| + |
Multiaminoacyl-tRNA synthetase | up-regulates quantity 
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270416 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270400 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270408 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270368 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270384 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270392 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270376 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270424 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270432 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 28271488 |
Aminoacyl-tRNA synthetases (AARSs) are essential enzymes that specifically aminoacylate one tRNA molecule by the cognate amino acid. In mammals, nine synthetases, those specific for amino acids Arg, Asp, Gln, Glu, Ile, Leu, Lys, Met and Pro, associate into a multi-aminoacyl-tRNA synthetase complex, an association which is believed to play a key role in the cellular organization of translation, but also in the regulation of the translational and nontranslational functions of these enzymes. |
|
| Publications: |
9 |
Organism: |
Homo Sapiens |
| + |
ACP3 | down-regulates quantity 
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269740 |
|
|
in vitro |
|
| pmid |
sentence |
| 18940592 |
Specifically, PAP dephosphorylates extracellular adenosine monophosphate (AMP) to adenosine and activates A1-adenosine receptors in dorsal spinal cord. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
NARS1 | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270458 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32788587 |
Asparaginyl-tRNA synthetase1 (NARS1) is a member of the ubiquitously expressed cytoplasmic Class IIa family of tRNA synthetases required for protein translation. Asparaginyl-tRNA synthetase1 (NARS1) belongs to the class IIa family, based upon a 7 beta-strand protein structure. There are two NARS genes: NARS1 functions in the cytoplasm while NARS2 functions in mitochondria, solely responsible for asparagine tRNA charging in these locations. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VARS1 | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270529 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30755602 |
Aminoacyl-tRNA synthetases (ARSs) function to transfer amino acids to cognate tRNA molecules, which are required for protein translation. VARS encodes the only known valine cytoplasmic-localized aminoacyl-tRNA synthetase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
L-aspartate(1-) | up-regulates quantity
precursor of
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267529 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29084849 |
Asparagine synthetase (ASNS) converts aspartate and glutamine to asparagine and glutamate in an ATP-dependent reaction. ASNS is present in most, if not all, mammalian organs, but varies widely in basal expression. Human ASNS activity is highly responsive to cellular stress, primarily by increased transcription from a single gene located on chromosome 7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Nucleotide Biosynthesis |
| + |
SARS1 | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270497 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24095058 |
As a member of the aminoacyl-tRNA synthetase family, seryl-tRNA synthetase (SerRS) catalyzes the aminoacylation reaction that charges serine onto its cognate tRNA for protein synthesis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NT5E | down-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269743 |
|
|
in vitro |
|
| pmid |
sentence |
| 31461341 |
Ecto-5'-nucleotidase [cluster of differentiation 73 (CD73)] is a ubiquitously expressed glycosylphosphatidylinositol-anchored glycoprotein that converts extracellular adenosine 5'-monophosphate to adenosine. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AMP | form complex 
binding
|
ETF |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269468 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33450351 |
Human ETF is nuclear encoded by two separate genes, ETFA and ETFB, respectively. After translation, the two subunits are imported to the mitochondrial matrix space and assemble into a heterodimer containing one FAD and one AMP as cofactors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATP | up-regulates quantity
precursor of
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267837 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33961946 |
Adenosine kinase (ADK) is the key regulator of adenosine and catalyzes the metabolism of adenosine to 5′-adenosine monophosphate. The enzyme exists in two isoforms: a long isoform (ADK-long, ADK-L) and a short isoform (ADK-short, ADK-S). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
ADK | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267840 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33961946 |
Adenosine kinase (ADK) is the key regulator of adenosine and catalyzes the metabolism of adenosine to 5′-adenosine monophosphate. The enzyme exists in two isoforms: a long isoform (ADK-long, ADK-L) and a short isoform (ADK-short, ADK-S). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
D-glucopyranose | down-regulates 
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-69249 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10409121 |
The activation in response to glucose removal appeared to be due to changes in the concentration of the known regulators of the cascade, i.e. Amp and atp, since ampk activation was associated with a large increase in the cellular amp. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
adenosine | up-regulates quantity
precursor of
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265465 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18957298 |
Adenosine is an endogenous inhibitor of excitatory synaptic transmission with potent anticonvulsant properties in the mammalian brain. Given adenosine's important role in modulating synaptic transmission, several mechanisms exist to regulate its extracellular availability. One of these is the intracellular enzyme adenosine kinase (ADK), which phosphorylates adenosine to AMP. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
AMP | down-regulates activity
chemical inhibition
|
PRPS1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265737 |
|
|
|
|
| pmid |
sentence |
| 29074724 |
PRPS1 is inhibited by the nucleotide biosynthesis products ADP, AMP, and GDP |
|
| Publications: |
1 |
| + |
N(6)-(1,2-dicarboxylatoethyl)-AMP(4-) | up-regulates quantity
precursor of
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268067 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22812634 |
ADSL carries out two non-sequential steps of de novo AMP synthesis, the conversion of succinylaminoimidazolecarboxamide ribonucleotide (SAICAR) and succinyladenosine monophosphate (SAMP) into aminoimidazolecarboxamide ribotide (AICAR) and adenosine monophosphate (AMP), respectively, with the concomitant release of fumarate in each case |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
AMP | up-regulates quantity
precursor of
|
adenosine |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269741 |
|
|
in vitro |
|
| pmid |
sentence |
| 31461341 |
Ecto-5'-nucleotidase [cluster of differentiation 73 (CD73)] is a ubiquitously expressed glycosylphosphatidylinositol-anchored glycoprotein that converts extracellular adenosine 5'-monophosphate to adenosine. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269738 |
|
|
in vitro |
|
| pmid |
sentence |
| 18940592 |
Specifically, PAP dephosphorylates extracellular adenosine monophosphate (AMP) to adenosine and activates A1-adenosine receptors in dorsal spinal cord. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| Pathways: | Nucleotide Biosynthesis |
| + |
Phenylalanyl-tRNA synthetase | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270441 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20223217 |
Here we report crystal structure of hcPheRS complexed with phenylalanine at 3.3 Å resolution. An essential feature of hcPheRS is a novel fold formed by the N-terminal part of the α subunit, whose functional role in tRNAPhe binding and complex formation was studied by truncation mutagenesis. Phenylalanine activation and formation of Phe-tRNAPhe catalyzed by modified hcPheRS have been compared with those of the wild-type enzyme. HcPheRS is a heterotetramer built of two αβ heterodimers. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ASNS | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267534 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29084849 |
Asparagine synthetase (ASNS) converts aspartate and glutamine to asparagine and glutamate in an ATP-dependent reaction. ASNS is present in most, if not all, mammalian organs, but varies widely in basal expression. Human ASNS activity is highly responsive to cellular stress, primarily by increased transcription from a single gene located on chromosome 7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Glutamine metabolism |
| + |
HARS1 | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270489 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10430027 |
Histidyl-tRNA synthetase (HisRS) is responsible for the synthesis of histidyl-transfer RNA, which is essential for the incorporation of histidine into proteins. This amino acid has uniquely moderate basic properties and is an important group in many catalytic functions of enzymes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GARS1 | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270481 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24898252 |
Aminoacyl-tRNA synthetases are an ancient enzyme family that specifically charges tRNA molecules with cognate amino acids for protein synthesis. Glycyl- tRNA synthetase (GlyRS) is one of the most intriguing aminoacyl-tRNA synthetases due to its divergent quaternary structure and abnormal charging properties. . In this study we report crystal structures of wild type and mutant hGlyRS in complex with tRNA and with small substrates and describe the molecular details of enzymatic recognition of the key tRNA identity elements in the acceptor stem and the anticodon loop. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WARS1 | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270513 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 14660560 |
Aminoacyl-tRNA synthetases (aaRSs)1 are a family of ancient enzymes that catalyze amino acid activation by ATP and the subsequent aminoacylation to its cognate tRNA. Alternative splicing produces two forms of hTrpRS in human cells: full-length hTrpRS (residues 1-471) and mini-hTrpRS (residues 48-471) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AARS1 | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270450 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32314272 |
Alanyl-tRNA synthetase 1 (AARS1) gene encodes a ubiquitously expressed class II enzyme that catalyzes the attachment of alanine to the cognate tRNA. AARS1 mutations are frequently responsible for autosomal dominant Charcot-Marie-Tooth disease type 2N (CMT2N). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
L-glutamine zwitterion | up-regulates quantity
precursor of
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267530 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29084849 |
Asparagine synthetase (ASNS) converts aspartate and glutamine to asparagine and glutamate in an ATP-dependent reaction. ASNS is present in most, if not all, mammalian organs, but varies widely in basal expression. Human ASNS activity is highly responsive to cellular stress, primarily by increased transcription from a single gene located on chromosome 7. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Aspartate and asparagine metabolism, Glutamine metabolism, Nucleotide Biosynthesis |
| + |
YARS1 | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270521 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16429158 |
YARS (also known as TyrRS) catalyzes the aminoacylation of tRNATyr with tyrosine by a two-step mechanism. Tyrosine is first activated by ATP to form tyrosyl-adenylate and is then transferred to tRNATyr |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TARS1 | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270505 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25824639 |
Here we show, using X-ray crystal structures and functional analyses, that a single molecule of borrelidin simultaneously occupies four distinct subsites within the catalytic domain of bacterial and human ThrRSs. These include the three substrate-binding sites for amino acid, ATP and tRNA associated with aminoacylation, and a fourth 'orthogonal' subsite created as a consequence of binding. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ADSL | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266607 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22812634 |
ADSL carries out two non-sequential steps of de novo AMP synthesis, the conversion of succinylaminoimidazolecarboxamide ribonucleotide (SAICAR) and succinyladenosine monophosphate (SAMP) into aminoimidazolecarboxamide ribotide (AICAR) and adenosine monophosphate (AMP), respectively, with the concomitant release of fumarate in each case |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Nucleotide Biosynthesis |
| + |
NARS2 | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270466 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 32788587 |
Asparaginyl-tRNA synthetase1 (NARS1) is a member of the ubiquitously expressed cytoplasmic Class IIa family of tRNA synthetases required for protein translation. Asparaginyl-tRNA synthetase1 (NARS1) belongs to the class IIa family, based upon a 7 beta-strand protein structure. There are two NARS genes: NARS1 functions in the cytoplasm while NARS2 functions in mitochondria, solely responsible for asparagine tRNA charging in these locations. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMP | down-regulates activity
chemical inhibition
|
MLXIPL |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255668 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 26984404 |
We discovered that protein-free extracts of high fat-fed livers contained, in addition to ketone bodies, a new metabolite, identified as AMP, which specifically activates the interaction between ChREBP and 14-3-3. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CARS1 | up-regulates quantity
chemical modification
|
AMP |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270473 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11347887 |
Cysteinyl-tRNA synthetase catalyzes the addition of cysteine to its cognate tRNA. Here we report the isolation of a fulllength cDNA that encodes a protein of 748 amino acids. The predicted protein sequence shows considerable similarity to other eukaryotic cysteinyltRNA synthetases in the carboxylterminus. Expression of the fulllength and alternative forms of the enzyme in E. coli generated functional proteins that were active in aminoacylation of human cytoplasmic tRNA with cysteine. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
AMP