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Showing Protein Heat shock cognate 71 kDa protein (HMDBP13799)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP13799
Secondary Accession Numbers None
Name Heat shock cognate 71 kDa protein
Synonyms
  1. Heat shock 70 kDa protein 8
  2. Lipopolysaccharide-associated protein 1
  3. LAP-1
  4. LPS-associated protein 1
Gene Name HSPA8
Protein Type Unknown
Biological Properties
General Function Not Available
Specific Function Molecular chaperone 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 (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488, PubMed:12526792). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488, PubMed:12526792). The affinity of HSP70 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 HSP70-associated 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 (PubMed:24318877, PubMed:27474739, PubMed:24121476, PubMed:26865365). Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 (PubMed:12526792). 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. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462). Interacts with VGF-derived peptide TLQP-21 (PubMed:28934328).
Pathways
  • Antigen processing and presentation
  • Endocytosis
  • Estrogen signaling pathway
  • Legionellosis
  • Lipid and atherosclerosis
  • Longevity regulating pathway - multiple species
  • MAPK signaling pathway
  • Measles
  • Prion disease
  • Protein processing in endoplasmic reticulum
  • Spliceosome
  • Toxoplasmosis
Reactions Not Available
GO Classification
Biological Process
cellular response to unfolded protein
regulation of postsynapse organization
chaperone cofactor-dependent protein refolding
protein refolding
neutrophil degranulation
regulation of mRNA stability
membrane organization
protein folding
ATP metabolic process
mRNA splicing, via spliceosome
regulation of protein stability
negative regulation of transcription, DNA-dependent
viral reproduction
cellular response to starvation
response to unfolded protein
cytokine-mediated signaling pathway
vesicle-mediated transport
regulation of protein-containing complex assembly
neurotransmitter secretion
chaperone-mediated autophagy
chaperone-mediated autophagy translocation complex disassembly
regulation of cell cycle
chaperone-mediated protein transport involved in chaperone-mediated autophagy
late endosomal microautophagy
post-Golgi vesicle-mediated transport
negative regulation of supramolecular fiber organization
positive regulation by host of viral genome replication
positive regulation of mRNA splicing, via spliceosome
protein targeting to lysosome involved in chaperone-mediated autophagy
regulation of cellular response to heat
regulation of protein complex stability
regulation of protein import
slow axonal transport
Cellular Component
cytosol
focal adhesion
cytoplasm
nucleolus
extracellular vesicular exosome
plasma membrane
dendrite
blood microparticle
perinuclear region of cytoplasm
nucleus
autophagosome
terminal button
nucleoplasm
spliceosomal complex
lysosomal lumen
melanosome
lysosome
ribonucleoprotein complex
extracellular region
glutamatergic synapse
presynaptic cytosol
extracellular space
late endosome
membrane
ficolin-1-rich granule lumen
lysosomal membrane
secretory granule lumen
chaperone complex
glycinergic synapse
lumenal side of lysosomal membrane
photoreceptor ribbon synapse
postsynaptic cytosol
postsynaptic specialization membrane
Prp19 complex
clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane
Molecular Function
protein folding chaperone
unfolded protein binding
ATP binding
C3HC4-type RING finger domain binding
G protein-coupled receptor binding
ubiquitin protein ligase binding
chaperone binding
phosphatidylserine binding
heat shock protein binding
RNA binding
cadherin binding
ATPase activity
enzyme binding
protein-macromolecule adaptor activity
clathrin-uncoating ATPase activity
MHC class II protein complex binding
misfolded protein binding
Cellular Location Not Available
Gene Properties
Chromosome Location Not Available
Locus Not Available
SNPs Not Available
Gene Sequence Not Available
Protein Properties
Number of Residues 646
Molecular Weight 70897.565
Theoretical pI 5.522
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P11142
UniProtKB/Swiss-Prot Entry Name HSP7C_HUMAN
PDB IDs
GenBank Gene ID Not Available
GeneCard ID Not Available
GenAtlas ID Not Available
HGNC ID Not Available
References
General References
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