Description: Homo sapiens calnexin (CANX), transcript variant 2, mRNA. RefSeq Summary (NM_001024649): This gene encodes a member of the calnexin family of molecular chaperones. The encoded protein is a calcium-binding, endoplasmic reticulum (ER)-associated protein that interacts transiently with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. It may also play a central role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Alternatively spliced transcript variants encoding different isoforms have been described. [provided by RefSeq, Jun 2018]. Transcript (Including UTRs) Position: hg19 chr5:179,125,930-179,158,639 Size: 32,710 Total Exon Count: 15 Strand: + Coding Region Position: hg19 chr5:179,132,683-179,155,645 Size: 22,963 Coding Exon Count: 14
ID:CALX_HUMAN DESCRIPTION: RecName: Full=Calnexin; AltName: Full=IP90; AltName: Full=Major histocompatibility complex class I antigen-binding protein p88; AltName: Full=p90; Flags: Precursor; FUNCTION: Calcium-binding protein that interacts with newly synthesized 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. SUBUNIT: Interacts with MAPK3/ERK1. Interacts with KCNH2. Associates with ribosomes. Interacts with SGIP1; involved in negative regulation of endocytosis (By similarity). The palmitoylated form interacts with the ribosome-translocon complex component SSR1, promoting efficient folding of glycoproteins. INTERACTION: Q92597:NDRG1; NbExp=2; IntAct=EBI-355947, EBI-716486; SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. The palmitoylated form preferentially localizes to the perinuclear rough ER. PTM: Phosphorylated at Ser-564 by MAPK3/ERK1. phosphorylation by MAPK3/ERK1 increases its association with ribosomes (By similarity). PTM: 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. SIMILARITY: Belongs to the calreticulin family. WEB RESOURCE: Name=Wikipedia; Note=Calnexin entry; URL="http://en.wikipedia.org/wiki/Calnexin";
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Genetic Association Studies of Complex Diseases and Disorders
Genetic Association Database (archive): CANX CDC HuGE Published Literature: CANX Positive Disease Associations: nephrogenic diabetes insipidus Related Studies:
nephrogenic diabetes insipidus Morello JP et al. 2001, Association of calnexin with wild type and mutant AVPR2 that causes nephrogenic diabetes insipidus., Biochemistry. 2001 Jun;40(23):6766-75.
[PubMed 11389590]
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P27824
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Biological Process: GO:0002474 antigen processing and presentation of peptide antigen via MHC class I GO:0006457 protein folding GO:0007568 aging GO:0009306 protein secretion GO:0019886 antigen processing and presentation of exogenous peptide antigen via MHC class II GO:0034975 protein folding in endoplasmic reticulum GO:0048488 synaptic vesicle endocytosis GO:0061077 chaperone-mediated protein folding GO:0070106 interleukin-27-mediated signaling pathway GO:0070757 interleukin-35-mediated signaling pathway GO:0072583 clathrin-dependent endocytosis
KEGG - Kyoto Encyclopedia of Genes and Genomes hsa04612 - Antigen processing and presentation
BioCarta from NCI Cancer Genome Anatomy Project h_eradPathway - ER¿associated degradation (ERAD) Pathway
Reactome (by CSHL, EBI, and GO)
Protein P27824 (Reactome details) participates in the following event(s):
R-HSA-2130478 Interaction of invariant chain trimer and MHC II alpha beta dimer R-HSA-8950387 CANX binds EBI3 R-HSA-8951500 Dissociation of CANX from nonameric complex R-HSA-548890 Removal of the third glucose by glucosidase II and release from the chaperone R-HSA-2213241 Formation of nonameric complex R-HSA-535717 Binding of calnexin/calreticulin to the unfolded protein R-HSA-983145 Binding of newly synthesized MHC class I heavy chain (HC) with calnexin R-HSA-983146 Interaction of beta-2-microglobulin (B2M) chain with class I HC R-HSA-901047 Binding of ERp57 R-HSA-983148 Interaction of Erp57 with MHC class I HC R-HSA-2132295 MHC class II antigen presentation R-HSA-9020956 Interleukin-27 signaling R-HSA-8984722 Interleukin-35 Signalling R-HSA-901042 Calnexin/calreticulin cycle R-HSA-1280218 Adaptive Immune System R-HSA-447115 Interleukin-12 family signaling R-HSA-983170 Antigen Presentation: Folding, assembly and peptide loading of class I MHC R-HSA-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle R-HSA-168256 Immune System R-HSA-449147 Signaling by Interleukins R-HSA-983169 Class I MHC mediated antigen processing & presentation R-HSA-446203 Asparagine N-linked glycosylation R-HSA-1280215 Cytokine Signaling in Immune system R-HSA-597592 Post-translational protein modification R-HSA-392499 Metabolism of proteins
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