3i8z: Difference between revisions

Revision as of 08:00, 1 November 2017

Crystal structure of human chromobox homolog 4 (CBX4)

Structural highlights

3i8z is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3i8y, 3i90, 3i91
Gene:	CBX4 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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:https://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:https://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:https://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:https://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:https://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:https://dx.doi.org/10.1074/jbc.M112.390120

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OCA

[1] Kagey MH, Melhuish TA, Wotton D. The polycomb protein Pc2 is a SUMO E3. Cell. 2003 Apr 4;113(1):127-37. PMID:12679040

[2] 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:https://dx.doi.org/M504477200

[3] 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:https://dx.doi.org/S1097-2765(06)00563-6

[4] 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

[5] 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:https://dx.doi.org/10.1074/jbc.M112.390120

[6] Kagey MH, Melhuish TA, Wotton D. The polycomb protein Pc2 is a SUMO E3. Cell. 2003 Apr 4;113(1):127-37. PMID:12679040

[7] 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:https://dx.doi.org/M504477200

[8] 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:https://dx.doi.org/S1097-2765(06)00563-6

[9] 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

[10] 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:https://dx.doi.org/10.1074/jbc.M112.390120

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@@ Line 1: / Line 1: @@
 ==Crystal structure of human chromobox homolog 4 (CBX4)==
 <StructureSection load='3i8z' size='340' side='right' caption='[[3i8z]], [[Resolution|resolution]] 1.51&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3i8y|3i8y]], [[3i90|3i90]], [[3i91|3i91]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CBX4 ([http://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://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3i8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i8z OCA], [http://pdbe.org/3i8z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3i8z RCSB], [http://www.ebi.ac.uk/pdbsum/3i8z PDBsum]</span></td></tr>
+<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=3i8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3i8z OCA], [http://pdbe.org/3i8z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3i8z RCSB], [http://www.ebi.ac.uk/pdbsum/3i8z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3i8z ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 36: / Line 37: @@
 [[Category: Weigelt, J]]
 [[Category: Zhihong, L]]
+[[Category: Alternative splicing]]
 [[Category: Cbx4]]
 [[Category: Chromatin regulator]]
@@ Line 46: / Line 48: @@
 [[Category: Transcription]]
 [[Category: Transcription regulation]]
+[[Category: Ubl conjugation]]
 [[Category: Ubl conjugation pathway]]

3i8z: Difference between revisions

Revision as of 08:00, 1 November 2017

Crystal structure of human chromobox homolog 4 (CBX4)

Structural highlights

Function

Evolutionary Conservation

References

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