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Wars2 Wars2 Etfb Etfb Qars Qars Cars Cars Rars Rars Cry1 Cry1 Trmu Trmu Iars Iars Mars Mars Wars Wars Flad1 Flad1 Ctu2 Ctu2 Asns Asns Nmnat3 Nmnat3 Coasy Coasy Yars Yars Nmnat1 Nmnat1 Ass1 Ass1 Dph6 Dph6 Lars Lars Cry2 Cry2 Vars Vars Pcyt1a Pcyt1a Yars2 Yars2 Mars2 Mars2 Vars2 Vars2 Cars2 Cars2 Eprs Eprs Pcyt1b Pcyt1b Nmnat2 Nmnat2 Ctu1 Ctu1 Lars2 Lars2 Etfa Etfa Nadsyn1 Nadsyn1 Ears2 Ears2 Rars2 Rars2 Papss1 Papss1 Gmps Gmps Iars2 Iars2 Asnsd1 Asnsd1 Pcyt2 Pcyt2 Papss2 Papss2
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query proteins and first shell of interactors
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second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Wars2Tryptophan--tRNA ligase, mitochondrial; Mitochondrial aminoacyl-tRNA synthetase that activate and transfer the amino acids to their corresponding tRNAs during the translation of mitochondrial genes and protein synthesis. (360 aa)
EtfbElectron transfer flavoprotein subunit beta; Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF- ubiquinone oxidoreductase (By similarity). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism. ETFB binds an AMP molecule that probably has a purely structural role (By similarity). (255 aa)
QarsGlutamine--tRNA ligase; Glutamine--tRNA ligase. Plays a critical role in brain development; Belongs to the class-I aminoacyl-tRNA synthetase family. (775 aa)
CarsCysteine--tRNA ligase, cytoplasmic. (831 aa)
RarsArginine--tRNA ligase, cytoplasmic; Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis. Modulates the secretion of AIMP1 and may be involved in generation of the inflammatory cytokine EMAP2 from AIMP1. (660 aa)
Cry1Cryptochrome-1; Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal [...] (606 aa)
TrmuMitochondrial tRNA-specific 2-thiouridylase 1; Catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln). Required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. ATP is required to activate the C2 atom of the wobble base. (417 aa)
IarsIsoleucine--tRNA ligase, cytoplasmic; Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA; Belongs to the class-I aminoacyl-tRNA synthetase family. (1262 aa)
MarsMethionine--tRNA ligase, cytoplasmic; Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Plays a role in the synthesis of ribosomal RNA in the nucleolus; Belongs to the class-I aminoacyl-tRNA synthetase family. (910 aa)
WarsTryptophan--tRNA ligase, cytoplasmic; T1-TrpRS has aminoacylation activity while T2-TrpRS lacks it. T1-TrpRS and T2-TrpRS possess angiostatic activity. T2-TrpRS inhibits fluid shear stress-activated responses of endothelial cells. Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression (By similarity). (481 aa)
Flad1Molybdenum cofactor biosynthesis protein-like region; Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme; In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily. (492 aa)
Ctu2Cytoplasmic tRNA 2-thiolation protein 2; Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with CTU1/ATPBD3 that ligates sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position. Belongs to the CTU2/NCS2 family. (514 aa)
AsnsAsparagine synthetase [glutamine-hydrolyzing]. (561 aa)
Nmnat3Nicotinamide/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 [...] (245 aa)
CoasyPhosphopantetheine adenylyltransferase; Bifunctional enzyme that catalyzes the fourth and fifth sequential steps of CoA biosynthetic pathway. The fourth reaction is catalyzed by the phosphopantetheine adenylyltransferase, coded by the coaD domain; the fifth reaction is catalyzed by the dephospho-CoA kinase, coded by the coaE domain. May act as a point of CoA biosynthesis regulation; In the central section; belongs to the eukaryotic CoaD family. (563 aa)
YarsTyrosine--tRNA ligase, cytoplasmic, N-terminally processed; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr); Belongs to the class-I aminoacyl-tRNA synthetase family. (564 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 (By similarity). Can use triazofurin monophosphate (TrMP) as substrate (By similarity). Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+) (By similarity). For the pyrophosphorolytic activity, prefers NAD(+) and NaAD as substrates and degrades NADH, nicotinic acid adenine dinucleotide phosphate (NHD) [...] (285 aa)
Ass1Argininosuccinate synthase; One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues. (412 aa)
Dph6Diphthine--ammonia ligase; Amidase that catalyzes the last step of diphthamide biosynthesis using ammonium and ATP. Diphthamide biosynthesis consists in the conversion of an L-histidine residue in the translation elongation factor 2 (EEF2) to diphthamide (By similarity). Belongs to the Diphthine--ammonia ligase family. (267 aa)
LarsLeucine--tRNA ligase, cytoplasmic; Catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Exhibits a post-transfer editing activity to hydrolyze mischarged tRNAs; Belongs to the class-I aminoacyl-tRNA synthetase family. (1178 aa)
Cry2Cryptochrome-2; Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal [...] (592 aa)
VarsValine--tRNA ligase. (1263 aa)
Pcyt1aCholine-phosphate cytidylyltransferase A; Controls phosphatidylcholine synthesis; Belongs to the cytidylyltransferase family. (367 aa)
Yars2Tyrosine--tRNA ligase, mitochondrial; Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two- step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). Belongs to the class-I aminoacyl-tRNA synthetase family. (472 aa)
Mars2Methionine--tRNA ligase, mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family. (586 aa)
Vars2Valine--tRNA ligase, mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family. (1060 aa)
Cars2Probable cysteine--tRNA ligase, mitochondrial. (552 aa)
EprsBifunctional glutamate/proline--tRNA ligase; Multifunctional protein which is primarily part of the aminoacyl-tRNA synthetase multienzyme complex, also know as multisynthetase complex, that catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA (By similarity). The phosphorylation of EPRS1, induced by interferon-gamma, dissociates the protein from the aminoacyl-tRNA synthetase multienzyme complex [...] (1512 aa)
Pcyt1bCholine-phosphate cytidylyltransferase B; Controls phosphatidylcholine synthesis. Belongs to the cytidylyltransferase family. (369 aa)
Nmnat2Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2; Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor. Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP (By similarity). Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate but with a lower efficiency (By similarity). Cannot use triazofurin monophosphate (TrMP) as substrate (By similarity). Also catalyzes the reverse reaction, i.e. the pyrophosphorolytic cleavage of NAD(+) (By similarity). For the pyrophosphorolytic a [...] (307 aa)
Ctu1Cytoplasmic tRNA 2-thiolation protein 1; Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated URM1 onto the uridine of tRNAs at wobble position; Belongs to the TtcA family. CTU1/NCS6/ATPBD3 subfamily. (420 aa)
Lars2Probable leucine--tRNA ligase, mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family. (902 aa)
EtfaElectron transfer flavoprotein subunit alpha, mitochondrial; Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF- ubiquinone oxidoreductase (ETF dehydrogenase). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism. (333 aa)
Nadsyn1Glutamine-dependent NAD(+) synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source. (725 aa)
Ears2Probable glutamate--tRNA ligase, mitochondrial; Catalyzes the attachment of glutamate to tRNA(Glu) in a two- step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). (523 aa)
Rars2Probable arginine--tRNA ligase, mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family. (578 aa)
Papss1Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1; 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. Required [...] (624 aa)
GmpsGMP synthase [glutamine-hydrolyzing]; Involved in the de novo synthesis of guanine nucleotides which are not only essential for DNA and RNA synthesis, but also provide GTP, which is involved in a number of cellular processes important for cell division. (693 aa)
Iars2Isoleucine--tRNA ligase, mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family. (1012 aa)
Asnsd1Asparagine synthetase domain-containing protein 1. (627 aa)
Pcyt2Ethanolamine-phosphate cytidylyltransferase; Plays an important role in the biosynthesis of the phospholipid phosphatidylethanolamine. Catalyzes the formation of CDP- ethanolamine (By similarity). (404 aa)
Papss2Bifunctional 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 [...] (621 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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