O43776 (SYNC_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 105.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Asparagine--tRNA ligase, cytoplasmic EC=6.1.1.22 Alternative name(s): Asparaginyl-tRNA synthetase Short name=AsnRS | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 548 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 | |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Protein biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Aminoacyl-tRNA synthetase Ligase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological process | asparaginyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytosol Traceable author statement. Source: Reactome soluble fractionTraceable author statement. Source: ProtInc |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine-tRNA ligase activityTraceable author statement. Source: ProtInc 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.5 | ||||||
| Chain | 2 – 548 | 547 | Asparagine--tRNA ligase, cytoplasmic | PRO_0000176496 | |||||
Amino acid modifications | |||||||||
| Modified residue | 61 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 244 | 1 | N6-acetyllysine Ref.7 | ||||||
| Modified residue | 482 | 1 | Phosphoserine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 391 | 1 | M → V in BAD96555. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression in Escherichia coli and characterization as human autoantigen." Beaulande M., Tarbouriech N., Haertlein M. Nucleic Acids Res. 26:521-524(1998) [PubMed: 9421509] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "Human asparaginyl-tRNA synthetase: molecular cloning and the inference of the evolutionary history of Asx-tRNA synthetase family." Shiba K., Motegi H., Yoshida M., Noda T. Nucleic Acids Res. 26:5045-5051(1998) [PubMed: 9801298] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [3] | Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver. |
| [4] | "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: Colon. |
| [5] | "Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini." Xu G., Shin S.B., Jaffrey S.R. Proc. Natl. Acad. Sci. U.S.A. 106:19310-19315(2009) [PubMed: 19892738] [Abstract] Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 2-12. Tissue: Leukemic T-cell. |
| [6] | "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [7] | "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-244, MASS SPECTROMETRY. |
| [8] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AJ000334 mRNA. Translation: CAA04008.1. D84273 mRNA. Translation: BAA34600.1. AK222835 mRNA. Translation: BAD96555.1. BC001687 mRNA. Translation: AAH01687.1. |
| IPI | IPI00306960. |
| RefSeq | NP_004530.1. NM_004539.3. |
| UniGene | Hs.465224. |
3D structure databases | |
| ProteinModelPortal | O43776. |
| SMR | O43776. Positions 115-548. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | O43776. 3 interactions. |
| MINT | MINT-5003848. |
| STRING | O43776. |
PTM databases | |
| PhosphoSite | O43776. |
Proteomic databases | |
| PeptideAtlas | O43776. |
| PRIDE | O43776. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000256854; ENSP00000256854; ENSG00000134440. |
| GeneID | 4677. |
| KEGG | hsa:4677. |
| NMPDR | fig|9606.3.peg.15060. |
| UCSC | uc002lgs.2. human. |
Organism-specific databases | |
| CTD | 4677. |
| GeneCards | GC18M055242. |
| H-InvDB | HIX0014473. |
| HGNC | HGNC:7643. NARS. |
| MIM | 108410. gene. |
| neXtProt | NX_O43776. |
| PharmGKB | PA31447. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG07882. |
| GeneTree | ENSGT00550000074893. |
| HOGENOM | HBG745843. |
| HOVERGEN | HBG059844. |
| InParanoid | O43776. |
| OMA | CMVQTQV. |
| OrthoDB | EOG4G1MG6. |
| PhylomeDB | O43776. |
Enzyme and pathway databases | |
| BRENDA | 6.1.1.22. 2681. |
| Reactome | REACT_71. Gene Expression. |
Gene expression databases | |
| ArrayExpress | O43776. |
| Bgee | O43776. |
| CleanEx | HS_ASNS. HS_NARS. |
| Genevestigator | O43776. |
| GermOnline | ENSG00000134440. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II. IPR004522. Asn-tRNA-synth_IIb. IPR002312. Asp/Asn-tRNA-synth_IIb. IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR004365. NA-bd_OB_tRNA-helicase. [Graphical view] |
| Gene3D | G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit. |
| KO | K01893. |
| PANTHER | PTHR22594. aa-tRNA-synt_II. 1 hit. PTHR22594:SF6. PTHR22594:SF6. 1 hit. |
| Pfam | PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view] |
| PRINTS | PR01042. TRNASYNTHASP. |
| SUPFAM | SSF50249. Nucleic_acid_OB. 1 hit. |
| TIGRFAMs | TIGR00457. AsnS. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| DrugBank | DB00174. L-Asparagine. |
| NextBio | 18028. |
| SOURCE | Search... |
Entry information
| Entry name | SYNC_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O43776 Secondary accession number(s): Q53GU6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| 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 18 Human chromosome 18: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with