POP5

POP5
Identifiers
Aliases	POP5 , HSPC004, RPP2, RPP20, hPop5, POP5 homolog, ribonuclease P/MRP subunit
External IDs	OMIM: 609992 MGI: 2151221 HomoloGene: 41076 GeneCards: POP5
Gene location (Human)
Chr.	Chromosome 12 (human)
End	120,581,402 bp
Gene location (Mouse)
Chr.	Chromosome 5 (mouse)
End	115,383,410 bp
RNA expression pattern
	Top expressed in
	right adrenal gland; ; anterior pituitary; ; right lobe of thyroid gland; ; left lobe of thyroid gland; ; right lobe of liver; ; right uterine tube; ; spleen; ; body of pancreas; ; rectum; ; left coronary artery;
	Top expressed in
	superior frontal gyrus; ; yolk sac; ; facial motor nucleus; ; proximal tubule; ; kidney; ; thymus; ; anterior horn of spinal cord; ; morula; ; adrenal gland; ; lip;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	ribonuclease activity ; protein binding ; hydrolase activity ; ribonuclease P activity ;
Cellular component	nucleolus ; nucleolar ribonuclease P complex ; nucleus ; nucleoplasm ; ribonuclease MRP complex ; multimeric ribonuclease P complex ;
Biological process	RNA metabolic process ; RNA phosphodiester bond hydrolysis ; RNA phosphodiester bond hydrolysis, endonucleolytic ; tRNA processing ; protein lipoylation ; tRNA 5'-leader removal ; rRNA processing ;
	Sources:Amigo / QuickGO
Orthologs
	51367
	117109
	ENSG00000167272
	ENSMUSG00000060152
	Q969H6
	Q9DB28
	NM_015918 ; NM_198201 ; NM_198202
	NM_026398
	NP_057002 ; NP_937845
	NP_080674 ; NP_001390591
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated January 01, 2024

Ribonuclease P/MRP protein subunit POP5 is an enzyme that in humans is encoded by the POP5 gene.^[5]^[6]

Related Research Articles

Ribonuclease P is a type of ribonuclease which cleaves RNA. RNase P is unique from other RNases in that it is a ribozyme – a ribonucleic acid that acts as a catalyst in the same way that a protein-based enzyme would. Its function is to cleave off an extra, or precursor, sequence of RNA on tRNA molecules. Further, RNase P is one of two known multiple turnover ribozymes in nature, the discovery of which earned Sidney Altman and Thomas Cech the Nobel Prize in Chemistry in 1989: in the 1970s, Altman discovered the existence of precursor tRNA with flanking sequences and was the first to characterize RNase P and its activity in processing of the 5' leader sequence of precursor tRNA. Recent findings also reveal that RNase P has a new function. It has been shown that human nuclear RNase P is required for the normal and efficient transcription of various small noncoding RNAs, such as tRNA, 5S rRNA, SRP RNA and U6 snRNA genes, which are transcribed by RNA polymerase III, one of three major nuclear RNA polymerases in human cells.

Exosome component 10, also known as EXOSC10, is a human gene, the protein product of which is part of the exosome complex and is an autoantigen is patients with certain auto immune diseases, most notably scleromyositis.

Exosome complex exonuclease RRP44 or Dis3 is an enzyme that in humans is encoded by the DIS3 gene. Its protein product is an RNase enzyme homologous to the yeast protein Rrp44, and can be part of the exosome complex in the nucleus of eukaryotic cells.

Ribonuclease P protein subunit p20 is an enzyme that in humans is encoded by the POP7 gene.

Ribonuclease P protein subunit p40 is an enzyme that in humans is encoded by the RPP40 gene.

Ribonucleases P/MRP protein subunit POP1 is a protein that in humans is encoded by the POP1 gene.

Exosome component 8, also known as EXOSC8, is a human gene, the protein product of which is part of the exosome complex.

Exosome component 7, also known as EXOSC7, is a human gene, the protein product of which is part of the exosome complex.

Exosome component 3, also known as EXOSC3, is a human gene, which is part of the exosome complex.

Exosome component 9, also known as EXOSC9, is a human gene, the protein product of which is part of the exosome complex and is an autoantigen is patients with certain auto immune diseases, most notably scleromyositis.

Exosome component 4, also known as EXOSC4, is a human gene, which is part of the exosome complex.

3'-5' exoribonuclease CSL4 homolog is an enzyme that in humans is encoded by the EXOSC1 gene.

Exosome component 5, also known as EXOSC5, is a human gene, which is part of the exosome complex.

Ribonuclease P protein subunit p30 is an enzyme that in humans is encoded by the RPP30 gene.

Ribonuclease P protein subunit p38 is an enzyme that in humans is encoded by the RPP38 gene.

Ribonuclease P protein subunit p14 is an enzyme that in humans is encoded by the RPP14 gene.

RNA component of mitochondrial RNA processing endoribonuclease, also known as RMRP, is a human gene.

Ribonuclease P protein subunit p29 is an enzyme that in humans is encoded by the POP4 gene.

Exosome complex exonuclease MTR3 is an enzyme that in humans is encoded by the EXOSC6 gene.

Ribonuclease H2 subunit A, also known as RNase H2 subunit A, is an enzyme that in humans is encoded by the RNASEH2A gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000167272 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000060152 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ van Eenennaam H, Lugtenberg D, Vogelzangs JH, van Venrooij WJ, Pruijn GJ (Aug 2001). "hPop5, a protein subunit of the human RNase MRP and RNase P endoribonucleases" (PDF). J Biol Chem. 276 (34): 31635–41. doi: 10.1074/jbc.M103399200 . PMID 11413139.
↑ "Entrez Gene: POP5 processing of precursor 5, ribonuclease P/MRP subunit (S. cerevisiae)".

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
van Eenennaam H, Pruijn GJ, van Venrooij WJ (1999). "hPop4: a new protein subunit of the human RNase MRP and RNase P ribonucleoprotein complexes". Nucleic Acids Res. 27 (12): 2465–72. doi:10.1093/nar/27.12.2465. PMC 148449 . PMID 10352175.
Hu RM, Han ZG, Song HD, et al. (2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 97 (17): 9543–8. Bibcode:2000PNAS...97.9543H. doi: 10.1073/pnas.160270997 . PMC 16901 . PMID 10931946.
Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC 310934 . PMID 11042152.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "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. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Welting TJ, van Venrooij WJ, Pruijn GJ (2004). "Mutual interactions between subunits of the human RNase MRP ribonucleoprotein complex". Nucleic Acids Res. 32 (7): 2138–46. doi:10.1093/nar/gkh539. PMC 407822 . PMID 15096576.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi: 10.1016/j.cell.2006.09.026 . PMID 17081983. S2CID 7827573.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000167272 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000060152 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid11413139-5] van Eenennaam H, Lugtenberg D, Vogelzangs JH, van Venrooij WJ, Pruijn GJ (Aug 2001). "hPop5, a protein subunit of the human RNase MRP and RNase P endoribonucleases" (PDF). J Biol Chem. 276 (34): 31635–41. doi: 10.1074/jbc.M103399200 . PMID 11413139.

[entrez-6] "Entrez Gene: POP5 processing of precursor 5, ribonuclease P/MRP subunit (S. cerevisiae)".

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POP5

Related Research Articles

References

Further reading