UniProt Protein Function: | NARF: 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. [provided by RefSeq, Jul 2008]Chromosomal Location of Human Ortholog: 17q25.3Cellular Component: lamin filament; nuclear lamina; nuclear lumenMolecular Function: lamin binding |
UniProt Protein Details: | |
NCBI Summary: | 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. [provided by RefSeq, Jul 2008] |
UniProt Code: | Q9UHQ1 |
NCBI GenInfo Identifier: | 74735021 |
NCBI Gene ID: | 26502 |
NCBI Accession: | Q9UHQ1.1 |
UniProt Secondary Accession: | Q9UHQ1,Q96AY9, Q9BWC6, A6NCJ3, B3KPX2, K4DI98 |
UniProt Related Accession: | Q9UHQ1 |
Molecular Weight: | 44,681 Da |
NCBI Full Name: | Nuclear prelamin A recognition factor |
NCBI Synonym Full Names: | nuclear prelamin A recognition factor |
NCBI Official Symbol: | NARF |
NCBI Official Synonym Symbols: | IOP2 |
NCBI Protein Information: | nuclear prelamin A recognition factor |
UniProt Protein Name: | Nuclear prelamin A recognition factor |
UniProt Synonym Protein Names: | Iron-only hydrogenase-like protein 2; IOP2 |
Protein Family: | Nuclear prelamin A recognition factor |
UniProt Gene Name: | NARF |
UniProt Entry Name: | NARF_HUMAN |