1ll8
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ll8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LL8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ll8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LL8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LL8 FirstGlance]. <br> | ||
- | </td></tr><tr><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> | + | </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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ll8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ll8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ll8 RCSB], [http://www.ebi.ac.uk/pdbsum/1ll8 PDBsum]</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=1ll8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ll8 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ll8 RCSB], [http://www.ebi.ac.uk/pdbsum/1ll8 PDBsum]</span></td></tr> |
- | <table> | + | </table> |
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/PASK_HUMAN PASK_HUMAN]] Serine/threonine-protein kinase involved in energy homeostasis and protein translation. Phosphorylates EEF1A1, GYS1, PDX1 and RPS6. Probably plays a role under changing environmental conditions (oxygen, glucose, nutrition), rather than under standard conditions. Acts as a sensor involved in energy homeostasis: regulates glycogen synthase synthesis by mediating phosphorylation of GYS1, leading to GYS1 inactivation. May be involved in glucose-stimulated insulin production in pancreas and regulation of glucagon secretion by glucose in alpha cells; however such data require additional evidences. May play a role in regulation of protein translation by phosphorylating EEF1A1, leading to increase translation efficiency. May also participate to respiratory regulation.<ref>PMID:16275910</ref> <ref>PMID:17052199</ref> <ref>PMID:17595531</ref> <ref>PMID:21181396</ref> <ref>PMID:21418524</ref> <ref>PMID:20943661</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Non-specific serine/threonine protein kinase]] | [[Category: Non-specific serine/threonine protein kinase]] | ||
- | [[Category: Amezcua, C A | + | [[Category: Amezcua, C A]] |
- | [[Category: Gardner, K H | + | [[Category: Gardner, K H]] |
- | [[Category: Harper, S M | + | [[Category: Harper, S M]] |
- | [[Category: Rutter, J | + | [[Category: Rutter, J]] |
[[Category: Kinase regulation]] | [[Category: Kinase regulation]] | ||
[[Category: Ligand binding]] | [[Category: Ligand binding]] |
Revision as of 12:44, 25 December 2014
Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation
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