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SACS
Co-chaperone which acts as a regulator of the Hsp70 chaperone machinery and may be involved in the processing of other ataxia-linked proteins. Highly expressed in the central nervous system. Also found in skeletal muscle and at low levels in pancreas. 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: 13q12.12 |
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Cellular Component:
axon; cell body fiber; cytoplasm; dendrite; mitochondrion; nucleus
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Molecular Function:
chaperone binding; Hsp70 protein binding; proteasome binding
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Biological Process:
negative regulation of inclusion body assembly; protein folding
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Disease: Spastic Ataxia, Charlevoix-saguenay Type
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Reference #:
Q9NZJ4
(UniProtKB)
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Alt. Names/Synonyms: ARSACS; DKFZp686B15167; DnaJ homolog subfamily C member 29; DNAJC29; KIAA0730; PPP1R138; protein phosphatase 1, regulatory subunit 138; SACS; Sacsin; sacsin molecular chaperone; spastic ataxia of Charlevoix-Saguenay (sacsin); SPAX6
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Gene Symbols: SACS
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Molecular weight:
521,126 Da
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Basal Isoelectric point:
6.63
Predict pI for various phosphorylation states
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