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General description of the gene and the encoded protein(s) using information from HGNC and Ensembl, as well as predictions made by the Human Protein Atlas project.
Gene namei
Official gene symbol, which is typically a short form of the gene name, according to HGNC.
All transcripts of all genes have been analyzed regarding the location(s) of corresponding protein based on prediction methods for signal peptides and transmembrane regions.
Genes with at least one transcript predicted to encode a secreted protein, according to prediction methods or to UniProt location data, have been further annotated and classified with the aim to determine if the corresponding protein(s) are secreted or actually retained in intracellular locations or membrane-attached.
Remaining genes, with no transcript predicted to encode a secreted protein, will be assigned the prediction-based location(s).
The annotated location overrules the predicted location, so that a gene encoding a predicted secreted protein that has been annotated as intracellular will have intracellular as the final location.
Gene information from Ensembl and Entrez, as well as links to available gene identifiers are displayed here. Information was retrieved from Ensembl if not indicated otherwise.
Chromosome
6
Cytoband
p21.33
Chromosome location (bp)
31827738 - 31830254
Number of transcriptsi
Number of protein-coding transcripts from the gene as defined by Ensembl.
Useful information about the protein provided by UniProt.
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 1,2,3. 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 4. 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 5. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling 6. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation 7....show less
Molecular function (UniProt)i
Keywords assigned by UniProt to proteins due to their particular molecular function.
Chaperone, Host cell receptor for virus entry, Receptor
Biological process (UniProt)i
Keywords assigned by UniProt to proteins because they are involved in a particular biological process.
Host-virus interaction, Stress response
Ligand (UniProt)i
Keywords assigned by UniProt to proteins because they bind, are associated with, or whose activity is dependent of some molecule.
ATP-binding, Nucleotide-binding
Gene summary (Entrez)i
Useful information about the gene from Entrez
This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. [provided by RefSeq, Jul 2008]...show less
PROTEIN INFORMATIONi
The protein information section displays alternative protein-coding transcripts (splice variants) encoded by this gene according to the Ensembl database.
The Splice variant identifier links to the Ensembl website protein summary for the selected splice variant. The data in the Swissprot and TrEMBL columns links to corresponding pages in the UniProt database.
The protein classes assigned to this protein are shown if expanding the data in the protein class column. Parent protein classes are in bold font and subclasses are listed under the parent class.
The length of the protein (amino acid residues according to Ensembl), molecular mass (kDalton), predicted signal peptide and number of predicted transmembrane region(s) according to in-house majority decision methods based on sets of predictors are also reported.
P0DMV9 [Direct mapping] Heat shock 70 kDa protein 1B
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A8K5I0 [Target identity:100%; Query identity:100%] Epididymis secretory protein Li 103; Epididymis secretory sperm binding protein; HSPA1A; HSPA1B; Heat shock 70kDa protein 1A; Heat shock 70kDa protein 1B; cDNA FLJ75127, highly similar to Homo sapiens heat shock 70kDa protein 1A, mRNA
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Predicted intracellular proteins Intracellular proteins predicted by MDM and MDSEC Mapped to neXtProt neXtProt - Evidence at protein level
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GO:0000166[nucleotide binding] GO:0001618[virus receptor activity] GO:0001664[G protein-coupled receptor binding] GO:0003723[RNA binding] GO:0005102[signaling receptor binding] GO:0005515[protein binding] GO:0005524[ATP binding] GO:0005576[extracellular region] GO:0005634[nucleus] GO:0005654[nucleoplasm] GO:0005737[cytoplasm] GO:0005739[mitochondrion] GO:0005783[endoplasmic reticulum] GO:0005813[centrosome] GO:0005814[centriole] GO:0005815[microtubule organizing center] GO:0005829[cytosol] GO:0005856[cytoskeleton] GO:0005886[plasma membrane] GO:0005925[focal adhesion] GO:0006402[mRNA catabolic process] GO:0006457[protein folding] GO:0008285[negative regulation of cell population proliferation] GO:0010628[positive regulation of gene expression] GO:0016192[vesicle-mediated transport] GO:0016234[inclusion body] GO:0016235[aggresome] GO:0016607[nuclear speck] GO:0016887[ATP hydrolysis activity] GO:0019899[enzyme binding] GO:0030308[negative regulation of cell growth] GO:0031072[heat shock protein binding] GO:0031396[regulation of protein ubiquitination] GO:0031397[negative regulation of protein ubiquitination] GO:0031625[ubiquitin protein ligase binding] GO:0031982[vesicle] GO:0032436[positive regulation of proteasomal ubiquitin-dependent protein catabolic process] GO:0032757[positive regulation of interleukin-8 production] GO:0032991[protein-containing complex] GO:0034599[cellular response to oxidative stress] GO:0034605[cellular response to heat] GO:0034620[cellular response to unfolded protein] GO:0042026[protein refolding] GO:0042826[histone deacetylase binding] GO:0043066[negative regulation of apoptotic process] GO:0044183[protein folding chaperone] GO:0045648[positive regulation of erythrocyte differentiation] GO:0046034[ATP metabolic process] GO:0046718[viral entry into host cell] GO:0047485[protein N-terminus binding] GO:0048471[perinuclear region of cytoplasm] GO:0050821[protein stabilization] GO:0051082[unfolded protein binding] GO:0051085[chaperone cofactor-dependent protein refolding] GO:0051092[positive regulation of NF-kappaB transcription factor activity] GO:0051787[misfolded protein binding] GO:0055131[C3HC4-type RING finger domain binding] GO:0060548[negative regulation of cell death] GO:0070062[extracellular exosome] GO:0070370[cellular heat acclimation] GO:0070434[positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway] GO:0071383[cellular response to steroid hormone stimulus] GO:0072562[blood microparticle] GO:0090063[positive regulation of microtubule nucleation] GO:0090084[negative regulation of inclusion body assembly] GO:0140545[ATP-dependent protein disaggregase activity] GO:0140662[ATP-dependent protein folding chaperone] GO:1901673[regulation of mitotic spindle assembly] GO:1903265[positive regulation of tumor necrosis factor-mediated signaling pathway] GO:1904813[ficolin-1-rich granule lumen] GO:1990904[ribonucleoprotein complex] GO:2001240[negative regulation of extrinsic apoptotic signaling pathway in absence of ligand]
The Human Protein Atlas project is funded
