<http://purl.uniprot.org/SHA-384/AE6EE48347ABCF0120F35EA97E5125FBB48279797AC7C5439AAF04ADB402DA4C8608A0E3BB186D376C2E9C28D209E683> <http://www.w3.org/1999/02/22-rdf-syntax-ns#type> <http://purl.uniprot.org/core/Function_Annotation> .
<http://purl.uniprot.org/SHA-384/AE6EE48347ABCF0120F35EA97E5125FBB48279797AC7C5439AAF04ADB402DA4C8608A0E3BB186D376C2E9C28D209E683> <http://www.w3.org/2000/01/rdf-schema#comment> "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 (By similarity)." .
<http://purl.uniprot.org/uniprot/P60487> <http://purl.uniprot.org/core/annotation> <http://purl.uniprot.org/SHA-384/AE6EE48347ABCF0120F35EA97E5125FBB48279797AC7C5439AAF04ADB402DA4C8608A0E3BB186D376C2E9C28D209E683> .
<http://purl.uniprot.org/uniprot/Q8VD52> <http://purl.uniprot.org/core/annotation> <http://purl.uniprot.org/SHA-384/AE6EE48347ABCF0120F35EA97E5125FBB48279797AC7C5439AAF04ADB402DA4C8608A0E3BB186D376C2E9C28D209E683> .
<http://purl.uniprot.org/uniprot/Q3ZBF9> <http://purl.uniprot.org/core/annotation> <http://purl.uniprot.org/SHA-384/AE6EE48347ABCF0120F35EA97E5125FBB48279797AC7C5439AAF04ADB402DA4C8608A0E3BB186D376C2E9C28D209E683> .
<http://linkedlifedata.com/resource/#_51335A4246390011> <http://www.w3.org/1999/02/22-rdf-syntax-ns#subject> <http://purl.uniprot.org/SHA-384/AE6EE48347ABCF0120F35EA97E5125FBB48279797AC7C5439AAF04ADB402DA4C8608A0E3BB186D376C2E9C28D209E683> .