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.
Protein type: Chaperone
Chromosomal Location of Human Ortholog: 13q12.12
Cellular Component:  axon; cell body fiber; cytoplasm; dendrite; mitochondrion; nucleus
Molecular Function:  chaperone binding; Hsp70 protein binding; proteasome binding
Biological Process:  negative regulation of inclusion body assembly; protein folding
Disease: Spastic Ataxia, Charlevoix-saguenay Type
Reference #:  Q9NZJ4 (UniProtKB)
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
Gene Symbols: SACS
Molecular weight: 521,126 Da
Basal Isoelectric point: 6.63  Predict pI for various phosphorylation states
Select Structure to View Below

SACS

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  cBioPortal  |  CCLE  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB