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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
9
Cytoband
p21.1
Chromosome location (bp)
33025273 - 33039907
Number of transcriptsi
Number of protein-coding transcripts from the gene as defined by Ensembl.
Useful information about the protein provided by UniProt.
Co-chaperone for HSPA8/Hsc70 1. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) 2. Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis 3. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV 4....show less
Molecular function (UniProt)i
Keywords assigned by UniProt to proteins due to their particular molecular function.
Chaperone
Ligand (UniProt)i
Keywords assigned by UniProt to proteins because they bind, are associated with, or whose activity is dependent of some molecule.
Metal-binding, Zinc
Gene summary (Entrez)i
Useful information about the gene from Entrez
This gene encodes a member of the DnaJ family of proteins, which act as heat shock protein 70 cochaperones. Heat shock proteins facilitate protein folding, trafficking, prevention of aggregation, and proteolytic degradation. Members of this family are characterized by a highly conserved N-terminal J domain, a glycine/phenylalanine-rich region, four CxxCxGxG zinc finger repeats, and a C-terminal substrate-binding domain. The J domain mediates the interaction with heat shock protein 70 to recruit substrates and regulate ATP hydrolysis activity. In humans, this gene has been implicated in positive regulation of virus replication through co-option by the influenza A virus. Several pseudogenes of this gene are found on other chromosomes. [provided by RefSeq, Sep 2015]...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 ENSP identifier links to the Ensembl website protein summary, while the ENST identifier links to the Ensembl website transcript summary for the selected splice variant. The data in the UniProt column can be expanded to show links to all matching UniProt identifiers for this protein.
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 Gene Ontology terms assigned to this protein are listed if expanding the Gene ontology column. The length of the protein (amino acid residues according to Ensembl), molecular mass (kDalton), predicted signal peptide (according to a majority of the signal peptide predictors SPOCTOPUS, SignalP 4.0, and Phobius) and the number of predicted transmembrane region(s) (according to MDM) are also reported.
P31689 [Direct mapping] DnaJ homolog subfamily A member 1
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Predicted intracellular proteins Intracellular proteins predicted by MDM and MDSEC Mapped to neXtProt neXtProt - Evidence at protein level Protein evidence (Kim et al 2014) Protein evidence (Ezkurdia et al 2014)
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GO:0001664[G protein-coupled receptor binding] GO:0001671[ATPase activator activity] GO:0005515[protein binding] GO:0005524[ATP binding] GO:0005634[nucleus] GO:0005737[cytoplasm] GO:0005739[mitochondrion] GO:0005783[endoplasmic reticulum] GO:0005829[cytosol] GO:0006457[protein folding] GO:0006986[response to unfolded protein] GO:0007283[spermatogenesis] GO:0009408[response to heat] GO:0015630[microtubule cytoskeleton] GO:0016020[membrane] GO:0030317[flagellated sperm motility] GO:0030521[androgen receptor signaling pathway] GO:0030544[Hsp70 protein binding] GO:0030957[Tat protein binding] GO:0031072[heat shock protein binding] GO:0031397[negative regulation of protein ubiquitination] GO:0031625[ubiquitin protein ligase binding] GO:0042026[protein refolding] GO:0043065[positive regulation of apoptotic process] GO:0043066[negative regulation of apoptotic process] GO:0043231[intracellular membrane-bounded organelle] GO:0043508[negative regulation of JUN kinase activity] GO:0046872[metal ion binding] GO:0048471[perinuclear region of cytoplasm] GO:0050750[low-density lipoprotein particle receptor binding] GO:0051082[unfolded protein binding] GO:0051087[chaperone binding] GO:0051223[regulation of protein transport] GO:0055131[C3HC4-type RING finger domain binding] GO:0070062[extracellular exosome] GO:0070585[protein localization to mitochondrion] GO:0098554[cytoplasmic side of endoplasmic reticulum membrane] GO:1901998[toxin transport] GO:1903748[negative regulation of establishment of protein localization to mitochondrion] GO:1905259[negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway]
The Human Protein Atlas project is funded
