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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.
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| Protein type: Chaperone |
| Chromosomal Location of Human Ortholog: 17q21.2 |
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Cellular Component:
cytoplasm; cytoskeleton; cytosol; nucleoplasm
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Molecular Function:
heat shock protein binding; protein binding
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Biological Process:
chaperone cofactor-dependent protein refolding; protein folding; regulation of cellular response to heat
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Reference #:
Q99615
(UniProtKB)
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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
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Gene Symbols: DNAJC7
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Molecular weight:
56,441 Da
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Basal Isoelectric point:
6.56
Predict pI for various phosphorylation states
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