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Sptlc2 Sptlc2 Pnpo Pnpo Shmt1 Shmt1 Gcat Gcat Tat Tat Cbs Cbs Cth Cth Alas1 Alas1 Thnsl2 Thnsl2 Odc1 Odc1 Gcat-2 Gcat-2 Phykpl Phykpl Ddc Ddc Phospho2 Phospho2 Sds Sds Sgpl1 Sgpl1 Kyat1 Kyat1 Accs Accs Kyat3 Kyat3 Accsl Accsl Gad1 Gad1 Pdxp Pdxp Oat Oat Aadat Aadat Gadl1 Gadl1 Etnppl Etnppl Pygl Pygl Srr Srr Alas2 Alas2 Mocos Mocos Abat Abat Fasn Fasn Thnsl1 Thnsl1 Sptlc3 Sptlc3 Pygm Pygm Got1l1 Got1l1 Pygb Pygb Gpt2 Gpt2 Got2 Got2 Plpbp Plpbp Bcat2 Bcat2 Bcat1 Bcat1 Sdsl Sdsl Sepsecs Sepsecs Nfs1 Nfs1 Hdc Hdc Kynu Kynu Gad2 Gad2 Scly Scly Agxt Agxt Shmt2 Shmt2 Got1 Got1 Gldc Gldc Psat1 Psat1 Csad Csad Pdxdc1 Pdxdc1 Gpt Gpt Agxt2 Agxt2 Sptlc1 Sptlc1
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Sptlc2Serine palmitoyltransferase 2; Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC2-SPTSSB complex displays a preference for C18-CoA substrate (By similarity). Plays an important role in de novo sphyngolipid biosynthesis which is crucial for adipogenesis. (560 aa)
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)
Shmt1Serine hydroxymethyltransferase, cytosolic; Interconversion of serine and glycine. (478 aa)
Gcat2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. (416 aa)
TatTyrosine aminotransferase; Transaminase involved in tyrosine breakdown. Converts tyrosine to p-hydroxyphenylpyruvate. Can catalyze the reverse reaction, using glutamic acid, with 2-oxoglutarate as cosubstrate (in vitro). Has much lower affinity and transaminase activity for phenylalanine. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (454 aa)
CbsCystathionine beta-synthase; Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L- homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine (By similarity). Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons (By similarity). (561 aa)
CthCystathionine gamma-lyase; Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target protei [...] (398 aa)
Alas15-aminolevulinate synthase, nonspecific, mitochondrial; Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. (642 aa)
Thnsl2Threonine synthase-like 2; Acts as a catabolic phospho-lyase on both gamma- and beta- phosphorylated substrates. Degrades O-phospho-threonine (PThr) to alpha-ketobutyrate, ammonia and phosphate. Also degrades O-phospho- homoserine (PHS), but this is not its physiological substrate. Belongs to the threonine synthase family. (483 aa)
Odc1Ornithine decarboxylase; Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine. Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis. (461 aa)
Gcat-22-amino-3-ketobutyrate coenzyme A ligase, mitochondrial. (382 aa)
Phykpl5-phosphohydroxy-L-lysine phospho-lyase; Catalyzes the pyridoxal-phosphate-dependent breakdown of 5- phosphohydroxy-L-lysine, converting it to ammonia, inorganic phosphate and 2-aminoadipate semialdehyde; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (467 aa)
DdcAromatic-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; Belongs to the group II decarboxylase family. (480 aa)
Phospho2Pyridoxal 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 (By similarity). (241 aa)
SdsL-serine dehydratase/L-threonine deaminase; Belongs to the serine/threonine dehydratase family. (327 aa)
Sgpl1Sphingosine-1-phosphate lyase 1; Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis. Required for global lipid homeostasis in liver and cholesterol homeostasis in fibroblasts. Involved in the regulation of pro- inflammatory response and neutrophil trafficking. Modulates neuronal autophagy via phosphoethanolamine production which regulates accumulation of aggregate-prone proteins such as APP. Seems to play a role in establishing neuronal contact sites and [...] (568 aa)
Kyat1Kynurenine--oxoglutarate transaminase 1; Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Metabolizes the cysteine conjugates of certain halogenated alkenes and alkanes to form reactive metabolites. Catalyzes the beta-elimination of S-conjugates and Se-conjugates of L-(seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity); Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (424 aa)
Accs1-aminocyclopropane-1-carboxylate synthase-like protein 1; Does not catalyze the synthesis of 1-aminocyclopropane-1- carboxylate but is capable of catalyzing the deamination of L- vinylglycine; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (502 aa)
Kyat3Kynurenine--oxoglutarate transaminase 3; Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). May catalyze the beta-elimination of S-conjugates and Se-conjugates of L- (seleno)cysteine, resulting in the cleavage of the C-S or C-Se bond (By similarity). Has transaminase activity towards L-kynurenine, tryptophan, phenylalanine, serine, cysteine, methionine, histidine, glutamine and asparagine with glyoxylate as an amino group acceptor (in vitro). Has lower activity with 2-oxoglutarate as amino group acceptor (in vitro). (455 aa)
AccslProbable inactive 1-aminocyclopropane-1-carboxylate synthase-like protein 2. (580 aa)
Gad1Glutamate decarboxylase 1; Catalyzes the production of GABA; Belongs to the group II decarboxylase family. (593 aa)
PdxpPyridoxal 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 (By similarity). Pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'- phosphate (PMP), with [...] (292 aa)
OatOrnithine aminotransferase, mitochondrial. (439 aa)
AadatKynurenine/alpha-aminoadipate aminotransferase, mitochondrial; Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro) (By similarity). Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (425 aa)
Gadl1Acidic amino acid decarboxylase GADL1; Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L- alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. The preferred substrate is L- aspartate. Does not exhibit any decarboxylation activity toward glutamate. (502 aa)
EtnpplEthanolamine-phosphate phospho-lyase; Catalyzes the pyridoxal-phosphate-dependent breakdown of phosphoethanolamine, converting it to ammonia, inorganic phosphate and acetaldehyde. (499 aa)
PyglGlycogen phosphorylase, liver form; 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). (850 aa)
SrrSerine racemase; Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine. (339 aa)
Alas25-aminolevulinate synthase, erythroid-specific, mitochondrial. (587 aa)
MocosMolybdenum cofactor sulfurase; Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. (862 aa)
Abat4-aminobutyrate aminotransferase, mitochondrial; Catalyzes the conversion of gamma-aminobutyrate and L-beta- aminoisobutyrate to succinate semialdehyde and methylmalonate semialdehyde, respectively. Can also convert delta-aminovalerate and beta-alanine (By similarity). (500 aa)
Fasn3-hydroxyacyl-[acyl-carrier-protein] dehydratase; Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities as an acyl carrier protein. (2504 aa)
Thnsl1Threonine synthase-like 1. (747 aa)
Sptlc3Serine palmitoyltransferase 3; Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. SPT complexes containing SPTLC3 generate shorter chain sphingoid bases compared to complexes containing SPTLC2. The SPTLC1- SPTLC3-SPTSSA isozyme uses C12-CoA, C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. On the other hand, the SPTLC1- SPTLC3-SPTSSB has the ability to use a broader range of acyl-CoAs without apparent prefe [...] (563 aa)
PygmGlycogen phosphorylase, muscle form; 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. (842 aa)
Got1l1Putative aspartate aminotransferase, cytoplasmic 2; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (404 aa)
PygbGlycogen phosphorylase, brain form; Glycogen phosphorylase that regulates glycogen mobilization. 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. (843 aa)
Gpt2Alanine aminotransferase 2; Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. (522 aa)
Got2Aspartate aminotransferase, mitochondrial; Catalyzes the irreversible transamination of the L-tryptophan metabolite L-kynurenine to form kynurenic acid (KA). Plays a key role in amino acid metabolism. Important for metabolite exchange between mitochondria and cytosol. Facilitates cellular uptake of long-chain free fatty acids. (430 aa)
PlpbpPyridoxal phosphate homeostasis protein; Pyridoxal 5'-phosphate (PLP)-binding protein, which may be involved in intracellular homeostatic regulation of pyridoxal 5'- phosphate (PLP), the active form of vitamin B6. (274 aa)
Bcat2Branched-chain-amino-acid aminotransferase, mitochondrial; Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids. (393 aa)
Bcat1Branched-chain-amino-acid aminotransferase, cytosolic; Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. (453 aa)
SdslSerine dehydratase-like; Has low serine dehydratase and threonine dehydratase activity; Belongs to the serine/threonine dehydratase family. (329 aa)
SepsecsO-phosphoseryl-tRNA(Sec) selenium transferase; Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl- tRNA(Sec) required for selenoprotein biosynthesis. Belongs to the SepSecS family. (504 aa)
Nfs1Cysteine desulfurase, mitochondrial; Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe- S) clusters. May be involved in the biosynthesis of molybdenum cofactor (By similarity); Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily. (459 aa)
HdcHistidine decarboxylase; Catalyzes the biosynthesis of histamine from histidine. (662 aa)
KynuKynureninase; Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3- hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3- hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity. (465 aa)
Gad2Glutamate decarboxylase 2; Catalyzes the production of GABA. (585 aa)
SclySelenocysteine lyase; Catalyzes the decomposition of L-selenocysteine to L-alanine and elemental selenium; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. (432 aa)
AgxtSerine--pyruvate aminotransferase, mitochondrial; Dual metabolic roles of gluconeogenesis (in the mitochondria) and glyoxylate detoxification (in the peroxisomes). (414 aa)
Shmt2Serine hydroxymethyltransferase, mitochondrial; Catalyzes the cleavage of serine to glycine accompanied with the production of 5,10-methylenetetrahydrofolate, an essential intermediate for purine biosynthesis (By similarity). Serine provides the major source of folate one-carbon in cells by catalyzing the transfer of one carbon from serine to tetrahydrofolate (By similarity). Contributes to the de novo mitochondrial thymidylate biosynthesis pathway via its role in glycine and tetrahydrofolate metabolism: thymidylate biosynthesis is required to prevent uracil accumulation in mtDNA (By s [...] (504 aa)
Got1Aspartate aminotransferase, cytoplasmic; Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic glucose synthesis during development and in adipocyte glyceroneogenesis. Using L-cysteine as substrate, regulates levels of mercaptopyruvate, an important source of hydrogen sulfide. Mercaptopyruvate is converted into H(2)S via the action of 3-m [...] (413 aa)
GldcGlycine dehydrogenase (decarboxylating), mitochondrial; The glycine cleavage system catalyzes the degradation of glycine. The P protein (GLDC) binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (GCSH) (By similarity). Belongs to the GcvP family. (1025 aa)
Psat1Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine. (370 aa)
CsadCysteine sulfinic acid decarboxylase; Catalyzes the decarboxylation of L-aspartate, 3-sulfino-L- alanine (cysteine sulfinic acid), and L-cysteate to beta-alanine, hypotaurine and taurine, respectively. The preferred substrate is 3- sulfino-L-alanine. Does not exhibit any decarboxylation activity toward glutamate. (493 aa)
Pdxdc1Pyridoxal-dependent decarboxylase domain-containing protein 1; Belongs to the group II decarboxylase family. (789 aa)
GptAlanine aminotransferase 1; Catalyzes the reversible transamination between alanine and 2-oxoglutarate to form pyruvate and glutamate. Participates in cellular nitrogen metabolism and also in liver gluconeogenesis starting with precursors transported from skeletal muscles (By similarity). (496 aa)
Agxt2Alanine--glyoxylate aminotransferase 2, mitochondrial; Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure. (541 aa)
Sptlc1Serine palmitoyltransferase 1; Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1- SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates. The SPTLC1-SPTLC2-SPTSSB complex displays a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme has the ability to use a broader range of acyl-CoAs (By [...] (473 aa)
Your Current Organism:
Mus musculus
NCBI taxonomy Id: 10090
Other names: LK3 transgenic mice, M. musculus, Mus sp. 129SV, house mouse, mouse, nude mice, transgenic mice
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