DnaJ homolog subfamily A member 1; heat shock 40 kD protein 4; DnaJ protein homolog 2; HDJ-2; HSJ-2; HSDJ (DNAJA1 DNAJ2 HDJ2 HSJ2 HSPF4)
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Function
- interacts with Hsp70 through its J domain
- co-chaperone of Hsc70
- may diminish protein aggregation[3]
- over-expression reduces ischemic injury in vivo[3]
- seems to play a role in protein import into mitochondria
Structure
- contains 1 CR-type Zn+2 finger
- contains 1 J domain
Compartment
membrane; lipid-anchor (farnesyl)
More general terms
References
- ↑ Martinus RD et al Role of chaperones in the biogenesis and maintenance of the mitochondrion. FASEB J 9:371 1995 PMID: https://www.ncbi.nlm.nih.gov/pubmed/7896006
- ↑ prosite :accession {PS00636 PS00637}
- ↑ 3.0 3.1 3.2 Giffard RG, Xu L, Zhao H, Carrico W, Ouyang Y, Qiao Y, Sapolsky R, Steinberg G, Hu B, Yenari MA. Chaperones, protein aggregation, and brain protection from hypoxic/ischemic injury. J Exp Biol. 2004 Aug;207(Pt 18):3213-20. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/15299042
- ↑ UniProt http://www.uniprot.org/uniprot/P31689.html