HSP105 a molecular chaperone of the heat shock protein 70 family. Has ATPase activity. Expressed at especially high levels in mammalian brain and has been shown to suppress apoptosis in neuronal cells and to prevent the aggregation of proteins following heat shock. Known to interact with a variety of proteins including alpha-tubulin and the androgen receptor. Two alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Chaperone; Heat shock protein
Chromosomal Location of Human Ortholog: 5 G3|5 89.18 cM
Cellular Component:  cytoplasm; cytosol; extracellular region; nucleoplasm; nucleus; protein-containing complex
Molecular Function:  adenyl-nucleotide exchange factor activity; alpha-tubulin binding; ATP binding; nucleotide binding; protein binding
Biological Process:  chaperone cofactor-dependent protein refolding; negative regulation of apoptotic signaling pathway; negative regulation of establishment of protein localization to mitochondrion; negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide; negative regulation of neuron apoptotic process; negative regulation of p38MAPK cascade; positive regulation of MHC class I biosynthetic process; positive regulation of NK T cell activation; positive regulation of protein tyrosine kinase activity; positive regulation of transcription by RNA polymerase II; regulation of microtubule cytoskeleton organization; response to unfolded protein
Reference #:  Q61699 (UniProtKB)
Alt. Names/Synonyms: 105kDa; 42 degrees C-HSP; AI790491; heat shock 105kDa/110kDa protein 1; Heat shock 110 kDa protein; Heat shock protein 105 kDa; heat shock protein 110; heat shock protein, 105 kDa; Heat shock-related 100 kDa protein E7I; HS105; HSP-E7I; Hsp105; HSP105 42 C-HSP; Hsp110; Hsph1; Kiaa0201; OTTMUSP00000023701; OTTMUSP00000023705
Gene Symbols: Hsph1
Molecular weight: 96,407 Da
Basal Isoelectric point: 5.39  Predict pI for various phosphorylation states
Select Structure to View Below


Protein Structure Not Found.

Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene