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3oln

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Current revision (09:41, 6 September 2023) (edit) (undo)
 
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<StructureSection load='3oln' size='340' side='right'caption='[[3oln]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3oln' size='340' side='right'caption='[[3oln]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3oln]] is a 2 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=3OLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OLN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3oln]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OLN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OLN FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1z6u|1z6u]], [[1wy8|1wy8]], [[2e6s|2e6s]]</div></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NIRF, RNF107, RNF107;, UHRF2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oln OCA], [https://pdbe.org/3oln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oln RCSB], [https://www.ebi.ac.uk/pdbsum/3oln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oln ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3oln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oln OCA], [https://pdbe.org/3oln PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3oln RCSB], [https://www.ebi.ac.uk/pdbsum/3oln PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3oln ProSAT]</span></td></tr>
</table>
</table>
== Disease ==
== Disease ==
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[[https://www.uniprot.org/uniprot/UHRF2_HUMAN UHRF2_HUMAN]] Associated with various cancers. DNA copy number loss is found in multiple kinds of malignancies originating from the brain, breast, stomach, kidney, hematopoietic tissue and lung.
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[https://www.uniprot.org/uniprot/UHRF2_HUMAN UHRF2_HUMAN] Associated with various cancers. DNA copy number loss is found in multiple kinds of malignancies originating from the brain, breast, stomach, kidney, hematopoietic tissue and lung.
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/UHRF2_HUMAN UHRF2_HUMAN]] E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131.<ref>PMID:12176013</ref> <ref>PMID:15178429</ref> <ref>PMID:14741369</ref> <ref>PMID:15361834</ref> <ref>PMID:21952639</ref> <ref>PMID:23404503</ref>
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[https://www.uniprot.org/uniprot/UHRF2_HUMAN UHRF2_HUMAN] E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131.<ref>PMID:12176013</ref> <ref>PMID:15178429</ref> <ref>PMID:14741369</ref> <ref>PMID:15361834</ref> <ref>PMID:21952639</ref> <ref>PMID:23404503</ref>
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Arrowsmith, C H]]
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[[Category: Arrowsmith CH]]
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[[Category: Avvakumov, G V]]
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[[Category: Avvakumov GV]]
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[[Category: Bochkarev, A]]
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[[Category: Bochkarev A]]
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[[Category: Bountra, C]]
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[[Category: Bountra C]]
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[[Category: Dhe-Paganon, S]]
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[[Category: Dhe-Paganon S]]
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[[Category: Edwards, A M]]
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[[Category: Edwards AM]]
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[[Category: Structural genomic]]
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[[Category: Walker JR]]
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[[Category: Walker, J R]]
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[[Category: Weigelt J]]
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[[Category: Weigelt, J]]
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[[Category: Xue S]]
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[[Category: Xue, S]]
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[[Category: All beta protein]]
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[[Category: Dna-binding]]
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[[Category: Ligase]]
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[[Category: Metal-binding]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Phosphorylation]]
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[[Category: Sgc]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Ubl conjugation pathway]]
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[[Category: Zinc-finger]]
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Current revision

Crystal structure of the SRA domain of E3 ubiquitin-protein ligase UHRF2

PDB ID 3oln

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