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UniProtKB - O43776 (SYNC_HUMAN)
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>sp|O43776|SYNC_HUMAN Asparagine--tRNA ligase, cytoplasmic OS=Homo sapiens OX=9606 GN=NARS1 PE=1 SV=1 MVLAELYVSDREGSDATGDGTKEKPFKTGLKALMTVGKEPFPTIYVDSQKENERWNVISK SQLKNIKKMWHREQMKSESREKKEAEDSLRREKNLEEAKKITIKNDPSLPEPKCVKIGAL EGYRGQRVKVFGWVHRLRRQGKNLMFLVLRDGTGYLQCVLADELCQCYNGVLLSTESSVA VYGMLNLTPKGKQAPGGHELSCDFWELIGLAPAGGADNLINEESDVDVQLNNRHMMIRGE NMSKILKARSMVTRCFRDHFFDRGYYEVTPPTLVQTQVEGGATLFKLDYFGEEAFLTQSS QLYLETCLPALGDVFCIAQSYRAEQSRTRRHLAEYTHVEAECPFLTFDDLLNRLEDLVCD VVDRILKSPAGSIVHELNPNFQPPKRPFKRMNYSDAIVWLKEHDVKKEDGTFYEFGEDIP EAPERLMTDTINEPILLCRFPVEIKSFYMQRCPEDSRLTESVDVLMPNVGEIVGGSMRIF DSEEILAGYKREGIDPTPYYWYTDQRKYGTCPHGGYGLGLERFLTWILNRYHIRDVCLYP RFVQRCTPCommunity curation ()Add a publicationFeedback
Protein
Asparagine--tRNA ligase, cytoplasmic
Gene
NARS1
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
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).
5 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION. - Ref.8"Histidyl-tRNA synthetase and asparaginyl-tRNA synthetase, autoantigens in myositis, activate chemokine receptors on T lymphocytes and immature dendritic cells."
Howard O.M., Dong H.F., Yang D., Raben N., Nagaraju K., Rosen A., Casciola-Rosen L., Haertlein M., Kron M., Yang D., Yiadom K., Dwivedi S., Plotz P.H., Oppenheim J.J.
J. Exp. Med. 196:781-791(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.18"Unique N-terminal extension domain of human asparaginyl-tRNA synthetase elicits CCR3-mediated chemokine activity."
Park J.S., Park M.C., Lee K.Y., Goughnour P.C., Jeong S.J., Kim H.S., Kim H.J., Lee B.J., Kim S., Han B.W.
Int. J. Biol. Macromol. 120:835-845(2018) [PubMed] [Europe PMC] [Abstract] - Ref.19"De novo and bi-allelic pathogenic variants in NARS1 cause neurodevelopmental delay due to toxic gain-of-function and partial loss-of-function effects."
SYNAPS Study Group
Manole A., Efthymiou S., O'Connor E., Mendes M.I., Jennings M., Maroofian R., Davagnanam I., Mankad K., Lopez M.R., Salpietro V., Harripaul R., Badalato L., Walia J., Francklyn C.S., Athanasiou-Fragkouli A., Sullivan R., Desai S., Baranano K. , Zafar F., Rana N., Ilyas M., Horga A., Kara M., Mattioli F., Goldenberg A., Griffin H., Piton A., Henderson L.B., Kara B., Aslanger A.D., Raaphorst J., Pfundt R., Portier R., Shinawi M., Kirby A., Christensen K.M., Wang L., Rosti R.O., Paracha S.A., Sarwar M.T., Jenkins D., Ahmed J., Santoni F.A., Ranza E., Iwaszkiewicz J., Cytrynbaum C., Weksberg R., Wentzensen I.M., Guillen Sacoto M.J., Si Y., Telegrafi A., Andrews M.V., Baldridge D., Gabriel H., Mohr J., Oehl-Jaschkowitz B., Debard S., Senger B., Fischer F., van Ravenwaaij C., Fock A.J.M., Stevens S.J.C., Baehler J., Nasar A., Mantovani J.F., Manzur A., Sarkozy A., Smith D.E.C., Salomons G.S., Ahmed Z.M., Riazuddin S., Riazuddin S., Usmani M.A., Seibt A., Ansar M., Antonarakis S.E., Vincent J.B., Ayub M., Grimmel M., Jelsig A.M., Hjortshoej T.D., Karstensen H.G., Hummel M., Haack T.B., Jamshidi Y., Distelmaier F., Horvath R., Gleeson J.G., Becker H., Mandel J.L., Koolen D.A., Houlden H.
Am. J. Hum. Genet. 107:311-324(2020) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NEDMILG PRO-11; MET-17; GLU-60; 90-ARG--PRO-548 DEL; CYS-132; PRO-350; ALA-356; THR-422; ILE-459 AND CYS-545, VARIANTS NEDMILEG LEU-322; SER-509 AND 534-ARG--PRO-548 DEL, INVOLVEMENT IN NEDMILG, INVOLVEMENT IN NEDMILEG, CHARACTERIZATION OF VARIANT NEDMILG PRO-11, CHARACTERIZATION OF VARIANTS NEDMILEG LEU-322 AND 534-ARG--PRO-548 DEL, FUNCTION, CATALYTIC ACTIVITY. - Ref.20"Loss of NARS1 impairs progenitor proliferation in cortical brain organoids and leads to microcephaly."
Wang L., Li Z., Sievert D., Smith D.E.C., Mendes M.I., Chen D.Y., Stanley V., Ghosh S., Wang Y., Kara M., Aslanger A.D., Rosti R.O., Houlden H., Salomons G.S., Gleeson J.G.
Nat. Commun. 11:4038-4038(2020) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN NEDMILG, VARIANTS NEDMILG MET-17; ALA-356 AND CYS-545, CHARACTERIZATION OF VARIANT NEDMILG MET-17, FUNCTION, CATALYTIC ACTIVITY.
Miscellaneous
Autoantibodies to NARS1, are often detected in sera from patients with interstitial lung disease (ILD).1 Publication
Manual assertion based on experiment ini
- Ref.7"Anti-KS: identification of autoantibodies to asparaginyl-transfer RNA synthetase associated with interstitial lung disease."
Hirakata M., Suwa A., Nagai S., Kron M.A., Trieu E.P., Mimori T., Akizuki M., Targoff I.N.
J. Immunol. 162:2315-2320(1999) [PubMed] [Europe PMC] [Abstract]Cited for: AUTOANTIBODIES.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
- ATPEC:6.1.1.22
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Manual assertion based on experiment ini
- Ref.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] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION. - Ref.19"De novo and bi-allelic pathogenic variants in NARS1 cause neurodevelopmental delay due to toxic gain-of-function and partial loss-of-function effects."
SYNAPS Study Group
Manole A., Efthymiou S., O'Connor E., Mendes M.I., Jennings M., Maroofian R., Davagnanam I., Mankad K., Lopez M.R., Salpietro V., Harripaul R., Badalato L., Walia J., Francklyn C.S., Athanasiou-Fragkouli A., Sullivan R., Desai S., Baranano K. , Zafar F., Rana N., Ilyas M., Horga A., Kara M., Mattioli F., Goldenberg A., Griffin H., Piton A., Henderson L.B., Kara B., Aslanger A.D., Raaphorst J., Pfundt R., Portier R., Shinawi M., Kirby A., Christensen K.M., Wang L., Rosti R.O., Paracha S.A., Sarwar M.T., Jenkins D., Ahmed J., Santoni F.A., Ranza E., Iwaszkiewicz J., Cytrynbaum C., Weksberg R., Wentzensen I.M., Guillen Sacoto M.J., Si Y., Telegrafi A., Andrews M.V., Baldridge D., Gabriel H., Mohr J., Oehl-Jaschkowitz B., Debard S., Senger B., Fischer F., van Ravenwaaij C., Fock A.J.M., Stevens S.J.C., Baehler J., Nasar A., Mantovani J.F., Manzur A., Sarkozy A., Smith D.E.C., Salomons G.S., Ahmed Z.M., Riazuddin S., Riazuddin S., Usmani M.A., Seibt A., Ansar M., Antonarakis S.E., Vincent J.B., Ayub M., Grimmel M., Jelsig A.M., Hjortshoej T.D., Karstensen H.G., Hummel M., Haack T.B., Jamshidi Y., Distelmaier F., Horvath R., Gleeson J.G., Becker H., Mandel J.L., Koolen D.A., Houlden H.
Am. J. Hum. Genet. 107:311-324(2020) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NEDMILG PRO-11; MET-17; GLU-60; 90-ARG--PRO-548 DEL; CYS-132; PRO-350; ALA-356; THR-422; ILE-459 AND CYS-545, VARIANTS NEDMILEG LEU-322; SER-509 AND 534-ARG--PRO-548 DEL, INVOLVEMENT IN NEDMILG, INVOLVEMENT IN NEDMILEG, CHARACTERIZATION OF VARIANT NEDMILG PRO-11, CHARACTERIZATION OF VARIANTS NEDMILEG LEU-322 AND 534-ARG--PRO-548 DEL, FUNCTION, CATALYTIC ACTIVITY. - Ref.20"Loss of NARS1 impairs progenitor proliferation in cortical brain organoids and leads to microcephaly."
Wang L., Li Z., Sievert D., Smith D.E.C., Mendes M.I., Chen D.Y., Stanley V., Ghosh S., Wang Y., Kara M., Aslanger A.D., Rosti R.O., Houlden H., Salomons G.S., Gleeson J.G.
Nat. Commun. 11:4038-4038(2020) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN NEDMILG, VARIANTS NEDMILG MET-17; ALA-356 AND CYS-545, CHARACTERIZATION OF VARIANT NEDMILG MET-17, FUNCTION, CATALYTIC ACTIVITY.
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Manual assertion based on experiment ini
- Ref.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] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION. - Ref.19"De novo and bi-allelic pathogenic variants in NARS1 cause neurodevelopmental delay due to toxic gain-of-function and partial loss-of-function effects."
SYNAPS Study Group
Manole A., Efthymiou S., O'Connor E., Mendes M.I., Jennings M., Maroofian R., Davagnanam I., Mankad K., Lopez M.R., Salpietro V., Harripaul R., Badalato L., Walia J., Francklyn C.S., Athanasiou-Fragkouli A., Sullivan R., Desai S., Baranano K. , Zafar F., Rana N., Ilyas M., Horga A., Kara M., Mattioli F., Goldenberg A., Griffin H., Piton A., Henderson L.B., Kara B., Aslanger A.D., Raaphorst J., Pfundt R., Portier R., Shinawi M., Kirby A., Christensen K.M., Wang L., Rosti R.O., Paracha S.A., Sarwar M.T., Jenkins D., Ahmed J., Santoni F.A., Ranza E., Iwaszkiewicz J., Cytrynbaum C., Weksberg R., Wentzensen I.M., Guillen Sacoto M.J., Si Y., Telegrafi A., Andrews M.V., Baldridge D., Gabriel H., Mohr J., Oehl-Jaschkowitz B., Debard S., Senger B., Fischer F., van Ravenwaaij C., Fock A.J.M., Stevens S.J.C., Baehler J., Nasar A., Mantovani J.F., Manzur A., Sarkozy A., Smith D.E.C., Salomons G.S., Ahmed Z.M., Riazuddin S., Riazuddin S., Usmani M.A., Seibt A., Ansar M., Antonarakis S.E., Vincent J.B., Ayub M., Grimmel M., Jelsig A.M., Hjortshoej T.D., Karstensen H.G., Hummel M., Haack T.B., Jamshidi Y., Distelmaier F., Horvath R., Gleeson J.G., Becker H., Mandel J.L., Koolen D.A., Houlden H.
Am. J. Hum. Genet. 107:311-324(2020) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NEDMILG PRO-11; MET-17; GLU-60; 90-ARG--PRO-548 DEL; CYS-132; PRO-350; ALA-356; THR-422; ILE-459 AND CYS-545, VARIANTS NEDMILEG LEU-322; SER-509 AND 534-ARG--PRO-548 DEL, INVOLVEMENT IN NEDMILG, INVOLVEMENT IN NEDMILEG, CHARACTERIZATION OF VARIANT NEDMILG PRO-11, CHARACTERIZATION OF VARIANTS NEDMILEG LEU-322 AND 534-ARG--PRO-548 DEL, FUNCTION, CATALYTIC ACTIVITY. - Ref.20"Loss of NARS1 impairs progenitor proliferation in cortical brain organoids and leads to microcephaly."
Wang L., Li Z., Sievert D., Smith D.E.C., Mendes M.I., Chen D.Y., Stanley V., Ghosh S., Wang Y., Kara M., Aslanger A.D., Rosti R.O., Houlden H., Salomons G.S., Gleeson J.G.
Nat. Commun. 11:4038-4038(2020) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN NEDMILG, VARIANTS NEDMILG MET-17; ALA-356 AND CYS-545, CHARACTERIZATION OF VARIANT NEDMILG MET-17, FUNCTION, CATALYTIC ACTIVITY.
Source: Rhea- Search for this reaction in UniProtKB.
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+L-asparagine- Search proteins in UniProtKB for this molecule.
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AMP 3'-end residuezoom- Search proteins in UniProtKB for this molecule.
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3'-(L-asparaginyl)adenylyl groupzoom- Search proteins in UniProtKB for this molecule.
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<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- asparagine-tRNA ligase activity Source: UniProtKB
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- Ref.19"De novo and bi-allelic pathogenic variants in NARS1 cause neurodevelopmental delay due to toxic gain-of-function and partial loss-of-function effects."
SYNAPS Study Group
Manole A., Efthymiou S., O'Connor E., Mendes M.I., Jennings M., Maroofian R., Davagnanam I., Mankad K., Lopez M.R., Salpietro V., Harripaul R., Badalato L., Walia J., Francklyn C.S., Athanasiou-Fragkouli A., Sullivan R., Desai S., Baranano K. , Zafar F., Rana N., Ilyas M., Horga A., Kara M., Mattioli F., Goldenberg A., Griffin H., Piton A., Henderson L.B., Kara B., Aslanger A.D., Raaphorst J., Pfundt R., Portier R., Shinawi M., Kirby A., Christensen K.M., Wang L., Rosti R.O., Paracha S.A., Sarwar M.T., Jenkins D., Ahmed J., Santoni F.A., Ranza E., Iwaszkiewicz J., Cytrynbaum C., Weksberg R., Wentzensen I.M., Guillen Sacoto M.J., Si Y., Telegrafi A., Andrews M.V., Baldridge D., Gabriel H., Mohr J., Oehl-Jaschkowitz B., Debard S., Senger B., Fischer F., van Ravenwaaij C., Fock A.J.M., Stevens S.J.C., Baehler J., Nasar A., Mantovani J.F., Manzur A., Sarkozy A., Smith D.E.C., Salomons G.S., Ahmed Z.M., Riazuddin S., Riazuddin S., Usmani M.A., Seibt A., Ansar M., Antonarakis S.E., Vincent J.B., Ayub M., Grimmel M., Jelsig A.M., Hjortshoej T.D., Karstensen H.G., Hummel M., Haack T.B., Jamshidi Y., Distelmaier F., Horvath R., Gleeson J.G., Becker H., Mandel J.L., Koolen D.A., Houlden H.
Am. J. Hum. Genet. 107:311-324(2020) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NEDMILG PRO-11; MET-17; GLU-60; 90-ARG--PRO-548 DEL; CYS-132; PRO-350; ALA-356; THR-422; ILE-459 AND CYS-545, VARIANTS NEDMILEG LEU-322; SER-509 AND 534-ARG--PRO-548 DEL, INVOLVEMENT IN NEDMILG, INVOLVEMENT IN NEDMILEG, CHARACTERIZATION OF VARIANT NEDMILG PRO-11, CHARACTERIZATION OF VARIANTS NEDMILEG LEU-322 AND 534-ARG--PRO-548 DEL, FUNCTION, CATALYTIC ACTIVITY. - Ref.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] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION.
- ATP binding Source: UniProtKB-KW
- CCR3 chemokine receptor binding Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.18"Unique N-terminal extension domain of human asparaginyl-tRNA synthetase elicits CCR3-mediated chemokine activity."
Park J.S., Park M.C., Lee K.Y., Goughnour P.C., Jeong S.J., Kim H.S., Kim H.J., Lee B.J., Kim S., Han B.W.
Int. J. Biol. Macromol. 120:835-845(2018) [PubMed] [Europe PMC] [Abstract]
- nucleic acid binding Source: InterPro
- protein dimerization activity Source: UniProtKBInferred from direct assayi
- Ref.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] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION.
GO - Biological processi
- asparaginyl-tRNA aminoacylation Source: UniProtKBInferred from direct assayi
- Ref.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] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION.
- cell migration Source: UniProtKBInferred from direct assayi
- Ref.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] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION.
- cerebral cortex development Source: UniProtKBInferred from mutant phenotypei
- Ref.20"Loss of NARS1 impairs progenitor proliferation in cortical brain organoids and leads to microcephaly."
Wang L., Li Z., Sievert D., Smith D.E.C., Mendes M.I., Chen D.Y., Stanley V., Ghosh S., Wang Y., Kara M., Aslanger A.D., Rosti R.O., Houlden H., Salomons G.S., Gleeson J.G.
Nat. Commun. 11:4038-4038(2020) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN NEDMILG, VARIANTS NEDMILG MET-17; ALA-356 AND CYS-545, CHARACTERIZATION OF VARIANT NEDMILG MET-17, FUNCTION, CATALYTIC ACTIVITY.
- tRNA aminoacylation for protein translation Source: Reactome
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Aminoacyl-tRNA synthetase, Ligase |
| Biological process | Protein biosynthesis |
| Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 6.1.1.22, 2681 |
Pathway Commons web resource for biological pathway data More...PathwayCommonsi | O43776 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-379716, Cytosolic tRNA aminoacylation |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Asparagine--tRNA ligase, cytoplasmic (EC:6.1.1.22
Manual assertion based on experiment ini
Alternative name(s): Asparaginyl-tRNA synthetase Short name: AsnRS Asparaginyl-tRNA synthetase 1Imported <p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:NARS1Imported Manual assertion inferred from database entriesi Synonyms:NARS, NRS1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Human Gene Nomenclature Database More...HGNCi | HGNC:7643, NARS1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 108410, gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O43776 |
Eukaryotic Pathogen, Vector and Host Database Resources More...VEuPathDBi | HostDB:ENSG00000134440 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.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] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION.
- Cytoplasm 1 Publication
Cytosol
- cytosol Source: HPA
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- "Large-scale proteomics and phosphoproteomics of urinary exosomes."
Gonzales P.A., Pisitkun T., Hoffert J.D., Tchapyjnikov D., Star R.A., Kleta R., Wang N.S., Knepper M.A.
J Am Soc Nephrol 20:363-379(2009) [PubMed] [Europe PMC] [Abstract] - "In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine."
Principe S., Jones E.E., Kim Y., Sinha A., Nyalwidhe J.O., Brooks J., Semmes O.J., Troyer D.A., Lance R.S., Kislinger T., Drake R.R.
Proteomics 13:1667-1671(2013) [PubMed] [Europe PMC] [Abstract]
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Other locations
- cytoplasm Source: ProtInc
<p>Traceable Author Statement</p>
<p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p>
Traceable author statementi
- Ref.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] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION.
- cytoplasm Source: ProtInc
<p>Traceable Author Statement</p>
<p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p>
Traceable author statementi
Keywords - Cellular componenti
Cytoplasm<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Neurodevelopmental disorder with microcephaly, impaired language, and gait abnormalities (NEDMILG)2 PublicationsManual assertion based on experiment ini
- Ref.19"De novo and bi-allelic pathogenic variants in NARS1 cause neurodevelopmental delay due to toxic gain-of-function and partial loss-of-function effects."
SYNAPS Study Group
Manole A., Efthymiou S., O'Connor E., Mendes M.I., Jennings M., Maroofian R., Davagnanam I., Mankad K., Lopez M.R., Salpietro V., Harripaul R., Badalato L., Walia J., Francklyn C.S., Athanasiou-Fragkouli A., Sullivan R., Desai S., Baranano K. , Zafar F., Rana N., Ilyas M., Horga A., Kara M., Mattioli F., Goldenberg A., Griffin H., Piton A., Henderson L.B., Kara B., Aslanger A.D., Raaphorst J., Pfundt R., Portier R., Shinawi M., Kirby A., Christensen K.M., Wang L., Rosti R.O., Paracha S.A., Sarwar M.T., Jenkins D., Ahmed J., Santoni F.A., Ranza E., Iwaszkiewicz J., Cytrynbaum C., Weksberg R., Wentzensen I.M., Guillen Sacoto M.J., Si Y., Telegrafi A., Andrews M.V., Baldridge D., Gabriel H., Mohr J., Oehl-Jaschkowitz B., Debard S., Senger B., Fischer F., van Ravenwaaij C., Fock A.J.M., Stevens S.J.C., Baehler J., Nasar A., Mantovani J.F., Manzur A., Sarkozy A., Smith D.E.C., Salomons G.S., Ahmed Z.M., Riazuddin S., Riazuddin S., Usmani M.A., Seibt A., Ansar M., Antonarakis S.E., Vincent J.B., Ayub M., Grimmel M., Jelsig A.M., Hjortshoej T.D., Karstensen H.G., Hummel M., Haack T.B., Jamshidi Y., Distelmaier F., Horvath R., Gleeson J.G., Becker H., Mandel J.L., Koolen D.A., Houlden H.
Am. J. Hum. Genet. 107:311-324(2020) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NEDMILG PRO-11; MET-17; GLU-60; 90-ARG--PRO-548 DEL; CYS-132; PRO-350; ALA-356; THR-422; ILE-459 AND CYS-545, VARIANTS NEDMILEG LEU-322; SER-509 AND 534-ARG--PRO-548 DEL, INVOLVEMENT IN NEDMILG, INVOLVEMENT IN NEDMILEG, CHARACTERIZATION OF VARIANT NEDMILG PRO-11, CHARACTERIZATION OF VARIANTS NEDMILEG LEU-322 AND 534-ARG--PRO-548 DEL, FUNCTION, CATALYTIC ACTIVITY. - Ref.20"Loss of NARS1 impairs progenitor proliferation in cortical brain organoids and leads to microcephaly."
Wang L., Li Z., Sievert D., Smith D.E.C., Mendes M.I., Chen D.Y., Stanley V., Ghosh S., Wang Y., Kara M., Aslanger A.D., Rosti R.O., Houlden H., Salomons G.S., Gleeson J.G.
Nat. Commun. 11:4038-4038(2020) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN NEDMILG, VARIANTS NEDMILG MET-17; ALA-356 AND CYS-545, CHARACTERIZATION OF VARIANT NEDMILG MET-17, FUNCTION, CATALYTIC ACTIVITY.
Ref.19
"De novo and bi-allelic pathogenic variants in NARS1 cause neurodevelopmental delay due to toxic gain-of-function and partial loss-of-function effects."
SYNAPS Study Group
Manole A., Efthymiou S., O'Connor E., Mendes M.I., Jennings M., Maroofian R., Davagnanam I., Mankad K., Lopez M.R., Salpietro V., Harripaul R., Badalato L., Walia J., Francklyn C.S., Athanasiou-Fragkouli A., Sullivan R., Desai S., Baranano K. , Zafar F., Rana N., Ilyas M., Horga A., Kara M., Mattioli F., Goldenberg A., Griffin H., Piton A., Henderson L.B., Kara B., Aslanger A.D., Raaphorst J., Pfundt R., Portier R., Shinawi M., Kirby A., Christensen K.M., Wang L., Rosti R.O., Paracha S.A., Sarwar M.T., Jenkins D., Ahmed J., Santoni F.A., Ranza E., Iwaszkiewicz J., Cytrynbaum C., Weksberg R., Wentzensen I.M., Guillen Sacoto M.J., Si Y., Telegrafi A., Andrews M.V., Baldridge D., Gabriel H., Mohr J., Oehl-Jaschkowitz B., Debard S., Senger B., Fischer F., van Ravenwaaij C., Fock A.J.M., Stevens S.J.C., Baehler J., Nasar A., Mantovani J.F., Manzur A., Sarkozy A., Smith D.E.C., Salomons G.S., Ahmed Z.M., Riazuddin S., Riazuddin S., Usmani M.A., Seibt A., Ansar M., Antonarakis S.E., Vincent J.B., Ayub M., Grimmel M., Jelsig A.M., Hjortshoej T.D., Karstensen H.G., Hummel M., Haack T.B., Jamshidi Y., Distelmaier F., Horvath R., Gleeson J.G., Becker H., Mandel J.L., Koolen D.A., Houlden H.
Am. J. Hum. Genet. 107:311-324(2020) [PubMed] [Europe PMC] [Abstract]
SYNAPS Study Group
Manole A., Efthymiou S., O'Connor E., Mendes M.I., Jennings M., Maroofian R., Davagnanam I., Mankad K., Lopez M.R., Salpietro V., Harripaul R., Badalato L., Walia J., Francklyn C.S., Athanasiou-Fragkouli A., Sullivan R., Desai S., Baranano K. , Zafar F., Rana N., Ilyas M., Horga A., Kara M., Mattioli F., Goldenberg A., Griffin H., Piton A., Henderson L.B., Kara B., Aslanger A.D., Raaphorst J., Pfundt R., Portier R., Shinawi M., Kirby A., Christensen K.M., Wang L., Rosti R.O., Paracha S.A., Sarwar M.T., Jenkins D., Ahmed J., Santoni F.A., Ranza E., Iwaszkiewicz J., Cytrynbaum C., Weksberg R., Wentzensen I.M., Guillen Sacoto M.J., Si Y., Telegrafi A., Andrews M.V., Baldridge D., Gabriel H., Mohr J., Oehl-Jaschkowitz B., Debard S., Senger B., Fischer F., van Ravenwaaij C., Fock A.J.M., Stevens S.J.C., Baehler J., Nasar A., Mantovani J.F., Manzur A., Sarkozy A., Smith D.E.C., Salomons G.S., Ahmed Z.M., Riazuddin S., Riazuddin S., Usmani M.A., Seibt A., Ansar M., Antonarakis S.E., Vincent J.B., Ayub M., Grimmel M., Jelsig A.M., Hjortshoej T.D., Karstensen H.G., Hummel M., Haack T.B., Jamshidi Y., Distelmaier F., Horvath R., Gleeson J.G., Becker H., Mandel J.L., Koolen D.A., Houlden H.
Am. J. Hum. Genet. 107:311-324(2020) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NEDMILG PRO-11; MET-17; GLU-60; 90-ARG--PRO-548 DEL; CYS-132; PRO-350; ALA-356; THR-422; ILE-459 AND CYS-545, VARIANTS NEDMILEG LEU-322; SER-509 AND 534-ARG--PRO-548 DEL, INVOLVEMENT IN NEDMILG, INVOLVEMENT IN NEDMILEG, CHARACTERIZATION OF VARIANT NEDMILG PRO-11, CHARACTERIZATION OF VARIANTS NEDMILEG LEU-322 AND 534-ARG--PRO-548 DEL, FUNCTION, CATALYTIC ACTIVITY.
Ref.20
"Loss of NARS1 impairs progenitor proliferation in cortical brain organoids and leads to microcephaly."
Wang L., Li Z., Sievert D., Smith D.E.C., Mendes M.I., Chen D.Y., Stanley V., Ghosh S., Wang Y., Kara M., Aslanger A.D., Rosti R.O., Houlden H., Salomons G.S., Gleeson J.G.
Nat. Commun. 11:4038-4038(2020) [PubMed] [Europe PMC] [Abstract]
Wang L., Li Z., Sievert D., Smith D.E.C., Mendes M.I., Chen D.Y., Stanley V., Ghosh S., Wang Y., Kara M., Aslanger A.D., Rosti R.O., Houlden H., Salomons G.S., Gleeson J.G.
Nat. Commun. 11:4038-4038(2020) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN NEDMILG, VARIANTS NEDMILG MET-17; ALA-356 AND CYS-545, CHARACTERIZATION OF VARIANT NEDMILG MET-17, FUNCTION, CATALYTIC ACTIVITY.
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive neurodevelopmental disorder characterized by global developmental delay apparent in infancy, moderate to profound intellectual disability, poor or absent speech and language, delayed walking with variable gait abnormalities, and progressive microcephaly. Additional variable features include hypotonia, early-onset seizures, and a peripheral demyelinating or axonal peripheral sensorimotor neuropathy.
Related information in OMIMNeurodevelopmental disorder with microcephaly, impaired language, epilepsy, and gait abnormalities (NEDMILEG)1 PublicationManual assertion based on experiment ini
- Ref.19"De novo and bi-allelic pathogenic variants in NARS1 cause neurodevelopmental delay due to toxic gain-of-function and partial loss-of-function effects."
SYNAPS Study Group
Manole A., Efthymiou S., O'Connor E., Mendes M.I., Jennings M., Maroofian R., Davagnanam I., Mankad K., Lopez M.R., Salpietro V., Harripaul R., Badalato L., Walia J., Francklyn C.S., Athanasiou-Fragkouli A., Sullivan R., Desai S., Baranano K. , Zafar F., Rana N., Ilyas M., Horga A., Kara M., Mattioli F., Goldenberg A., Griffin H., Piton A., Henderson L.B., Kara B., Aslanger A.D., Raaphorst J., Pfundt R., Portier R., Shinawi M., Kirby A., Christensen K.M., Wang L., Rosti R.O., Paracha S.A., Sarwar M.T., Jenkins D., Ahmed J., Santoni F.A., Ranza E., Iwaszkiewicz J., Cytrynbaum C., Weksberg R., Wentzensen I.M., Guillen Sacoto M.J., Si Y., Telegrafi A., Andrews M.V., Baldridge D., Gabriel H., Mohr J., Oehl-Jaschkowitz B., Debard S., Senger B., Fischer F., van Ravenwaaij C., Fock A.J.M., Stevens S.J.C., Baehler J., Nasar A., Mantovani J.F., Manzur A., Sarkozy A., Smith D.E.C., Salomons G.S., Ahmed Z.M., Riazuddin S., Riazuddin S., Usmani M.A., Seibt A., Ansar M., Antonarakis S.E., Vincent J.B., Ayub M., Grimmel M., Jelsig A.M., Hjortshoej T.D., Karstensen H.G., Hummel M., Haack T.B., Jamshidi Y., Distelmaier F., Horvath R., Gleeson J.G., Becker H., Mandel J.L., Koolen D.A., Houlden H.
Am. J. Hum. Genet. 107:311-324(2020) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NEDMILG PRO-11; MET-17; GLU-60; 90-ARG--PRO-548 DEL; CYS-132; PRO-350; ALA-356; THR-422; ILE-459 AND CYS-545, VARIANTS NEDMILEG LEU-322; SER-509 AND 534-ARG--PRO-548 DEL, INVOLVEMENT IN NEDMILG, INVOLVEMENT IN NEDMILEG, CHARACTERIZATION OF VARIANT NEDMILG PRO-11, CHARACTERIZATION OF VARIANTS NEDMILEG LEU-322 AND 534-ARG--PRO-548 DEL, FUNCTION, CATALYTIC ACTIVITY.
Ref.19
"De novo and bi-allelic pathogenic variants in NARS1 cause neurodevelopmental delay due to toxic gain-of-function and partial loss-of-function effects."
SYNAPS Study Group
Manole A., Efthymiou S., O'Connor E., Mendes M.I., Jennings M., Maroofian R., Davagnanam I., Mankad K., Lopez M.R., Salpietro V., Harripaul R., Badalato L., Walia J., Francklyn C.S., Athanasiou-Fragkouli A., Sullivan R., Desai S., Baranano K. , Zafar F., Rana N., Ilyas M., Horga A., Kara M., Mattioli F., Goldenberg A., Griffin H., Piton A., Henderson L.B., Kara B., Aslanger A.D., Raaphorst J., Pfundt R., Portier R., Shinawi M., Kirby A., Christensen K.M., Wang L., Rosti R.O., Paracha S.A., Sarwar M.T., Jenkins D., Ahmed J., Santoni F.A., Ranza E., Iwaszkiewicz J., Cytrynbaum C., Weksberg R., Wentzensen I.M., Guillen Sacoto M.J., Si Y., Telegrafi A., Andrews M.V., Baldridge D., Gabriel H., Mohr J., Oehl-Jaschkowitz B., Debard S., Senger B., Fischer F., van Ravenwaaij C., Fock A.J.M., Stevens S.J.C., Baehler J., Nasar A., Mantovani J.F., Manzur A., Sarkozy A., Smith D.E.C., Salomons G.S., Ahmed Z.M., Riazuddin S., Riazuddin S., Usmani M.A., Seibt A., Ansar M., Antonarakis S.E., Vincent J.B., Ayub M., Grimmel M., Jelsig A.M., Hjortshoej T.D., Karstensen H.G., Hummel M., Haack T.B., Jamshidi Y., Distelmaier F., Horvath R., Gleeson J.G., Becker H., Mandel J.L., Koolen D.A., Houlden H.
Am. J. Hum. Genet. 107:311-324(2020) [PubMed] [Europe PMC] [Abstract]
SYNAPS Study Group
Manole A., Efthymiou S., O'Connor E., Mendes M.I., Jennings M., Maroofian R., Davagnanam I., Mankad K., Lopez M.R., Salpietro V., Harripaul R., Badalato L., Walia J., Francklyn C.S., Athanasiou-Fragkouli A., Sullivan R., Desai S., Baranano K. , Zafar F., Rana N., Ilyas M., Horga A., Kara M., Mattioli F., Goldenberg A., Griffin H., Piton A., Henderson L.B., Kara B., Aslanger A.D., Raaphorst J., Pfundt R., Portier R., Shinawi M., Kirby A., Christensen K.M., Wang L., Rosti R.O., Paracha S.A., Sarwar M.T., Jenkins D., Ahmed J., Santoni F.A., Ranza E., Iwaszkiewicz J., Cytrynbaum C., Weksberg R., Wentzensen I.M., Guillen Sacoto M.J., Si Y., Telegrafi A., Andrews M.V., Baldridge D., Gabriel H., Mohr J., Oehl-Jaschkowitz B., Debard S., Senger B., Fischer F., van Ravenwaaij C., Fock A.J.M., Stevens S.J.C., Baehler J., Nasar A., Mantovani J.F., Manzur A., Sarkozy A., Smith D.E.C., Salomons G.S., Ahmed Z.M., Riazuddin S., Riazuddin S., Usmani M.A., Seibt A., Ansar M., Antonarakis S.E., Vincent J.B., Ayub M., Grimmel M., Jelsig A.M., Hjortshoej T.D., Karstensen H.G., Hummel M., Haack T.B., Jamshidi Y., Distelmaier F., Horvath R., Gleeson J.G., Becker H., Mandel J.L., Koolen D.A., Houlden H.
Am. J. Hum. Genet. 107:311-324(2020) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NEDMILG PRO-11; MET-17; GLU-60; 90-ARG--PRO-548 DEL; CYS-132; PRO-350; ALA-356; THR-422; ILE-459 AND CYS-545, VARIANTS NEDMILEG LEU-322; SER-509 AND 534-ARG--PRO-548 DEL, INVOLVEMENT IN NEDMILG, INVOLVEMENT IN NEDMILEG, CHARACTERIZATION OF VARIANT NEDMILG PRO-11, CHARACTERIZATION OF VARIANTS NEDMILEG LEU-322 AND 534-ARG--PRO-548 DEL, FUNCTION, CATALYTIC ACTIVITY.
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant neurodevelopmental disorder characterized by global developmental delay apparent in infancy, delayed walking, ataxia, spasticity, impaired intellectual development with poor or absent speech and language, progressive microcephaly, and early-onset seizures in most patients. Facial dysmorphism and a demyelinating peripheral neuropathy may also be observed.
Related information in OMIMKeywords - Diseasei
Disease variant, Epilepsy, Mental retardation, NeurodegenerationOrganism-specific databases
DisGeNET More...DisGeNETi | 4677 |
| MIMi | 619091, phenotype 619092, phenotype |
Open Targets More...OpenTargetsi | ENSG00000134440 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA31447 |
Miscellaneous databases
Pharos NIH Druggable Genome Knowledgebase More...Pharosi | O43776, Tbio |
Chemistry databases
Drug and drug target database More...DrugBanki | DB00174, Asparagine |
Genetic variation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | NARS |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000176496 | 1 – 548 | Asparagine--tRNA ligase, cytoplasmicAdd BLAST | 548 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 61 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 244 | N6-acetyllysineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| Modified residuei | 482 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| Modified residuei | 490 | N6-acetyllysineBy similarity Manual assertion inferred from sequence similarity toi | 1 |
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O43776 |
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | O43776 |
MassIVE - Mass Spectrometry Interactive Virtual Environment More...MassIVEi | O43776 |
MaxQB - The MaxQuant DataBase More...MaxQBi | O43776 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O43776 |
PeptideAtlas More...PeptideAtlasi | O43776 |
PRoteomics IDEntifications database More...PRIDEi | O43776 |
ProteomicsDB: a multi-organism proteome resource More...ProteomicsDBi | 4098 49167 [O43776-1] |
PTM databases
GlyGen: Computational and Informatics Resources for Glycoscience More...GlyGeni | O43776, 1 site, 1 O-linked glycan (1 site) |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O43776 |
MetOSite database of methionine sulfoxide sites More...MetOSitei | O43776 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O43776 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | O43776 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000134440, Expressed in metanephros and 244 other tissues |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | O43776, baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O43776, HS |
Organism-specific databases
Human Protein Atlas More...HPAi | ENSG00000134440, Low tissue specificity |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer.
1 PublicationManual assertion based on experiment ini
- Ref.18"Unique N-terminal extension domain of human asparaginyl-tRNA synthetase elicits CCR3-mediated chemokine activity."
Park J.S., Park M.C., Lee K.Y., Goughnour P.C., Jeong S.J., Kim H.S., Kim H.J., Lee B.J., Kim S., Han B.W.
Int. J. Biol. Macromol. 120:835-845(2018) [PubMed] [Europe PMC] [Abstract]
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
O43776
| With | #Exp. | IntAct |
|---|---|---|
| ATXN1 [P54253] | 4 | EBI-373505,EBI-930964 |
GO - Molecular functioni
- CCR3 chemokine receptor binding Source: UniProtKBInferred from direct assayi
- Ref.18"Unique N-terminal extension domain of human asparaginyl-tRNA synthetase elicits CCR3-mediated chemokine activity."
Park J.S., Park M.C., Lee K.Y., Goughnour P.C., Jeong S.J., Kim H.S., Kim H.J., Lee B.J., Kim S., Han B.W.
Int. J. Biol. Macromol. 120:835-845(2018) [PubMed] [Europe PMC] [Abstract]
- protein dimerization activity Source: UniProtKBInferred from direct assayi
- Ref.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] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, FUNCTION.
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 110758, 94 interactors |
Protein interaction database and analysis system More...IntActi | O43776, 30 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000256854 |
Miscellaneous databases
RNAct, Protein-RNA interaction predictions for model organisms. More...RNActi | O43776, protein |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 5 – 8 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 10 – 12 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 15 – 17 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 20 – 24 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 29 – 34 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 38 – 40 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 43 – 47 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 55 – 57 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 60 – 73 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 14 | |
| Helixi | 117 – 123 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 126 – 140 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 15 | |
| Turni | 141 – 143 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 144 – 150 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 155 – 161 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 163 – 166 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 168 – 172 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 178 – 187 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 195 – 197 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 198 – 209 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 226 – 231 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 233 – 236 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 240 – 262 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 23 | |
| Beta strandi | 272 – 275 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 286 – 289 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 292 – 296 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 301 – 311 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 312 – 321 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 333 – 344 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
| Helixi | 347 – 367 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 21 | |
| Helixi | 371 – 377 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 389 – 392 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 393 – 402 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 408 – 410 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 421 – 431 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 435 – 438 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 442 – 444 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 455 – 466 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 12 | |
| Turni | 467 – 469 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 470 – 478 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 482 – 492 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 497 – 499 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 500 – 503 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 504 – 506 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 513 – 519 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Helixi | 520 – 527 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 533 – 536 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 537 – 539 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O43776 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1 – 25 | DisorderedSequence analysis <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More...</a></p> Automatic assertion according to sequence analysisi Add BLAST | 25 | |
| Regioni | 69 – 91 | DisorderedSequence analysis Automatic assertion according to sequence analysisi Add BLAST | 23 |
<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
The N-terminal domain (1-77) recruits and activates specific immune cells by interacting with CCR3-expressing cells.1 Publication
Manual assertion based on experiment ini
- Ref.18"Unique N-terminal extension domain of human asparaginyl-tRNA synthetase elicits CCR3-mediated chemokine activity."
Park J.S., Park M.C., Lee K.Y., Goughnour P.C., Jeong S.J., Kim H.S., Kim H.J., Lee B.J., Kim S., Han B.W.
Int. J. Biol. Macromol. 120:835-845(2018) [PubMed] [Europe PMC] [Abstract]
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the class-II aminoacyl-tRNA synthetase family.Curated
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0555, Eukaryota |
Ensembl GeneTree More...GeneTreei | ENSGT01030000234618 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_004553_2_10_1 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O43776 |
Identification of Orthologs from Complete Genome Data More...OMAi | SHVEAEC |
Database of Orthologous Groups More...OrthoDBi | 1056670at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | O43776 |
TreeFam database of animal gene trees More...TreeFami | TF105664 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR004364, Aa-tRNA-synt_II IPR006195, aa-tRNA-synth_II IPR004522, Asn-tRNA-ligase IPR002312, Asp/Asn-tRNA-synth_IIb IPR012340, NA-bd_OB-fold IPR004365, NA-bd_OB_tRNA |
Pfam protein domain database More...Pfami | View protein in Pfam PF00152, tRNA-synt_2, 1 hit PF01336, tRNA_anti-codon, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR01042, TRNASYNTHASP |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50249, SSF50249, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00457, asnS, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50862, AA_TRNA_LIGASE_II, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basketThis entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All
Isoform 1 (identifier: O43776-1) [UniParc]FASTAAdd to basketAdded to basket
This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
« Hide
Show »10 20 30 40 50
MVLAELYVSD REGSDATGDG TKEKPFKTGL KALMTVGKEP FPTIYVDSQK
60 70 80 90 100
ENERWNVISK SQLKNIKKMW HREQMKSESR EKKEAEDSLR REKNLEEAKK
110 120 130 140 150
ITIKNDPSLP EPKCVKIGAL EGYRGQRVKV FGWVHRLRRQ GKNLMFLVLR
160 170 180 190 200
DGTGYLQCVL ADELCQCYNG VLLSTESSVA VYGMLNLTPK GKQAPGGHEL
210 220 230 240 250
SCDFWELIGL APAGGADNLI NEESDVDVQL NNRHMMIRGE NMSKILKARS
260 270 280 290 300
MVTRCFRDHF FDRGYYEVTP PTLVQTQVEG GATLFKLDYF GEEAFLTQSS
310 320 330 340 350
QLYLETCLPA LGDVFCIAQS YRAEQSRTRR HLAEYTHVEA ECPFLTFDDL
360 370 380 390 400
LNRLEDLVCD VVDRILKSPA GSIVHELNPN FQPPKRPFKR MNYSDAIVWL
410 420 430 440 450
KEHDVKKEDG TFYEFGEDIP EAPERLMTDT INEPILLCRF PVEIKSFYMQ
460 470 480 490 500
RCPEDSRLTE SVDVLMPNVG EIVGGSMRIF DSEEILAGYK REGIDPTPYY
510 520 530 540
WYTDQRKYGT CPHGGYGLGL ERFLTWILNR YHIRDVCLYP RFVQRCTP
Length:548
Mass (Da):62,943
Last modified:June 1, 1998 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iCDD442C4E962CDDB
Isoform 2 (identifier: O43776-2) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
141-173: GKNLMFLVLRDGTGYLQCVLADELCQCYNGVLL → VSVLQWSSLVHGEQCCSVWNAKSYPKGQAGSRW
174-547: Missing.
« Hide
Show »10 20 30 40 50
MVLAELYVSD REGSDATGDG TKEKPFKTGL KALMTVGKEP FPTIYVDSQK
60 70 80 90 100
ENERWNVISK SQLKNIKKMW HREQMKSESR EKKEAEDSLR REKNLEEAKK
110 120 130 140 150
ITIKNDPSLP EPKCVKIGAL EGYRGQRVKV FGWVHRLRRQ VSVLQWSSLV
160 170
HGEQCCSVWN AKSYPKGQAG SRWP
<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket| Entry | Entry name | Protein names | Gene names | Length | Annotation | ||
|---|---|---|---|---|---|---|---|
| K7EPK2 | K7EPK2_HUMAN | Asparagine--tRNA ligase, cytoplasmi... Asparagine--tRNA ligase, cytoplasmic | NARS1 | 163 | Annotation score: Annotation score:1 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
| K7EMQ6 | K7EMQ6_HUMAN | Asparagine--tRNA ligase, cytoplasmi... Asparagine--tRNA ligase, cytoplasmic | NARS1 | 128 | Annotation score: Annotation score:1 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
| K7EQ35 | K7EQ35_HUMAN | Asparagine--tRNA ligase, cytoplasmi... Asparagine--tRNA ligase, cytoplasmic | NARS1 | 167 | Annotation score: Annotation score:1 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
| K7EIU7 | K7EIU7_HUMAN | Asparagine--tRNA ligase, cytoplasmi... Asparagine--tRNA ligase, cytoplasmic | NARS1 | 162 | Annotation score: Annotation score:1 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
| K7EJ19 | K7EJ19_HUMAN | Asparagine--tRNA ligase, cytoplasmi... Asparagine--tRNA ligase, cytoplasmic | NARS1 | 136 | Annotation score: Annotation score:1 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
| K7ENF0 | K7ENF0_HUMAN | Asparagine--tRNA ligase, cytoplasmi... Asparagine--tRNA ligase, cytoplasmic | NARS1 | 47 | Annotation score: Annotation score:1 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 391 | M → V in BAD96555 (Ref. 4) Curated | 1 |
Natural variant
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AJ000334 mRNA Translation: CAA04008.1 D84273 mRNA Translation: BAA34600.1 AK294364 mRNA Translation: BAG57627.1 AC100847 Genomic DNA No translation available. AK222835 mRNA Translation: BAD96555.1 BC001687 mRNA Translation: AAH01687.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS32837.1 [O43776-1] |
NCBI Reference Sequences More...RefSeqi | NP_004530.1, NM_004539.3 [O43776-1] |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000256854; ENSP00000256854; ENSG00000134440 [O43776-1] ENST00000540592; ENSP00000442496; ENSG00000134440 [O43776-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 4677 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:4677 |
UCSC genome browser More...UCSCi | uc002lgs.4, human [O43776-1] |
Keywords - Coding sequence diversityi
Alternative splicing<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| O43776 | Asparagine--tRNA ligase, cytoplasmic (Fragment) | 163 | UniRef100_O43776 | |||
| Asparagine--tRNA ligase, cytoplasmic (Fragment) | 128 | |||||
| O43776-2 | Asparagine--tRNA ligase, cytoplasmic (Fragment) | 162 | UniRef100_O43776-2 |
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| O43776 | Asparagine--tRNA ligase, cytoplasmic | 558 | UniRef90_O43776 | |||
| Asparagine--tRNA ligase, cytoplasmic (Fragment) | 163 | |||||
| Asparagine--tRNA ligase | 601 | |||||
| Asparagine--tRNA ligase | 566 | |||||
| Asparagine--tRNA ligase | 566 | |||||
| +101 | ||||||
| O43776-2 | Asparagine--tRNA ligase, cytoplasmic (Fragment) | 162 | UniRef90_O43776-2 | |||
| NARS isoform 7 | 174 | |||||
| NARS isoform 7 | 174 | |||||
| NARS isoform 10 (Fragment) | 162 | |||||
| NARS isoform 6 (Fragment) | 162 | |||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| O43776 | Asparagine--tRNA ligase, cytoplasmic | 558 | UniRef50_O43776 | |||
| Asparagine--tRNA ligase, cytoplasmic (Fragment) | 163 | |||||
| Asparagine--tRNA ligase | 601 | |||||
| Asparagine--tRNA ligase | 566 | |||||
| Asparagine--tRNA ligase | 566 | |||||
| +237 | ||||||
| O43776-2 | Asparagine--tRNA ligase, cytoplasmic (Fragment) | 162 | UniRef50_O43776-2 | |||
| NARS isoform 7 | 174 | |||||
| NARS isoform 7 | 174 | |||||
| Asparaginyl-tRNA synthetase 1 | 177 | |||||
| OB domain-containing protein | 174 | |||||
| +3 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AJ000334 mRNA Translation: CAA04008.1 D84273 mRNA Translation: BAA34600.1 AK294364 mRNA Translation: BAG57627.1 AC100847 Genomic DNA No translation available. AK222835 mRNA Translation: BAD96555.1 BC001687 mRNA Translation: AAH01687.1 |
| CCDSi | CCDS32837.1 [O43776-1] |
| RefSeqi | NP_004530.1, NM_004539.3 [O43776-1] |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 4ZYA | X-ray | 1.65 | A/B | 4-77 | [»] | |
| 5XIX | X-ray | 2.25 | A/B/C/D | 98-548 | [»] | |
| SMRi | O43776 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGRIDi | 110758, 94 interactors |
| IntActi | O43776, 30 interactors |
| STRINGi | 9606.ENSP00000256854 |
Chemistry databases
| DrugBanki | DB00174, Asparagine |
PTM databases
| GlyGeni | O43776, 1 site, 1 O-linked glycan (1 site) |
| iPTMneti | O43776 |
| MetOSitei | O43776 |
| PhosphoSitePlusi | O43776 |
| SwissPalmi | O43776 |
Genetic variation databases
| BioMutai | NARS |
Proteomic databases
| EPDi | O43776 |
| jPOSTi | O43776 |
| MassIVEi | O43776 |
| MaxQBi | O43776 |
| PaxDbi | O43776 |
| PeptideAtlasi | O43776 |
| PRIDEi | O43776 |
| ProteomicsDBi | 4098 49167 [O43776-1] |
Protocols and materials databases
ABCD curated depository of sequenced antibodies More...ABCDi | O43776, 3 sequenced antibodies |
Antibodypedia a portal for validated antibodies More...Antibodypediai | 9706, 189 antibodies |
The DNASU plasmid repository More...DNASUi | 4677 |
Genome annotation databases
| Ensembli | ENST00000256854; ENSP00000256854; ENSG00000134440 [O43776-1] ENST00000540592; ENSP00000442496; ENSG00000134440 [O43776-2] |
| GeneIDi | 4677 |
| KEGGi | hsa:4677 |
| UCSCi | uc002lgs.4, human [O43776-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 4677 |
| DisGeNETi | 4677 |
GeneCards: human genes, protein and diseases More...GeneCardsi | NARS1 |
| HGNCi | HGNC:7643, NARS1 |
| HPAi | ENSG00000134440, Low tissue specificity |
| MIMi | 108410, gene 619091, phenotype 619092, phenotype |
| neXtProti | NX_O43776 |
| OpenTargetsi | ENSG00000134440 |
| PharmGKBi | PA31447 |
| VEuPathDBi | HostDB:ENSG00000134440 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
| eggNOGi | KOG0555, Eukaryota |
| GeneTreei | ENSGT01030000234618 |
| HOGENOMi | CLU_004553_2_10_1 |
| InParanoidi | O43776 |
| OMAi | SHVEAEC |
| OrthoDBi | 1056670at2759 |
| PhylomeDBi | O43776 |
| TreeFami | TF105664 |
Enzyme and pathway databases
| BRENDAi | 6.1.1.22, 2681 |
| PathwayCommonsi | O43776 |
| Reactomei | R-HSA-379716, Cytosolic tRNA aminoacylation |
Miscellaneous databases
BioGRID ORCS database of CRISPR phenotype screens More...BioGRID-ORCSi | 4677, 800 hits in 986 CRISPR screens |
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | NARS, human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | NARS_(gene) |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 4677 |
| Pharosi | O43776, Tbio |
Protein Ontology More...PROi | PR:O43776 |
| RNActi | O43776, protein |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
| Bgeei | ENSG00000134440, Expressed in metanephros and 244 other tissues |
| ExpressionAtlasi | O43776, baseline and differential |
| Genevisiblei | O43776, HS |
Family and domain databases
| InterProi | View protein in InterPro IPR004364, Aa-tRNA-synt_II IPR006195, aa-tRNA-synth_II IPR004522, Asn-tRNA-ligase IPR002312, Asp/Asn-tRNA-synth_IIb IPR012340, NA-bd_OB-fold IPR004365, NA-bd_OB_tRNA |
| Pfami | View protein in Pfam PF00152, tRNA-synt_2, 1 hit PF01336, tRNA_anti-codon, 1 hit |
| PRINTSi | PR01042, TRNASYNTHASP |
| SUPFAMi | SSF50249, SSF50249, 1 hit |
| TIGRFAMsi | TIGR00457, asnS, 1 hit |
| PROSITEi | View protein in PROSITE PS50862, AA_TRNA_LIGASE_II, 1 hit |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | SYNC_HUMAN | |
| <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | O43776Primary (citable) accession number: O43776 Secondary accession number(s): B4DG16, Q53GU6 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 15, 1998 |
| Last sequence update: | June 1, 1998 | |
| Last modified: | September 29, 2021 | |
| This is version 189 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | 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. | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
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