Mouse Anti-HSPA5 Recombinant Antibody (A300) (CBMAB-AP3209LY)

Heat Shock Protein Family A (Hsp70) Member 5

The protein encoded by this gene is a member of the heat shock protein 70 (HSP70) family. It is localized in the lumen of the endoplasmic reticulum (ER), and is involved in the folding and assembly of proteins in the ER. As this protein interacts with many ER proteins, it may play a key role in monitoring protein transport through the cell.[provided by RefSeq, Sep 2010]

Heat Shock Protein Family A (Hsp70) Member 5; Heat Shock 70kDa Protein 5 (Glucose-Regulated Protein, 78kDa); Endoplasmic Reticulum Lumenal Ca(2+)-Binding Protein Grp78; Immunoglobulin Heavy Chain-Binding Protein; Glucose-Regulated Protein, 78kDa; GRP78; BIP; Heat Shock 70kD Protein 5 (Glucose-Regulated Protein, 78kD);

CSB-MA599866

Cellular response to antibiotic Source: Ensembl
Cellular response to calcium ion Source: Ensembl
Cellular response to cAMP Source: Ensembl
Cellular response to gamma radiation Source: Ensembl
Cellular response to glucose starvation Source: UniProtKB
Cellular response to interleukin-4 Source: Ensembl
Cellular response to manganese ion Source: Ensembl
Cellular response to nerve growth factor stimulus Source: Ensembl
Cellular response to unfolded protein Source: GO_Central
Cellular response to xenobiotic stimulus Source: Ensembl
Cerebellar Purkinje cell layer development Source: Ensembl
Cerebellum structural organization Source: Ensembl
Chaperone cofactor-dependent protein refolding Source: GO_Central
Endoplasmic reticulum unfolded protein response Source: GO_Central
ER overload response Source: Ensembl
Luteolysis Source: Ensembl
Maintenance of protein localization in endoplasmic reticulum Source: UniProtKB
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of IRE1-mediated unfolded protein response Source: UniProtKB
Negative regulation of protein-containing complex assembly Source: UniProtKB
Negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
Neuron apoptotic process Source: Ensembl
Neuron differentiation Source: Ensembl
Positive regulation of cell migration Source: UniProtKB
Positive regulation of neuron projection development Source: Ensembl
Positive regulation of protein ubiquitination Source: Ensembl
Positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
Posttranslational protein targeting to membrane, translocation Source: UniProtKB
Protein folding in endoplasmic reticulum Source: ParkinsonsUK-UCL
Protein refolding Source: GO_Central
Regulation of ATF6-mediated unfolded protein response Source: ParkinsonsUK-UCL
Regulation of IRE1-mediated unfolded protein response Source: ParkinsonsUK-UCL
Regulation of PERK-mediated unfolded protein response Source: ParkinsonsUK-UCL
Regulation of protein folding in endoplasmic reticulum Source: BHF-UCL
Response to cocaine Source: Ensembl
Response to methamphetamine hydrochloride Source: Ensembl
Stress response to metal ion Source: Ensembl
Substantia nigra development Source: UniProtKB
Toxin transport Source: Ensembl
Ubiquitin-dependent ERAD pathway Source: GO_Central

Endoplasmic reticulum lumen; Cytoplasm; Melanosome; Cell surface. Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:12643545). Localizes to the cell surface of epithelial cells in response to high levels of free iron (PubMed:20484814, PubMed:24355926, PubMed:27159390).

Autoantigen in rheumatoid arthritis.

AMPylated by FICD (PubMed:25601083). In unstressed cells, AMPylation at Thr-518 by FICD inactivates the chaperome activity: AMPylated form is locked in a relatively inert state and only weakly stimulated by J domain-containing proteins (By similarity). In response to endoplasmic reticulum stress, de-AMPylation by the same protein, FICD, restores the chaperone activity (By similarity).