STRINGSTRING
SIRT7 SIRT7 SIRT2 SIRT2 SIRT3 SIRT3 NT5C1A NT5C1A NT5C1B NT5C1B BST1 BST1 NT5C NT5C PNP PNP NT5C2 NT5C2 SIRT1 SIRT1 SIRT6 SIRT6 ENPP3 ENPP3 SIRT4 SIRT4 AOX2 AOX2 NUDT12 NUDT12 LOC511161 LOC511161 NT5M NT5M NMRK2 NMRK2 AOX4 AOX4 ENPP1 ENPP1 AOX1 AOX1 NMNAT1 NMNAT1 NMNAT2 NMNAT2 NADK2 NADK2 QPRT QPRT NMRK1 NMRK1 NAMPT NAMPT CD38 CD38 NT5E NT5E NNT NNT NADK NADK SIRT5 SIRT5 NADSYN1 NADSYN1
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.
Node Color
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
SIRT7NAD-dependent protein deacetylase sirtuin-7; NAD-dependent protein-lysine deacylase that can act both as a deacetylase or deacylase (desuccinylase, depropionylase and deglutarylase), depending on the context. Specifically mediates deacetylation of histone H3 at 'Lys-18' (H3K18Ac). In contrast to other histone deacetylases, displays strong preference for a specific histone mark, H3K18Ac, directly linked to control of gene expression. H3K18Ac is mainly present around the transcription start site of genes and has been linked to activation of nuclear hormone receptors; SIRT7 thereby acts a [...] (400 aa)
SIRT2NAD-dependent protein deacetylase; NAD-dependent protein deacetylase. (427 aa)
SIRT3NAD-dependent protein deacetylase; NAD-dependent protein deacetylase. (333 aa)
NT5C1A5'-nucleotidase, cytosolic IA. (365 aa)
NT5C1BUncharacterized protein. (564 aa)
BST1Bone marrow stromal cell antigen 1. (318 aa)
NT5C5', 3'-nucleotidase, cytosolic. (401 aa)
PNPPurine nucleoside phosphorylase; The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta- (deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. (330 aa)
NT5C2Cytosolic purine 5'-nucleotidase; May have a critical role in the maintenance of a constant composition of intracellular purine/pyrimidine nucleotides in cooperation with other nucleotidases. Preferentially hydrolyzes inosine 5'-monophosphate (IMP) and other purine nucleotides. (568 aa)
SIRT1Sirtuin 1. (734 aa)
SIRT6SIRT6 protein. (359 aa)
ENPP3Ectonucleotide pyrophosphatase/phosphodiesterase family member 3; Hydrolase that metabolizes extracellular nucleotides, including ATP, GTP, UTP and CTP (By similarity). Limits mast cell and basophil responses during inflammation and during the chronic phases of allergic responses by eliminating the extracellular ATP that functions as signaling molecule and activates basophils and mast cells and induces the release of inflammatory cytokines. Metabolizes extracellular ATP in the lumen of the small intestine, and thereby prevents ATP-induced apoptosis of intestinal plasmacytoid dendritic [...] (874 aa)
SIRT4NAD-dependent protein lipoamidase sirtuin-4, mitochondrial; Acts as NAD-dependent protein lipoamidase, ADP-ribosyl transferase and deacetylase. Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications. Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner. Catalyzes the transfer of ADP- ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity. Acts as a negative regulator of mitoc [...] (315 aa)
AOX2Aldehyde oxidase 3L1. (1342 aa)
NUDT12Peroxisomal 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. (444 aa)
LOC511161Uncharacterized protein. (347 aa)
NT5M5',3'-nucleotidase, mitochondrial. (225 aa)
NMRK2Integrin beta 1 binding protein 3. (195 aa)
AOX4Aldehyde oxidase 4. (1335 aa)
ENPP1Ectonucleotide pyrophosphatase/phosphodiesterase 1. (924 aa)
AOX1Aldehyde oxidase 1; 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. Is probably involved in the regulation of reactive oxygen species homeostasis. May be a prominent source of superoxide generation via the one-electron reduction of molecular oxygen. Also may catalyze nitric oxide (NO) production via the [...] (1337 aa)
NMNAT1Nicotinamide/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 [...] (281 aa)
NMNAT2Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2; Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor (By similarity). 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 substra [...] (366 aa)
NADK2NAD kinase 2, mitochondrial; Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to yield NADP(+). Can use both ATP or inorganic polyphosphate as the phosphoryl donor. (464 aa)
QPRTNicotinate-nucleotide pyrophosphorylase [carboxylating]; Involved in the catabolism of quinolinic acid (QA). Belongs to the NadC/ModD family. (305 aa)
NMRK1Nicotinamide riboside kinase 1. (199 aa)
NAMPTNicotinamide phosphoribosyltransferase; Belongs to the NAPRTase family. (491 aa)
CD38CD38 molecule. (299 aa)
NT5E5'-nucleotidase; Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. (574 aa)
NNTNAD(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 (By similarity). May play a role in reactive oxygen species (ROS) detoxification in the adrenal gland (By similarity). In the N-terminal section; belongs to the AlaDH/PNT family. (1086 aa)
NADKNAD kinase. (522 aa)
SIRT5NAD-dependent protein deacylase sirtuin-5, mitochondrial; NAD-dependent lysine demalonylase, desuccinylase and deglutarylase that specifically removes malonyl, succinyl and glutaryl groups on target proteins. Activates CPS1 and contributes to the regulation of blood ammonia levels during prolonged fasting: acts by mediating desuccinylation and deglutarylation of CPS1, thereby increasing CPS1 activity in response to elevated NAD levels during fasting. Activates SOD1 by mediating its desuccinylation, leading to reduced reactive oxygen species. Activates SHMT2 by mediating its desuccinyla [...] (310 aa)
NADSYN1Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. (706 aa)
Your Current Organism:
Bos taurus
NCBI taxonomy Id: 9913
Other names: B. taurus, Bos bovis, Bos primigenius taurus, Bovidae sp. Adi Nefas, bovine, cattle, cow, dairy cow, domestic cattle, domestic cow
Server load: low (16%) [HD]