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Protein

Asparagine--tRNA ligase, cytoplasmic

Gene

NARS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn).

GO - Molecular functioni

  • asparagine-tRNA ligase activity Source: ProtInc
  • ATP binding Source: UniProtKB-KW
  • nucleic acid binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.1.1.22. 2681.
ReactomeiR-HSA-379716. Cytosolic tRNA aminoacylation.

Names & Taxonomyi

Protein namesi
Recommended name:
Asparagine--tRNA ligase, cytoplasmic (EC:6.1.1.22)
Alternative name(s):
Asparaginyl-tRNA synthetase
Short name:
AsnRS
Gene namesi
Name:NARS
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:7643. NARS.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • mitochondrion Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31447.

Chemistry

DrugBankiDB00174. L-Asparagine.

Polymorphism and mutation databases

BioMutaiNARS.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 548548Asparagine--tRNA ligase, cytoplasmicPRO_0000176496Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611PhosphoserineCombined sources
Modified residuei244 – 2441N6-acetyllysineCombined sources
Modified residuei482 – 4821PhosphoserineBy similarity
Modified residuei490 – 4901N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO43776.
MaxQBiO43776.
PaxDbiO43776.
PeptideAtlasiO43776.
PRIDEiO43776.

PTM databases

iPTMnetiO43776.
PhosphoSiteiO43776.
SwissPalmiO43776.

Expressioni

Gene expression databases

BgeeiO43776.
CleanExiHS_ASNS.
HS_NARS.
ExpressionAtlasiO43776. baseline and differential.
GenevisibleiO43776. HS.

Organism-specific databases

HPAiCAB034257.
HPA040017.

Interactioni

Protein-protein interaction databases

BioGridi110758. 63 interactions.
IntActiO43776. 11 interactions.
MINTiMINT-5003848.
STRINGi9606.ENSP00000256854.

Structurei

3D structure databases

ProteinModelPortaliO43776.
SMRiO43776. Positions 115-548.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0555. Eukaryota.
COG0017. LUCA.
GeneTreeiENSGT00550000074893.
HOGENOMiHOG000226035.
HOVERGENiHBG059844.
InParanoidiO43776.
KOiK01893.
OMAiSHVEAEC.
OrthoDBiEOG7KQ21G.
PhylomeDBiO43776.
TreeFamiTF105664.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
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.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF16. PTHR22594:SF16. 1 hit.
PfamiPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00457. asnS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43776-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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

        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
Checksum:iCDD442C4E962CDDB
GO
Isoform 2 (identifier: O43776-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     141-173: GKNLMFLVLRDGTGYLQCVLADELCQCYNGVLL → VSVLQWSSLVHGEQCCSVWNAKSYPKGQAGSRW
     174-547: Missing.

Note: No experimental confirmation available.
Show »
Length:174
Mass (Da):20,033
Checksum:i594E9ED90ED09E4B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti391 – 3911M → V in BAD96555 (Ref. 4) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei141 – 17333GKNLM…NGVLL → VSVLQWSSLVHGEQCCSVWN AKSYPKGQAGSRW in isoform 2. 1 PublicationVSP_056201Add
BLAST
Alternative sequencei174 – 547374Missing in isoform 2. 1 PublicationVSP_056202Add
BLAST

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.
CCDSiCCDS32837.1. [O43776-1]
RefSeqiNP_004530.1. NM_004539.3. [O43776-1]
UniGeneiHs.465224.

Genome annotation databases

EnsembliENST00000256854; ENSP00000256854; ENSG00000134440. [O43776-1]
ENST00000540592; ENSP00000442496; ENSG00000134440. [O43776-2]
GeneIDi4677.
KEGGihsa:4677.
UCSCiuc002lgs.4. human. [O43776-1]

Keywords - Coding sequence diversityi

Alternative splicing

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.
CCDSiCCDS32837.1. [O43776-1]
RefSeqiNP_004530.1. NM_004539.3. [O43776-1]
UniGeneiHs.465224.

3D structure databases

ProteinModelPortaliO43776.
SMRiO43776. Positions 115-548.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110758. 63 interactions.
IntActiO43776. 11 interactions.
MINTiMINT-5003848.
STRINGi9606.ENSP00000256854.

Chemistry

DrugBankiDB00174. L-Asparagine.

PTM databases

iPTMnetiO43776.
PhosphoSiteiO43776.
SwissPalmiO43776.

Polymorphism and mutation databases

BioMutaiNARS.

Proteomic databases

EPDiO43776.
MaxQBiO43776.
PaxDbiO43776.
PeptideAtlasiO43776.
PRIDEiO43776.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256854; ENSP00000256854; ENSG00000134440. [O43776-1]
ENST00000540592; ENSP00000442496; ENSG00000134440. [O43776-2]
GeneIDi4677.
KEGGihsa:4677.
UCSCiuc002lgs.4. human. [O43776-1]

Organism-specific databases

CTDi4677.
GeneCardsiNARS.
HGNCiHGNC:7643. NARS.
HPAiCAB034257.
HPA040017.
MIMi108410. gene.
neXtProtiNX_O43776.
PharmGKBiPA31447.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0555. Eukaryota.
COG0017. LUCA.
GeneTreeiENSGT00550000074893.
HOGENOMiHOG000226035.
HOVERGENiHBG059844.
InParanoidiO43776.
KOiK01893.
OMAiSHVEAEC.
OrthoDBiEOG7KQ21G.
PhylomeDBiO43776.
TreeFamiTF105664.

Enzyme and pathway databases

BRENDAi6.1.1.22. 2681.
ReactomeiR-HSA-379716. Cytosolic tRNA aminoacylation.

Miscellaneous databases

ChiTaRSiNARS. human.
GeneWikiiNARS_(gene).
GenomeRNAii4677.
NextBioi18028.
PROiO43776.
SOURCEiSearch...

Gene expression databases

BgeeiO43776.
CleanExiHS_ASNS.
HS_NARS.
ExpressionAtlasiO43776. baseline and differential.
GenevisibleiO43776. HS.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
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.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF16. PTHR22594:SF16. 1 hit.
PfamiPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00457. asnS. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Amygdala.
  4. 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] (ISOFORM 1).
    Tissue: Liver.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Colon.
  7. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE [LARGE SCALE ANALYSIS] OF 2-12.
    Tissue: Leukemic T-cell.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYNC_HUMAN
AccessioniPrimary (citable) accession number: O43776
Secondary accession number(s): B4DG16, Q53GU6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: June 1, 1998
Last modified: May 11, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.