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Protein

Asparagine--tRNA ligase, cytoplasmic

Gene

Nars

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1917473. Nars.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Asparagine--tRNA ligase, cytoplasmicPRO_0000176497Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei72 – 721PhosphoserineBy similarity
Modified residuei255 – 2551N6-acetyllysineBy similarity
Modified residuei493 – 4931PhosphoserineCombined sources
Modified residuei501 – 5011N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8BP47.
MaxQBiQ8BP47.
PaxDbiQ8BP47.
PRIDEiQ8BP47.

PTM databases

iPTMnetiQ8BP47.
PhosphoSiteiQ8BP47.

Expressioni

Gene expression databases

BgeeiQ8BP47.
CleanExiMM_NARS.
GenevisibleiQ8BP47. MM.

Interactioni

Protein-protein interaction databases

BioGridi213922. 1 interaction.
IntActiQ8BP47. 5 interactions.
MINTiMINT-1856285.
STRINGi10090.ENSMUSP00000025483.

Structurei

3D structure databases

ProteinModelPortaliQ8BP47.
SMRiQ8BP47. Positions 126-559.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0555. Eukaryota.
COG0017. LUCA.
GeneTreeiENSGT00550000074893.
HOGENOMiHOG000226035.
HOVERGENiHBG059844.
InParanoidiQ8BP47.
KOiK01893.
OMAiSHVEAEC.
OrthoDBiEOG7KQ21G.
PhylomeDBiQ8BP47.
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]

Sequencei

Sequence statusi: Complete.

Q8BP47-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSEVIRGTA EMVLAELYVS DREGNDATGD GTKEKPFKTG LKALMTVGKE
60 70 80 90 100
PFPTIYVDSQ KENERWDVIS KSQMKNIKKM WHREQMKNDS REKKEAEDNL
110 120 130 140 150
RREKNLEEAK KIIIKNDPSL PEPACVKISA LEGYRGQRVK VFGWVHRLRR
160 170 180 190 200
QGKNLMFLVL RDGTGYLQCV LSDDLCQCYN GVVLSTESSV AVYGTLNLTP
210 220 230 240 250
KGKQAPGGHE LSCDFWELVG LAPAGGADNL INEESDVDVQ LNNRHMMIRG
260 270 280 290 300
ENMSKILKAR SMITRCFRDH FFDRGYCEVT TPTLVQTQVE GGATLFKLDY
310 320 330 340 350
FGEEAFLTQS SQLYLETCLP ALGDVFCIAQ SYRAEQSRTR RHLAEFTHVE
360 370 380 390 400
AECPFLTFED LLNRLEDLVC DVVDRVLKSP VASIVYELNP NFKPPKRPFR
410 420 430 440 450
RMNYSDAIEW LKEHDVKKED GTFYEFGDDI PEAPERLMTD TINEPILLCR
460 470 480 490 500
FPVEIKSFYM QRCPEDPRLT ESVDVLMPNV GEIVGGSMRS WDSEEILEGY
510 520 530 540 550
KREGIDPAPY YWYTDQRKYG TCPHGGYGLG LERFLSWILN RYHIRDVCLY

PRFLQRCRP
Length:559
Mass (Da):64,279
Last modified:July 1, 2008 - v2
Checksum:iD5F4025B57580DBD
GO

Sequence cautioni

The sequence AAH52849.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB29032.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151Missing in BAB29032 (PubMed:16141072).Curated
Sequence conflicti82 – 821H → R in BAB29032 (PubMed:16141072).Curated
Sequence conflicti309 – 3091Q → E in BAB29032 (PubMed:16141072).Curated
Sequence conflicti469 – 4691L → P in BAE43117 (PubMed:16141072).Curated
Sequence conflicti526 – 5261G → E in AAH52849 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013880 mRNA. Translation: BAB29032.1. Different initiation.
AK077699 mRNA. Translation: BAC36965.1.
AK172657 mRNA. Translation: BAE43117.1.
BC052849 mRNA. Translation: AAH52849.1. Different initiation.
CCDSiCCDS50308.1.
RefSeqiNP_001136422.1. NM_001142950.1.
NP_081626.2. NM_027350.3.
UniGeneiMm.29192.

Genome annotation databases

EnsembliENSMUST00000025483; ENSMUSP00000025483; ENSMUSG00000024587.
GeneIDi70223.
KEGGimmu:70223.
UCSCiuc008fek.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK013880 mRNA. Translation: BAB29032.1. Different initiation.
AK077699 mRNA. Translation: BAC36965.1.
AK172657 mRNA. Translation: BAE43117.1.
BC052849 mRNA. Translation: AAH52849.1. Different initiation.
CCDSiCCDS50308.1.
RefSeqiNP_001136422.1. NM_001142950.1.
NP_081626.2. NM_027350.3.
UniGeneiMm.29192.

3D structure databases

ProteinModelPortaliQ8BP47.
SMRiQ8BP47. Positions 126-559.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213922. 1 interaction.
IntActiQ8BP47. 5 interactions.
MINTiMINT-1856285.
STRINGi10090.ENSMUSP00000025483.

PTM databases

iPTMnetiQ8BP47.
PhosphoSiteiQ8BP47.

Proteomic databases

EPDiQ8BP47.
MaxQBiQ8BP47.
PaxDbiQ8BP47.
PRIDEiQ8BP47.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025483; ENSMUSP00000025483; ENSMUSG00000024587.
GeneIDi70223.
KEGGimmu:70223.
UCSCiuc008fek.2. mouse.

Organism-specific databases

CTDi4677.
MGIiMGI:1917473. Nars.

Phylogenomic databases

eggNOGiKOG0555. Eukaryota.
COG0017. LUCA.
GeneTreeiENSGT00550000074893.
HOGENOMiHOG000226035.
HOVERGENiHBG059844.
InParanoidiQ8BP47.
KOiK01893.
OMAiSHVEAEC.
OrthoDBiEOG7KQ21G.
PhylomeDBiQ8BP47.
TreeFamiTF105664.

Miscellaneous databases

ChiTaRSiNars. mouse.
NextBioi331190.
PROiQ8BP47.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BP47.
CleanExiMM_NARS.
GenevisibleiQ8BP47. MM.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Embryo and Spleen.
  2. "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].
    Strain: C3H/He.
    Tissue: Osteoblast.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSYNC_MOUSE
AccessioniPrimary (citable) accession number: Q8BP47
Secondary accession number(s): Q3T9A7, Q7TPX0, Q9CRY5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: July 1, 2008
Last modified: March 16, 2016
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. 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.