HSPA8 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0006986Biological processresponse to unfolded protein
GO_1990834Biological processresponse to odorant
GO_0044829Biological processpositive regulation by host of viral genome replication
GO_0061635Biological processregulation of protein complex stability
GO_0046034Biological processATP metabolic process
GO_0014823Biological processresponse to activity
GO_0009267Biological processcellular response to starvation
GO_0001916Biological processpositive regulation of T cell mediated cytotoxicity
GO_0021549Biological processcerebellum development
GO_0009410Biological processresponse to xenobiotic stimulus
GO_0051085Biological processchaperone cofactor-dependent protein refolding
GO_0051726Biological processregulation of cell cycle
GO_0070301Biological processcellular response to hydrogen peroxide
GO_0007519Biological processskeletal muscle tissue development
GO_1902904Biological processnegative regulation of supramolecular fiber organization
GO_0045862Biological processpositive regulation of proteolysis
GO_0030900Biological processforebrain development
GO_0071383Biological processcellular response to steroid hormone stimulus
GO_0071276Biological processcellular response to cadmium ion
GO_0001822Biological processkidney development
GO_0061738Biological processlate endosomal microautophagy
GO_0000398Biological processmRNA splicing, via spliceosome
GO_0061684Biological processchaperone-mediated autophagy
GO_0006606Biological processprotein import into nucleus
GO_0098880Biological processmaintenance of postsynaptic specialization structure
GO_0010667Biological processnegative regulation of cardiac muscle cell apoptotic process
GO_0044743Biological processprotein transmembrane import into intracellular organelle
GO_0044849Biological processestrous cycle
GO_0032355Biological processresponse to estradiol
GO_1904589Biological processregulation of protein import
GO_1904592Biological processpositive regulation of protein refolding
GO_1900226Biological processnegative regulation of NLRP3 inflammasome complex assembly
GO_1990832Biological processslow axonal transport
GO_0048026Biological processpositive regulation of mRNA splicing, via spliceosome
GO_0045471Biological processresponse to ethanol
GO_0072318Biological processclathrin coat disassembly
GO_0043254Biological processregulation of protein-containing complex assembly
GO_0010045Biological processresponse to nickel cation
GO_0097214Biological processpositive regulation of lysosomal membrane permeability
GO_0045892Biological processnegative regulation of DNA-templated transcription
GO_0032570Biological processresponse to progesterone
GO_0000082Biological processG1/S transition of mitotic cell cycle
GO_0050766Biological processpositive regulation of phagocytosis
GO_0016191Biological processsynaptic vesicle uncoating
GO_0034605Biological processcellular response to heat
GO_0061024Biological processmembrane organization
GO_0006457Biological processprotein folding
GO_0061740Biological processprotein targeting to lysosome involved in chaperone-mediated autophagy
GO_0042026Biological processprotein refolding
GO_1904764Biological processchaperone-mediated autophagy translocation complex disassembly
GO_0031647Biological processregulation of protein stability
GO_0099175Biological processregulation of postsynapse organization
GO_0098978Cellular componentglutamatergic synapse
GO_0061202Cellular componentclathrin-sculpted gamma-aminobutyric acid transport vesicle membrane
GO_0043195Cellular componentterminal bouton
GO_0000974Cellular componentPrp19 complex
GO_0009986Cellular componentcell surface
GO_1904813Cellular componentficolin-1-rich granule lumen
GO_0098684Cellular componentphotoreceptor ribbon synapse
GO_0008021Cellular componentsynaptic vesicle
GO_0043202Cellular componentlysosomal lumen
GO_0099634Cellular componentpostsynaptic specialization membrane
GO_0005634Cellular componentnucleus
GO_0005730Cellular componentnucleolus
GO_0005576Cellular componentextracellular region
GO_0098690Cellular componentglycinergic synapse
GO_0070062Cellular componentextracellular exosome
GO_0005654Cellular componentnucleoplasm
GO_0005882Cellular componentintermediate filament
GO_0005770Cellular componentlate endosome
GO_1990904Cellular componentribonucleoprotein complex
GO_0005615Cellular componentextracellular space
GO_0005886Cellular componentplasma membrane
GO_0005874Cellular componentmicrotubule
GO_0098575Cellular componentlumenal side of lysosomal membrane
GO_0016020Cellular componentmembrane
GO_0043198Cellular componentdendritic shaft
GO_0043204Cellular componentperikaryon
GO_0034774Cellular componentsecretory granule lumen
GO_0072562Cellular componentblood microparticle
GO_0014069Cellular componentpostsynaptic density
GO_0099524Cellular componentpostsynaptic cytosol
GO_0005776Cellular componentautophagosome
GO_0005737Cellular componentcytoplasm
GO_0005765Cellular componentlysosomal membrane
GO_0043197Cellular componentdendritic spine
GO_0005681Cellular componentspliceosomal complex
GO_0048471Cellular componentperinuclear region of cytoplasm
GO_0001917Cellular componentphotoreceptor inner segment
GO_1990836Cellular componentlysosomal matrix
GO_0005925Cellular componentfocal adhesion
GO_0101031Cellular componentprotein folding chaperone complex
GO_0005829Cellular componentcytosol
GO_0099523Cellular componentpresynaptic cytosol
GO_0042470Cellular componentmelanosome
GO_1990833Molecular functionclathrin-uncoating ATPase activity
GO_0031625Molecular functionubiquitin protein ligase binding
GO_0031686Molecular functionA1 adenosine receptor binding
GO_0001664Molecular functionG protein-coupled receptor binding
GO_0005524Molecular functionATP binding
GO_0140545Molecular functionATP-dependent protein disaggregase activity
GO_0044183Molecular functionprotein folding chaperone
GO_0051082Molecular functionunfolded protein binding
GO_0140597Molecular functionprotein carrier chaperone
GO_0023026Molecular functionMHC class II protein complex binding
GO_0019899Molecular functionenzyme binding
GO_0043531Molecular functionADP binding
GO_1904593Molecular functionprostaglandin binding
GO_0055131Molecular functionC3HC4-type RING finger domain binding
GO_0042277Molecular functionpeptide binding
GO_0031072Molecular functionheat shock protein binding
GO_0001786Molecular functionphosphatidylserine binding
GO_0051087Molecular functionprotein-folding chaperone binding
GO_0030674Molecular functionprotein-macromolecule adaptor activity
GO_0003723Molecular functionRNA binding
GO_0005515Molecular functionprotein binding
GO_0045296Molecular functioncadherin binding
GO_0140662Molecular functionATP-dependent protein folding chaperone
GO_0016887Molecular functionATP hydrolysis activity

IV. Literature review

[source]
Gene nameHSPA8
Protein nameHeat shock cognate 71 kDa protein (EC 3.6.4.10) (Heat shock 70 kDa protein 8) (Lipopolysaccharide-associated protein 1) (LAP-1) (LPS-associated protein 1)
Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8)
SynonymsHSC70
hCG_2032950
HSPA10
HEL-S-72p
HEL-33
HSP73
DescriptionFUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, chaperone-mediated autophagy, activation of proteolysis of misfolded proteins, formation and dissociation of protein complexes, and antigen presentation. 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 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 . 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 . Plays a critical role in mitochondrial import, delivers preproteins to the mitochondrial import receptor TOMM70 . 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 . Substrate recognition component in chaperone-mediated autophagy (CMA), a selective protein degradation process that mediates degradation of proteins with a -KFERQ motif: HSPA8/HSC70 specifically recognizes and binds cytosolic proteins bearing a -KFERQ motif and promotes their recruitment to the surface of the lysosome where they bind to lysosomal protein LAMP2 . KFERQ motif-containing proteins are eventually transported into the lysosomal lumen where they are degraded . In conjunction with LAMP2, facilitates MHC class II presentation of cytoplasmic antigens by guiding antigens to the lysosomal membrane for interaction with LAMP2 which then elicits MHC class II presentation of peptides to the cell membrane . Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 . It is recruited to clathrin-coated vesicles through its interaction with DNAJC6 leading to activation of HSPA8/HSC70 ATPase activity and therefore uncoating of clathrin-coated vesicles (By similarity). .

AccessionsENST00000453788.6 [P11142-2]
ENST00000534319.5
E9PN89
ENST00000532636.5 [P11142-1]
ENST00000528292.5
E9PQQ4
Q96H53
E9PN25
ENST00000533540.5
ENST00000525463.5
ENST00000526110.5
E9PQK7
ENST00000525624.5
ENST00000530391.1
E9PM13
ENST00000527387.5
E9PPY6
P11142
ENST00000532182.5
ENST00000227378.7 [P11142-1]
E9PNE6
ENST00000526686.1
A8K7Q2
E9PK54
E9PS65
ENST00000524552.5
V9HW22
ENST00000524590.5
E9PKE3
ENST00000534624.6 [P11142-1]
E9PI65
Q96IS6
E9PLF4
ENST00000534567.5