| IED ID | IndEnz0002009039 |
| Enzyme Type ID | protease009039 |
| Protein Name |
Asparagine--tRNA ligase, cytoplasmic EC 6.1.1.22 Asparaginyl-tRNA synthetase AsnRS Asparaginyl-tRNA synthetase 1 |
| Gene Name | NARS1 NARS NRS |
| Organism | Homo sapiens (Human) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human) |
| Enzyme Sequence | MVLAELYVSDREGSDATGDGTKEKPFKTGLKALMTVGKEPFPTIYVDSQKENERWNVISKSQLKNIKKMWHREQMKSESREKKEAEDSLRREKNLEEAKKITIKNDPSLPEPKCVKIGALEGYRGQRVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTESSVAVYGMLNLTPKGKQAPGGHELSCDFWELIGLAPAGGADNLINEESDVDVQLNNRHMMIRGENMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSSQLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCDVVDRILKSPAGSIVHELNPNFQPPKRPFKRMNYSDAIVWLKEHDVKKEDGTFYEFGEDIPEAPERLMTDTINEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSMRIFDSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYPRFVQRCTP |
| Enzyme Length | 548 |
| Uniprot Accession Number | O43776 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + H(+) + L-asparaginyl-tRNA(Asn); Xref=Rhea:RHEA:11180, Rhea:RHEA-COMP:9659, Rhea:RHEA-COMP:9674, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58048, ChEBI:CHEBI:78442, ChEBI:CHEBI:78515, ChEBI:CHEBI:456215; EC=6.1.1.22; Evidence={ECO:0000269|PubMed:32738225, ECO:0000269|PubMed:32788587, ECO:0000269|PubMed:9421509}; |
| DNA Binding | |
| EC Number | 6.1.1.22 |
| Enzyme Function | FUNCTION: Catalyzes the attachment of asparagine to tRNA(Asn) in a two-step reaction: asparagine is first activated by ATP to form Asn-AMP and then transferred to the acceptor end of tRNA(Asn) (PubMed:9421509, PubMed:32738225, PubMed:32788587). In addition to its essential role in protein synthesis, acts as a signaling molecule that induced migration of CCR3-expressing cells (PubMed:30171954, PubMed:12235211). Has an essential role in the development of the cerebral cortex, being required for proper proliferation of radial glial cells (PubMed:32788587). {ECO:0000269|PubMed:12235211, ECO:0000269|PubMed:30171954, ECO:0000269|PubMed:32738225, ECO:0000269|PubMed:32788587, ECO:0000269|PubMed:9421509}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Alternative sequence (2); Beta strand (22); Chain (1); Helix (21); Modified residue (4); Natural variant (13); Region (2); Sequence conflict (1); Turn (4) |
| Keywords | 3D-structure;ATP-binding;Acetylation;Alternative splicing;Aminoacyl-tRNA synthetase;Cytoplasm;Direct protein sequencing;Disease variant;Epilepsy;Ligase;Mental retardation;Neurodegeneration;Nucleotide-binding;Phosphoprotein;Protein biosynthesis;Reference proteome |
| Interact With | P54253 |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:9421509}. |
| Modified Residue | MOD_RES 61; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"; MOD_RES 244; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 482; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:Q8BP47"; MOD_RES 490; /note="N6-acetyllysine"; /evidence="ECO:0000250|UniProtKB:Q8BP47" |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 4ZYA; 5XIX; |
| Mapped Pubmed ID | 15231747; 16713569; 17353931; 19738201; 20711500; 20877624; 23752268; 23902751; 25609649; 25665578; 26638075; 27161446; |
| Motif | |
| Gene Encoded By | |
| Mass | 62,943 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:11180 |
| Cross Reference Brenda | 6.1.1.22; |