| + |
ATP(4-) | up-regulates quantity 
precursor of
|
ADP(3-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269098 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10101268 |
The enzymes PtdIns 4-kinase (PI4K, for nomenclature see [3]) and PtdIns(4)P 5-kinase (PI4P5K) catalyse the phosphorylation of PtdIns at the D4 and consecutively at the D5 position. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268084 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19286649 |
ATP citrate lyase (ACL) is a cytosolic enzyme that catalyzes the synthesis of acetyl-CoA and oxaloacetate using citrate, CoA, and ATP as substrates and Mg(2+) as a necessary cofactor. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
DGUOK | down-regulates quantity 
chemical modification
|
ATP(4-) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280569 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17073823 |
DGUOK [dG (deoxyguanosine) kinase] is one of the two mitochondrial deoxynucleoside salvage pathway enzymes involved in precursor synthesis for mtDNA (mitochondrial DNA) replication. DGUOK is responsible for the initial rate-limiting phosphorylation of the purine deoxynucleosides, using a nucleoside triphosphate as phosphate donor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TK2 | down-regulates quantity
chemical modification
|
ATP(4-) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280578 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25215937 |
Thymidine kinase 2 (TK2, EC 27.1.21) catalyzes the transfer of the γ-phosphate group from ATP to the 5′-hydroxyl group of thymidine (dT), deoxycytidine (dC), or deoxyuridine (dU) to form their corresponding monophosphates. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UCKL1 | down-regulates quantity
chemical modification
|
ATP(4-) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280589 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 35583288 |
Uridine-cytidine kinase like-1 (UCKL-1) is a largely uncharacterized protein with high sequence similarity to other uridine-cytidine kinases (UCKs). UCKs play an important role in the pyrimidine salvage pathway, catalyzing the phosphorylation of uridine and cytidine to UMP and CMP, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UCK1 | down-regulates quantity
chemical modification
|
ATP(4-) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280597 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27239701 |
Uridine-cytidine kinase (UCK) is a pyrimidine ribonucleoside kinase that catalyses the first step of the pyrimidine salvage pathway, the phosphorylation of uridine and cytidine to UMP and CMP, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UCK2 | down-regulates quantity
chemical modification
|
ATP(4-) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280605 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27239701 |
Uridine-cytidine kinase (UCK) is a pyrimidine ribonucleoside kinase that catalyses the first step of the pyrimidine salvage pathway, the phosphorylation of uridine and cytidine to UMP and CMP, respectively. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TK1 | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280517 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17407781 |
The two dTTP biosynthetic routes are the de novo and the salvage pathways. Human thymidine kinase 1 (hTK1) catalyzes the first enzymatic step in the salvage pathway converting thymidine into thymidine monophosphate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ATP(4-) | up-regulates activity
chemical activation
|
P2RY2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257563 |
|
|
Homo sapiens |
HEK-293A Cell |
| pmid |
sentence |
| 31160049 |
Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signaling. | We defined positive coupling if any member of the subfamily scored LogRAi ≥ -1 and negative coupling if all of the members scored LogRAi < -1 (Figure 3A-B). ROC analysis gives AUC = 0.78 (Figure S4A) when considering high-confidence known coupling data and suggested a threshold of LogRAi ≥ -1.0 for defining true couplings. | The score associated to this interaction has a LogRAi ≥ -1.0. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
WARS1 | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270511 |
|
|
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 |
| + |
SARS1 | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270495 |
|
|
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 |
| + |
Multiaminoacyl-tRNA synthetase | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270412 |
|
|
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-270364 |
|
|
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-270396 |
|
|
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-270380 |
|
|
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-270372 |
|
|
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-270404 |
|
|
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-270388 |
|
|
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-270428 |
|
|
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-270420 |
|
|
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 |
| + |
HARS1 | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270487 |
|
|
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 |
| + |
DCK | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280558 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20637175 |
Human deoxycytidine kinase (dCK4; EC 2.7.1.74) catalyzes the phosphorylation of 2′-deoxycytidine (dCyd), 2′-deoxyadenosine and 2′-deoxyguanosine to their corresponding monophosphate forms, using ATP or UTP as phosphoryl donors. This reaction is the first and rate-limiting step of the deoxyribonucleoside salvage pathway, which provides deoxynucleoside triphosphates for DNA replication and repair as an alternative to de novo nucleotide synthesis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PIP5K1C | down-regulates activity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277285 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9367159 |
Phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2), a key molecule in the phosphoinositide signalling pathway, was thought to be synthesized exclusively by phosphorylation of PtdIns-4-P at the D-5 position of the inositol ring. The enzymes that produce PtdIns-4,5-P2 in vitro fall into two related subfamilies (type I and type II PtdInsP-5-OH kinases, or PIP(5)Ks) based on their enzymatic properties and sequence similarities |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AARS1 | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270448 |
|
|
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 |
| + |
GARS1 | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270479 |
|
|
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 |
| + |
CARS1 | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270471 |
|
|
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 |
| + |
ACSM3 | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280410 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40953271 |
Acyl-CoA synthetase medium-chain family member 3 (ACSM3) mainly accounts for catalyzing the MCFAs to produce the corresponding acyl-CoA, which is crucial for FAO |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YARS1 | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270519 |
|
|
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 |
| + |
ATP(4-) | up-regulates activity
chemical activation
|
P2RY4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257564 |
|
|
Homo sapiens |
HEK-293A Cell |
| pmid |
sentence |
| 31160049 |
Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signaling. | We defined positive coupling if any member of the subfamily scored LogRAi ≥ -1 and negative coupling if all of the members scored LogRAi < -1 (Figure 3A-B). ROC analysis gives AUC = 0.78 (Figure S4A) when considering high-confidence known coupling data and suggested a threshold of LogRAi ≥ -1.0 for defining true couplings. | The score associated to this interaction has a LogRAi ≥ -1.0. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NARS2 | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270463 |
|
|
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 |
| + |
ATP(4-) | up-regulates activity
chemical activation
|
P2RY11 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257559 |
|
|
Homo sapiens |
HEK-293A Cell |
| pmid |
sentence |
| 31160049 |
Here we systematically quantified ligand-induced interactions between 148 GPCRs and all 11 unique G alpha subunit C-termini. For each receptor, we probed chimeric G alpha subunit activation via a transforming growth factor-alpha (TGF alpha) shedding response in HEK293 cells lacking endogenous Gq/11- and G12/13- signaling. | We defined positive coupling if any member of the subfamily scored LogRAi ≥ -1 and negative coupling if all of the members scored LogRAi < -1 (Figure 3A-B). ROC analysis gives AUC = 0.78 (Figure S4A) when considering high-confidence known coupling data and suggested a threshold of LogRAi ≥ -1.0 for defining true couplings. | The score associated to this interaction has a LogRAi ≥ -1.0. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PI4K2B | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269100 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10101268 |
The enzymes PtdIns 4-kinase (PI4K, for nomenclature see [3]) and PtdIns(4)P 5-kinase (PI4P5K) catalyse the phosphorylation of PtdIns at the D4 and consecutively at the D5 position. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TARS1 | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270503 |
|
|
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 |
| + |
Phenylalanyl-tRNA synthetase | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270437 |
|
|
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 |
| + |
PI4KA | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269096 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10101268 |
The enzymes PtdIns 4-kinase (PI4K, for nomenclature see [3]) and PtdIns(4)P 5-kinase (PI4P5K) catalyse the phosphorylation of PtdIns at the D4 and consecutively at the D5 position. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NARS1 | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270455 |
|
|
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 |
| + |
ACLY | down-regulates quantity by destabilization
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268082 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19286649 |
ATP citrate lyase (ACL) is a cytosolic enzyme that catalyzes the synthesis of acetyl-CoA and oxaloacetate using citrate, CoA, and ATP as substrates and Mg(2+) as a necessary cofactor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
VARS1 | down-regulates quantity
chemical modification
|
ATP(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270527 |
|
|
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 |
| + |
ATP(4-) | up-regulates quantity
precursor of
|
2'-3'-cGAMP(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276594 |
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| pmid |
sentence |
| 23258413 |
Cytosolic DNA induces interferons through the production of cyclic guanosine monophosphate-adenosine monophosphate (cyclic GMP-AMP, or cGAMP), which binds to and activates the adaptor protein STING. Through biochemical fractionation and quantitative mass spectrometry, we identified a cGAMP synthase (cGAS), which belongs to the nucleotidyltransferase family. |
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| Publications: |
1 |
4.0
ATP(4-)