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 Size
small nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
second shell of interactors
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 each other.
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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 | NMRK2 | nicotinamide riboside kinase 2; Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN). Reduces laminin matrix deposition and cell adhesion to laminin, but not to fibronectin. Involved in the regulation of PXN at the protein level and of PXN tyrosine phosphorylation. May play a role in the regulation of terminal myogenesis (230 aa) | ||
 | PYGL | phosphorylase, glycogen, liver; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity) (847 aa) | ||
 | PYGB | phosphorylase, glycogen; brain; Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity) (843 aa) | ||
 | PANK3 | pantothenate kinase 3; Plays a role in the physiological regulation of the intracellular CoA concentration (By similarity) (370 aa) | ||
 | NT5C3 | 5’-nucleotidase, cytosolic III (336 aa) | ||
 | NT5C | 5’, 3’-nucleotidase, cytosolic; Dephosphorylates the 5’ and 2’(3’)-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP (201 aa) | ||
 | NT5E | 5’-nucleotidase, ecto (CD73); Hydrolyzes extracellular nucleotides into membrane permeable nucleosides. Exhibits AMP-, NAD-, and NMN-nucleosidase activities (574 aa) | ||
 | GYS2 | glycogen synthase 2 (liver); Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan (703 aa) | ||
 | NNT | nicotinamide nucleotide transhydrogenase; 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 (1086 aa) | ||
 | ACPT | acid phosphatase, testicular; Dephosphorylates receptor tyrosine-protein kinase erbB-4 and inhibits the ligand-induced proteolytic cleavage (426 aa) | ||
 | ACP1 | acid phosphatase 1, soluble; Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Isoform 3 does not possess phosphatase activity (158 aa) | ||
 | PGM2L1 | phosphoglucomutase 2-like 1; Glucose 1,6-bisphosphate synthase using 1,3- bisphosphoglycerate as a phosphate donor and a series of 1- phosphate sugars as acceptors, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-phosphate and deoxyribose 1- phosphate. 5 or 6-phosphosugars are bad substrates, with the exception of glucose 6-phosphate. Also synthesizes ribose 1,5- bisphosphate. Has only low phosphopentomutase and phosphoglucomutase activities (622 aa) | ||
 | GYS1 | glycogen synthase 1 (muscle); Transfers the glycosyl residue from UDP-Glc to the non- reducing end of alpha-1,4-glucan (737 aa) | ||
 | ACPP | acid phosphatase, prostate; A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma (418 aa) | ||
 | NADSYN1 | NAD synthetase 1 (706 aa) | ||
 | NADK | NAD kinase (591 aa) | ||
 | PPCDC | phosphopantothenoylcysteine decarboxylase; Necessary for the biosynthesis of coenzyme A. Catalyzes the decarboxylation of 4-phosphopantothenoylcysteine to form 4’- phosphopantotheine (204 aa) | ||
 | ENPP3 | ectonucleotide pyrophosphatase/phosphodiesterase 3; Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD (By similarity) (875 aa) | ||
 | NMRK1 | nicotinamide riboside kinase 1; Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN). The enzyme also phosphorylates the antitumor drugs tiazofurin and 3- deazaguanosine (199 aa) | ||
 | RFK | riboflavin kinase; Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin-mononucleotide (FMN), hence rate-limiting enzyme in the synthesis of FAD. Essential for TNF-induced reactive oxygen species (ROS) production. Through its interaction with both TNFRSF1A and CYBA, physically and functionally couples TNFRSF1A to NADPH oxidase. TNF-activation of RFK may enhance the incorporation of FAD in NADPH oxidase, a critical step for the assembly and activation of NADPH oxidase (155 aa) | ||
 | 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 (612 aa) | ||
 | NT5M | 5’,3’-nucleotidase, mitochondrial; Dephosphorylates specifically the 5’ and 2’(3’)- phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP (228 aa) | ||
 | QPRT | quinolinate phosphoribosyltransferase; Involved in the catabolism of quinolinic acid (QA) (297 aa) | ||
 | NAPRT1 | nicotinate phosphoribosyltransferase domain containing 1; Catalyzes the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN). Essential for NA to increase cellular NAD levels and prevent oxidative stress of the cells (538 aa) | ||
 | PAPSS2 | 3’-phosphoadenosine 5’-phosphosulfate synthase 2; Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5’-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3’-phosphoadenylylsulfate (PAPS- activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate- activation pathway. May have a important [...] (619 aa) | ||
 | ENSG00000250741 | NT5C1B-RDH14 readthrough (602 aa) | ||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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