RLIM — Ring finger protein, LIM domain interacting
RLIM 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.
RLIM's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| Macrophages | ER-Golgi Trafficking Vesicular traficking | ADD1, AFTPH, AZIN1, COPA, DYNC1H1, HNRNPC, JOSD1, LCP2 +23 more | View in SCUBA |
| Mucosal-associated invariant T cell | Splicing Regulation RNA processing & translation | AREG, ARHGAP9, AZIN1, CCNH, CLK1, DDX24, DNAJB6, IL23R +9 more |
About the gene
| Synonyms | MGC15161, NY-REN-43, RNF12 |
|---|---|
| Chromosome | X: 74582976-74614624 |
| Predicted location | Intracellular |
| Essential gene | No |
| Protein class | Disease related genes, Enzymes, Human disease related genes, Potential drug targets, Predicted intracellular proteins |
| Molecular function | Transferase |
| Biological process | Transcription, Transcription regulation, Ubl conjugation pathway |
Function
E3 ubiquitin-protein ligase. Acts as a negative coregulator for LIM homeodomain transcription factors by mediating the ubiquitination and subsequent degradation of LIM cofactors LDB1 and LDB2 and by mediating the recruitment the SIN3a/histone deacetylase corepressor complex. Ubiquitination and degradation of LIM cofactors LDB1 and LDB2 allows DNA-bound LIM homeodomain transcription factors to interact with other protein partners such as RLIM. Plays a role in telomere length-mediated growth suppression by mediating the ubiquitination and degradation of TERF1. By targeting ZFP42 for degradation, acts as an activator of random inactivation of X chromosome in the embryo, a stochastic process in which one X chromosome is inactivated to minimize sex-related dosage differences of X-encoded genes in somatic cells of female placental mammals
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.