Statistics
241 human active and 13 inactive phosphatases in total;
194 phosphatases have substrate data;
--------------------------------
336 protein substrates;
83 non-protein substrates;
1215 dephosphorylation interactions;
--------------------------------
299 KEGG pathways;
876 Reactome pathways;
--------------------------------
last scientific update:
11 Mar, 2019
194 phosphatases have substrate data;
--------------------------------
336 protein substrates;
83 non-protein substrates;
1215 dephosphorylation interactions;
--------------------------------
299 KEGG pathways;
876 Reactome pathways;
--------------------------------
last scientific update:
11 Mar, 2019
Top
PDXP
Gene Name  | PDXP (QuickGO) | (A quick tutorial to explore the interactive visualization) |
| Synonyms | PDXP, CIN, PLP, PLPP | |
| Protein Name | PDXP |
|
|
Alternative Name(s) |
Pyridoxal phosphate phosphatase;PLP phosphatase;3.1.3.3;3.1.3.74;Chronophin; | |
| EntrezGene ID | 57026 (Comparative Toxicogenomics) | |
| UniProt AC (Human) | Q96GD0 (protein sequence) | |
| Enzyme Class | EC 3.1.3.3 3.1.3.74 (BRENDA ) | |
| Molecular Weight | 31698 Dalton | |
| Protein Length | 296 amino acids (AA) | |
| Genome Browsers | NCBI | ENSG00000241360 (Ensembl) | | |
| Crosslinking annotations | Query our ID-mapping table | |
| Orthologues | Quest For Orthologues (QFO) | GeneTree | |
| Classification | Superfamily: HAD | Historic class: HAD-like hydrolase | CATH ID: 3.40.50.1000 | SCOP Fold: HAD | |
| Phosphatase activity | active | Catalytic signature motif: unknown | |
| Domain organization, Expression, Diseases | (show / hide) |
| Protein Domain | InterPro | Pfam | SMART | 3D Structure | PDB | DrugPort | ModBase | SwissModel |
| Polypeptide organization (Pfam) | No Pfam domain found | ||
| Catalytic Site | Mechanism and Catalytic Site Atlas | ||
| Gene Expression | Gene Expression Atlas | Diseases | OMIM | DisGeNet | COSMIC | ClinVar |
| Protein-protein interactions | STRING | IntAct | MINT | BioGRID | ||
| Phosphosites | Phospho.ELM | PhosphoSitePlus | ||
| Localization, Function, Catalytic activity and Sequence | (show / hide) |
| Localization (UniProt annotation) | |||
| Cytoplasm, cytosol Cytoplasm, cytoskeleton Cell projection, ruffle membrane Cell projection, lamellipodiummembrane Cell membrane Note=Colocalizes with the actincytoskeleton in membrane ruffles and lamellipodia Diffuselydistributed throughout the cytosol during pro-metaphase andmetaphase Detected at the dynamic cell poles during telophaseDetected at the cleavage furrow and contractile ring duringcytokinesis Transiently detected at the plasma membrane in latestages of cytokinesis Detected at the midbody | |||
| Function (UniProt annotation) | |||
| Protein serine phosphatase that dephosphorylates 'Ser-3'in cofilin and probably also dephosphorylates phospho-serineresidues in DSTN Regulates cofilin-dependent actin cytoskeletonreorganization Required for normal progress through mitosis andnormal cytokinesis Does not dephosphorylate phospho-threonines inLIMK1 Does not dephosphorylate peptides containing phospho-tyrosine (PubMed:15580268) Pyridoxal phosphate (PLP) phosphatase,which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order ofsubstrate preference PLP > PNP > PMP (PubMed:14522954) | |||
| Catalytic Activity (UniProt annotation) | |||
| Pyridoxal 5'-phosphate + H(2)O = pyridoxal +phosphate O-phospho-L(or D)-serine + H(2)O = L(or D)-serine + phosphate | |||
| Protein Sequence | |||
| MARCERLRGAALRDVLGRAQGVLFDCDGVLWNGERAVPGAPELLERLARAGKAALFVSNNSRRARPELALRFARLGFGGL RAEQLFSSALCAARLLRQRLPGPPDAPGAVFVLGGEGLRAELRAAGLRLAGDPSAGDGAAPRVRAVLVGYDEHFSFAKLR EACAHLRDPECLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFECITENFSIDPARTLMVGDRL ETDILFGHRCGMTTVLTLTGVSRLEEAQAYLAAGQHDLVPHYYVESIADLTEGLED |
| Motif information from Eukaryotic Linear Motif atlas (ELM) | (show / hide) |
ELM Motif | Motif Instance | Description | Motif Regex |
| NA | NA | NA | NA |
| Gene Ontology (P: Process; F: Function and C: Component terms) | (show / hide) | |
| GO:0000287 | F:magnesium ion binding |
| GO:0004647 | F:phosphoserine phosphatase activity |
| GO:0004721 | F:phosphoprotein phosphatase activity |
| GO:0005829 | C:cytosol |
| GO:0005856 | C:cytoskeleton |
| GO:0005911 | C:cell-cell junction |
| GO:0006470 | P:protein dephosphorylation |
| GO:0007088 | P:regulation of mitotic nuclear division |
| GO:0030836 | P:positive regulation of actin filament depolymerization |
| GO:0031072 | F:heat shock protein binding |
| GO:0031247 | P:actin rod assembly |
| GO:0031258 | C:lamellipodium membrane |
| GO:0032361 | P:pyridoxal phosphate catabolic process |
| GO:0032465 | P:regulation of cytokinesis |
| GO:0032587 | C:ruffle membrane |
| GO:0033883 | F:pyridoxal phosphatase activity |
| GO:0042803 | F:protein homodimerization activity |
| GO:0071318 | P:cellular response to ATP |
| GO:0098519 | F:nucleotide phosphatase activity |
