This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2jv0
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
==SET domain of RIZ1 tumor suppressor (PRDM2)== | ==SET domain of RIZ1 tumor suppressor (PRDM2)== | ||
| - | <StructureSection load='2jv0' size='340' side='right' caption='[[2jv0]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''> | + | <StructureSection load='2jv0' size='340' side='right'caption='[[2jv0]], [[NMR_Ensembles_of_Models | 16 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2jv0]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2jv0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JV0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JV0 FirstGlance]. <br> |
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IAS:BETA-L-ASPARTIC+ACID'>IAS</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=IAS:BETA-L-ASPARTIC+ACID'>IAS</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qpw|2qpw]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qpw|2qpw]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRDM2, RIZ ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRDM2, RIZ ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2jv0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jv0 OCA], [https://pdbe.org/2jv0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jv0 RCSB], [https://www.ebi.ac.uk/pdbsum/2jv0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jv0 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/PRDM2_HUMAN PRDM2_HUMAN]] S-adenosyl-L-methionine-dependent histone methyltransferase that specifically methylates 'Lys-9' of histone H3. May function as a DNA-binding transcription factor. Binds to the macrophage-specific TPA-responsive element (MTE) of the HMOX1 (heme oxygenase 1) gene and may act as a transcriptional activator of this gene.<ref>PMID:14633678</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 35: | Line 35: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Briknarova, K]] | [[Category: Briknarova, K]] | ||
[[Category: Activator]] | [[Category: Activator]] | ||
Current revision
SET domain of RIZ1 tumor suppressor (PRDM2)
| |||||||||||
Categories: Human | Large Structures | Briknarova, K | Activator | Alternative initiation | Dna-binding | Histone lysine methyltransferase | Hkmt | Metal-binding | Nucleus | Phosphorylation | Pr domain | Prdm2 | Protein lysine methyltransferase | Riz1 | Set domain | Transcription | Transcription regulation | Zinc-finger

