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2ybx
From Proteopedia
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<StructureSection load='2ybx' size='340' side='right'caption='[[2ybx]], [[Resolution|resolution]] 2.56Å' scene=''> | <StructureSection load='2ybx' size='340' side='right'caption='[[2ybx]], [[Resolution|resolution]] 2.56Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2ybx]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2ybx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YBX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YBX FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene></td></tr> | ||
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/1-phosphatidylinositol-5-phosphate_4-kinase 1-phosphatidylinositol-5-phosphate 4-kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.149 2.7.1.149] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ybx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ybx OCA], [https://pdbe.org/2ybx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ybx RCSB], [https://www.ebi.ac.uk/pdbsum/2ybx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ybx ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/PI42A_HUMAN PI42A_HUMAN]] Precursor B-cell acute lymphoblastic leukemia. |
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/PI42A_HUMAN PI42A_HUMAN]] Catalyzes the phosphorylation of phosphatidylinositol 5-phosphate (PtdIns5P) on the fourth hydroxyl of the myo-inositol ring, to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). May exert its function by regulating the levels of PtdIns5P, which functions in the cytosol by increasing AKT activity and in the nucleus signals through ING2. May regulate the pool of cytosolic PtdIns5P in response to the activation of tyrosine phosphorylation. May negatively regulate insulin-stimulated glucose uptake by lowering the levels of PtdIns5P. May be involved in thrombopoiesis, and the terminal maturation of megakaryocytes and regulation of their size.<ref>PMID:18364242</ref> |
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 12:26, 27 April 2022
Crystal Structure of Human Phosphatidylinositol-5-phosphate 4-kinase type-2 alpha
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Categories: 1-phosphatidylinositol-5-phosphate 4-kinase | Human | Large Structures | Arrowsmith, C H | Berglund, H | Bountra, C | Collins, R | Edwards, A M | Ekblad, T | Flodin, S | Graslund, S | Karlberg, T | Kotenyova, T | Kouznetsova, E | Moche, M | Nordlund, P | Nyman, T | Persson, C | Schuler, H | Siponen, M I | Thorsell, A G | Tresaugues, L | Wahlberg, E | Weigelt, J | Kinase | Signalling | Transferase
