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Q922B2 (SYDC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. Feed History...

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

Names and origin

Protein namesRecommended name:
Aspartate--tRNA ligase, cytoplasmic
EC=6.1.1.12
Alternative name(s):
Aspartyl-tRNA synthetase
Short name=AspRS
Gene names
Name:Dars
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 length501 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.

Catalytic activity

ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp).

Subunit structure

Homodimer; also part of a multisubunit complex that groups AIMP1, AIMP2, EEF1A1 and tRNA ligases for Arg, Asp, Glu, Gln, Ile, Leu, Lys, Met and Pro.

Subcellular location

Cytoplasm.

Sequence similarities

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

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 processaspartyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

aspartate-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

Chain1 – 501501Aspartate--tRNA ligase, cytoplasmic
PRO_0000111011

Amino acid modifications

Modified residue741N6-acetyllysine By similarity
Modified residue2381Phosphoserine By similarity
Modified residue2491Phosphoserine By similarity
Modified residue3741N6-acetyllysine By similarity

Experimental info

Sequence conflict41T → A in AAH08638. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q922B2 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: FC309A0CE55D36E6

FASTA50157,147
        10         20         30         40         50         60 
MPSTNASRKG QEKPREIVDA AEDYAKERYG ISSMIQSQEK PDRVLVRVKD LTVQKADDVV 

        70         80         90        100        110        120 
WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ MVKFAANINK ESIIDVEGVV 

       130        140        150        160        170        180 
RKVNQKIGSC TQQDVELHVQ KIYVISLAEP RLPLQLDDAI RPEVEGEEDG RATVNQDTRL 

       190        200        210        220        230        240 
DNRVIDLRTS TSQAIFRLQS GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF 

       250        260        270        280        290        300 
KNNAYLAQSP QLYKQMCICA DFEKVFCIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH 

       310        320        330        340        350        360 
EVVEEIADTL VQIFKGLQER FQTEIQTVSK QFPCEPFKFL EPTLRLEYCE ALAMLREAGV 

       370        380        390        400        410        420 
EMDDEEDLST PNEKLLGRLV KEKYDTDFYV LDKYPLAVRP FYTMPDPRNP KQSNSYDMFM 

       430        440        450        460        470        480 
RGEEILSGAQ RIHDPQLLTE RALHHGIDLE KIKAYIDSFR FGAPPHAGGG IGLERVTMLF 

       490        500 
LGLHNVRQTS MFPRDPKRLT P

« 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: Bone marrow and Thymus.
[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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK151027 mRNA. Translation: BAE30045.1.
AK151897 mRNA. Translation: BAE30780.1.
AK152304 mRNA. Translation: BAE31110.1.
AK152562 mRNA. Translation: BAE31315.1.
AK153256 mRNA. Translation: BAE31847.1.
AK153299 mRNA. Translation: BAE31881.1.
AK169716 mRNA. Translation: BAE41327.1.
BC008638 mRNA. Translation: AAH08638.1.
IPIIPI00122743.
RefSeqNP_803228.2. NM_177445.5.
UniGeneMm.28693.
Mm.431446.

3D structure databases

ProteinModelPortalQ922B2.
SMRQ922B2. Positions 22-501.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ922B2.

PTM databases

PhosphoSiteQ922B2.

Proteomic databases

PRIDEQ922B2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027602; ENSMUSP00000027602; ENSMUSG00000026356.
GeneID226414.
KEGGmmu:226414.

Organism-specific databases

CTD1615.
MGIMGI:2442544. Dars.

Phylogenomic databases

GeneTreeENSGT00550000074880.
HOGENOMHBG745843.
HOVERGENHBG001028.
InParanoidQ922B2.
OrthoDBEOG470TH2.
PhylomeDBQ922B2.

Gene expression databases

ArrayExpressQ922B2.
BgeeQ922B2.
CleanExMM_DARS.
GenevestigatorQ922B2.
GermOnlineENSMUSG00000026356. Mus musculus.

Family and domain databases

InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004523. Asp-tRNA-synth_IIb_arc/euk.
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.
KOK01876.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PTHR22594:SF10. PTHR22594:SF10. 1 hit.
PfamPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
TIGRFAMsTIGR00458. AspS_arch. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio378138.
SOURCESearch...

Entry information

Entry nameSYDC_MOUSE
AccessionPrimary (citable) accession number: Q922B2
Secondary accession number(s): Q3U987
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: July 27, 2011
Last modified: January 25, 2012
This is version 82 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