6rcm - Revision history

OCA at 12:18, 24 January 2024

OCA — Wed, 24 Jan 2024 12:18:50 GMT

←Older revision		Revision as of 12:18, 24 January 2024
Line 3:		Line 3:
	<StructureSection load='6rcm' size='340' side='right'caption='[[6rcm]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='6rcm' size='340' side='right'caption='[[6rcm]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6rcm]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RCM OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://proteopedia.org/fgij/fg.htm?mol=6RCM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6rcm]] 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=6RCM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RCM FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K0N:(~{E})-~{N}-(5-~{tert}-butyl-1,3,4-thiadiazol-2-yl)-2-cyano-3-(3-methoxy-4-oxidanyl-phenyl)prop-2-enamide'>K0N</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene~~></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]] 1.7Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6rb1\|6rb1]], [[6rcb\|6rcb]]</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K0N:(~{E})-~{N}-(5-~{tert}-butyl-1,3,4-thiadiazol-2-yl)-2-cyano-3-(3-methoxy-4-oxidanyl-phenyl)prop-2-enamide'>K0N</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=6rcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rcm OCA], [https://pdbe.org/6rcm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rcm RCSB], [https://www.ebi.ac.uk/pdbsum/6rcm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rcm ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://proteopedia.org/fgij/fg.htm?mol=6rcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rcm OCA], [~~http~~://pdbe.org/6rcm PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=6rcm RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/6rcm PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=6rcm ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>	+	[https://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 6rcm" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 6rcm" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Casein kinase 3D structures\|Casein kinase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Non-specific serine/threonine protein kinase~~]]	+	[[Category: Battistutta R]]
-	[[Category: ~~Battistutta, R~~]]	+	[[Category: Dalle Vedove A]]
-	[[Category: Lolli, G]]	+	[[Category: Lolli G]]
-	[[Category: Ribaudo, G]]	+	[[Category: Ribaudo G]]
-	~~[[Category: Vedove, A Dalle~~]]	+	[[Category: Zagotto G]]
-	[[Category: Zagotto, G]]	+	[[Category: Zanforlin E]]
-	[[Category: Zanforlin, E]]	+
-	~~[[Category: Kinase domain]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 06:05, 22 April 2020

OCA — Wed, 22 Apr 2020 06:05:27 GMT

←Older revision		Revision as of 06:05, 22 April 2020
Line 3:		Line 3:
	<StructureSection load='6rcm' size='340' side='right'caption='[[6rcm]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='6rcm' size='340' side='right'caption='[[6rcm]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[6rcm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RCM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RCM FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[6rcm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RCM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RCM FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K0N:(~{E})-~{N}-(5-~{tert}-butyl-1,3,4-thiadiazol-2-yl)-2-cyano-3-(3-methoxy-4-oxidanyl-phenyl)prop-2-enamide'>K0N</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K0N:(~{E})-~{N}-(5-~{tert}-butyl-1,3,4-thiadiazol-2-yl)-2-cyano-3-(3-methoxy-4-oxidanyl-phenyl)prop-2-enamide'>K0N</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6rb1\|6rb1]], [[6rcb\|6rcb]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6rb1\|6rb1]], [[6rcb\|6rcb]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CSNK2A1, CK2A1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6rcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rcm OCA], [http://pdbe.org/6rcm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rcm RCSB], [http://www.ebi.ac.uk/pdbsum/6rcm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rcm ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6rcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rcm OCA], [http://pdbe.org/6rcm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rcm RCSB], [http://www.ebi.ac.uk/pdbsum/6rcm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rcm ProSAT]</span></td></tr>
Line 11:		Line 12:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>		[[http://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Protein kinase CK2 sustains cancer growth, especially in hematological malignancies. Its inhibitor SRPIN803, based on a 6-methylene-5-imino-1,3,4-thiadiazolopyrimidin-7-one scaffold, showed notable specificity. Our synthesis of the initially proposed SRPIN803 resulted in its constitutional isomer SRPIN803-revised, where the 2-cyano-2-propenamide group does not cyclise and fuse to the thiadiazole ring. Its crystallographic structure in complex with CK2alpha identifies the structural determinants of the reported specificity. SRPIN803-revised explores the CK2 open hinge conformation, extremely rare among kinases, also interacting with side chains from this region. Its optimization lead to the more potent compound 4, which inhibits endocellular CK2, significantly affects viability of tumour cells and shows remarkable selectivity on a panel of 320 kinases.
		+
		+	A novel class of selective CK2 inhibitors targeting its open hinge conformation.,Dalle Vedove A, Zonta F, Zanforlin E, Demitri N, Ribaudo G, Cazzanelli G, Ongaro A, Sarno S, Zagotto G, Battistutta R, Ruzzene M, Lolli G Eur J Med Chem. 2020 Mar 25;195:112267. doi: 10.1016/j.ejmech.2020.112267. PMID:32283296<ref>PMID:32283296</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 6rcm" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
	[[Category: Non-specific serine/threonine protein kinase]]		[[Category: Non-specific serine/threonine protein kinase]]

OCA at 06:52, 8 April 2020

OCA — Wed, 08 Apr 2020 06:52:43 GMT

←Older revision		Revision as of 06:52, 8 April 2020
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 6rcm ~~is ON HOLD~~	+	==Human protein kinase CK2 alpha in complex with 2-cyano-2-propenamide compound 3==
-		+	<StructureSection load='6rcm' size='340' side='right'caption='[[6rcm]], [[Resolution\|resolution]] 1.70Å' scene=''>
-	~~Authors~~: ~~Dalle Vedove, A~~., ~~Zanforlin~~, E., ~~Ribaudo~~, G., ~~Zagotto~~, G., ~~Battistutta~~, R., ~~Lolli~~, G.	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[6rcm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RCM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6RCM FirstGlance]. <br>
-	~~Description~~: ~~Human~~ protein kinase ~~CK2 alpha in~~ complex ~~with 2~~-~~cyano~~-2-~~propenamide compound 3~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K0N:(~{E})-~{N}-(5-~{tert}-butyl-1,3,4-thiadiazol-2-yl)-2-cyano-3-(3-methoxy-4-oxidanyl-phenyl)prop-2-enamide'>K0N</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-	[[Category: ~~Unreleased~~ Structures]]	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[6rb1\|6rb1]], [[6rcb\|6rcb]]</td></tr>
-	[[Category: ~~Dalle Vedove~~, A]]	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase Non-specific serine/threonine protein kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.1 2.7.11.1] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6rcm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rcm OCA], [http://pdbe.org/6rcm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rcm RCSB], [http://www.ebi.ac.uk/pdbsum/6rcm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rcm ProSAT]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/CSK21_HUMAN CSK21_HUMAN]] Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine. Regulates numerous cellular processes, such as cell cycle progression, apoptosis and transcription, as well as viral infection. May act as a regulatory node which integrates and coordinates numerous signals leading to an appropriate cellular response. During mitosis, functions as a component of the p53/TP53-dependent spindle assembly checkpoint (SAC) that maintains cyclin-B-CDK1 activity and G2 arrest in response to spindle damage. Also required for p53/TP53-mediated apoptosis, phosphorylating 'Ser-392' of p53/TP53 following UV irradiation. Can also negatively regulate apoptosis. Phosphorylates the caspases CASP9 and CASP2 and the apoptotic regulator NOL3. Phosphorylation protects CASP9 from cleavage and activation by CASP8, and inhibits the dimerization of CASP2 and activation of CASP8. Regulates transcription by direct phosphorylation of RNA polymerases I, II, III and IV. Also phosphorylates and regulates numerous transcription factors including NF-kappa-B, STAT1, CREB1, IRF1, IRF2, ATF1, SRF, MAX, JUN, FOS, MYC and MYB. Phosphorylates Hsp90 and its co-chaperones FKBP4 and CDC37, which is essential for chaperone function. Regulates Wnt signaling by phosphorylating CTNNB1 and the transcription factor LEF1. Acts as an ectokinase that phosphorylates several extracellular proteins. During viral infection, phosphorylates various proteins involved in the viral life cycles of EBV, HSV, HBV, HCV, HIV, CMV and HPV.<ref>PMID:11239457</ref> <ref>PMID:11704824</ref> <ref>PMID:16193064</ref> <ref>PMID:19188443</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Large Structures]]
		+	[[Category: Non-specific serine/threonine protein kinase]]
		+	[[Category: Battistutta, R]]
	[[Category: Lolli, G]]		[[Category: Lolli, G]]
	[[Category: Ribaudo, G]]		[[Category: Ribaudo, G]]
		+	[[Category: Vedove, A Dalle]]
	[[Category: Zagotto, G]]		[[Category: Zagotto, G]]
	[[Category: Zanforlin, E]]		[[Category: Zanforlin, E]]
-	[[Category: ~~Battistutta, R~~]]	+	[[Category: Kinase domain]]
		+	[[Category: Transferase]]

OCA: Protected "6rcm" [edit=sysop:move=sysop]

OCA — Wed, 17 Apr 2019 04:28:22 GMT

Protected "6rcm" [edit=sysop:move=sysop]

←Older revision

Revision as of 04:28, 17 April 2019

OCA: New page: '''Unreleased structure''' The entry 6rcm is ON HOLD Authors: Dalle Vedove, A., Zanforlin, E., Ribaudo, G., Zagotto, G., Battistutta, R., Lolli, G. Description: Human protein kinase CK...

OCA — Wed, 17 Apr 2019 04:28:20 GMT

New page: '''Unreleased structure''' The entry 6rcm is ON HOLD Authors: Dalle Vedove, A., Zanforlin, E., Ribaudo, G., Zagotto, G., Battistutta, R., Lolli, G. Description: Human protein kinase CK...

New page

'''Unreleased structure'''

The entry 6rcm is ON HOLD

Authors: Dalle Vedove, A., Zanforlin, E., Ribaudo, G., Zagotto, G., Battistutta, R., Lolli, G.

Description: Human protein kinase CK2 alpha in complex with 2-cyano-2-propenamide compound 3
[[Category: Unreleased Structures]]
[[Category: Dalle Vedove, A]]
[[Category: Lolli, G]]
[[Category: Ribaudo, G]]
[[Category: Zagotto, G]]
[[Category: Zanforlin, E]]
[[Category: Battistutta, R]]