DNAJC7 Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to the cytoplasm. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
Protein type: Chaperone
Chromosomal Location of Human Ortholog: 17q21.2
Cellular Component:  cytoplasm; cytoskeleton; cytosol; nucleoplasm
Molecular Function:  heat shock protein binding; protein binding
Biological Process:  chaperone cofactor-dependent protein refolding; protein folding; regulation of cellular response to heat
Reference #:  Q99615 (UniProtKB)
Alt. Names/Synonyms: DJ11; DJC7; DnaJ (Hsp40) homolog, subfamily C, member 7; DnaJ heat shock protein family (Hsp40) member C7; 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
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DNAJC7

Protein Structure Not Found.

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