| FANCL Protein | |
|---|---|
| Protein Name | Fanconi anemia group L protein |
| Alternative Names | FA-L, FANCL, E3 ligase |
| Molecular Weight | 43 kDa |
| Length | 380 amino acids |
| UniProt ID | Q9NXF1 |
| Cellular Location | Nucleus |
The FANCL protein is the catalytic E3 ubiquitin ligase subunit of the Fanconi anemia (FA) core complex. It catalyzes the monoubiquitination of FANCD2 and FANCI, the central activation step in the FA DNA damage response pathway. FANCL contains a RING finger domain that confers E3 ubiquitin ligase activity and works with the E2 conjugating enzyme UBE2T to transfer ubiquitin to FANCD2.
FANCL is a 380 amino acid protein with a molecular weight of approximately 43 kDa. The protein contains multiple functional domains including an N-terminal L(1) domain that mediates protein-protein interactions, a RING finger domain that coordinates zinc ions and catalyzes ubiquitin transfer, and a C-terminal domain that interacts with other FA core complex members. The catalytic RING finger domain is essential for FANCL's E3 ubiquitin ligase function.
FANCL contains:
FANCL is the E3 ligase that:
The study of Fancl Protein has evolved significantly over the past decades. Research in this area has revealed important insights into the underlying mechanisms of neurodegeneration and continues to drive therapeutic development.
Historical context and key discoveries in this field have shaped our current understanding and will continue to guide future research directions.