
Metal binding site: 193 193 Zinc 1.
Metal binding site: 196 196 Zinc 1.
Modified residue: 66 66 N6-acetyllysine.
Modified residue: 83 83 Phosphoserine.
Modified residue: 335 335 Phosphoserine.
Modified residue: 381 381 Phosphotyrosine.
Modified residue: 394 394 Cysteine methyl ester.
Protein Length
397 AA.
Protein Sequence
(Canonical)
MVKETTYYDV LGVKPNATQE ELKKAYRKLA LKYHPDKNPN EGEKFKQISQ AYEVLSDAKK  60
RELYDKGGEQ AIKEGGAGGG FGSPMDIFDM FFGGGGRMQR ERRGKNVVHQ LSVTLEDLYN  120
GATRKLALQK NVICDKCEGR GGKKGAVECC PNCRGTGMQI RIHQIGPGMV QQIQSVCMEC  180
QGHGERISPK DRCKSCNGRK IVREKKILEV HIDKGMKDGQ KITFHGEGDQ EPGLEPGDII  240
IVLDQKDHAV FTRRGEDLFM CMDIQLVEAL CGFQKPISTL DNRTIVITSH PGQIVKHGDI  300
KCVLNEGMPI YRRPYEKGRL IIEFKVNFPE NGFLSPDKLS LLEKLLPERK EVEETDEMDQ  360
VELVDFDPNQ ERRRHYNGEA YEDDEHHPRG GVQCQTS                           397
FASTA
(Canonical)
>LipidDB-9606-00553|P31689
MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKK
RELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYN
GATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMEC
QGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDII
IVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDI
KCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQ
VELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS
Gene Ontology
GO:0098554; C:cytoplasmic side of endoplasmic reticulum membrane; TAS:ParkinsonsUK-UCL
GO:0005829; C:cytosol; IDA:UniProt
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0016020; C:membrane; IDA:UniProtKB
GO:0005739; C:mitochondrion; IEA:UniProtKB-KW
GO:0005634; C:nucleus; IEA:UniProtKB-KW
GO:0005524; F:ATP binding; IEA:InterPro
GO:0051087; F:chaperone binding; IDA:UniProtKB
GO:0001664; F:G-protein coupled receptor binding; IPI:ParkinsonsUK-UCL
GO:0030544; F:Hsp70 protein binding; IDA:UniProtKB
GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:MGI
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL
GO:0030521; P:androgen receptor signaling pathway; IEA:Ensembl
GO:0042769; P:DNA damage response, detection of DNA damage; IEA:Ensembl
GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB
GO:0043508; P:negative regulation of JUN kinase activity; IMP:UniProtKB
GO:0031397; P:negative regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL
GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB
GO:0006457; P:protein folding; TAS:ProtInc
GO:0070585; P:protein localization to mitochondrion; IMP:UniProtKB
GO:0051223; P:regulation of protein transport; IDA:UniProtKB
GO:0009408; P:response to heat; IEA:InterPro
GO:0006986; P:response to unfolded protein; TAS:ProtInc
GO:0030317; P:sperm motility; IEA:Ensembl
GO:0007283; P:spermatogenesis; IEA:Ensembl
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;