C1GALT1C1: Core 1 Synthase, Glycoprotein-N-Acetylgalactosamine 3-Beta-Galactosyltransferase 1, C1GALT1-Specific Chaperone 1
A critical chaperone for O-glycosylation, implicated in IgA nephropathy, cancer, and thrombocytopenia.
Gene Information Card
| Symbol | C1GALT1C1 |
|---|---|
| Full Name | Core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1, C1GALT1-specific chaperone 1 |
| Gene Type | protein coding |
| Chromosomal Location | Xq24 |
| NCBI Gene ID | 29071 ncbi.nlm.nih.gov/gene/29071 |
| Ensembl ID | ENSG00000171155 |
| UniProt ID | Q9NS00 |
| OMIM ID | 300611 |
| HGNC ID | 21038 |
| Aliases | C1GALT1C1, C1GALT1-specific chaperone 1, COSMC, core 1 beta-1,3-galactosyltransferase-specific chaperone 1, FLJ12627 |
Description
C1GALT1C1 encodes a molecular chaperone essential for the proper folding and stability of core 1 synthase (C1GALT1), the enzyme that catalyzes the addition of galactose to N-acetylgalactosamine to form the core 1 O-glycan (T antigen). This chaperone is required for the biosynthesis of O-glycans on mucins and other glycoproteins. Defects in C1GALT1C1 lead to reduced core 1 O-glycosylation, resulting in abnormal glycosylation patterns associated with diseases such as IgA nephropathy, cancer, and thrombocytopenia.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| IgA nephropathy | Reduced C1GALT1C1 expression leads to decreased core 1 O-glycosylation of IgA1, resulting in galactose-deficient IgA1 that is recognized by autoantibodies, forming immune complexes that deposit in the glomeruli. | PMID: 22493496; 26060113 |
| Colorectal cancer | Loss of C1GALT1C1 expression leads to truncated O-glycans (T antigen) on cell surface, promoting tumor invasion and metastasis. | PMID: 23108138; 26921328 |
| Thrombocytopenia (platelet-type bleeding disorder) | Mutations in C1GALT1C1 cause reduced T antigen on platelets, leading to impaired platelet function and bleeding. | PMID: 26060113; 26921328 |
| T-cell lymphoma | Altered O-glycosylation due to C1GALT1C1 deficiency may contribute to malignant transformation. | PMID: 26921328 |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Colon | 12.4 | Medium |
| Small intestine | 11.2 | Medium |
| Kidney | 8.5 | Low |
| Liver | 6.3 | Low |
| Lung | 5.1 | Low |
| Spleen | 4.8 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HeLa | 15.2 | Cervical cancer cell line |
| HCT116 | 12.8 | Colorectal cancer cell line |
| MCF7 | 9.4 | Breast cancer cell line |
| A549 | 7.1 | Lung cancer cell line |
| HEK293 | 6.5 | Embryonic kidney cell line |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.238C>T (p.Arg80Ter) | Nonsense | Rare | Loss of function, reduced chaperone activity |
| c.377G>A (p.Arg126His) | Missense | Rare | Impaired chaperone function, reduced C1GALT1 activity |
| c.1A>G (p.Met1Val) | Start codon loss | Rare | Loss of protein expression |
| c.482delC (p.Pro161LeufsTer5) | Frameshift | Rare | Truncated protein, loss of function |
Mutation functional classification
Loss of Function (LOF)
Most reported mutations are loss-of-function, leading to reduced or absent chaperone activity, resulting in defective O-glycosylation.
Gain of Function (GOF)
No gain-of-function mutations have been reported.
Dominant Negative (DN)
No dominant-negative effects have been described; the gene is X-linked, and hemizygous males are affected, while heterozygous females may show variable expression due to X-inactivation.
View complete mutation data：
Gene Ontology (GO)
| • chaperone binding | • protein folding |
| • protein glycosylation | • endoplasmic reticulum |
| • Golgi apparatus | • response to unfolded protein |
Pathways
• O-glycan biosynthesis
• Mucin-type O-glycan biosynthesis
• Protein processing in endoplasmic reticulum
Protein Summary
The C1GALT1C1 protein is a type II transmembrane chaperone localized in the endoplasmic reticulum and Golgi apparatus. It forms a complex with C1GALT1, stabilizing the enzyme and ensuring its proper folding and transport to the Golgi. Without C1GALT1C1, C1GALT1 is misfolded and degraded, leading to loss of core 1 O-glycan synthesis. The protein is essential for normal O-glycosylation of mucins and other glycoproteins, and its dysfunction is linked to multiple diseases.
Related Services
Related Products
| Product name | Cat.No. | Species | Gene ID | |
|---|---|---|---|---|
| C1GALT1C1 Knockout HEK293 Cell Line | EDJ-KQ3969 | Human | 29071 | Details Get a Quote |
| C1GALT1C1L Knockout HEK293 Cell Line | EDJ-KQ12583 | Human | 728819 | Details Get a Quote |
| C1GALT1C1 Knockout A-549 Cell Line | EDJ-KQ26247 | Human | 29071 | Details Get a Quote |
| C1GALT1C1 Knockout HCT 116 Cell Line | EDJ-KQ26248 | Human | 29071 | Details Get a Quote |
| C1GALT1C1 Knockout HeLa Cell Line | EDJ-KQ26249 | Human | 29071 | Details Get a Quote |
| C1GALT1C1L Knockout HeLa Cell Line | EDJ-KQ40312 | Human | 728819 | Details Get a Quote |
| C1GALT1C1L Knockout A-549 Cell Line | EDJ-KQ41609 | Human | 728819 | Details Get a Quote |
| C1GALT1C1L Knockout HCT 116 Cell Line | EDJ-KQ77550 | Human | 728819 | Details Get a Quote |
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