SETMAR

SET domain and mariner transposase fusion gene
Rendering based on PDB 3BO5​.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 3BO5​, 3F2K​, 3K9J​, 3K9K​
Identifiers
Symbols	SETMAR ; HsMar1; METNASE; Mar1
External IDs	OMIM: 609834 MGI: 1921979 HomoloGene: 121979 GeneCards: SETMAR Gene
EC number	2.1.1.43
Gene ontology Molecular function • single-stranded DNA endodeoxyribonuclease activity • double-stranded DNA binding • single-stranded DNA binding • endonuclease activity • protein binding • zinc ion binding • histone methyltransferase activity (H3-K4 specific) • protein homodimerization activity • structure-specific DNA binding • DNA topoisomerase binding • histone methyltransferase activity (H3-K36 specific) Cellular component • condensed chromosome • nucleus • site of double-strand break Biological process • DNA double-strand break processing • DNA catabolic process, endonucleolytic • double-strand break repair via nonhomologous end joining • cell proliferation • histone H3-K36 methylation • DNA integration • replication fork processing • mitotic DNA integrity checkpoint • histone H3-K4 methylation • negative regulation of cell cycle arrest • nucleic acid phosphodiester bond hydrolysis • histone H3-K36 dimethylation • positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity • positive regulation of double-strand break repair via nonhomologous end joining • negative regulation of chromosome organization Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6419	74729
Ensembl	ENSG00000170364	ENSMUSG00000034639
UniProt	Q53H47	Q80UJ9
RefSeq (mRNA)	NM_001243723	n/a
RefSeq (protein)	NP_001230652	n/a
Location (UCSC)	Chr 3: 4.3 – 4.32 Mb	Chr 6: 108.03 – 108.04 Mb
PubMed search

Histone-lysine N-methyltransferase SETMAR is an enzyme that in humans is encoded by the SETMAR gene.^[1][2]

Model organisms

Setmar knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Normal
Homozygous Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Abnormal[3]
Clinical chemistry	Normal
Plasma immunoglobulins	Normal
Haematology	Normal
Peripheral blood lymphocytes	Abnormal[4]
Micronucleus test	Normal
Heart weight	Normal
Skin Histopathology	Normal
Brain histopathology	Normal
Salmonella infection	Normal[5]
Citrobacter infection	Normal[6]
All tests and analysis from[7][8]

Model organisms have been used in the study of SETMAR function. A conditional knockout mouse line, called Setmar^{tm1a(EUCOMM)Wtsi[9][10]} was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.^[11][12][13]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.^[7][14] Twenty five tests were carried out on mutant mice and two significant abnormalities were observed.^[7] Homozygous mutant animals of both sex had abnormal retinal pigmentation and morphology, while males also had atypical peripheral blood lymphocyte parameters.^[7]

References

1. Robertson HM, Zumpano KL (Feb 1998). "Molecular evolution of an ancient mariner transposon, Hsmar1, in the human genome". Gene 205 (1-2): 203–17. doi:10.1016/S0378-1119(97)00472-1. PMID 9461395.
2. "Entrez Gene: SETMAR SET domain and mariner transposase fusion gene".
3. "Eye morphology data for Setmar". Wellcome Trust Sanger Institute.
4. "Peripheral blood lymphocytes data for Setmar". Wellcome Trust Sanger Institute.
5. "Salmonella infection data for Setmar". Wellcome Trust Sanger Institute.
6. "Citrobacter infection data for Setmar". Wellcome Trust Sanger Institute.
7. Gerdin, AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
8. Mouse Resources Portal, Wellcome Trust Sanger Institute.
9. "International Knockout Mouse Consortium".
10. "Mouse Genome Informatics".
11. Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
12. Dolgin, Elie (2011). "Mouse library set to be knockout". Nature 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
13. International Mouse Knockout Consortium; Collins, FS; Rossant, J; Wurst, W (2007). "A Mouse for All Reasons". Cell 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
14. van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.

Further reading

• Berry R, Stevens TJ, Walter NA, et al. (1995). "Gene-based sequence-tagged-sites (STSs) as the basis for a human gene map.". Nat. Genet. 10 (4): 415–23. doi:10.1038/ng0895-415. PMID 7670491.
• 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.
• Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
• Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
• 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.
• 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.
• 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.
• Lee SH, Oshige M, Durant ST, et al. (2006). "The SET domain protein Metnase mediates foreign DNA integration and links integration to nonhomologous end-joining repair.". Proc. Natl. Acad. Sci. U.S.A. 102 (50): 18075–80. Bibcode:2005PNAS..10218075L. doi:10.1073/pnas.0503676102. PMC 1312370. PMID 16332963.
• Cordaux R, Udit S, Batzer MA, Feschotte C (2006). "Birth of a chimeric primate gene by capture of the transposase gene from a mobile element.". Proc. Natl. Acad. Sci. U.S.A. 103 (21): 8101–6. Bibcode:2006PNAS..103.8101C. doi:10.1073/pnas.0601161103. PMC 1472436. PMID 16672366.
• Keravala A, Liu D, Lechman ER, et al. (2007). "Hyperactive Himar1 transposase mediates transposition in cell culture and enhances gene expression in vivo.". Hum. Gene Ther. 17 (10): 1006–18. doi:10.1089/hum.2006.17.ft-245. PMID 16989604.
• Liu D, Bischerour J, Siddique A, et al. (2007). "The human SETMAR protein preserves most of the activities of the ancestral Hsmar1 transposase.". Mol. Cell. Biol. 27 (3): 1125–32. doi:10.1128/MCB.01899-06. PMC 1800679. PMID 17130240.
• Miskey C, Papp B, Mátés L, et al. (2007). "The ancient mariner sails again: transposition of the human Hsmar1 element by a reconstructed transposase and activities of the SETMAR protein on transposon ends.". Mol. Cell. Biol. 27 (12): 4589–600. doi:10.1128/MCB.02027-06. PMC 1900042. PMID 17403897.
• Roman Y, Oshige M, Lee YJ, et al. (2007). "Biochemical characterization of a SET and transposase fusion protein, Metnase: its DNA binding and DNA cleavage activity.". Biochemistry 46 (40): 11369–76. doi:10.1021/bi7005477. PMC 3374406. PMID 17877369.