SETD7

Histone-lysine N-methyltransferase SETD7 is an enzyme that in humans is encoded by the SETD7 gene.

SETD7
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1H3I, 1MT6, 1MUF, 1N6A, 1N6C, 1O9S, 1XQH, 2F69, 3CBM, 3CBO, 3CBP, 3M53, 3M54, 3M55, 3M56, 3M57, 3M58, 3M59, 3M5A, 3OS5, 3VUZ, 3VV0, 4E47, 4J7F, 4J8O, 4JDS, 4JLG, 5EG2, 5AYF
Identifiers
Aliases	SETD7, KMT7, SET7, SET7/9, SET9, SET domain containing lysine methyltransferase 7, SET domain containing 7, histone lysine methyltransferase
External IDs	OMIM: 606594; MGI: 1920501; HomoloGene: 12741; GeneCards: SETD7; OMA:SETD7 - orthologs
Gene location (Human) Chr. Chromosome 4 (human) Band 4q31.1 Start 139,495,941 bp End 139,606,699 bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3|3 C Start 51,422,740 bp End 51,468,300 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tibialis anterior muscle deltoid muscle cardiac muscle tissue of right atrium myocardium of left ventricle skin of arm quadriceps femoris muscle Skeletal muscle tissue of rectus abdominis biceps brachii vastus lateralis muscle Skeletal muscle tissue of biceps brachii Top expressed in triceps brachii muscle temporal muscle sternocleidomastoid muscle ciliary body digastric muscle lobe of cerebellum cerebellar vermis ankle lateral geniculate nucleus epithelium of lens More reference expression data BioGPS More reference expression data
Gene ontology Molecular function methyltransferase activity transferase activity p53 binding chromatin binding protein-lysine N-methyltransferase activity protein binding histone-lysine N-methyltransferase activity Cellular component nucleoplasm chromosome nucleolus nucleus Biological process regulation of transcription, DNA-templated peptidyl-lysine monomethylation transcription, DNA-templated cellular response to DNA damage stimulus positive regulation of transcription, DNA-templated peptidyl-lysine methylation methylation heterochromatin organization peptidyl-lysine dimethylation histone lysine methylation response to ethanol regulation of histone H3-K9 methylation chromatin organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 80854 73251 Ensembl ENSG00000145391 ENSMUSG00000037111 UniProt Q8WTS6 Q8VHL1 RefSeq (mRNA) NM_001306199 NM_001306200 NM_030648 NM_080793 RefSeq (protein) NP_001293128 NP_001293129 NP_085151 NP_542983 Location (UCSC) Chr 4: 139.5 – 139.61 Mb Chr 3: 51.42 – 51.47 Mb PubMed search
Wikidata
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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. doi:10.1093/dnares/7.6.347. PMID 11214970.
• 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. doi:10.1016/S0092-8674(02)00964-9. PMID 12372304. S2CID 14727763.
• 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. S2CID 28718612.
• 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.
• 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. PMC 140100. PMID 12514135.
• Xiao B, Jing C, Wilson JR, et al. (2003). "Structure and catalytic mechanism of the human histone methyltransferase SET7/9" (PDF). Nature. 421 (6923): 652–6. Bibcode:2003Natur.421..652X. doi:10.1038/nature01378. PMID 12540855. S2CID 4423407.
• 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. PMC 196026. PMID 12670868.
• 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. CiteSeerX 10.1.1.320.8454. doi:10.1016/S1097-2765(04)00182-0. PMID 15099517.
• 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.
• Chuikov S, Kurash JK, Wilson JR, et al. (2004). "Regulation of p53 activity through lysine methylation". Nature. 432 (7015): 353–60. Bibcode:2004Natur.432..353C. doi:10.1038/nature03117. PMID 15525938. S2CID 4398310.
• 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. S2CID 38483056.
• 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. S2CID 10003129.