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Q8BGV0 (SYNM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. 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:
Probable asparagine--tRNA ligase, mitochondrial
EC=6.1.1.22
Alternative name(s):
Asparaginyl-tRNA synthetase
Short name=AsnRS
Gene names
Name:Nars2
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 length477 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

Ontologies

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

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

asparagine-tRNA ligase activity

Inferred from sequence or structural similarity. Source: UniProtKB

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1414Mitochondrion Potential
Chain15 – 477463Probable asparagine--tRNA ligase, mitochondrial
PRO_0000250723

Amino acid modifications

Modified residue3531N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BGV0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 6CCBAC318E7830DD

FASTA47753,962
        10         20         30         40         50         60 
MLGARRLLGA LRLCSSVSCP RPRASAKMRV RDALRVQDAR GECVTVQGWI RSVRSQKEVL 

        70         80         90        100        110        120 
FLHVNDGSSL ESLQIVADSS FDSRELTFGS SVQVQGQLVK SQSKRQNVEL KAEKIEVIGD 

       130        140        150        160        170        180 
CEAKAFPIKY KERHPLEYLR QYPHLRCRTN ALGSILRVRS EATAAIHSYF KDNGFVHIHT 

       190        200        210        220        230        240 
PVLTSNDCEG AGELFQVEPS SKIKGPKESF FDVPAFLTVS GQLHLEVMSG AFTQVFTFGP 

       250        260        270        280        290        300 
TFRAENSQSR RHLAEFYMVE AEISFVESLQ DLMQVMEELF KATTEMVLSH CPEDVELCHQ 

       310        320        330        340        350        360 
FIAAGQKGRL EHMLKNNFLI ISYTEAIEIL KQASQNFAFT PKWGVDLQTE HEKYLVRHCG 

       370        380        390        400        410        420 
NIPVFVINYP SELKPFYMRE NEDGPQNTVA AVDLLVPGVG ELFGGSLREE RYHVLEQRLA 

       430        440        450        460        470 
RSGLTKAYQW YLDLRKFGSV PHGGFGMGFE RYLQCILGVD NIKDVIPFPR FTHSCLL

« 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.
Tissue: Cerebellum, Hippocampus, Hypothalamus and Medulla oblongata.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK046799 mRNA. Translation: BAC32875.1.
AK047091 mRNA. Translation: BAC32958.1.
AK050718 mRNA. Translation: BAC34391.1.
AK138260 mRNA. Translation: BAE23597.1.
AK164179 mRNA. Translation: BAE37666.1.
IPIIPI00312759.
RefSeqNP_705819.3. NM_153591.4.
UniGeneMm.274864.

3D structure databases

HSSPHSSP built from PDB template 1X56 based on UniProtKB O57980.
ProteinModelPortalQ8BGV0.
SMRQ8BGV0. Positions 37-476.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8BGV0.

PTM databases

PhosphoSiteQ8BGV0.

Proteomic databases

PRIDEQ8BGV0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000044466; ENSMUSP00000044937; ENSMUSG00000018995.
GeneID244141.
KEGGmmu:244141.
NMPDRfig|10090.3.peg.16965.
UCSCuc009iiw.2. mouse.

Organism-specific databases

CTD79731.
MGIMGI:2142075. Nars2.

Phylogenomic databases

eggNOGroNOG05217.
HOGENOMHBG745843.
HOVERGENHBG067799.
InParanoidQ8BGV0.
OMAAIHRFFH.
OrthoDBEOG4DJJWB.
PhylomeDBQ8BGV0.

Gene expression databases

ArrayExpressQ8BGV0.
BgeeQ8BGV0.
GenevestigatorQ8BGV0.
GermOnlineENSMUSG00000018995. 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

NextBio386127.
SOURCESearch...

Entry information

Entry nameSYNM_MOUSE
AccessionPrimary (citable) accession number: Q8BGV0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 79 of the entry and version 1 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