3rd2

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<StructureSection load='3rd2' size='340' side='right'caption='[[3rd2]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='3rd2' size='340' side='right'caption='[[3rd2]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rd2]] is a 1 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=3RD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RD2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rd2]] 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=3RD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RD2 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NFATC2IP, NIP45 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 1.6&#8491;</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=3rd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rd2 OCA], [https://pdbe.org/3rd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rd2 RCSB], [https://www.ebi.ac.uk/pdbsum/3rd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rd2 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=3rd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rd2 OCA], [https://pdbe.org/3rd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rd2 RCSB], [https://www.ebi.ac.uk/pdbsum/3rd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rd2 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/NF2IP_HUMAN NF2IP_HUMAN]] In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter; this leads to enhancement of histone H4 'Arg-3'-methylation and facilitates subsequent histone acetylation at the IL4 locus, thus promotes robust cytokine expression (By similarity). Down-regulates formation of poly-SUMO chains by UBE2I/UBC9 (By similarity).
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[https://www.uniprot.org/uniprot/NF2IP_HUMAN NF2IP_HUMAN] In T-helper 2 (Th2) cells, regulates the magnitude of NFAT-driven transcription of a specific subset of cytokine genes, including IL3, IL4, IL5 and IL13, but not IL2. Recruits PRMT1 to the IL4 promoter; this leads to enhancement of histone H4 'Arg-3'-methylation and facilitates subsequent histone acetylation at the IL4 locus, thus promotes robust cytokine expression (By similarity). Down-regulates formation of poly-SUMO chains by UBE2I/UBC9 (By similarity).
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Global sumoylation, SUMO chain formation and genome stabilization are all outputs generated by a limited repertoire of enzymes. Mechanisms driving selectivity for each of these processes are largely uncharacterized. Here, through crystallographic analyses we show that the SUMO E2 Ubc9 forms a non-covalent complex with a SUMO-like domain of Rad60 (SLD2). Ubc9:SLD2 and Ubc9:SUMO non-covalent complexes are structurally analogous, suggesting that differential recruitment of Ubc9 by SUMO or Rad60 provides a novel means for such selectivity. Indeed, deconvoluting Ubc9 function by disrupting either the Ubc9:SLD2 or Ubc9:SUMO non-covalent complex reveals distinct roles in facilitating sumoylation. Ubc9:SLD2 acts in the Nse2 SUMO E3 ligase-dependent pathway for DNA repair, whereas Ubc9:SUMO instead promotes global sumoylation and chain formation, via the Pli1 E3 SUMO ligase. Moreover, this Pli1-dependent SUMO chain formation causes the genome instability phenotypes of SUMO-targeted ubiquitin ligase (STUbL) mutants. Overall, we determine that unexpectedly, Ubc9 non-covalent partner choice dictates the role of sumoylation in distinct cellular pathways.
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DNA Repair and Global Sumoylation are Regulated by Distinct Ubc9 Non-covalent Complexes.,Prudden J, Perry JJ, Nie M, Vashisht AA, Arvai AS, Hitomi C, Guenther G, Wohlschlegel JA, Tainer JA, Boddy MN Mol Cell Biol. 2011 Mar 28. PMID:21444718<ref>PMID:21444718</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3rd2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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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: Arvai, A S]]
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[[Category: Arvai AS]]
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[[Category: Perry, J J.P]]
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[[Category: Perry JJP]]
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[[Category: Tainer, J A]]
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[[Category: Tainer JA]]
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[[Category: Protein:protein interaction]]
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[[Category: Sumo-like domain 2]]
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[[Category: Transcription]]
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[[Category: Ubc9]]
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Current revision

NIP45 SUMO-like Domain 2

PDB ID 3rd2

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