| ID | Sequence | Length | GC content |
|---|---|---|---|
| CUUUCUGCAGCAGGAACCGCGGCUGCUGGACAAGAGGGGUGCGGUGGAU… | 2066 nt | 0.6089 | |
| CUUCCUCCCACAGAACCCGUUUCGGGCCUCAGAGCGUCUGGUGAGAUGC… | 1962 nt | 0.6081 | |
| CUUUCUGCAGCAGGAACCGCGGCUGCUGGACAAGAGGGGUGCGGUGGAU… | 2100 nt | 0.6110 | |
| CUUUCUGCAGCAGGAACCGCGGCUGCUGGACAAGAGGGGUGCGGUGGAU… | 2096 nt | 0.6112 | |
| CUUUCUGCAGCAGGAACCGCGGCUGCUGGACAAGAGGGGUGCGGUGGAU… | 2079 nt | 0.6099 | |
| CUUUCUGCAGCAGGAACCGCGGCUGCUGGACAAGAGGGGUGCGGUGGAU… | 2070 nt | 0.6087 | |
| CAGGAACCGCGGCUGCUGGACAAGAGGGGUGCGGUGGAUACUGACCUUU… | 2079 nt | 0.6065 |
This gene encodes the beta-subunit of glucosidase II, an N-linked glycan-processing enzyme in the endoplasmic reticulum. The encoded protein is an acidic phosphoprotein known to be a substrate for protein kinase C. Mutations in this gene have been associated with the autosomal dominant polycystic liver disease. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]
A study in human patients with sepsis demonstrated that the PRKCSH exhibited increased polyadenylation in viral compared to bacterial infection samples, identifying it as a candidate gene for differential polyadenylation analysis between infection types [He et al. DOI:10.1186/s12879-025-11078-z]. A study in rats demonstrated that the mRNA Pld1, identified as a hub gene within a protein-protein interaction network from a constructed ceRNA network, was upregulated in the cavernous nerve crush model group and was suggested to be regulated by the miRNAs rno-let-7a-2-3p and rno-miR-129-2-3p [Huang et al. DOI:10.1080/21655979.2021.1973863].