The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

SETD7  -  SET domain containing (lysine...

Homo sapiens

Synonyms: H3-K4-HMTase SETD7, Histone H3-K4 methyltransferase SETD7, Histone-lysine N-methyltransferase SETD7, KIAA1717, KMT7, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of SETD7

  • To delineate the underlying mechanism, we investigated the role of two H3K4 methyltransferases, Set1 and Set7/9, in the lytic infection of HSV-1 [1].

High impact information on SETD7

  • Set9 methylates specifically lysine 4 (K4) of histone H3 (H3-K4) and potentiates transcription activation [2].
  • Methylation of histone H3-K4 by Set9 precludes the association of NuRD with the H3 tail [2].
  • We demonstrate that SET7/9 can transfer two but not three methyl groups to unmodified Lys4 of H3 without substrate dissociation [3].
  • Here we report the structure of the SET7/9 protein in the absence and presence of its cofactor product, S-adenosyl-L-homocysteine (AdoHcy) [4].
  • Genotyping of Weber Screening Set 9 (387 short tandem-repeat polymorphisms with average spacing approximately 9 cM [range 1-19 cM]) was performed by the Mammalian Genotyping Service of Marshfield Laboratory. Presented here are the results for the 366 autosomal markers [5].

Biological context of SETD7


Associations of SETD7 with chemical compounds

  • Collectively, our data reveal that SET7/9 recognizes a conserved K/R-S/T/A motif preceding the lysine substrate and has a propensity to bind aspartates and asparagines on the C-terminal side of the lysine target [6].
  • Chromatin immunoprecipitation revealed that SET7/9 small interfering RNA could reduce TNF-alpha-induced recruitment of NF-kappaB p65 to inflammatory gene promoters [9].

Regulatory relationships of SETD7

  • Set9 regulates the expression of p53 target genes in a manner dependent on the p53-methylation site [7].

Other interactions of SETD7

  • Human SET7/9 is a protein lysine methyltransferase (PKMT) that methylates histone H3, the tumor suppressor p53 and the TBP-associated factor TAF10 [6].
  • Thus, translocations of the MLL gene, by itself coding for a histone H3K4 methyltransferase, are presumably not randomly chosen, rather functionally selected.Leukemia (2006) 20, 777-784. doi:10.1038/sj.leu.2404150; published online 2 March 2006 [10].


  1. Trimethylation of histone H3 lysine 4 by Set1 in the lytic infection of human herpes simplex virus 1. Huang, J., Kent, J.R., Placek, B., Whelan, K.A., Hollow, C.M., Zeng, P.Y., Fraser, N.W., Berger, S.L. J. Virol. (2006) [Pubmed]
  2. Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation. Nishioka, K., Chuikov, S., Sarma, K., Erdjument-Bromage, H., Allis, C.D., Tempst, P., Reinberg, D. Genes Dev. (2002) [Pubmed]
  3. Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet. Kwon, T., Chang, J.H., Kwak, E., Lee, C.W., Joachimiak, A., Kim, Y.C., Lee, J., Cho, Y. EMBO J. (2003) [Pubmed]
  4. The active site of the SET domain is constructed on a knot. Jacobs, S.A., Harp, J.M., Devarakonda, S., Kim, Y., Rastinejad, F., Khorasanizadeh, S. Nat. Struct. Biol. (2002) [Pubmed]
  5. Genome scan for loci involved in cleft lip with or without cleft palate, in Chinese multiplex families. Marazita, M.L., Field, L.L., Cooper, M.E., Tobias, R., Maher, B.S., Peanchitlertkajorn, S., Liu, Y.E. Am. J. Hum. Genet. (2002) [Pubmed]
  6. Structural basis for the methylation site specificity of SET7/9. Couture, J.F., Collazo, E., Hauk, G., Trievel, R.C. Nat. Struct. Mol. Biol. (2006) [Pubmed]
  7. Regulation of p53 activity through lysine methylation. Chuikov, S., Kurash, J.K., Wilson, J.R., Xiao, B., Justin, N., Ivanov, G.S., McKinney, K., Tempst, P., Prives, C., Gamblin, S.J., Barlev, N.A., Reinberg, D. Nature (2004) [Pubmed]
  8. Repression of p53 activity by Smyd2-mediated methylation. Huang, J., Perez-Burgos, L., Placek, B.J., Sengupta, R., Richter, M., Dorsey, J.A., Kubicek, S., Opravil, S., Jenuwein, T., Berger, S.L. Nature (2006) [Pubmed]
  9. Role of the histone H3 lysine 4 methyltransferase, SET7/9, in the regulation of NF-kappaB-dependent inflammatory genes. Relevance to diabetes and inflammation. Li, Y., Reddy, M.A., Miao, F., Shanmugam, N., Yee, J.K., Hawkins, D., Ren, B., Natarajan, R. J. Biol. Chem. (2008) [Pubmed]
  10. The MLL recombinome of acute leukemias. Meyer, C., Schneider, B., Jakob, S., Strehl, S., Attarbaschi, A., Schnittger, S., Schoch, C., Jansen, M.W., van Dongen, J.J., den Boer, M.L., Pieters, R., Ennas, M.G., Angelucci, E., Koehl, U., Greil, J., Griesinger, F., Zur Stadt, U., Eckert, C., Szczepański, T., Niggli, F.K., Schäfer, B.W., Kempski, H., Brady, H.J., Zuna, J., Trka, J., Nigro, L.L., Biondi, A., Delabesse, E., Macintyre, E., Stanulla, M., Schrappe, M., Haas, O.A., Burmeister, T., Dingermann, T., Klingebiel, T., Marschalek, R. Leukemia (2006) [Pubmed]
WikiGenes - Universities