CANX (Calnexin) - Gene and Protein Overview
A comprehensive resource on the CANX gene, its protein calnexin, associated diseases, expression, mutations, and functional roles.
Gene Information Card
| Symbol | CANX |
|---|---|
| Full Name | Calnexin |
| Gene Type | Protein coding |
| Chromosomal Location | 5q35.3 |
| NCBI Gene ID | 821 ncbi.nlm.nih.gov/gene/821 |
| Ensembl ID | ENSG00000127022 |
| UniProt ID | P27824 |
| OMIM ID | 114217 |
| HGNC ID | 1463 |
| Aliases | CNX, IP90, P90 |
Description
The CANX gene encodes calnexin, a calcium-binding, endoplasmic reticulum (ER)-associated protein that functions as a molecular chaperone. Calnexin is a type I integral membrane protein that transiently binds to newly synthesized N-linked glycoproteins, facilitating proper folding, quality control, and retention of misfolded proteins in the ER. It is a key component of the calnexin/calreticulin cycle, which ensures the correct folding of glycoproteins and targets terminally misfolded proteins for ER-associated degradation (ERAD).
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Hereditary spastic paraplegia (HSP) | Mutations in CANX have been associated with autosomal recessive HSP, potentially affecting protein folding and ER homeostasis in neurons. | ClinVar, OMIM |
| Cancer (various types) | Altered calnexin expression has been observed in several cancers, influencing tumor progression and immune evasion through modulation of MHC class I antigen presentation. | COSMIC, PubMed |
| Diabetes mellitus | Calnexin is involved in the folding of proinsulin; dysregulation may contribute to beta-cell dysfunction and insulin deficiency. | PubMed |
| Viral infections | Calnexin interacts with viral glycoproteins, facilitating viral entry and replication; some viruses exploit calnexin for immune evasion. | PubMed |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Liver | 20.1 | Medium |
| Pancreas | 18.5 | Medium |
| Kidney | 17.3 | Medium |
| Brain | 15.2 | Medium |
| Heart | 14.8 | Medium |
| Lung | 13.9 | Medium |
| Spleen | 12.4 | Low |
| Testis | 11.2 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HepG2 (liver cancer) | 22.5 | High expression |
| A549 (lung cancer) | 19.8 | Moderate expression |
| MCF7 (breast cancer) | 18.2 | Moderate expression |
| K562 (leukemia) | 16.4 | Moderate expression |
| HEK293 (embryonic kidney) | 20.0 | High expression |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.1135C>T (p.Arg379Ter) | Nonsense | Rare | Premature truncation, likely loss of function |
| c.148G>A (p.Gly50Ser) | Missense | Rare | Potential disruption of lectin-binding domain |
| c.1655A>G (p.Tyr552Cys) | Missense | Rare | May affect protein stability |
| c.1021dup (p.Leu341ProfsTer5) | Frameshift | Rare | Loss of function |
Mutation functional classification
Loss of Function (LOF)
Loss-of-function mutations in CANX, such as nonsense or frameshift variants, lead to truncated or absent calnexin, impairing glycoprotein folding and ER quality control, which may contribute to neurodegeneration.
Gain of Function (GOF)
No clear gain-of-function mutations have been reported for CANX; most pathogenic variants are loss-of-function.
Dominant Negative (DN)
Dominant-negative effects are not well documented; however, missense mutations in the lectin-binding domain could potentially interfere with wild-type calnexin function in a dominant-negative manner, though evidence is limited.
View complete mutation data：
Gene Ontology (GO)
| • calcium ion binding | • chaperone binding |
| • glycoprotein binding | • protein folding |
| • endoplasmic reticulum | • calnexin cycle |
| • response to unfolded protein | • ER-associated degradation |
Pathways
• Calnexin/calreticulin cycle
• ER-associated degradation (ERAD)
• Antigen processing and presentation
• Protein processing in endoplasmic reticulum
Protein Summary
Calnexin is a 67 kDa type I transmembrane protein localized to the endoplasmic reticulum. It consists of a large N-terminal luminal domain that binds to monoglucosylated N-glycans on nascent glycoproteins, a transmembrane domain, and a short cytoplasmic tail. Calnexin functions as a lectin chaperone, promoting proper folding and preventing aggregation. It also participates in calcium homeostasis and the unfolded protein response. Post-translational modifications include phosphorylation and O-glycosylation, which regulate its activity.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| CANX Knockout HEK293 Cell Line | EDJ-KQ2728 | Human | 821 | Details Get a Quote |
| CANX Knockout HeLa Cell Line | EDJ-KQ22216 | Human | 821 | Details Get a Quote |
| CANX Knockout A-549 Cell Line | EDJ-KQ23587 | Human | 821 | Details Get a Quote |
| CANX Knockout HCT 116 Cell Line | EDJ-KQ23588 | Human | 821 | Details Get a Quote |
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