CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019269
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyridoxal phosphate phosphatase 
Protein Synonyms/Alias
 PLP phosphatase; Chronophin 
Gene Name
 PDXP 
Gene Synonyms/Alias
 CIN; PLP; PLPP 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
52ERLARAGKAALFVSNubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
Functional Description
 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. 
Sequence Annotation
 REGION 58 62 Substrate binding.
 ACT_SITE 25 25 Nucleophile.
 ACT_SITE 27 27 Proton donor (Probable).
 METAL 25 25 Magnesium.
 METAL 27 27 Magnesium; via carbonyl oxygen.
 METAL 238 238 Magnesium.
 BINDING 182 182 Substrate.
 BINDING 213 213 Substrate.  
Keyword
 3D-structure; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Hydrolase; Magnesium; Membrane; Metal-binding; Pyridoxal phosphate; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 296 AA 
Protein Sequence
MARCERLRGA ALRDVLGRAQ GVLFDCDGVL WNGERAVPGA PELLERLARA GKAALFVSNN 60
SRRARPELAL RFARLGFGGL RAEQLFSSAL CAARLLRQRL PGPPDAPGAV FVLGGEGLRA 120
ELRAAGLRLA GDPSAGDGAA PRVRAVLVGY DEHFSFAKLR EACAHLRDPE CLLVATDRDP 180
WHPLSDGSRT PGTGSLAAAV ETASGRQALV VGKPSPYMFE CITENFSIDP ARTLMVGDRL 240
ETDILFGHRC GMTTVLTLTG VSRLEEAQAY LAAGQHDLVP HYYVESIADL TEGLED 296 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
 GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
 GO:0031072; F:heat shock protein binding; IDA:MGI.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
 GO:0004647; F:phosphoserine phosphatase activity; IEA:EC.
 GO:0033883; F:pyridoxal phosphatase activity; IEA:EC.
 GO:0031247; P:actin rod assembly; IDA:MGI.
 GO:0071318; P:cellular response to ATP; IDA:MGI.
 GO:0030836; P:positive regulation of actin filament depolymerization; IMP:UniProtKB.
 GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
 GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB.
 GO:0007088; P:regulation of mitosis; IMP:UniProtKB. 
Interpro
 IPR023214; HAD-like_dom.
 IPR006357; HAD-SF_hydro_IIA.
 IPR023215; NPhePase-like_dom.
 IPR006349; PGP_euk. 
Pfam
 PF13344; Hydrolase_6 
SMART
  
PROSITE
  
PRINTS