2kne: Difference between revisions

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 ==Calmodulin wraps around its binding domain in the plasma membrane CA2+ pump anchored by a novel 18-1 motif==
-<StructureSection load='2kne' size='340' side='right'caption='[[2kne]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2kne' size='340' side='right'caption='[[2kne]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2kne]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KNE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2KNE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2kne]] is a 2 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=2KNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KNE FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CALM, CALM1, CALM2, CALM3, CALML2, CAM, CAM1, CAM2, CAM3, CAMB, CAMC, CAMIII ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), ATP2B4, hCG_18445, RP11-397P13.1-001 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=2kne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kne OCA], [http://pdbe.org/2kne PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2kne RCSB], [http://www.ebi.ac.uk/pdbsum/2kne PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2kne 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=2kne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kne OCA], [https://pdbe.org/2kne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kne RCSB], [https://www.ebi.ac.uk/pdbsum/2kne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kne ProSAT]</span></td></tr>
 </table>
+== Disease ==
+[https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of CPVT4.  The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of LQT14.
 == Function ==
-[[http://www.uniprot.org/uniprot/AT2B4_HUMAN AT2B4_HUMAN]] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of calcium out of the cell.
+[https://www.uniprot.org/uniprot/CALM1_HUMAN CALM1_HUMAN] Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (PubMed:16760425). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).<ref>PMID:16760425</ref> <ref>PMID:23893133</ref> <ref>PMID:26969752</ref> <ref>PMID:27165696</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 38: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Atanasova, E]]
+[[Category: Atanasova E]]
-[[Category: Filoteo, A G]]
+[[Category: Filoteo AG]]
-[[Category: Juranic, N]]
+[[Category: Juranic N]]
-[[Category: Macura, S]]
+[[Category: Macura S]]
-[[Category: Penniston, J T]]
+[[Category: Penniston JT]]
-[[Category: Prendergast, F G]]
+[[Category: Prendergast FG]]
-[[Category: Strehler, E E]]
+[[Category: Strehler EE]]
-[[Category: Acetylation]]
-[[Category: Atp-binding]]
-[[Category: Calcium]]
-[[Category: Calcium pump]]
-[[Category: Calmodulin]]
-[[Category: Hydrolase]]
-[[Category: Isopeptide bond]]
-[[Category: Membrane]]
-[[Category: Metal transport]]
-[[Category: Methylation]]
-[[Category: Nucleotide-binding]]
-[[Category: Phosphoprotein]]
-[[Category: Polymorphism]]
-[[Category: Protein/peptide]]
-[[Category: Transmembrane]]
-[[Category: Ubl conjugation]]