Matches in DBpedia 2016-04 for { <http://dbpedia.org/resource/SET_domain> ?p ?o }
- SET_domain abstract "The SET domain is a protein domain. It was originally identified as part of a larger conserved region present in the Drosophila Trithorax protein and was subsequently identified in the Drosophila Su(var)3-9 and 'Enhancer of zeste' proteins, from which the acronym SET is derived.The SET domain appears generally as one part of a larger multidomain protein, and recently there were described three structures of very different proteins with distinct domain compositions: Neurospora crassa DIM-5, a member of the Su(var) family of HKMTs which methylate histone H3 on lysine 9,human SET7 (also called SET9), which methylates H3 on lysine 4 and garden pea Rubisco LSMT, an enzyme that does not modify histones, but instead methylates lysine 14 in the flexible tail of the large subunit of the enzyme Rubisco. The SET domain itself turned out to be an uncommon structure. Although in all three studies, electron density maps revealed the location of the AdoMet or AdoHcy cofactor, the SET domain bears no similarity at all to the canonical/AdoMet-dependent methyltransferase fold. Strictly conserved in the C-terminal motif of the SET domain tyrosine could be involved in abstracting a proton from the protonated amino group of the substrate lysine, promoting its nucleophilic attack on the sulphonium methyl group of the AdoMet cofactor. In contrast to the AdoMet-dependent protein methyltranferases of the classical type, which tend to bind their polypeptide substrates on top of the cofactor, it is noted from the Rubisco LSMT structure that the AdoMet seems to bind in a separate cleft, suggesting how a polypeptide substrate could be subjected to multiple rounds of methylation without having to be released from the enzyme. In contrast, SET7/9 is able to add only a single methyl group to its substrate. It has been demonstrated that association of SET domain and myotubularin-related proteins modulates growth control. The SET domain-containing Drosophila melanogaster (Fruit fly) protein, enhancer of zeste, has a function in segment determination and the mammalian homologue may be involved in the regulation of gene transcription and chromatin structure.Histone lysine methylation is part of the histone code that regulated chromatin function and epigenetic control of gene function. Histone lysine methyltransferases (HMTase) differ both in their substrate specificity for the various acceptor lysines as well as in their product specificity for the number of methyl groups (one, two, or three) they transfer. With just one exception, the HMTases belong to SET family that can be classified according to the sequences surrounding the SET domain. Structural studies on the human SET7/9, a mono-methylase, have revealed the molecular basis for the specificity of the enzyme for the histone-target and the roles of the invariant residues in the SET domain in determining the methylation specificities.The pre-SET domain, as found in the SUV39 SET family, contains nine invariant cysteine residues that are grouped into two segments separated by a region of variable length. These 9 cysteines coordinate 3 zinc ions to form a triangular cluster, where each of the zinc ions is coordinated by 4 four cysteines to give a tetrahedral configuration. The function of this domain is structural, holding together 2 long segments of random coils.The C-terminal region including the post-SET domain is disordered when not interacting with a histone tail and in the absence of zinc. The three conserved cysteines in the post-SET domain form a zinc-binding site when coupled to a fourth conserved cysteine in the knot-like structure close to the SET domain active site. The structured post-SET region brings in the C-terminal residues that participate in S-adenosylmethine-binding and histone tail interactions. The three conserved cysteine residues are essential for HMTase activity, as replacement with serine abolishes HMTase activity.".
- SET_domain symbol "SET".
- SET_domain thumbnail PDB_1n3j_EBI.jpg?width=300.
- SET_domain wikiPageID "32548064".
- SET_domain wikiPageLength "8749".
- SET_domain wikiPageOutDegree "98".
- SET_domain wikiPageRevisionID "705625818".
- SET_domain wikiPageWikiLink ASH1L.
- SET_domain wikiPageWikiLink Active_site.
- SET_domain wikiPageWikiLink BAT8.
- SET_domain wikiPageWikiLink Biomolecular_structure.
- SET_domain wikiPageWikiLink Category:Protein_families.
- SET_domain wikiPageWikiLink Cell_growth.
- SET_domain wikiPageWikiLink Chromatin.
- SET_domain wikiPageWikiLink Cis-Regulatory_element.
- SET_domain wikiPageWikiLink Cofactor_(biochemistry).
- SET_domain wikiPageWikiLink Conserved_sequence.
- SET_domain wikiPageWikiLink Cysteine.
- SET_domain wikiPageWikiLink Drosophila.
- SET_domain wikiPageWikiLink EHMT1.
- SET_domain wikiPageWikiLink EHMT2.
- SET_domain wikiPageWikiLink EZH1.
- SET_domain wikiPageWikiLink EZH2.
- SET_domain wikiPageWikiLink Electron.
- SET_domain wikiPageWikiLink Enzyme.
- SET_domain wikiPageWikiLink Epigenetics.
- SET_domain wikiPageWikiLink FP13812.
- SET_domain wikiPageWikiLink Gene.
- SET_domain wikiPageWikiLink Histone.
- SET_domain wikiPageWikiLink Histone_code.
- SET_domain wikiPageWikiLink Homo_sapiens.
- SET_domain wikiPageWikiLink Homology_(biology).
- SET_domain wikiPageWikiLink Ion.
- SET_domain wikiPageWikiLink KMT2A.
- SET_domain wikiPageWikiLink KMT2C.
- SET_domain wikiPageWikiLink Lysine.
- SET_domain wikiPageWikiLink MLL2.
- SET_domain wikiPageWikiLink MLL5.
- SET_domain wikiPageWikiLink Mammal.
- SET_domain wikiPageWikiLink Methyl_group.
- SET_domain wikiPageWikiLink Methylation.
- SET_domain wikiPageWikiLink Methyltransferase.
- SET_domain wikiPageWikiLink Molecular_binding.
- SET_domain wikiPageWikiLink NSD1.
- SET_domain wikiPageWikiLink Nucleic_acid_structure.
- SET_domain wikiPageWikiLink Nucleophile.
- SET_domain wikiPageWikiLink PRDM1.
- SET_domain wikiPageWikiLink PRDM2.
- SET_domain wikiPageWikiLink PRDM5.
- SET_domain wikiPageWikiLink Peptide.
- SET_domain wikiPageWikiLink Product_(chemistry).
- SET_domain wikiPageWikiLink Promoter_(genetics).
- SET_domain wikiPageWikiLink Protein.
- SET_domain wikiPageWikiLink Protein_folding.
- SET_domain wikiPageWikiLink Protein_structure.
- SET_domain wikiPageWikiLink Proton.
- SET_domain wikiPageWikiLink Protonation.
- SET_domain wikiPageWikiLink Regulation.
- SET_domain wikiPageWikiLink Residue_(chemistry).
- SET_domain wikiPageWikiLink SETD1A.
- SET_domain wikiPageWikiLink SETD2.
- SET_domain wikiPageWikiLink SETD3.
- SET_domain wikiPageWikiLink SETD4.
- SET_domain wikiPageWikiLink SETD5.
- SET_domain wikiPageWikiLink SETD6.
- SET_domain wikiPageWikiLink SETD7.
- SET_domain wikiPageWikiLink SETD8.
- SET_domain wikiPageWikiLink SETDB1.
- SET_domain wikiPageWikiLink SETDB2.
- SET_domain wikiPageWikiLink SETMAR.
- SET_domain wikiPageWikiLink SMYD1.
- SET_domain wikiPageWikiLink SMYD3.
- SET_domain wikiPageWikiLink SMYD4.
- SET_domain wikiPageWikiLink SMYD5.
- SET_domain wikiPageWikiLink SUV39H1.
- SET_domain wikiPageWikiLink SUV39H2.
- SET_domain wikiPageWikiLink SUV420H1.
- SET_domain wikiPageWikiLink SUV420H2.
- SET_domain wikiPageWikiLink Sensitivity_and_specificity.
- SET_domain wikiPageWikiLink Sequence_(biology).
- SET_domain wikiPageWikiLink Serine.
- SET_domain wikiPageWikiLink Structural_motif.
- SET_domain wikiPageWikiLink Substrate_(biology).
- SET_domain wikiPageWikiLink Substrate_(chemistry).
- SET_domain wikiPageWikiLink Tetrahedron.
- SET_domain wikiPageWikiLink Transcription_(genetics).
- SET_domain wikiPageWikiLink Tyrosine.
- SET_domain wikiPageWikiLink WBP7.
- SET_domain wikiPageWikiLink WHSC1.
- SET_domain wikiPageWikiLink WHSC1L1.
- SET_domain wikiPageWikiLink Zinc.
- SET_domain wikiPageWikiLinkText "SET domain".
- SET_domain caption "structure and substrate of a histone h3 lysine methyltransferase from paramecium bursaria chlorella virus 1".
- SET_domain interpro "IPR001214".
- SET_domain name "SET".
- SET_domain pfam "PF00856".
- SET_domain scop "1".
- SET_domain smart "SM0468".
- SET_domain symbol "SET".
- SET_domain wikiPageUsesTemplate Template:Infobox_protein_family.