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NADSYN1 protein (human) - STRING interaction network
"NADSYN1" - Glutamine-dependent NAD(+) synthetase in Homo sapiens
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Predicted Interactions
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NADSYN1Glutamine-dependent NAD(+) synthetase; NAD synthetase 1; In the C-terminal section; belongs to the NAD synthetase family (706 aa)    
Predicted Functional Partners:
NMNAT3
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 3; Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Can also use GTP and ITP as nucleotide donors. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, can use NAD(+), NADH, NaAD, nicotinic acid adenine dinucleotide phosphate (NHD), nicotinamide guanine dinucleo [...] (215 aa)
   
 
  0.981
NMNAT2
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2; Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency. Cannot use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity prefers NAD(+), NADH and NaAD as substrates and degrades nicotinic acid adenine dinucleotide phosphate (NHD) less effectively. Fails to cleave phosphory [...] (307 aa)
   
 
  0.980
NMNAT1
Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1; Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as substrate. Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+). For the pyrophosphorolytic activity, prefers NAD(+) and NaAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) and nicotinamide guanine dinucleotide (NGD) less [...] (279 aa)
   
 
  0.977
NADK
NAD kinase; Belongs to the NAD kinase family (591 aa)
   
 
  0.972
NADK2
NAD kinase 2, mitochondrial; Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to yield NADP(+). Can use both ATP or inorganic polyphosphate as the phosphoryl donor. Also has weak NADH kinase activity in vitro; however NADH kinase activity is much weaker than the NAD(+) kinase activity and may not be relevant in vivo (442 aa)
     
 
  0.937
NNT
NAD(P) transhydrogenase, mitochondrial; The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane. May play a role in reactive oxygen species (ROS) detoxification in the adrenal gland; In the N-terminal section; belongs to the AlaDH/PNT family (1086 aa)
     
 
  0.930
NUDT12
Peroxisomal NADH pyrophosphatase NUDT12; Hydrolyzes NAD(P)H to NMNH and AMP (2’,5’-ADP), and diadenosine diphosphate to AMP. Has also activity towards NAD(P)(+), ADP-ribose and diadenosine triphosphate. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle; Belongs to the Nudix hydrolase family. NudC subfamily (462 aa)
   
 
  0.921
BST1
ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2; Synthesizes the second messagers cyclic ADP-ribose and nicotinate-adenine dinucleotide phosphate, the former a second messenger that elicits calcium release from intracellular stores. May be involved in pre-B-cell growth; Belongs to the ADP-ribosyl cyclase family (318 aa)
         
  0.908
ENPP3
Ectonucleotide pyrophosphatase/phosphodiesterase family member 3; Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD; CD molecules (875 aa)
   
 
    0.902
ENPP1
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1; By generating PPi, plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. PPi inhibits mineralization by binding to nascent hydroxyapatite (HA) crystals, thereby preventing further growth of these crystals. Preferentially hydrolyzes ATP, but can also hydrolyze other nucleoside 5’ triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3’,5’-cAMP to AMP. May also be [...] (925 aa)
   
 
    0.902
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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