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Reviewed, UniProtKB/Swiss-Prot Q96I59 (SYNM_HUMAN)

Last modified October 13, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable asparaginyl-tRNA synthetase, mitochondrial
    EC=6.1.1.22
Alternative name(s):
    Asparagine--tRNA ligase
      Short name=AsnRS
Gene names
Name: NARS2
OrganismHomo sapiens (Human) [Complete 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 1414Mitochondrion Potential
Chain15 – 477463Probable asparaginyl-tRNA synthetase, mitochondrial
PRO_0000250722

Amino acid modifications

Modified residue3531N6-acetyllysine Ref.4

Natural variations

Natural variant871T → N: dbSNP rs10501429.
VAR_052636

Sequences

Sequence LengthMass (Da)Tools
Q96I59-1 [UniParc].

Last modified March 1, 2004. Version 2.
Checksum: B2841FB3078E8865

FASTA47754,077
        10         20         30         40         50         60 
MLGVRCLLRS VRFCSSAPFP KHKPSAKLSV RDALGAQNAS GERIKIQGWI RSVRSQKEVL 

        70         80         90        100        110        120 
FLHVNDGSSL ESLQVVADSG LDSRELTFGS 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]"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].
Tissue: Brain.
[2]"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: 15779907] [Abstract]
Cited for: IDENTIFICATION.
[3]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-353, MASS SPECTROMETRY.

Cross-references

Sequence databases

BC007800 mRNA. Translation: AAH07800.2.
IPIIPI00101664.
RefSeqNP_078954.4.
UniGeneHs.503389

3D structure databases

HSSPHSSP built from PDB template 1N9W based on UniProtKB Q9LCY8.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ96I59.

Proteomic databases

PRIDEQ96I59.

Genome annotation databases

EnsemblENST00000281038; ENSP00000281038; ENSG00000137513; Homo sapiens. [Genome view]
GeneID79731.
KEGGhsa:79731.
UCSCuc001ozi.1. human.

Organism-specific databases

GeneCardsGC11M077825.
HGNCHGNC:26274. NARS2.
HPAHPA026793.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ96I59.

Enzyme and pathway databases

BRENDA6.1.1.22. 247.
ReactomeREACT_71. Gene Expression.

Gene expression databases

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

Family and domain databases

InterProIPR004364. 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]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
TIGRFAMsTIGR00457. asnS. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00174. L-Asparagine.
NextBio69114.

Entry information

Entry nameSYNM_HUMAN
AccessionPrimary (citable) accession number: Q96I59
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2004
Last modified: October 13, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents