RFFL — Ring finger and FYVE like domain containing E3 ubiquitin protein ligase
RFFL 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.
RFFL's module in each cell type
| Cell type | Module | Shares the module with | |
|---|---|---|---|
| CD4⁺ T cells | Vesicle trafficking Housekeeping | AP2A1, APPL2, ARHGAP35, ATAD2, DHX30, DYRK1B, ERP44, FAM91A1 +21 more | View in SCUBA |
| Gamma-delta T cells | T Cell Calcium-Cytoskeletal T cell maturation | CASP8, CRACR2A, GCNT1, IKZF3, IQGAP1, MAP4, PRKAR1A, PSEN1 +5 more |
About the gene
| Synonyms | CARP-2, CARP2, fring, rififylin, RNF189, RNF34L |
|---|---|
| Chromosome | 17: 35005990-35089319 |
| Predicted location | Intracellular |
| Essential gene | No |
| Protein class | Enzymes, Predicted intracellular proteins |
| Molecular function | Transferase |
| Biological process | Apoptosis, Ubl conjugation pathway |
Function
E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Mediates 'Lys-48'-linked polyubiquitination of PRR5L and its subsequent proteasomal degradation thereby indirectly regulating cell migration through the mTORC2 complex. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis. Negatively regulates the tumor necrosis factor-mediated signaling pathway through targeting of RIPK1 to ubiquitin-mediated proteasomal degradation. Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation. Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN. May also play a role in endocytic recycling.
Human Protein Atlas · Open Targets · UniProt
Gene annotation from the Human Protein Atlas and UniProt; see sources & licences.