4tvr: Difference between revisions

Revision as of 13:00, 24 June 2015

Tandem Tudor and PHD domains of UHRF2

Structural highlights

4tvr is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	UNX, ZN
Related:	3oln, 1z6u
Resources:	FirstGlance, OCA, RCSB, PDBsum

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]

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:https://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:https://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:https://dx.doi.org/10.1074/jbc.M112.438234

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OCA

[1] 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

[2] 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:https://dx.doi.org/10.1016/j.bbrc.2004.04.190

[3] 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

[4] 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

[5] 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:https://dx.doi.org/10.4161/cc.10.19.17176

[6] 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:https://dx.doi.org/10.1074/jbc.M112.438234

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Tandem Tudor and PHD domains of UHRF2==
+<StructureSection load='4tvr' size='340' side='right' caption='[[4tvr]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
-The entry 4tvr is ON HOLD  until Aug 22 2016
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4tvr]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TVR FirstGlance]. <br>
-Authors: Walker, J.R., Dong, A., Zhang, Q., Ong, M., Duan, S., Li, Y., Bountra, C., Weigelt, J., Edwards, A.M., Arrowsmith, C.H., Tong, Y., STRUCTURAL GENOMICS CONSORTIUM (SGC)
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3oln|3oln]], [[1z6u|1z6u]]</td></tr>
-Description: Tandem Tudor and PHD domains of UHRF2
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tvr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4tvr RCSB], [http://www.ebi.ac.uk/pdbsum/4tvr PDBsum]</span></td></tr>
-[[Category: Unreleased Structures]]
+</table>
+== 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.
+== 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>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Arrowsmith, C H]]
+[[Category: Bountra, C]]
 [[Category: Dong, A]]
+[[Category: Duan, S]]
+[[Category: Edwards, A M]]
 [[Category: Li, Y]]
-[[Category: Walker, J.R]]
-[[Category: Bountra, C]]
-[[Category: Arrowsmith, C.H]]
 [[Category: Ong, M]]
-[[Category: Duan, S]]
+[[Category: Structural genomic]]
 [[Category: Tong, Y]]
-[[Category: Edwards, A.M]]
+[[Category: Walker, J R]]
-[[Category: Structural Genomics Consortium (Sgc)]]
 [[Category: Weigelt, J]]
 [[Category: Zhang, Q]]
+[[Category: Ligase]]
+[[Category: Phd]]
+[[Category: Tandem tudor]]

4tvr: Difference between revisions

Revision as of 13:00, 24 June 2015

Tandem Tudor and PHD domains of UHRF2

Structural highlights

Disease

Function

References

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