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Q8BP47 (SYNC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Asparagine--tRNA ligase, cytoplasmic
EC=6.1.1.22
Alternative name(s):
Asparaginyl-tRNA synthetase
Short name=AsnRS
Gene names
Name:Nars
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length559 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family.

Sequence caution

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

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processasparaginyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

asparagine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 559558Asparagine--tRNA ligase, cytoplasmic
PRO_0000176497

Amino acid modifications

Modified residue721Phosphoserine By similarity
Modified residue2551N6-acetyllysine By similarity
Modified residue4931Phosphoserine Ref.3

Experimental info

Sequence conflict151Missing in BAB29032. Ref.1
Sequence conflict821H → R in BAB29032. Ref.1
Sequence conflict3091Q → E in BAB29032. Ref.1
Sequence conflict4691L → P in BAE43117. Ref.1
Sequence conflict5261G → E in AAH52849. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8BP47 [UniParc].

Last modified July 1, 2008. Version 2.
Checksum: D5F4025B57580DBD

FASTA55964,279
        10         20         30         40         50         60 
MSSEVIRGTA EMVLAELYVS DREGNDATGD GTKEKPFKTG LKALMTVGKE PFPTIYVDSQ 

        70         80         90        100        110        120 
KENERWDVIS KSQMKNIKKM WHREQMKNDS REKKEAEDNL RREKNLEEAK KIIIKNDPSL 

       130        140        150        160        170        180 
PEPACVKISA LEGYRGQRVK VFGWVHRLRR QGKNLMFLVL RDGTGYLQCV LSDDLCQCYN 

       190        200        210        220        230        240 
GVVLSTESSV AVYGTLNLTP KGKQAPGGHE LSCDFWELVG LAPAGGADNL INEESDVDVQ 

       250        260        270        280        290        300 
LNNRHMMIRG ENMSKILKAR SMITRCFRDH FFDRGYCEVT TPTLVQTQVE GGATLFKLDY 

       310        320        330        340        350        360 
FGEEAFLTQS SQLYLETCLP ALGDVFCIAQ SYRAEQSRTR RHLAEFTHVE AECPFLTFED 

       370        380        390        400        410        420 
LLNRLEDLVC DVVDRVLKSP VASIVYELNP NFKPPKRPFR RMNYSDAIEW LKEHDVKKED 

       430        440        450        460        470        480 
GTFYEFGDDI PEAPERLMTD TINEPILLCR FPVEIKSFYM QRCPEDPRLT ESVDVLMPNV 

       490        500        510        520        530        540 
GEIVGGSMRS WDSEEILEGY KREGIDPAPY YWYTDQRKYG TCPHGGYGLG LERFLSWILN 

       550 
RYHIRDVCLY PRFLQRCRP

« Hide

References

[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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C3H/He.
Tissue: Osteoblast.
[3]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK013880 mRNA. Translation: BAB29032.1. Different initiation.
AK077699 mRNA. Translation: BAC36965.1.
AK172657 mRNA. Translation: BAE43117.1.
BC052849 mRNA. Translation: AAH52849.1. Different initiation.
IPIIPI00223415.
RefSeqNP_001136422.1. NM_001142950.1.
NP_081626.2. NM_027350.3.
UniGeneMm.482137.

3D structure databases

ProteinModelPortalQ8BP47.
SMRQ8BP47. Positions 126-559.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8BP47. 1 interaction.
STRINGQ8BP47.

PTM databases

PhosphoSiteQ8BP47.

Proteomic databases

PRIDEQ8BP47.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025483; ENSMUSP00000025483; ENSMUSG00000024587.
GeneID70223.
KEGGmmu:70223.
UCSCuc008fek.2. mouse.

Organism-specific databases

CTD4677.
MGIMGI:1917473. Nars.

Phylogenomic databases

eggNOGroNOG10195.
GeneTreeENSGT00550000074893.
HOGENOMHBG745843.
HOVERGENHBG059844.
InParanoidQ8BP47.
OrthoDBEOG4G1MG6.

Gene expression databases

ArrayExpressQ8BP47.
BgeeQ8BP47.
CleanExMM_NARS.
GenevestigatorQ8BP47.
GermOnlineENSMUSG00000024587. Mus musculus.

Family and domain databases

InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004522. Asn-tRNA-synth_IIb.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01893.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PTHR22594:SF6. PTHR22594:SF6. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMsTIGR00457. AsnS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio331190.
SOURCESearch...

Entry information

Entry nameSYNC_MOUSE
AccessionPrimary (citable) accession number: Q8BP47
Secondary accession number(s): Q3T9A7, Q7TPX0, Q9CRY5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: July 1, 2008
Last modified: January 25, 2012
This is version 78 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents