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| | <StructureSection load='3i8z' size='340' side='right'caption='[[3i8z]], [[Resolution|resolution]] 1.51Å' scene=''> | | <StructureSection load='3i8z' size='340' side='right'caption='[[3i8z]], [[Resolution|resolution]] 1.51Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3i8z]] 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=3I8Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I8Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3i8z]] 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=3I8Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3I8Z FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3i8y|3i8y]], [[3i90|3i90]], [[3i91|3i91]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.51Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBX4 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=3i8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i8z OCA], [https://pdbe.org/3i8z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i8z RCSB], [https://www.ebi.ac.uk/pdbsum/3i8z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i8z 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=3i8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i8z OCA], [https://pdbe.org/3i8z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3i8z RCSB], [https://www.ebi.ac.uk/pdbsum/3i8z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3i8z ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CBX4_HUMAN CBX4_HUMAN]] E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression.<ref>PMID:12679040</ref> <ref>PMID:16061479</ref> <ref>PMID:17018294</ref> <ref>PMID:21282530</ref> <ref>PMID:22825850</ref> Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.<ref>PMID:12679040</ref> <ref>PMID:16061479</ref> <ref>PMID:17018294</ref> <ref>PMID:21282530</ref> <ref>PMID:22825850</ref>
| + | [https://www.uniprot.org/uniprot/CBX4_HUMAN CBX4_HUMAN] E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression.<ref>PMID:12679040</ref> <ref>PMID:16061479</ref> <ref>PMID:17018294</ref> <ref>PMID:21282530</ref> <ref>PMID:22825850</ref> Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.<ref>PMID:12679040</ref> <ref>PMID:16061479</ref> <ref>PMID:17018294</ref> <ref>PMID:21282530</ref> <ref>PMID:22825850</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Amaya, M F]] | + | [[Category: Amaya MF]] |
| - | [[Category: Arrowsmith, C H]] | + | [[Category: Arrowsmith CH]] |
| - | [[Category: Bochkarev, A]] | + | [[Category: Bochkarev A]] |
| - | [[Category: Bountra, C]] | + | [[Category: Bountra C]] |
| - | [[Category: Edwards, A M]] | + | [[Category: Edwards AM]] |
| - | [[Category: Kozieradzki, I]] | + | [[Category: Kozieradzki I]] |
| - | [[Category: Loppnau, P]] | + | [[Category: Loppnau P]] |
| - | [[Category: Min, J]] | + | [[Category: Min J]] |
| - | [[Category: Ouyang, H]] | + | [[Category: Ouyang H]] |
| - | [[Category: Structural genomic]]
| + | [[Category: Weigelt J]] |
| - | [[Category: Weigelt, J]] | + | [[Category: Zhihong L]] |
| - | [[Category: Zhihong, L]] | + | |
| - | [[Category: Alternative splicing]]
| + | |
| - | [[Category: Cbx4]]
| + | |
| - | [[Category: Chromatin regulator]]
| + | |
| - | [[Category: Chromobox homolog 4]]
| + | |
| - | [[Category: Isopeptide bond]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Repressor]]
| + | |
| - | [[Category: Sgc]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Transcription regulation]]
| + | |
| - | [[Category: Ubl conjugation]]
| + | |
| - | [[Category: Ubl conjugation pathway]]
| + | |
| Structural highlights
Function
CBX4_HUMAN E3 SUMO-protein ligase which facilitates SUMO1 conjugation by UBE2I. Involved in the sumoylation of HNRNPK, a p53/TP53 transcriptional coactivator, hence indirectly regulates p53/TP53 transcriptional activation resulting in p21/CDKN1A expression.[1] [2] [3] [4] [5] Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.[6] [7] [8] [9] [10]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Kagey MH, Melhuish TA, Wotton D. The polycomb protein Pc2 is a SUMO E3. Cell. 2003 Apr 4;113(1):127-37. PMID:12679040
- ↑ Long J, Zuo D, Park M. Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates transcriptional repression of E-cadherin. J Biol Chem. 2005 Oct 21;280(42):35477-89. Epub 2005 Aug 1. PMID:16061479 doi:http://dx.doi.org/M504477200
- ↑ Roscic A, Moller A, Calzado MA, Renner F, Wimmer VC, Gresko E, Ludi KS, Schmitz ML. Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity by its substrate protein HIPK2. Mol Cell. 2006 Oct 6;24(1):77-89. PMID:17018294 doi:http://dx.doi.org/S1097-2765(06)00563-6
- ↑ Vandamme J, Volkel P, Rosnoblet C, Le Faou P, Angrand PO. Interaction proteomics analysis of polycomb proteins defines distinct PRC1 complexes in mammalian cells. Mol Cell Proteomics. 2011 Apr;10(4):M110.002642. doi: 10.1074/mcp.M110.002642., Epub 2011 Jan 31. PMID:21282530 doi:10.1074/mcp.M110.002642
- ↑ Pelisch F, Pozzi B, Risso G, Munoz MJ, Srebrow A. DNA damage-induced heterogeneous nuclear ribonucleoprotein K sumoylation regulates p53 transcriptional activation. J Biol Chem. 2012 Aug 31;287(36):30789-99. doi: 10.1074/jbc.M112.390120. Epub, 2012 Jul 23. PMID:22825850 doi:http://dx.doi.org/10.1074/jbc.M112.390120
- ↑ Kagey MH, Melhuish TA, Wotton D. The polycomb protein Pc2 is a SUMO E3. Cell. 2003 Apr 4;113(1):127-37. PMID:12679040
- ↑ Long J, Zuo D, Park M. Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates transcriptional repression of E-cadherin. J Biol Chem. 2005 Oct 21;280(42):35477-89. Epub 2005 Aug 1. PMID:16061479 doi:http://dx.doi.org/M504477200
- ↑ Roscic A, Moller A, Calzado MA, Renner F, Wimmer VC, Gresko E, Ludi KS, Schmitz ML. Phosphorylation-dependent control of Pc2 SUMO E3 ligase activity by its substrate protein HIPK2. Mol Cell. 2006 Oct 6;24(1):77-89. PMID:17018294 doi:http://dx.doi.org/S1097-2765(06)00563-6
- ↑ Vandamme J, Volkel P, Rosnoblet C, Le Faou P, Angrand PO. Interaction proteomics analysis of polycomb proteins defines distinct PRC1 complexes in mammalian cells. Mol Cell Proteomics. 2011 Apr;10(4):M110.002642. doi: 10.1074/mcp.M110.002642., Epub 2011 Jan 31. PMID:21282530 doi:10.1074/mcp.M110.002642
- ↑ Pelisch F, Pozzi B, Risso G, Munoz MJ, Srebrow A. DNA damage-induced heterogeneous nuclear ribonucleoprotein K sumoylation regulates p53 transcriptional activation. J Biol Chem. 2012 Aug 31;287(36):30789-99. doi: 10.1074/jbc.M112.390120. Epub, 2012 Jul 23. PMID:22825850 doi:http://dx.doi.org/10.1074/jbc.M112.390120
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