Reviewed, UniProtKB/Swiss-Prot Q8BGV0 (SYNM_MOUSE)

Names and origin

Protein names

Recommended name:
    Probable asparaginyl-tRNA synthetase, mitochondrial
    EC=6.1.1.22
Alternative name(s):
    Asparagine--tRNA ligase
      Short name=AsnRS

Gene names

Name:

Nars2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	477 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Protein biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation
Gene Ontology (GO)
Biological process	asparaginyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro aspartyl-tRNA aminoacylation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine-tRNA ligase activity Inferred from sequence or structural similarity. Source: UniProtKB aspartate-tRNA ligase activity Inferred from electronic annotation. Source: InterPro nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 14	14	Mitochondrion Potential
	Chain	15 – 477	463	Probable asparaginyl-tRNA synthetase, mitochondrial		PRO_0000250723
Amino acid modifications
	Modified residue	353	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8BGV0-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 6CCBAC318E7830DD	FASTA	477	53,962
	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

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. , 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
EMBLGenBankDDBJ	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.
IPI	IPI00312759.
RefSeq	NP_705819.3.
UniGene	Mm.274864
3D structure databases
HSSP	HSSP built from PDB template 1N9W based on UniProtKB Q9LCY8.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8BGV0.
Proteomic databases
PRIDE	Q8BGV0.
Genome annotation databases
Ensembl	ENSMUST00000044466; ENSMUSP00000044937; ENSMUSG00000018995; Mus musculus. [Genome view]
GeneID	244141.
KEGG	mmu:244141.
NMPDR	fig|10090.3.peg.16965.
UCSC	uc009iiw.1. mouse.
Organism-specific databases
CTD	244141.
MGI	MGI:2142075. Nars2.
Phylogenomic databases
HOVERGEN	Q8BGV0.
OMA	VGELCGG.
Enzyme and pathway databases
BRENDA	6.1.1.22. 244.
Gene expression databases
ArrayExpress	Q8BGV0.
Bgee	Q8BGV0.
Genevestigator	Q8BGV0.
GermOnline	ENSMUSG00000018995. Mus musculus.
Family and domain databases
InterPro	IPR004364. aa-tRNA-synt_II. IPR018150. aa-tRNA-synt_II-like. IPR006195. aa-tRNA-synth_II_cons-reg. IPR004522. Asn-tRNA-synth_IIb. IPR002312. Asp-tRNA-synth_IIb. IPR012340. NA-bd_OB-fold. IPR004365. NA_bd_OB_tRNA-helicase. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
PANTHER	PTHR22594. aa-tRNA-synt_II. 1 hit.
Pfam	PF00152. tRNA-synt_2. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PRINTS	PR01042. TRNASYNTHASP.
TIGRFAMs	TIGR00457. asnS. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	386127.
SOURCE	Search...

Entry information

Entry name

SYNM_MOUSE

Accession

Primary (citable) accession number: Q8BGV0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	March 1, 2003
Last modified:	November 3, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)