SETD7

SET domain containing (lysine methyltransferase) 7
File:PBB Protein SETD7 image.jpg PDB rendering based on 1h3i.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1h3i​, 1mt6​, 1muf​, 1n6a​, 1n6c​, 1o9s​, 1xqh​, 2f69​
Identifiers
Symbols	SETD7 ; SET7; FLJ21193; KIAA1717; SET7/9; SET9
External IDs	Template:OMIM5 Template:MGI HomoloGene: 12741
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
File:PBB GE SETD7 gnf1h04321 at tn.png
File:PBB GE SETD7 gnf1h08582 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

SET domain containing (lysine methyltransferase) 7, also known as SETD7, is a human gene.

Further reading

• Nagase T, Kikuno R, Hattori A; et al. (2001). "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 7 (6): 347–55. PMID 11214970.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Wang H, Cao R, Xia L; et al. (2002). "Purification and functional characterization of a histone H3-lysine 4-specific methyltransferase". Mol. Cell. 8 (6): 1207–17. PMID 11779497.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Nishioka K, Chuikov S, Sarma K; et al. (2002). "Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation". Genes Dev. 16 (4): 479–89. doi:10.1101/gad.967202. PMID 11850410.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Wilson JR, Jing C, Walker PA; et al. (2002). "Crystal structure and functional analysis of the histone methyltransferase SET7/9". Cell. 111 (1): 105–15. PMID 12372304.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Jacobs SA, Harp JM, Devarakonda S; et al. (2002). "The active site of the SET domain is constructed on a knot". Nat. Struct. Biol. 9 (11): 833–8. doi:10.1038/nsb861. PMID 12389038.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kwon T, Chang JH, Kwak E; et al. (2003). "Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet". EMBO J. 22 (2): 292–303. doi:10.1093/emboj/cdg025. PMID 12514135.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Xiao B, Jing C, Wilson JR; et al. (2003). "Structure and catalytic mechanism of the human histone methyltransferase SET7/9". Nature. 421 (6923): 652–6. doi:10.1038/nature01378. PMID 12540855.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Wysocka J, Myers MP, Laherty CD; et al. (2003). "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1". Genes Dev. 17 (7): 896–911. doi:10.1101/gad.252103. PMID 12670868.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kouskouti A, Scheer E, Staub A; et al. (2004). "Gene-specific modulation of TAF10 function by SET9-mediated methylation". Mol. Cell. 14 (2): 175–82. PMID 15099517.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Chuikov S, Kurash JK, Wilson JR; et al. (2004). "Regulation of p53 activity through lysine methylation". Nature. 432 (7015): 353–60. doi:10.1038/nature03117. PMID 15525938.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Couture JF, Collazo E, Hauk G, Trievel RC (2006). "Structural basis for the methylation site specificity of SET7/9". Nat. Struct. Mol. Biol. 13 (2): 140–6. doi:10.1038/nsmb1045. PMID 16415881.CS1 maint: Multiple names: authors list (link)
• Hayakawa T, Ohtani Y, Hayakawa N; et al. (2007). "RBP2 is an MRG15 complex component and down-regulates intragenic histone H3 lysine 4 methylation". Genes Cells. 12 (6): 811–26. doi:10.1111/j.1365-2443.2007.01089.x. PMID 17573780.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)