Binding Immunoglobulin Protein
| Gene Ontology | |
|---|---|
| Molecular function | • calcium ion binding • protein binding • ATP binding • ATPase activity • protein domain specific binding • protein binding, bridging • ubiquitin protein ligase binding • ribosome binding • unfolded protein binding • chaperone binding • misfolded protein binding |
| Cellular component | • nucleus • endoplasmic reticulum • endoplasmic reticulum lumen • endoplasmic reticulum membrane • endoplasmic reticulum-Golgi intermediate compartment • signalosome • cell surface • integral to endoplasmic reticulum membrane • midbody • endoplasmic reticulum chaperone complex • melanosome |
| Biological process | • platelet degranulation • ATP catabolic process • ER overload response • activation of signaling protein activity involved in unfolded protein response • blood coagulation • cerebellum structural organization • cerebellar Purkinje cell layer development • platelet activation • ER-associated protein catabolic process • negative regulation of transforming growth factor beta receptor signaling pathway • endoplasmic reticulum unfolded protein response • positive regulation of protein ubiquitination • cellular response to glucose starvation • negative regulation of apoptotic process • regulation of protein folding in endoplasmic reticulum |
| Sources: Amigo / QuickGO | |
128 – 128 Mb
34.77 – 34.78 Mb
'Binding immunoglobulin protein' (BiP) also known as 78 kDa glucose-regulated protein (GRP-78) or heat shock 70 kDa protein 5 (HSPA5) is a HSP70 molecular chaperone located in the lumen of the endoplasmic reticulum (ER) that binds newly-synthesized proteins as they are translocated into the ER, and maintains them in a state competent for subsequent folding and oligomerization. BiP is also an essential component of the translocation machinery, as well as playing a role in retrograde transport across the ER membrane of aberrant proteins destined for degradation by the proteasome. BiP is an abundant protein under all growth conditions, but its synthesis is markedly induced under conditions that lead to the accumulation of unfolded polypeptides in the ER. In humans, BiP is encoded by the HSPA5 gene.
Read more about Binding Immunoglobulin Protein: Function, Mechanism, Interactions, Immunological Properties
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