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Identification
HMDB Protein ID HMDBP14535
Secondary Accession Numbers None
Name Heat shock 70 kDa protein 1A
Synonyms
  1. Heat shock 70 kDa protein 1
  2. HSP70-1
  3. HSP70.1
Gene Name HSPA1A
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. 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. It 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 such as 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:24012426, PubMed:26865365, PubMed:24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed:27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed:27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed:24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed:23973223). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response (PubMed:9499401). Involved in the clearance of misfolded PRDM1/Blimp-1 proteins. Sequesters them in the cytoplasm and promotes their association with SYNV1/HRD1, leading to proteasomal degradation (PubMed:28842558).(Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.
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
chaperone cofactor-dependent protein refolding
protein refolding
positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway
neutrophil degranulation
positive regulation of interleukin-8 production
regulation of mRNA stability
negative regulation of protein ubiquitination
positive regulation of proteasomal ubiquitin-dependent protein catabolic process
negative regulation of apoptotic process
cellular heat acclimation
negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway
negative regulation of inclusion body assembly
negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway
negative regulation of transcription from RNA polymerase II promoter in response to stress
positive regulation of endoribonuclease activity
positive regulation of microtubule nucleation
positive regulation of RNA splicing
regulation of mitotic spindle assembly
protein stabilization
ATP metabolic process
chaperone-mediated protein complex assembly
regulation of protein ubiquitination
positive regulation of tumor necrosis factor-mediated signaling pathway
response to unfolded protein
negative regulation of cell growth
vesicle-mediated transport
negative regulation of transforming growth factor beta receptor signaling pathway
negative regulation of extrinsic apoptotic signaling pathway in absence of ligand
positive regulation of erythrocyte differentiation
negative regulation of cell proliferation
positive regulation of gene expression
negative regulation of cell death
positive regulation of NF-kappaB transcription factor activity
mRNA catabolic process
cellular response to heat
cellular response to oxidative stress
regulation of cellular response to heat
lysosomal transport
Cellular Component
cytosol
centrosome
protein-containing complex
focal adhesion
cytoplasm
centriole
endoplasmic reticulum
mitochondrion
extracellular vesicular exosome
plasma membrane
blood microparticle
perinuclear region of cytoplasm
aggresome
nucleus
nucleoplasm
nuclear speck
vesicle
ribonucleoprotein complex
extracellular region
inclusion body
ficolin-1-rich granule lumen
Molecular Function
protein folding chaperone
protein N-terminus binding
viral receptor activity
unfolded protein binding
denatured protein binding
histone deacetylase binding
ATP binding
C3HC4-type RING finger domain binding
G protein-coupled receptor binding
ubiquitin protein ligase binding
receptor binding
disordered domain specific binding
heat shock protein binding
RNA binding
cadherin binding
ATPase activity
enzyme binding
transcription corepressor activity
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 641
Molecular Weight 70051.65
Theoretical pI 5.652
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence Not Available
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P0DMV8
UniProtKB/Swiss-Prot Entry Name HS71A_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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