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BOP1
Identifiers
Aliases	BOP1, block of proliferation 1, BOP1 ribosomal biogenesis factor
External IDs	OMIM: 610596; MGI: 1334460; HomoloGene: 6612; GeneCards: BOP1; OMA:BOP1 - orthologs
Gene location (Human) Chr. Chromosome 8 (human) Band 8q24.3 Start 144,262,045 bp End 144,291,438 bp
Gene location (Mouse) Chr. Chromosome 15 (mouse) Band 15 D3|15 35.91 cM Start 76,337,189 bp End 76,361,477 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right lobe of thyroid gland right hemisphere of cerebellum left lobe of thyroid gland Pituitary Gland anterior pituitary right uterine tube gastrocnemius muscle right frontal lobe mucosa of transverse colon apex of heart Top expressed in otic placode saccule otic vesicle epiblast somite embryo embryo yolk sac primitive streak mandibular prominence More reference expression data BioGPS More reference expression data
Gene ontology Molecular function ribonucleoprotein complex binding protein binding RNA binding Cellular component nucleolus nucleus PeBoW complex nucleoplasm preribosome, large subunit precursor ribonucleoprotein complex Biological process ribosomal large subunit biogenesis cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) cell population proliferation ribosome biogenesis regulation of cell cycle rRNA processing maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) ribosomal large subunit assembly regulation of signal transduction by p53 class mediator maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23246 12181 Ensembl ENSG00000261236 ENSG00000285301 ENSMUSG00000022557 UniProt Q14137 P97452 RefSeq (mRNA) NM_015201 NM_013481 RefSeq (protein) NP_056016 NP_038509 Location (UCSC) Chr 8: 144.26 – 144.29 Mb Chr 15: 76.34 – 76.36 Mb PubMed search
Wikidata
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Ribosome biogenesis protein BOP1 is a protein that in humans is encoded by the BOP1 gene. It is a WD40 repeat-containing nucleolar protein involved in rRNA processing, thereby controlling the cell cycle. It is required for the maturation of the 25S and 5.8S ribosomal RNAs. It may serve as an essential factor in ribosome formation that coordinates processing of the spacer regions in pre-rRNA.

Function

The Pes1-Bop1 complex has several components: BOP1, GRWD1, PES1, ORC6L, and RPL3 and is involved in ribosome biogenesis and altered chromosome segregation. The overexpression of BOP1 increases the percentage of multipolar spindles in human cells. Deregulation of the BOP1 pathway may contribute to colorectal tumourigenesis in humans. Elevated levels of Bop1 induces Bop1/WDR12 and Bop1/Pes1 subcomplexes and the assembly and integrity of the PeBoW complex is highly sensitive to changes in Bop1 protein levels.

Nop7p-Erb1p-Ytm1p, found in yeast, is potentially the homologous complex of Pes1-Bop1-WDR12 as it is involved in the control of ribosome biogenesis and S phase entry. The integrity of the PeBoW complex is required for ribosome biogenesis and cell proliferation in mammalian cells. In Giardia, the species specific cytoskeleton protein, beta-giardin, interacts with Bop1.

Structure

BOP1 contains a conserved N-terminal domain, BOP1NT.

References

1. ^ ENSG00000285301 GRCh38: Ensembl release 89: ENSG00000261236, ENSG00000285301 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000022557 – 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.
5. Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N (Mar 1996). "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1". DNA Res. 2 (4): 167–74, 199–210. CiteSeerX 10.1.1.333.6945. doi:10.1093/dnares/2.4.167. PMID 8590280.
6. "Entrez Gene: BOP1 block of proliferation 1".
7. ^ Kim J, Goo SY, Chung HJ, Yang HW, Yong TS, Lee KH, Park SJ (January 2006). "Interaction of beta-giardin with the Bop1 protein in Giardia lamblia". Parasitol. Res. 98 (2): 138–44. doi:10.1007/s00436-005-0040-8. PMID 16362343. S2CID 24519868.
8. Killian A, Sarafan-Vasseur N, Sesboüé R, Le Pessot F, Blanchard F, Lamy A, Laurent M, Flaman JM, Frébourg T (September 2006). "Contribution of the BOP1 gene, located on 8q24, to colorectal tumorigenesis". Genes Chromosomes Cancer. 45 (9): 874–81. doi:10.1002/gcc.20351. PMID 16804918. S2CID 38299400.
9. Rohrmoser M, Hölzel M, Grimm T, Malamoussi A, Harasim T, Orban M, Pfisterer I, Gruber-Eber A, Kremmer E, Eick D (May 2007). "Interdependence of Pes1, Bop1, and WDR12 controls nucleolar localization and assembly of the PeBoW complex required for maturation of the 60S ribosomal subunit". Mol. Cell. Biol. 27 (10): 3682–94. doi:10.1128/MCB.00172-07. PMC 1899993. PMID 17353269.
10. Hölzel M, Rohrmoser M, Schlee M, Grimm T, Harasim T, Malamoussi A, Gruber-Eber A, Kremmer E, Hiddemann W, Bornkamm GW, Eick D (August 2005). "Mammalian WDR12 is a novel member of the Pes1-Bop1 complex and is required for ribosome biogenesis and cell proliferation". J. Cell Biol. 170 (3): 367–78. doi:10.1083/jcb.200501141. PMC 2171466. PMID 16043514.

External links

• Human BOP1 genome location and BOP1 gene details page in the UCSC Genome Browser.

Further reading

• Zhang Y, Koushik S, Dai R, Mivechi NF (1999). "Structural organization and promoter analysis of murine heat shock transcription factor-1 gene". J. Biol. Chem. 273 (49): 32514–21. doi:10.1074/jbc.273.49.32514. PMID 9829985.
• Nakatsura T, Senju S, Yamada K, Jotsuka T, Ogawa M, Nishimura Y (2001). "Gene cloning of immunogenic antigens overexpressed in pancreatic cancer". Biochem. Biophys. Res. Commun. 281 (4): 936–44. doi:10.1006/bbrc.2001.4377. PMID 11237751.
• Pestov DG, Strezoska Z, Lau LF (2001). "Evidence of p53-dependent cross-talk between ribosome biogenesis and the cell cycle: effects of nucleolar protein Bop1 on G(1)/S transition". Mol. Cell. Biol. 21 (13): 4246–55. doi:10.1128/MCB.21.13.4246-4255.2001. PMC 87085. PMID 11390653.
• Pestov DG, Stockelman MG, Strezoska Z, Lau LF (2001). "ERB1, the yeast homolog of mammalian Bop1, is an essential gene required for maturation of the 25S and 5.8S ribosomal RNAs". Nucleic Acids Res. 29 (17): 3621–30. doi:10.1093/nar/29.17.3621. PMC 55883. PMID 11522832.
• Andersen JS, Lyon CE, Fox AH, Leung AK, Lam YW, Steen H, Mann M, Lamond AI (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. Bibcode:2002CBio...12....1A. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298. S2CID 14132033.
• Strezoska Z, Pestov DG, Lau LF (2002). "Functional inactivation of the mouse nucleolar protein Bop1 inhibits multiple steps in pre-rRNA processing and blocks cell cycle progression". J. Biol. Chem. 277 (33): 29617–25. doi:10.1074/jbc.M204381200. PMID 12048210.
• Scherl A, Couté Y, Déon C, Callé A, Kindbeiter K, Sanchez JC, Greco A, Hochstrasser D, Diaz JJ (2003). "Functional proteomic analysis of human nucleolus". Mol. Biol. Cell. 13 (11): 4100–9. doi:10.1091/mbc.E02-05-0271. PMC 133617. PMID 12429849.
• Lapik YR, Fernandes CJ, Lau LF, Pestov DG (2004). "Physical and functional interaction between Pes1 and Bop1 in mammalian ribosome biogenesis". Mol. Cell. 15 (1): 17–29. doi:10.1016/j.molcel.2004.05.020. PMID 15225545.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
• Nousiainen M, Silljé HH, Sauer G, Nigg EA, Körner R (2006). "Phosphoproteome analysis of the human mitotic spindle". Proc. Natl. Acad. Sci. U.S.A. 103 (14): 5391–6. Bibcode:2006PNAS..103.5391N. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
• Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243. S2CID 14294292.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (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.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

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