2oyc
From Proteopedia
(Difference between revisions)
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<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=2oyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oyc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2oyc RCSB], [http://www.ebi.ac.uk/pdbsum/2oyc PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/2oyc TOPSAN]</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=2oyc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oyc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2oyc RCSB], [http://www.ebi.ac.uk/pdbsum/2oyc PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/2oyc TOPSAN]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PLPP_HUMAN PLPP_HUMAN]] Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho-tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP.<ref>PMID:14522954</ref> <ref>PMID:15580268</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 08:53, 24 December 2014
Crystal structure of human pyridoxal phosphate phosphatase
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