Reviewed,
UniProtKB/Swiss-Prot Q96I59 (SYNM_HUMAN)
Last modified
October 13, 2009.
Version 63.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Probable asparaginyl-tRNA synthetase, mitochondrial EC=6.1.1.22 Alternative name(s): Asparagine--tRNA ligase Short name=AsnRS | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Complete proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 477 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn). |
| Subcellular location | Mitochondrion matrix By similarity. |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Mitochondrion |
| Coding sequence diversity | Polymorphism |
| Domain | Transit peptide |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| PTM | Acetylation |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | asparaginyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro aspartyl-tRNA aminoacylationInferred from sequence or structural similarity. Source: UniProtKB |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine-tRNA ligase activityInferred from sequence or structural similarity. Source: UniProtKB aspartate-tRNA ligase activityInferred from electronic annotation. Source: InterPro nucleic acid bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 14 | 14 | Mitochondrion Potential | ||||||
| Chain | 15 – 477 | 463 | Probable asparaginyl-tRNA synthetase, mitochondrial | PRO_0000250722 | |||||
Amino acid modifications | |||||||||
| Modified residue | 353 | 1 | N6-acetyllysine Ref.4 | ||||||
Natural variations | |||||||||
| Natural variant | 87 | 1 | T → N: dbSNP rs10501429. | VAR_052636 | |||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [2] | "Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS." Bonnefond L., Fender A., Rudinger-Thirion J., Giege R., Florentz C., Sissler M. Biochemistry 44:4805-4816(2005) [PubMed: 15779907] [Abstract] Cited for: IDENTIFICATION. |
| [3] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| [4] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-353, MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| BC007800 mRNA. Translation: AAH07800.2. | |
| IPI | IPI00101664. |
| RefSeq | NP_078954.4. |
| UniGene | Hs.503389 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1N9W based on UniProtKB Q9LCY8. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q96I59. |
Proteomic databases | |
| PRIDE | Q96I59. |
Genome annotation databases | |
| Ensembl | ENST00000281038; ENSP00000281038; ENSG00000137513; Homo sapiens. [Genome view] |
| GeneID | 79731. |
| KEGG | hsa:79731. |
| UCSC | uc001ozi.1. human. |
Organism-specific databases | |
| GeneCards | GC11M077825. |
| HGNC | HGNC:26274. NARS2. |
| HPA | HPA026793. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | Q96I59. |
Enzyme and pathway databases | |
| BRENDA | 6.1.1.22. 247. |
| Reactome | REACT_71. Gene Expression. |
Gene expression databases | |
| ArrayExpress | Q96I59. |
| Bgee | Q96I59. |
| CleanEx | HS_NARS2. |
| Genevestigator | Q96I59. |
| GermOnline | ENSG00000137513. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II_cons-reg. IPR004522. Asn-tRNA-synth_IIb. IPR002312. Asp-tRNA-synth_IIb. IPR012340. NA-bd_OB-fold. IPR004365. NA_bd_OB_tRNA-helicase. [Graphical view] |
| Gene3D | G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. |
| PANTHER | PTHR22594. aa-tRNA-synt_II. 1 hit. |
| Pfam | PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view] |
| PRINTS | PR01042. TRNASYNTHASP. |
| TIGRFAMs | TIGR00457. asnS. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| DrugBank | DB00174. L-Asparagine. |
| NextBio | 69114. |
Entry information
| Entry name | SYNM_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q96I59 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Aminoacyl-tRNA synthetases List of aminoacyl-tRNA synthetase entries |
| Human chromosome 11 Human chromosome 11: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| SIMILARITY comments Index of protein domains and families |

Clusters with


