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2k28

From Proteopedia

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Revision as of 08:39, 14 June 2023

Solution NMR structure of the chromo domain of the chromobox protein homolog 4

Structural highlights

2k28 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
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: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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k28"

@@ Line 1: / Line 1: @@
 ==Solution NMR structure of the chromo domain of the chromobox protein homolog 4==
-<StructureSection load='2k28' size='340' side='right'caption='[[2k28]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2k28' size='340' side='right'caption='[[2k28]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2k28]] 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=2K28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K28 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2k28]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K28 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K28 FirstGlance]. <br>
-</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>
+</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=2k28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k28 OCA], [https://pdbe.org/2k28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k28 RCSB], [https://www.ebi.ac.uk/pdbsum/2k28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k28 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=2k28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k28 OCA], [https://pdbe.org/2k28 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k28 RCSB], [https://www.ebi.ac.uk/pdbsum/2k28 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k28 ProSAT]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 23: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Arrowsmith, C H]]
+[[Category: Arrowsmith CH]]
-[[Category: Bountra, C]]
+[[Category: Bountra C]]
-[[Category: Edwards, A M]]
+[[Category: Edwards AM]]
-[[Category: Fares, C]]
+[[Category: Fares C]]
-[[Category: Gutmanas, A]]
+[[Category: Gutmanas A]]
-[[Category: Kaustov, L]]
+[[Category: Kaustov L]]
-[[Category: Lemak, A]]
+[[Category: Lemak A]]
-[[Category: Loppnau, P]]
+[[Category: Loppnau P]]
-[[Category: Min, J]]
+[[Category: Min J]]
-[[Category: Quyang, H]]
+[[Category: Quyang H]]
-[[Category: Ravichandran, M]]
+[[Category: Ravichandran M]]
-[[Category: Structural genomic]]
+[[Category: Weigelt J]]
-[[Category: Weigelt, J]]
-[[Category: Alpha/beta protein]]
-[[Category: Alternative splicing]]
-[[Category: Chromatin regulator]]
-[[Category: Nucleus]]
-[[Category: Phosphoprotein]]
-[[Category: Repressor]]
-[[Category: Sgc]]
-[[Category: Transcription]]
-[[Category: Transcription regulation]]
-[[Category: Ubl conjugation]]
-[[Category: Ubl conjugation pathway]]

2k28

From Proteopedia

Revision as of 08:39, 14 June 2023

Solution NMR structure of the chromo domain of the chromobox protein homolog 4

Structural highlights

Function

Evolutionary Conservation

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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