HERC2 — HECT and RLD domain containing E3 ubiquitin protein ligase 2
HERC2 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.
HERC2's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Gamma-delta T cells | Translation & Proteostasis RNA processing & translation | ARAP2, ATG13, BRPF1, CLINT1, CRKL, E2F3, EEF2, EIF2AK2 +15 more | |
| Mucosal-associated invariant T cell | IL-12 Cytotoxic Effector cytotoxicity | ANKZF1, ATP8B2, CD84, CTSH, DIP2A, IL12RB1, LPCAT4, MBOAT1 +7 more |
About the gene
| Synonyms | D15F37S1, jdf2, p528 |
|---|---|
| Chromosome | 15: 28111040-28322179 |
| Predicted location | Intracellular, Membrane |
| Essential gene | No |
| Protein class | Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins, Predicted membrane proteins |
| Molecular function | Transferase |
| Biological process | DNA damage, DNA repair, Ubl conjugation pathway |
Function
E3 ubiquitin-protein ligase that regulates ubiquitin- dependent retention of repair proteins on damaged chromosomes. Recruited to sites of DNA damage in response to ionizing radiation (IR) and facilitates the assembly of UBE2N and RNF8 promoting DNA damage- induced formation of 'Lys-63'-linked ubiquitin chains. Acts as a mediator of binding specificity between UBE2N and RNF8. Involved in the maintenance of RNF168 levels. E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of XPA which influences the circadian oscillation of DNA excision repair activity. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. Also modulates iron metabolism by regulating the basal turnover of FBXL5.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.