| FANCM Protein | |
|---|---|
| Protein Name | Fanconi anemia group M protein |
| Alternative Names | FA-M, FANCM, MHF1 |
| Molecular Weight | 250 kDa |
| Length | 2148 amino acids |
| UniProt ID | Q8IWA5 |
| Cellular Location | Nucleus (chromatin) |
The FANCM protein is a DNA translocase and key component of the Fanconi anemia (FA) pathway. It recognizes DNA damage, particularly interstrand crosslinks (ICLs), and initiates the FA repair cascade by recruiting the FA core complex to damaged DNA. FANCM has ATP-dependent DNA helicase activity and can remodel stalled replication forks.
FANCM is a 647 amino acid protein with a molecular weight of approximately 71 kDa. It contains several functional domains: an N-terminal DEAH-box ATPase domain that provides DNA translocase activity, an HMME domain (helicase-Ski2p motif), and a C-terminal ERCC4 DNA-binding domain (also known as the XPF-family domain). FANCM forms a complex with FAAP24 and MHF1/MHF2 to target specific DNA structures.
FANCM is a large protein with:
FANCM is a DNA translocase that:
FANCM interacts with:
The study of Fancm 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.