Summary: BOP1NT (NUC169) domain
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BOP1 Edit Wikipedia article
| Block of proliferation 1 | |||||||||||||
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| Identifiers | |||||||||||||
| Symbols | BOP1; KIAA0124 | ||||||||||||
| External IDs | OMIM: 610596 MGI: 1334460 HomoloGene: 6612 GeneCards: BOP1 Gene | ||||||||||||
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| RNA expression pattern | |||||||||||||
| More reference expression data | |||||||||||||
| Orthologs | |||||||||||||
| Species | Human | Mouse | |||||||||||
| Entrez | 23246 | 12181 | |||||||||||
| Ensembl | ENSG00000170727 | ENSMUSG00000022557 | |||||||||||
| UniProt | Q14137 | P97452 | |||||||||||
| RefSeq (mRNA) | NM_015201.3 | NM_013481.1 | |||||||||||
| RefSeq (protein) | NP_056016.1 | NP_038509.1 | |||||||||||
| Location (UCSC) | Chr 8: 145.49 – 145.52 Mb |
Chr 15: 76.45 – 76.48 Mb |
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| PubMed search | [1] | [2] | |||||||||||
| BOP1NT | |||||||||
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| Identifiers | |||||||||
| Symbol | BOP1NT | ||||||||
| Pfam | PF08145 | ||||||||
| InterPro | IPR012953 | ||||||||
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Ribosome biogenesis protein BOP1 is a protein that in humans is encoded by the BOP1 gene.[1][2] 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]
BOP1 contains a conserved N-terminal domain, BOP1NT.
[edit] References
- ^ 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.
- ^ "Entrez Gene: BOP1 block of proliferation 1". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23246.
- ^ a b 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): 138â44. doi:10.1007/s00436-005-0040-8. PMID 16362343.
- ^ Killian A, Sarafan-Vasseur N, Sesboue R, Le Pessot F, Blanchard F, Lamy A, Laurent M, Flaman JM, Frebourg T (September 2006). "Contribution of the BOP1 gene, located on 8q24, to colorectal tumorigenesis". Genes Chromosomes Cancer 45 (9): 874â81. doi:10.1002/gcc.20351. PMID 16804918.
- ^ Rohrmoser M, Holzel 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): 3682â94. doi:10.1128/MCB.00172-07. PMC 1899993. PMID 17353269. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1899993/.
- ^ Holzel 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): 367â78. doi:10.1083/jcb.200501141. PMC 2171466. PMID 16043514. //www.ncbi.nlm.nih.gov/pmc/articles/PMC2171466/.
[edit] 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, et al. (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. //www.ncbi.nlm.nih.gov/pmc/articles/PMC87085/.
- 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. //www.ncbi.nlm.nih.gov/pmc/articles/PMC55883/.
- Andersen JS, Lyon CE, Fox AH, et al. (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, et al. (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. //www.ncbi.nlm.nih.gov/pmc/articles/PMC133617/.
- 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. //www.ncbi.nlm.nih.gov/pmc/articles/PMC139241/.
- 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.
- 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. //www.ncbi.nlm.nih.gov/pmc/articles/PMC528928/.
- Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
- Nousiainen M, Silljé HH, Sauer G, et al. (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. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1459365/.
- Beausoleil SA, Villén J, Gerber SA, et al. (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, 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.
- Ewing RM, Chu P, Elisma F, et al. (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. //www.ncbi.nlm.nih.gov/pmc/articles/PMC1847948/.
This article incorporates text from the public domain Pfam and InterPro IPR012953
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BOP1NT (NUC169) domain Provide feedback
This N terminal domain is found in BOP1-like WD40 proteins [1].
Literature references
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Staub E, Fiziev P, Rosenthal A, Hinzmann B; , Bioessays 2004;26:567-581.: Insights into the evolution of the nucleolus by an analysis of its protein domain repertoire. PUBMED:15112237 EPMC:15112237
External database links
| PANDIT: | PF08145 |
| Pseudofam: | PF08145 |
| SYSTERS: | BOP1NT |
This tab holds annotation information from the InterPro database.
InterPro entry IPR012953
This domain is found in the N-terminal region of BOP1-like WD40 proteins. Bop1 is a nucleolar protein involved in rRNA processing, thereby controlling the cell cycle [PUBMED:16362343]. 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.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Biological process | regulation of cell cycle (GO:0051726) |
| rRNA processing (GO:0006364) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (38) |
Full (353) |
Representative proteomes | NCBI (359) |
Meta (9) |
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| RP15 (96) |
RP35 (148) |
RP55 (210) |
RP75 (249) |
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| Jalview | ||||||||
| HTML | ||||||||
| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (38) |
Full (353) |
Representative proteomes | NCBI (359) |
Meta (9) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (96) |
RP35 (148) |
RP55 (210) |
RP75 (249) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
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Curation
| Seed source: | Staub E |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Staub E, Bateman A, Mistry J |
| Number in seed: | 38 |
| Number in full: | 353 |
| Average length of the domain: | 244.50 aa |
| Average identity of full alignment: | 45 % |
| Average coverage of the sequence by the domain: | 35.02 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 260 | ||||||||||||
| Family (HMM) version: | 7 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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