3f9w
From Proteopedia
(Difference between revisions)
Line 1: | Line 1: | ||
==Structural Insights into Lysine Multiple Methylation by SET Domain Methyltransferases, SET8-Y334F / H4-Lys20 / AdoHcy== | ==Structural Insights into Lysine Multiple Methylation by SET Domain Methyltransferases, SET8-Y334F / H4-Lys20 / AdoHcy== | ||
- | <StructureSection load='3f9w' size='340' side='right' caption='[[3f9w]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='3f9w' size='340' side='right'caption='[[3f9w]], [[Resolution|resolution]] 1.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3f9w]] is a 8 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3f9w]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F9W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F9W FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zkk|1zkk]], [[3f9x|3f9x]], [[3f9y|3f9y]], [[3f9z|3f9z]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zkk|1zkk]], [[3f9x|3f9x]], [[3f9y|3f9y]], [[3f9z|3f9z]]</div></td></tr> |
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SETD8, KMT5A, PRSET7, SET07, SET8 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SETD8, KMT5A, PRSET7, SET07, SET8 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Histone-lysine_N-methyltransferase Histone-lysine N-methyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.43 2.1.1.43] </span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3f9w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f9w OCA], [https://pdbe.org/3f9w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f9w RCSB], [https://www.ebi.ac.uk/pdbsum/3f9w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f9w ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/SETD8_HUMAN SETD8_HUMAN]] Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis. Nucleosomes are preferred as substrate compared to free histones. Mediates monomethylation of p53/TP53 at 'Lys-382', leading to repress p53/TP53-target genes.<ref>PMID:12086618</ref> <ref>PMID:12121615</ref> <ref>PMID:15200950</ref> <ref>PMID:16517599</ref> <ref>PMID:17707234</ref> <ref>PMID:15933069</ref> <ref>PMID:15933070</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 31: | Line 31: | ||
</div> | </div> | ||
<div class="pdbe-citations 3f9w" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3f9w" style="background-color:#fffaf0;"></div> | ||
+ | |||
+ | ==See Also== | ||
+ | *[[Histone methyltransferase 3D structures|Histone methyltransferase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Line 37: | Line 40: | ||
[[Category: Histone-lysine N-methyltransferase]] | [[Category: Histone-lysine N-methyltransferase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Brunzelle, J S]] | [[Category: Brunzelle, J S]] | ||
[[Category: Couture, J F]] | [[Category: Couture, J F]] |
Revision as of 19:51, 20 October 2021
Structural Insights into Lysine Multiple Methylation by SET Domain Methyltransferases, SET8-Y334F / H4-Lys20 / AdoHcy
|
Categories: Histone-lysine N-methyltransferase | Human | Large Structures | Brunzelle, J S | Couture, J F | Dirk, L M.A | Houtz, R L | Trievel, R C | Acetylation | Alternative splicing | Cell cycle | Cell division | Chromatin regulator | Chromosomal protein | Coiled coil | Dna-binding | Histone | Lysine | Methylation | Methyltransferase | Mitosis | Nucleosome core | Nucleus | Repressor | S-adenosyl-l-methionine | Set | Transcription | Transcription regulation | Transferase