• Version:
  • 11.0 [archived version]
STRINGSTRING
PSAT1 PSAT1 DDC DDC PDXP PDXP PHOSPHO2 PHOSPHO2 PDXK PDXK PNPO PNPO AOX1 AOX1 TBKBP1 TBKBP1 ALPI ALPI PRR15L PRR15L OSBPL7 OSBPL7
"PNPO" - Pyridoxine-5'-phosphate oxidase in Homo sapiens
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Score
PNPOPyridoxine-5’-phosphate oxidase; Catalyzes the oxidation of either pyridoxine 5’- phosphate (PNP) or pyridoxamine 5’-phosphate (PMP) into pyridoxal 5’-phosphate (PLP) (261 aa)    
Predicted Functional Partners:
PDXK
Pyridoxal kinase; Required for synthesis of pyridoxal-5-phosphate from vitamin B6; Belongs to the pyridoxine kinase family (312 aa)
   
 
  0.990
PHOSPHO2
Pyridoxal phosphate phosphatase PHOSPHO2; Phosphatase that has high activity toward pyridoxal 5’- phosphate (PLP). Also active at much lower level toward pyrophosphate, phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine, fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate; HAD Asp-based non-protein phosphatases (241 aa)
     
 
  0.952
PDXP
Pyridoxal phosphate phosphatase; 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 (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5’- phosphate (PNP) and pyridoxamine 5’-phosphate (PMP), with order of substr [...] (296 aa)
     
 
  0.942
AOX1
Aldehyde oxidase; Oxidase with broad substrate specificity, oxidizing aromatic azaheterocycles, such as N1-methylnicotinamide, N- methylphthalazinium and phthalazine, as well as aldehydes, such as benzaldehyde, retinal, pyridoxal, and vanillin. Plays a key role in the metabolism of xenobiotics and drugs containing aromatic azaheterocyclic substituents. Participates in the bioactivation of prodrugs such as famciclovir, catalyzing the oxidation step from 6-deoxypenciclovir to penciclovir, which is a potent antiviral agent. Is probably involved in the regulation of reactive oxygen species [...] (1338 aa)
         
  0.908
ALPI
Alkaline phosphatase, intestinal (528 aa)
         
  0.901
DDC
Aromatic-L-amino-acid decarboxylase; Catalyzes the decarboxylation of L-3,4- dihydroxyphenylalanine (DOPA) to dopamine, L-5-hydroxytryptophan to serotonin and L-tryptophan to tryptamine (480 aa)
           
  0.804
PSAT1
Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily (370 aa)
   
   
  0.744
PRR15L
Proline-rich protein 15-like protein; Proline rich 15 like; Belongs to the PRR15 family (103 aa)
           
  0.732
OSBPL7
Oxysterol-binding protein-related protein 7; Pleckstrin homology domain containing; Belongs to the OSBP family (842 aa)
           
  0.720
TBKBP1
TANK-binding kinase 1-binding protein 1; Adapter protein which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity (615 aa)
           
  0.714
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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