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. Homodimer. Ubiquitous. Highly expressed in all the regions of central nerve system except the spinal cord. Also expressed at high level in liver and testis. In fetus, it is weakly expressed in all organs except brain. Inhibited by NaF, Zn(2+), Ca(2+), Mn(2+) and EDTA. Belongs to the HAD-like hydrolase superfamily. Note: This description may include information from UniProtKB.
Protein type: EC 184.108.40.206; EC 220.127.116.11; Cell cycle regulation; Cofactor and Vitamin Metabolism - vitamin B6; Protein phosphatase, Ser/Thr (non-receptor)
Molecular Function: protein binding; phosphoserine phosphatase activity; heat shock protein binding; magnesium ion binding; phosphoprotein phosphatase activity; pyridoxal phosphatase activity
Biological Process: actin rod formation; positive regulation of actin filament depolymerization; pyridoxal phosphate catabolic process; regulation of mitosis; protein amino acid dephosphorylation; regulation of cytokinesis
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.