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Q96I59 (SYNM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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

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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length477 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

Mitochondrion matrix By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   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

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

   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_0000250722

Amino acid modifications

Modified residue3531N6-acetyllysine Ref.4

Natural variations

Natural variant871N → T. Ref.2
Corresponds to variant rs10501429 [ dbSNP | Ensembl ].
VAR_052636

Sequences

Sequence LengthMass (Da)Tools
Q96I59 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 1F4C78E0B6F5500C

FASTA47754,090
        10         20         30         40         50         60 
MLGVRCLLRS VRFCSSAPFP KHKPSAKLSV RDALGAQNAS GERIKIQGWI RSVRSQKEVL 

        70         80         90        100        110        120 
FLHVNDGSSL ESLQVVADSG LDSRELNFGS SVEVQGQLIK SPSKRQNVEL KAEKIKVIGN 

       130        140        150        160        170        180 
CDAKDFPIKY KERHPLEYLR QYPHFRCRTN VLGSILRIRS EATAAIHSFF KDSGFVHIHT 

       190        200        210        220        230        240 
PIITSNDSEG AGELFQLEPS GKLKVPEENF FNVPAFLTVS GQLHLEVMSG AFTQVFTFGP 

       250        260        270        280        290        300 
TFRAENSQSR RHLAEFYMIE AEISFVDSLQ DLMQVIEELF KATTMMVLSK CPEDVELCHK 

       310        320        330        340        350        360 
FIAPGQKDRL EHMLKNNFLI ISYTEAVEIL KQASQNFTFT PEWGADLRTE HEKYLVKHCG 

       370        380        390        400        410        420 
NIPVFVINYP LTLKPFYMRD NEDGPQHTVA AVDLLVPGVG ELFGGGLREE RYHFLEERLA 

       430        440        450        460        470 
RSGLTEVYQW YLDLRRFGSV PHGGFGMGFE RYLQCILGVD NIKDVIPFPR FPHSCLL 

« Hide

References

« Hide 'large scale' references
[1]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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], VARIANT THR-87.
Tissue: Brain.
[3]"Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS."
Bonnefond L., Fender A., Rudinger-Thirion J., Giege R., Florentz C., Sissler M.
Biochemistry 44:4805-4816(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION.
[4]"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-353, MASS SPECTROMETRY.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP003086 Genomic DNA. No translation available.
AP003110 Genomic DNA. No translation available.
BC007800 mRNA. Translation: AAH07800.2.
IPIIPI00101664.
RefSeqNP_078954.4. NM_024678.5.
UniGeneHs.503389.

3D structure databases

HSSPHSSP built from PDB template 1X56 based on UniProtKB O57980.
ProteinModelPortalQ96I59.
SMRQ96I59. Positions 41-472.
ModBaseSearch...

Protein-protein interaction databases

IntActQ96I59. 1 interaction.
STRING9606.ENSP00000281038.

PTM databases

PhosphoSiteQ96I59.

Polymorphism databases

DMDM296452944.

Proteomic databases

PaxDbQ96I59.
PRIDEQ96I59.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000281038; ENSP00000281038; ENSG00000137513.
GeneID79731.
KEGGhsa:79731.
UCSCuc001ozi.3. human.

Organism-specific databases

CTD79731.
GeneCardsGC11M078147.
HGNCHGNC:26274. NARS2.
HPAHPA026793.
MIM612803. gene.
neXtProtNX_Q96I59.
PharmGKBPA143485554.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0017.
HOGENOMHOG000226033.
HOVERGENHBG067799.
InParanoidQ96I59.
KOK01893.
OMADLWWYLD.
OrthoDBEOG4DJJWB.
PhylomeDBQ96I59.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ96I59.
BgeeQ96I59.
CleanExHS_NARS2.
GenevestigatorQ96I59.
GermOnlineENSG00000137513. Homo sapiens.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004522. Asn-tRNA-ligase_IIb.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
PANTHERPTHR22594. PTHR22594. 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

ChiTaRSNARS2. human.
DrugBankDB00174. L-Asparagine.
GenomeRNAi79731.
NextBio69114.
SOURCESearch...

Entry information

Entry nameSYNM_HUMAN
AccessionPrimary (citable) accession number: Q96I59
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: May 18, 2010
Last modified: May 1, 2013
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families