HSPA1B report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0090084Biological processnegative regulation of inclusion body assembly
GO_0008285Biological processnegative regulation of cell population proliferation
GO_1903265Biological processpositive regulation of tumor necrosis factor-mediated signaling pathway
GO_0006402Biological processmRNA catabolic process
GO_0034605Biological processcellular response to heat
GO_0032436Biological processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
GO_0010628Biological processpositive regulation of gene expression
GO_0071383Biological processcellular response to steroid hormone stimulus
GO_1901673Biological processregulation of mitotic spindle assembly
GO_0046034Biological processATP metabolic process
GO_0070370Biological processcellular heat acclimation
GO_0031396Biological processregulation of protein ubiquitination
GO_0051092Biological processpositive regulation of NF-kappaB transcription factor activity
GO_0046718Biological processsymbiont entry into host cell
GO_0034599Biological processcellular response to oxidative stress
GO_0031397Biological processnegative regulation of protein ubiquitination
GO_0043066Biological processnegative regulation of apoptotic process
GO_0050821Biological processprotein stabilization
GO_0070434Biological processpositive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway
GO_0090063Biological processpositive regulation of microtubule nucleation
GO_0032757Biological processpositive regulation of interleukin-8 production
GO_0042026Biological processprotein refolding
GO_0045648Biological processpositive regulation of erythrocyte differentiation
GO_2001240Biological processnegative regulation of extrinsic apoptotic signaling pathway in absence of ligand
GO_0051085Biological processchaperone cofactor-dependent protein refolding
GO_0030308Biological processnegative regulation of cell growth
GO_0005576Cellular componentextracellular region
GO_0048471Cellular componentperinuclear region of cytoplasm
GO_0005739Cellular componentmitochondrion
GO_0016607Cellular componentnuclear speck
GO_0005813Cellular componentcentrosome
GO_0016235Cellular componentaggresome
GO_0070062Cellular componentextracellular exosome
GO_0032991Cellular componentprotein-containing complex
GO_0005654Cellular componentnucleoplasm
GO_0005925Cellular componentfocal adhesion
GO_0005814Cellular componentcentriole
GO_0016234Cellular componentinclusion body
GO_0072562Cellular componentblood microparticle
GO_1904813Cellular componentficolin-1-rich granule lumen
GO_0005783Cellular componentendoplasmic reticulum
GO_0005829Cellular componentcytosol
GO_0005737Cellular componentcytoplasm
GO_1990904Cellular componentribonucleoprotein complex
GO_0031982Cellular componentvesicle
GO_0005634Cellular componentnucleus
GO_0019899Molecular functionenzyme binding
GO_0140545Molecular functionATP-dependent protein disaggregase activity
GO_0055131Molecular functionC3HC4-type RING finger domain binding
GO_0044183Molecular functionprotein folding chaperone
GO_0031072Molecular functionheat shock protein binding
GO_0005102Molecular functionsignaling receptor binding
GO_0031625Molecular functionubiquitin protein ligase binding
GO_0001618Molecular functionvirus receptor activity
GO_0051082Molecular functionunfolded protein binding
GO_0001664Molecular functionG protein-coupled receptor binding
GO_0042826Molecular functionhistone deacetylase binding
GO_0140662Molecular functionATP-dependent protein folding chaperone
GO_0005524Molecular functionATP binding
GO_0003723Molecular functionRNA binding
GO_0005515Molecular functionprotein binding
GO_0016887Molecular functionATP hydrolysis activity

IV. Literature review

[source]
Gene nameHSPA1B
Protein nameHeat shock 70 kDa protein 1B (Heat shock 70 kDa protein 2) (HSP70-2) (HSP70.2)
Heat shock 70 kDa protein 1B
SynonymsHSP72
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, 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 . 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 . 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 . Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling . Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation . .; FUNCTION: (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. .

AccessionsENST00000417199.4
A0A0G2JIW1
ENST00000450744.1
ENST00000445736.1
ENST00000375650.5
ENST00000391555.1
ENST00000391548.1
ENST00000545241.2
P0DMV9
ENST00000458062.3