CANX phospho S583
Function
Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse.
Post-translational modifications
Phosphorylated at Ser-564 by MAPK3/ERK1. Phosphorylation by MAPK3/ERK1 increases its association with ribosomes (By similarity).
Palmitoylation by DHHC6 leads to the preferential localization to the perinuclear rough ER. It mediates the association of calnexin with the ribosome-translocon complex (RTC) which is required for efficient folding of glycosylated proteins.
Ubiquitinated, leading to proteasomal degradation. Probably ubiquitinated by ZNRF4.
Sequence Similarities
Belongs to the calreticulin family.
Cellular localization
- Endoplasmic reticulum membrane
- Single-pass type I membrane protein
- Mitochondrion membrane
- Single-pass type I membrane protein
- Melanosome membrane
- Single-pass type I membrane protein
- Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:12643545, PubMed:17081065). The palmitoylated form preferentially localizes to the perinuclear rough ER (PubMed:22314232). Localizes to endoplasmic reticulum mitochondria-associated membrane (MAMs) that connect the endoplasmic reticulum and the mitochondria (By similarity).
Alternative names
Calnexin, IP90, Major histocompatibility complex class I antigen-binding protein p88, p90, CANX
Database links
Other research areas
- Neuroscience