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Protein Page:

DNAJC7 a co-chaperone protein that binds both Hsp70 and Hsp90 through its TPR domains. Its DnaJ domain stimulates ATP hydrolysis and polypeptide binding by Hsp70. Interacts with the proapoptotic and cell-cycle checkpoint protein Rad9. Rad9 transiently dissociates from Tpr2 following heat-shock or UV treatments. Note: This description may include information from UniProtKB.
Protein type: Chaperone
Chromosomal Location of Human Ortholog: 17q21.2
Cellular Component: cytoplasm; cytoskeleton; cytosol; extracellular exosome; membrane; nucleoplasm
Molecular Function: ATPase activator activity; heat shock protein binding; protein binding
Biological Process: positive regulation of ATPase activity; protein folding; regulation of cellular response to heat
Reference #:  Q99615 (UniProtKB)
Alt. Names/Synonyms: DJ11; DJC7; DnaJ (Hsp40) homolog, subfamily C, member 7; DnaJ homolog subfamily C member 7; DNAJC7; DNJC7; tetratricopeptide repeat domain 2; Tetratricopeptide repeat protein 2; TPR repeat protein 2; TPR2; TTC2
Gene Symbols: DNAJC7
Molecular weight: 56,441 Da
Basal Isoelectric point: 6.56  Predict pI for various phosphorylation states
Select Structure to View Below


Protein Structure Not Found.

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