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HSC70 iso2
a molecular chaperone of the heat shock protein 70 family implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1. Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1. Interacts with VGF-derived peptide TLQP-21. Belongs to the heat shock protein 70 family. Ubiquitous. 2 alternatively spliced human isoforms have been reported. Note: This description may include information from UniProtKB.
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| Protein type: Chaperone; Heat shock protein; Nucleolus; RNA-binding |
| Chromosomal Location of human Ortholog: 11q24.1 |
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Cellular Component:
autophagosome; clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; cytoplasm; cytosol; dendrite; extracellular exosome; extracellular region; ficolin-1-rich granule lumen; glutamatergic synapse; glycinergic synapse; late endosome; lumenal side of lysosomal membrane; lysosomal lumen; lysosomal membrane; lysosome; melanosome; nucleolus; nucleoplasm; nucleus; perinuclear region of cytoplasm; photoreceptor ribbon synapse; plasma membrane; postsynaptic cytosol; postsynaptic specialization membrane; presynaptic cytosol; protein folding chaperone complex; Prp19 complex; ribonucleoprotein complex; secretory granule lumen; spliceosomal complex; terminal bouton
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Molecular Function:
ATP binding; ATP hydrolysis activity; ATP-dependent protein disaggregase activity; ATP-dependent protein folding chaperone; C3HC4-type RING finger domain binding; clathrin-uncoating ATPase activity; enzyme binding; G protein-coupled receptor binding; heat shock protein binding; phosphatidylserine binding; protein binding; protein carrier chaperone; protein folding chaperone; protein-folding chaperone binding; protein-macromolecule adaptor activity; ubiquitin protein ligase binding; unfolded protein binding
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Biological Process:
ATP metabolic process; cellular response to starvation; cellular response to steroid hormone stimulus; chaperone cofactor-dependent protein refolding; chaperone-mediated autophagy; chaperone-mediated autophagy translocation complex disassembly; clathrin coat disassembly; late endosomal microautophagy; membrane organization; mRNA splicing, via spliceosome; negative regulation of DNA-templated transcription; negative regulation of NLRP3 inflammasome complex assembly; negative regulation of supramolecular fiber organization; positive regulation by host of viral genome replication; positive regulation of mRNA splicing, via spliceosome; protein folding; protein refolding; protein targeting to lysosome involved in chaperone-mediated autophagy; regulation of cell cycle; regulation of postsynapse organization; regulation of protein complex stability; regulation of protein import; regulation of protein stability; regulation of protein-containing complex assembly; response to unfolded protein; slow axonal transport
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Reference #:
P11142-2
(UniProtKB)
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Alt. Names/Synonyms: constitutive heat shock protein 70; epididymis luminal protein 33; epididymis secretory sperm binding protein Li 72p; Heat shock 70 kDa protein 8; heat shock 70kd protein 10; heat shock 70kDa protein 8; Heat shock cognate 71 kDa protein; heat shock cognate protein 54; heat shock protein family A (Hsp70) member 8; HEL-33; HEL-S-72p; HSC54; HSC70; HSC70 iso2; HSC71; HSP71; HSP73; HSP7C; HSPA10; HSPA8; LAP-1; LAP1; Lipopolysaccharide-associated protein 1; LPS-associated protein 1; N-myristoyltransferase inhibitor protein 71; NIP71
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Gene Symbols: HSPA8
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Molecular weight:
53,518 Da
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Basal Isoelectric point:
5.62
Predict pI for various phosphorylation states
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