Biology:POP1 (gene)
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Generic protein structure example |
Ribonucleases P/MRP protein subunit POP1 is a protein that in humans is encoded by the POP1 gene.[1][2]
Function
POP1 is a protein subunit of two different small nucleolar ribonucleoprotein complexes: the endoribonuclease for mitochondrial RNA processing complex and the ribonuclease P complex. This protein is a ribonuclease that localizes to the nucleus and functions in pre-RNA processing.[3]
Clinical significance
POP1 is also an autoantigen in patients suffering from connective tissue diseases. Mutations in the POP1 gene result in severe anauxetic dysplasia.[4]
Interactions
POP1 (gene) has been shown to interact with POP4.[5]
References
- ↑ "RNA-protein interactions in the human RNase MRP ribonucleoprotein complex". RNA 5 (4): 512–24. Apr 1999. doi:10.1017/S1355838299982079. PMID 10199568.
- ↑ "hPop1: an autoantigenic protein subunit shared by the human RNase P and RNase MRP ribonucleoproteins". EMBO J 15 (21): 5936–48. Jan 1997. doi:10.1002/j.1460-2075.1996.tb00980.x. PMID 8918471.
- ↑ "Entrez Gene: POP1 processing of precursor 1, ribonuclease P/MRP subunit (S. cerevisiae)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10940.
- ↑ Glazov, EA; Zankl, A; Donskoi, M; Kenna, TJ; Thomas, GP; Clark, GR; Duncan, EL; Brown, MA (Mar 2011). "Whole-Exome Re-Sequencing in a Family Quartet Identifies POP1 Mutations As the Cause of a Novel Skeletal Dysplasia.". PLOS Genetics 7 (3): e1002027. doi:10.1371/journal.pgen.1002027. PMID 21455487.
- ↑ Welting, Tim J M; van Venrooij Walther J; Pruijn Ger J M (2004). "Mutual interactions between subunits of the human RNase MRP ribonucleoprotein complex". Nucleic Acids Res. (England) 32 (7): 2138–46. doi:10.1093/nar/gkh539. PMID 15096576.
Further reading
- "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1.". DNA Res. 1 (5): 223–9. 1995. doi:10.1093/dnares/1.5.223. PMID 7584044.
- "A bidirectional promoter connects the p14.5 gene to the gene for RNase P and RNase MRP protein subunit hPOP1.". Biochem. Biophys. Res. Commun. 241 (1): 59–67. 1998. doi:10.1006/bbrc.1997.7772. PMID 9405234.
- "Partially processed pre-rRNA is preserved in association with processing components in nucleolus-derived foci during mitosis.". Mol. Biol. Cell 9 (9): 2407–22. 1999. doi:10.1091/mbc.9.9.2407. PMID 9725903.
- "Protein-RNA interactions in the subunits of human nuclear RNase P.". RNA 7 (7): 937–41. 2001. doi:10.1017/S1355838201010299. PMID 11455963.
- "Basic domains target protein subunits of the RNase MRP complex to the nucleolus independently of complex association.". Mol. Biol. Cell 12 (11): 3680–9. 2002. doi:10.1091/mbc.12.11.3680. PMID 11694598.
- "Directed proteomic analysis of the human nucleolus.". Curr. Biol. 12 (1): 1–11. 2002. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
- "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. 2003. doi:10.1073/pnas.242603899. PMID 12477932. Bibcode: 2002PNAS...9916899M.
- "Mutual interactions between subunits of the human RNase MRP ribonucleoprotein complex.". Nucleic Acids Res. 32 (7): 2138–46. 2004. doi:10.1093/nar/gkh539. PMID 15096576.
- "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. 2004. doi:10.1073/pnas.0404720101. PMID 15302935. Bibcode: 2004PNAS..10112130B.
- "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. 2005. doi:10.1038/nature03207. PMID 15635413. Bibcode: 2005Natur.433...77A.
- "Towards a proteome-scale map of the human protein-protein interaction network.". Nature 437 (7062): 1173–8. 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- "Differential association of protein subunits with the human RNase MRP and RNase P complexes.". RNA 12 (7): 1373–82. 2006. doi:10.1261/rna.2293906. PMID 16723659.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.