BOP1

Block of proliferation 1
Identifiers
Symbols	BOP1 ; KIAA0124
External IDs	OMIM: 610596 MGI: 1334460 HomoloGene: 6612 GeneCards: BOP1 Gene
Gene ontology Molecular function • protein binding • ribonucleoprotein complex binding • poly(A) RNA binding Cellular component • nucleoplasm • ribonucleoprotein complex • preribosome, large subunit precursor • PeBoW complex Biological process • cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) • maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) • cell proliferation • ribosome biogenesis • regulation of cell cycle Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	23246	12181
Ensembl	ENSG00000261236	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: 76.45 – 76.48 Mb
PubMed search

Ribosome biogenesis protein BOP1 is a protein that in humans is encoded by the BOP1 gene.^[1][2]

Function

It is a WD40 repeat-containing nucleolar protein involved in rRNA processing, thereby controlling the cell cycle.^[3] 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. 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.^[4] 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.^[5]

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.^[6] In Giardia, the species specific cytoskeleton protein, beta-giardin, interacts with Bop1.^[3]

Structure

BOP1NT
Identifiers
Symbol	BOP1NT
Pfam	PF08145
InterPro	IPR012953
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

BOP1 contains a conserved N-terminal domain, BOP1NT.

References

1. 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. doi:10.1093/dnares/2.4.167. PMID 8590280.
2. "Entrez Gene: BOP1 block of proliferation 1".
3. 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.
4. 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.
5. 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.
6. 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.

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. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
• 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. doi:10.1038/nature03207. PMID 15635413.
• 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. 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.
• 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.
• 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.

This article incorporates text from the public domain Pfam and InterPro IPR012953