| Nuclear Prelamin A Recognition Factor</title><base Target=_top></head><body Bgcolor=#ffffff Text=#00 | OKDB#: 3195 |
| Symbols: | symbols | Species: | human | ||
| Synonyms: | FLJ10067, DKFZp434G0420,NARF | Locus: | 17q25.3 in Homo sapiens |
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| General Comment | 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. Transcript variants encoding different isoforms and/or utilizing alternative polyadenylation sites exist although some variants do not have their full-length sequences defined. | ||||
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| Follicle stages | Primordial | ||||
| Comment | Arraztoa JA, et al 2005 reported the identification of genes expressed in primate primordial oocytes. | ||||
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| Mutations | 0 mutations | ||||
| Genomic Region | show genomic region | ||||
| Phenotypes and GWAS | show phenotypes and GWAS | ||||
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| created: | June 21, 2006, 12:54 p.m. | by: |
alex email:
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| last update: | June 21, 2006, 12:54 p.m. | by: | alex email: |
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