Nodes:
Network nodes represent proteins
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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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
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from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
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ADPRMManganese-dependent ADP-ribose/CDP-alcohol diphosphatase; Hydrolyzes ADP-ribose, IDP-ribose, CDP-glycerol, CDP-choline and CDP-ethanolamine, but not other non-reducing ADP-sugars or CDP- glucose. May be involved in immune cell signaling as suggested by the second-messenger role of ADP-ribose, which activates TRPM2 as a mediator of oxidative/nitrosative stress (By similarity). (342 aa)    
Predicted Functional Partners:
GPAM
Glycerol-3-phosphate acyltransferase 1, mitochondrial; Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis.
     
 0.919
GPD2
Glycerol-3-phosphate dehydrogenase, mitochondrial; Glycerol-3-phosphate dehydrogenase 2; Belongs to the FAD-dependent glycerol-3-phosphate dehydrogenase family.
   
 
 0.907
GPD1L
Glycerol-3-phosphate dehydrogenase 1-like protein; Plays a role in regulating cardiac sodium current; decreased enzymatic activity with resulting increased levels of glycerol 3- phosphate activating the DPD1L-dependent SCN5A phosphorylation pathway, may ultimately lead to decreased sodium current; cardiac sodium current may also be reduced due to alterations of NAD(H) balance induced by DPD1L; Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
   
 
 0.904
PRPS1
Ribose-phosphate pyrophosphokinase 1; Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis; Belongs to the ribose-phosphate pyrophosphokinase family.
   
 
 0.903
PGM2
Phosphoglucomutase-2; Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5- phosphopentoses. May also catalyze the interconversion of glucose-1- phosphate and glucose-6-phosphate. Has low glucose 1,6-bisphosphate synthase activity; Belongs to the phosphohexose mutase family.
  
 
 0.903
GPD1
Glycerol-3-phosphate dehydrogenase 1; Belongs to the NAD-dependent glycerol-3-phosphate dehydrogenase family.
     
 0.902
PGM1
Phosphoglucomutase-1; This enzyme participates in both the breakdown and synthesis of glucose; Belongs to the phosphohexose mutase family.
     
 0.902
PRPS2
Ribose-phosphate pyrophosphokinase 2; Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis; Belongs to the ribose-phosphate pyrophosphokinase family.
     
 0.902
NUDT5
ADP-sugar pyrophosphatase; Enzyme that can either act as an ADP-sugar pyrophosphatase in absence of diphosphate or catalyze the synthesis of ATP in presence of diphosphate. In absence of diphosphate, hydrolyzes with similar activities various modified nucleoside diphosphates such as ADP-ribose, ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP. Can also hydrolyze other nucleotide sugars with low activity. In presence of diphosphate, mediates the synthesis of ATP in the nucleus by catalyzing the conversion of ADP-ribose to ATP and ribose 5-phosphate. Nuclear ATP synthesis takes place w [...]
     
 0.902
PRPS1L1
Ribose-phosphate pyrophosphokinase 3; Catalyzes the synthesis of phosphoribosylpyrophosphate (PRPP) that is essential for nucleotide synthesis.
     
 0.902
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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