NARF Rabbit anti-Human, Mouse, Rat, Polyclonal, Proteintech

Description

• Several proteins have been found to be prenylated and methylated at their carboxyl-terminal ends
• Prenylation was initially believed to be important only for membrane attachment
• However, another role for prenylation appears to be its importance in protein-protein interactions
• The only nuclear proteins known to be prenylated in mammalian cells are prelamin A- and B-type lamins
• Prelamin A is farnesylated and carboxymethylated on the cysteine residue of a carboxyl-terminal CaaX motif
• This post-translationally modified cysteine residue is removed from prelamin A when it is endoproteolytically processed into mature lamin A
• The protein encoded by this gene binds to the prenylated prelamin A carboxyl-terminal tail domain
• It may be a component of a prelamin A endoprotease complex
• The encoded protein is located in the nucleus, where it partially colocalizes with the nuclear lamina
• It shares limited sequence similarity with iron-only bacterial hydrogenases
• Alternatively spliced transcript variants encoding different isoforms have been identified for this gene, including one with a novel exon that is generated by RNA editing.