| Standard Name | CNE1 |
|---|---|
| Systematic Name | YAL058W |
| Alias | FUN48 |
| Feature Type | ORF, Verified |
| Description | Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast (1, 2, 3, 4) |
| Name Description | CalNExin and calreticulin homolog |
| Chromosomal Location | |
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Gene Ontology Annotations All CNE1 GO evidence and references
| View Computational GO annotations for CNE1 | |
| Molecular Function | |
| Manually curated | |
| Biological Process | |
| Manually curated | |
| Cellular Component | |
| Manually curated |
Mutant phenotypes All CNE1 Phenotype evidence and references
interactions All CNE1 Interaction evidence and references
| 192 total interaction(s) for 103 unique genes/features. | |
| Physical Interactions |
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| Genetic Interactions |
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| Resources |
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Expression Summary
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| Resources |
Protein Information All CNE1 Protein evidence and references
| Localization | |
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| Phosphorylation | PhosphoGRID | PhosphoPep Database |
| Structure | |
| Homologs |
sequence information
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| Last Update | Coordinates: 2011-02-03 | Sequence: 1996-07-31 | ||||||||||||
| Subfeature details |
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Analyze Sequence
| S288C only | |
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| S288C vs. other species | |
| S288C vs. other strains |
Resources
| External Links | All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB |
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| Primary SGDID | S000000054 |
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References cited on this page View Complete Literature Guide for CNE1
| 1) | Parlati F, et al. (1995) Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus. J Biol Chem 270(1):244-53 |
| 2) | Xu X, et al. (2004) Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue. J Biochem 135(5):615-8 |
| 3) | Xu X, et al. (2004) P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue. FEBS Lett 570(1-3):155-60 |
| 4) | Kimura T, et al. (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41 |




