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Etfb Etfb Yars1 Yars1 Rars2 Rars2 Pcyt1b Pcyt1b Nmnat3 Nmnat3 Iars1 Iars1 Cars2 Cars2 Etfa Etfa Ctu1 Ctu1 Lars1 Lars1 Wars2 Wars2 Coasy Coasy Flad1 Flad1 Nadsyn1 Nadsyn1 Nmnat2 Nmnat2 Mars1 Mars1 Yars2 Yars2 Nmnat1 Nmnat1 Vars2 Vars2 Cars Cars Pcyt2 Pcyt2 Dph6 Dph6 Asnsd1 Asnsd1 Trmu Trmu Ears2 Ears2 Mars2 Mars2 Ctu2 Ctu2 Eprs Eprs Qars1 Qars1 Papss1 Papss1 Iars2 Iars2 Gmps Gmps Vars1 Vars1 Papss2 Papss2 Lars2 Lars2 Ass1 Ass1 Pcyt1a Pcyt1a Wars1 Wars1 Cry1 Cry1 Asns Asns Cry2 Cry2 Rars1 Rars1
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
Predicted Interactions
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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. 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)
Yars1Tyrosine--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)
Rars2Arginyl-tRNA synthetase 2, mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family. (578 aa)
Pcyt1bCholine-phosphate cytidylyltransferase B; Controls phosphatidylcholine synthesis. (369 aa)
Nmnat3Nicotinamide-nucleotide adenylyltransferase. (245 aa)
Iars1Isoleucine-tRNA synthetase (Predicted); Belongs to the class-I aminoacyl-tRNA synthetase family. (1262 aa)
Cars2Cysteinyl-tRNA synthetase 2, mitochondrial. (550 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) (Probable). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism. (333 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. (382 aa)
Lars1Leucyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (1178 aa)
Wars2Tryptophanyl tRNA synthetase 2 (mitochondrial); Belongs to the class-I aminoacyl-tRNA synthetase family. (360 aa)
CoasyCoenzyme A synthase. (563 aa)
Flad1FAD synthase; 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. (490 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)
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 [...] (307 aa)
Mars1Methionyl-tRNA synthetase; Belongs to the class-I aminoacyl-tRNA synthetase family. (902 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. (471 aa)
Nmnat1Nicotinamide-nucleotide adenylyltransferase. (285 aa)
Vars2Valine--tRNA ligase, mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family. (1060 aa)
CarsCysteinyl-tRNA synthetase (Predicted), isoform CRA_b. (748 aa)
Pcyt2Ethanolamine-phosphate cytidylyltransferase; Plays an important role in the biosynthesis of the phospholipid phosphatidylethanolamine. Catalyzes the formation of CDP- ethanolamine (By similarity); Belongs to the cytidylyltransferase family. (404 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 eEF-2 (EEF2) to diphthamide (By similarity). (268 aa)
Asnsd1Asparagine synthetase domain-containing 1. (627 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. Belongs to the MnmA/TRMU family. (441 aa)
Ears2Glutamyl-tRNA synthetase 2, mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family. (523 aa)
Mars2Methionine--tRNA ligase, mitochondrial-like; Belongs to the class-I aminoacyl-tRNA synthetase family. (586 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. (528 aa)
EprsGlutamyl-prolyl-tRNA synthetase. (1512 aa)
Qars1Glutamine--tRNA ligase; Glutamine--tRNA ligase. Plays a critical role in brain development; Belongs to the class-I aminoacyl-tRNA synthetase family. (775 aa)
Papss13'-phosphoadenosine 5'-phosphosulfate synthase 1. (623 aa)
Iars2Isoleucyl-tRNA synthetase 2, mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family. (1011 aa)
GmpsGMP synthase [glutamine-hydrolyzing]. (700 aa)
Vars1Valine--tRNA ligase. (1264 aa)
Papss23'-phosphoadenosine 5'-phosphosulfate synthase 2. (619 aa)
Lars2Leucyl-tRNA synthetase 2, mitochondrial; Belongs to the class-I aminoacyl-tRNA synthetase family. (902 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 (Probable). 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 (Probable). Indirectly, may be involved in the control of blood pressure. Belongs to the argininosuccinate synthase family. Type 1 subfamily. (412 aa)
Pcyt1aCholine-phosphate cytidylyltransferase A; Controls phosphatidylcholine synthesis; Belongs to the cytidylyltransferase family. (367 aa)
Wars1Tryptophan--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)
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 [...] (588 aa)
AsnsAsparagine synthetase [glutamine-hydrolyzing]. (561 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 [...] (594 aa)
Rars1Arginine--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. Belongs to the class-I aminoacyl-tRNA synthetase family. (660 aa)
Your Current Organism:
Rattus norvegicus
NCBI taxonomy Id: 10116
Other names: Buffalo rat, Norway rat, R. norvegicus, Rattus PC12 clone IS, Rattus sp. strain Wistar, Sprague-Dawley rat, Wistar rats, brown rat, laboratory rat, rat, rats, zitter rats
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