PLOD3 — Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3
PLOD3 belongs to a gene co-expression module in 2 of 28 SCUBA cell types. Each module groups genes that rise and fall together in that cell type; the genes it shares a module with are its closest co-expression partners there.
PLOD3's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| CD4⁺ T cells | Activated Effector ISG Anti-viral | GOLGA7B, KIF5C, KIT, MAP2K6, MVB12B, NMUR1, PLCG1, POC1B +8 more | View in SCUBA |
| Macrophages | Glycogen Metabolism Housekeeping | ARL2BP, BTF3L4, CAPN1, CD47, CRLS1, DCTD, DSTN, GLOD4 +24 more | View in SCUBA |
About the gene
| Synonyms | LH3 |
|---|---|
| Chromosome | 7: 101205977-101218420 |
| Predicted location | Intracellular, Secreted |
| Essential gene | No |
| Protein class | Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins, Predicted secreted proteins |
| Molecular function | Dioxygenase, Glycosyltransferase, Multifunctional enzyme, Oxidoreductase, Transferase |
Function
Multifunctional enzyme that catalyzes a series of essential post-translational modifications on Lys residues in procollagen. Plays a redundant role in catalyzing the formation of hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. Plays a redundant role in catalyzing the transfer of galactose onto hydroxylysine groups, giving rise to galactosyl 5-hydroxylysine. Has an essential role by catalyzing the subsequent transfer of glucose moieties, giving rise to 1,2-glucosylgalactosyl-5-hydroxylysine residues. Catalyzes hydroxylation and glycosylation of Lys residues in the MBL1 collagen- like domain, giving rise to hydroxylysine and 1,2-glucosylgalactosyl-5- hydroxylysine residues. Essential for normal biosynthesis and secretion of type IV collagens (Probable). Essential for normal formation of basement membranes (By similarity).
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.