RPN2: Ribophorin II – Key Subunit of the Oligosaccharyltransferase Complex
Comprehensive biomedical overview of RPN2, including genomic annotation, expression, disease associations, and functional classification.
Gene Information Card
| Symbol | RPN2 |
|---|---|
| Full Name | Ribophorin II |
| Gene Type | Protein coding |
| Chromosomal Location | 20q11.23 |
| NCBI Gene ID | 6185 ncbi.nlm.nih.gov/gene/6185 |
| Ensembl ID | ENSG00000101204 |
| UniProt ID | P04844 |
| OMIM ID | 180490 |
| HGNC ID | 10400 |
| Aliases | RPN-II, RIBOPHORIN II, OST2, SWP1 |
Description
RPN2 (ribophorin II) encodes a type I transmembrane protein that is a subunit of the oligosaccharyltransferase (OST) complex. The OST complex catalyzes the transfer of a high-mannose oligosaccharide from dolichol-phosphate to asparagine residues on nascent polypeptides in the lumen of the rough endoplasmic reticulum. RPN2 is essential for N-glycosylation and plays a role in protein folding, quality control, and trafficking. It is also implicated in cancer progression and drug resistance.
Disease Associations
| Disease category | Pathophysiological mechanism | Genomic evidence |
|---|---|---|
| Breast cancer | RPN2 overexpression enhances N-glycosylation of CD44 and promotes cancer stem cell properties; associated with poor prognosis. | PMID: 23382219; COSMIC |
| Gastric cancer | RPN2 upregulation correlates with lymph node metastasis and reduced survival; may regulate EMT via glycosylation. | PMID: 25695634; NCBI Gene |
| Colorectal cancer | RPN2 knockdown reduces cell proliferation and invasion; involved in Wnt/β-catenin signaling modulation. | PMID: 27323851; COSMIC |
| Hepatocellular carcinoma | RPN2 overexpression promotes metastasis through altered glycosylation of integrins. | PMID: 28289123; ClinVar |
Expression Profile
Tissue Expression
| Tissue | nTPM | level |
|---|---|---|
| Liver | 14.2 | Medium |
| Pancreas | 11.8 | Medium |
| Kidney | 9.5 | Medium |
| Breast | 8.1 | Medium |
| Colon | 7.6 | Low |
| Lung | 6.9 | Low |
| Brain | 3.2 | Low |
Cell Line Expression
| Cell Line | nTPM | Notes |
|---|---|---|
| HepG2 | 12.1 | Hepatocellular carcinoma cell line |
| MCF7 | 9.8 | Breast cancer cell line |
| A549 | 7.4 | Lung adenocarcinoma cell line |
| HT-29 | 6.5 | Colorectal adenocarcinoma cell line |
| K562 | 5.2 | Chronic myeloid leukemia cell line |
Data source：Human Protein Atlas（proteinatlas.org）
Mutations & Variants
Hotspot Mutations
| Variant | Type | Frequency | Functional Description |
|---|---|---|---|
| c.107C>T (p.Pro36Leu) | Missense | <0.1% | Unknown; rare variant in population databases |
| c.454G>A (p.Gly152Arg) | Missense | <0.1% | Reported in COSMIC; potential loss of function |
| c.788_789insA (p.Tyr263*) | Frameshift | <0.1% | Predicted loss of function; truncation |
Mutation functional classification
Loss of Function (LOF)
Frameshift and nonsense mutations (e.g., p.Tyr263*) are predicted to cause loss of function by truncating the protein, impairing OST complex assembly or activity.
Gain of Function (GOF)
No well-characterized gain-of-function mutations reported in RPN2.
Dominant Negative (DN)
No evidence for dominant-negative effects; RPN2 mutations are typically recessive or haploinsufficient.
View complete mutation data：
Gene Ontology (GO)
| • oligosaccharyl transferase activity (GO:0004576) | • protein N-linked glycosylation (GO:0006487) |
| • endoplasmic reticulum (GO:0005783) | • integral component of membrane (GO:0016021) |
| • oligosaccharyltransferase complex (GO:0008250) |
Pathways
• REAC:R-HSA-446203 – Asparagine N-linked glycosylation
• REAC:R-HSA-948021 – Transport to the Golgi and subsequent modification
• KEGG:00510 – N-Glycan biosynthesis
Protein Summary
Ribophorin II (RPN2) is a 631-amino-acid transmembrane protein localized to the rough endoplasmic reticulum. It is a non-catalytic subunit of the oligosaccharyltransferase (OST) complex, which is responsible for the initial step of N-glycosylation. RPN2 stabilizes the OST complex and facilitates substrate recognition. The protein contains a single transmembrane domain and a large luminal domain. Its expression is elevated in several cancers, where it contributes to malignant phenotypes through altered glycosylation of cell surface receptors.
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