4e53: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 3: / Line 3: @@
 <StructureSection load='4e53' size='340' side='right'caption='[[4e53]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4e53]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E53 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E53 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4e53]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4E53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E53 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4e50|4e50]]</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=4e53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e53 OCA], [https://pdbe.org/4e53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e53 RCSB], [https://www.ebi.ac.uk/pdbsum/4e53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e53 ProSAT]</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=4e53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e53 OCA], [http://pdbe.org/4e53 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e53 RCSB], [http://www.ebi.ac.uk/pdbsum/4e53 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e53 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[[https://www.uniprot.org/uniprot/CALM1_MOUSE CALM1_MOUSE]] 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. Is a regulator of voltage-dependent L-type calcium channels. Mediates calcium-dependent inactivation of CACNA1C. Positively regulates calcium-activated potassium channel activity of KCNN2. Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding. Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2 (By similarity).[UniProtKB:P0DP23][[https://www.uniprot.org/uniprot/NEUM_MOUSE NEUM_MOUSE]] This protein is associated with nerve growth. It is a major component of the motile 'growth cones' that form the tips of elongating axons. Plays a role in axonal and dendritic filopodia induction.[UniProtKB:P17677]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 25: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Kumar, V]]
+[[Category: Mus musculus]]
-[[Category: Sivaraman, J]]
+[[Category: Kumar V]]
-[[Category: Intrinsically unstructured protein]]
+[[Category: Sivaraman J]]
-[[Category: Iq motif]]
-[[Category: Neuromodulin]]
-[[Category: Protein binding]]