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| | <StructureSection load='1wy8' size='340' side='right'caption='[[1wy8]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | | <StructureSection load='1wy8' size='340' side='right'caption='[[1wy8]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1wy8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WY8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1WY8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1wy8]] 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=1WY8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WY8 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UHRF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UHRF2 ([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'>[http://proteopedia.org/fgij/fg.htm?mol=1wy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wy8 OCA], [http://pdbe.org/1wy8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wy8 RCSB], [http://www.ebi.ac.uk/pdbsum/1wy8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wy8 ProSAT], [http://www.topsan.org/Proteins/RSGI/1wy8 TOPSAN]</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=1wy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wy8 OCA], [https://pdbe.org/1wy8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wy8 RCSB], [https://www.ebi.ac.uk/pdbsum/1wy8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wy8 ProSAT], [https://www.topsan.org/Proteins/RSGI/1wy8 TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://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. | + | [[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 == |
| - | [[http://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> | + | [[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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
Disease
[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
[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.[1] [2] [3] [4] [5] [6]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Mori T, Li Y, Hata H, Ono K, Kochi H. NIRF, a novel RING finger protein, is involved in cell-cycle regulation. Biochem Biophys Res Commun. 2002 Aug 23;296(3):530-6. PMID:12176013
- ↑ Li Y, Mori T, Hata H, Homma Y, Kochi H. NIRF induces G1 arrest and associates with Cdk2. Biochem Biophys Res Commun. 2004 Jun 25;319(2):464-8. PMID:15178429 doi:http://dx.doi.org/10.1016/j.bbrc.2004.04.190
- ↑ Mori T, Li Y, Hata H, Kochi H. NIRF is a ubiquitin ligase that is capable of ubiquitinating PCNP, a PEST-containing nuclear protein. FEBS Lett. 2004 Jan 16;557(1-3):209-14. PMID:14741369
- ↑ Unoki M, Nishidate T, Nakamura Y. ICBP90, an E2F-1 target, recruits HDAC1 and binds to methyl-CpG through its SRA domain. Oncogene. 2004 Oct 7;23(46):7601-10. PMID:15361834 doi:10.1038/sj.onc.1208053
- ↑ Mori T, Ikeda DD, Fukushima T, Takenoshita S, Kochi H. NIRF constitutes a nodal point in the cell cycle network and is a candidate tumor suppressor. Cell Cycle. 2011 Oct 1;10(19):3284-99. doi: 10.4161/cc.10.19.17176. Epub 2011 Oct, 1. PMID:21952639 doi:http://dx.doi.org/10.4161/cc.10.19.17176
- ↑ Oh Y, Chung KC. UHRF2, a ubiquitin E3 ligase, acts as a small ubiquitin-like modifier E3 ligase for zinc finger protein 131. J Biol Chem. 2013 Mar 29;288(13):9102-11. doi: 10.1074/jbc.M112.438234. Epub 2013, Feb 12. PMID:23404503 doi:http://dx.doi.org/10.1074/jbc.M112.438234
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