4tvr: Difference between revisions
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New page: '''Unreleased structure''' The entry 4tvr is ON HOLD Authors: Walker, J.R., Dong, A., Zhang, Q., Ong, M., Duan, S., Li, Y., Bountra, C., Weigelt, J., Edwards, A.M., Arrowsmith, C.H., To... |
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==Tandem Tudor and PHD domains of UHRF2== | |||
<StructureSection load='4tvr' size='340' side='right'caption='[[4tvr]], [[Resolution|resolution]] 2.29Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4tvr]] is a 1 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=4TVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TVR FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.29Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=4tvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tvr OCA], [https://pdbe.org/4tvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tvr RCSB], [https://www.ebi.ac.uk/pdbsum/4tvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tvr ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[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 == | |||
[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== | |||
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Arrowsmith CH]] | |||
[[Category: Bountra C]] | |||
[[Category: Dong A]] | |||
[[Category: Duan S]] | |||
[[Category: Edwards AM]] | |||
[[Category: Li Y]] | |||
[[Category: Ong M]] | |||
[[Category: Tong Y]] | |||
[[Category: Walker JR]] | |||
[[Category: Weigelt J]] | |||
[[Category: Zhang Q]] | |||
Latest revision as of 07:23, 27 September 2023
Tandem Tudor and PHD domains of UHRF2
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