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Calnexin 1JHN.png
Aliases CANX, CNX, IP90, P90, calnexin
External IDs OMIM: 114217 MGI: 88261 HomoloGene: 1324 GeneCards: CANX
Gene location (Human)
Chromosome 5 (human)
Chr. Chromosome 5 (human)[1]
Chromosome 5 (human)
Genomic location for CANX
Genomic location for CANX
Band 5q35.3 Start 179,678,628 bp[1]
End 179,730,925 bp[1]
RNA expression pattern
PBB GE CANX 208853 s at fs.png

PBB GE CANX 208852 s at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 5: 179.68 – 179.73 Mb Chr 11: 50.29 – 50.33 Mb
PubMed search [3] [4]
View/Edit Human View/Edit Mouse

Calnexin (CNX) is a 67kDa integral protein (that appears variously as a 90kDa, 80kDa, or 75kDa band on western blotting depending on the source of the antibody) of the endoplasmic reticulum (ER). It consists of a large (50 kDa) N-terminal calcium-binding lumenal domain, a single transmembrane helix and a short (90 residues), acidic cytoplasmic tail.


Calnexin is a chaperone, characterized by assisting protein folding and quality control, ensuring that only properly folded and assembled proteins proceed further along the secretory pathway. It specifically acts to retain unfolded or unassembled N-linked glycoproteins in the ER. Calnexin binds only those N-glycoproteins that have GlcNAc2Man9Glc1 oligosaccharides. These monoglucosylated oligosaccharides result from the trimming of two glucose residues by the sequential action of two glucosidases, I and II. Glucosidase II can also remove the third and last glucose residue. If the glycoprotein is not properly folded, an enzyme called UGGT (for UDP-glucose:glycoprotein glucosyltransferase) will add the glucose residue back onto the oligosaccharide thus regenerating the glycoprotein's ability to bind to calnexin. The improperly-folded glycoprotein chain thus loiters in the ER, risking the encounter with MNS1 (alpha-mannosidase), which eventually sentences the underperforming glycoprotein to degradation by removing one of the nine mannose residues. If the protein is correctly translated, the chance of it being correctly folded before it encounters MNS1 is high.

Calnexin also functions as a chaperone for the folding of MHC class I α-chain in the membrane of the ER. As newly synthesized MHC class I α-chains enter the endoplasmic reticulum, calnexin binds on to them retaining them in a partly folded state.[5] After the β2-microglobulin binds to the MHC class I peptide-loading complex (PLC), calreticulin and ERp57 take over the job of chaperoning the MHC class I protein while the tapasin links the complex to the Transporter associated with antigen processing (TAP) complex. This association prepares the MHC class I for binding an antigen for presentation on the cell surface.


ATP and calcium ions are cofactors involved in substrate binding for calnexin.


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