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Protein

Aspartate--tRNA ligase, cytoplasmic

Gene

Dars

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei229 – 2291AspartateBy similarity
Binding sitei273 – 2731AspartateBy similarity
Binding sitei424 – 4241ATPBy similarity
Binding sitei427 – 4271AspartateBy similarity
Binding sitei431 – 4311AspartateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi273 – 2753ATPBy similarity
Nucleotide bindingi281 – 2833ATPBy similarity
Nucleotide bindingi472 – 4754ATPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi6.1.1.12. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate--tRNA ligase, cytoplasmic (EC:6.1.1.12)
Alternative name(s):
Aspartyl-tRNA synthetase
Short name:
AspRS
Gene namesi
Name:Dars
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2442544. Dars.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 501501Aspartate--tRNA ligase, cytoplasmicPRO_0000111011Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741N6-acetyllysineBy similarity
Modified residuei249 – 2491PhosphoserineBy similarity
Modified residuei374 – 3741N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ922B2.
MaxQBiQ922B2.
PaxDbiQ922B2.
PRIDEiQ922B2.

PTM databases

iPTMnetiQ922B2.
PhosphoSiteiQ922B2.
SwissPalmiQ922B2.

Expressioni

Gene expression databases

BgeeiQ922B2.
CleanExiMM_DARS.
ExpressionAtlasiQ922B2. baseline and differential.
GenevisibleiQ922B2. MM.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi230508. 3 interactions.
IntActiQ922B2. 2 interactions.
MINTiMINT-1856918.
STRINGi10090.ENSMUSP00000027602.

Structurei

3D structure databases

ProteinModelPortaliQ922B2.
SMRiQ922B2. Positions 21-495.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni251 – 2544AspartateBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0556. Eukaryota.
COG0017. LUCA.
GeneTreeiENSGT00550000074880.
HOGENOMiHOG000226032.
HOVERGENiHBG001028.
InParanoidiQ922B2.
KOiK01876.
OMAiHEVIDSI.
OrthoDBiEOG7P5T0X.
TreeFamiTF105676.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004523. Asp-tRNA_synthase_arc.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF33. PTHR22594:SF33. 1 hit.
PfamiPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00458. aspS_nondisc. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q922B2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSTNASRKG QEKPREIVDA AEDYAKERYG ISSMIQSQEK PDRVLVRVKD
60 70 80 90 100
LTVQKADDVV WVRARVHTSR AKGKQCFLVL RQQQFNVQAL VAVGDHASKQ
110 120 130 140 150
MVKFAANINK ESIIDVEGVV RKVNQKIGSC TQQDVELHVQ KIYVISLAEP
160 170 180 190 200
RLPLQLDDAI RPEVEGEEDG RATVNQDTRL DNRVIDLRTS TSQAIFRLQS
210 220 230 240 250
GICHLFRETL INKGFVEIQT PKIISAASEG GANVFTVSYF KNNAYLAQSP
260 270 280 290 300
QLYKQMCICA DFEKVFCIGP VFRAEDSNTH RHLTEFVGLD IEMAFNYHYH
310 320 330 340 350
EVVEEIADTL VQIFKGLQER FQTEIQTVSK QFPCEPFKFL EPTLRLEYCE
360 370 380 390 400
ALAMLREAGV EMDDEEDLST PNEKLLGRLV KEKYDTDFYV LDKYPLAVRP
410 420 430 440 450
FYTMPDPRNP KQSNSYDMFM RGEEILSGAQ RIHDPQLLTE RALHHGIDLE
460 470 480 490 500
KIKAYIDSFR FGAPPHAGGG IGLERVTMLF LGLHNVRQTS MFPRDPKRLT

P
Length:501
Mass (Da):57,147
Last modified:July 27, 2011 - v2
Checksum:iFC309A0CE55D36E6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41T → A in AAH08638 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15253.1.
RefSeqiNP_803228.2. NM_177445.5.
UniGeneiMm.28693.

Genome annotation databases

EnsembliENSMUST00000027602; ENSMUSP00000027602; ENSMUSG00000026356.
GeneIDi226414.
KEGGimmu:226414.
UCSCiuc007clp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS15253.1.
RefSeqiNP_803228.2. NM_177445.5.
UniGeneiMm.28693.

3D structure databases

ProteinModelPortaliQ922B2.
SMRiQ922B2. Positions 21-495.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230508. 3 interactions.
IntActiQ922B2. 2 interactions.
MINTiMINT-1856918.
STRINGi10090.ENSMUSP00000027602.

PTM databases

iPTMnetiQ922B2.
PhosphoSiteiQ922B2.
SwissPalmiQ922B2.

Proteomic databases

EPDiQ922B2.
MaxQBiQ922B2.
PaxDbiQ922B2.
PRIDEiQ922B2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027602; ENSMUSP00000027602; ENSMUSG00000026356.
GeneIDi226414.
KEGGimmu:226414.
UCSCiuc007clp.2. mouse.

Organism-specific databases

CTDi1615.
MGIiMGI:2442544. Dars.

Phylogenomic databases

eggNOGiKOG0556. Eukaryota.
COG0017. LUCA.
GeneTreeiENSGT00550000074880.
HOGENOMiHOG000226032.
HOVERGENiHBG001028.
InParanoidiQ922B2.
KOiK01876.
OMAiHEVIDSI.
OrthoDBiEOG7P5T0X.
TreeFamiTF105676.

Enzyme and pathway databases

BRENDAi6.1.1.12. 3474.

Miscellaneous databases

PROiQ922B2.
SOURCEiSearch...

Gene expression databases

BgeeiQ922B2.
CleanExiMM_DARS.
ExpressionAtlasiQ922B2. baseline and differential.
GenevisibleiQ922B2. MM.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004523. Asp-tRNA_synthase_arc.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF33. PTHR22594:SF33. 1 hit.
PfamiPF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR00458. aspS_nondisc. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSYDC_MOUSE
AccessioniPrimary (citable) accession number: Q922B2
Secondary accession number(s): Q3U987
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.