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Protein

Aspartate--tRNA ligase, mitochondrial

Gene

Dars2

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

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei265 – 2651AspartateBy similarity
Binding sitei534 – 5341ATPBy similarity
Binding sitei541 – 5411AspartateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi265 – 2673ATPBy similarity
Nucleotide bindingi583 – 5864ATPBy 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

Names & Taxonomyi

Protein namesi
Recommended name:
Aspartate--tRNA ligase, mitochondrial (EC:6.1.1.12)
Alternative name(s):
Aspartyl-tRNA synthetase
Short name:
AspRS
Gene namesi
Name:Dars2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:2442510. Dars2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4646MitochondrionSequence analysisAdd
BLAST
Chaini47 – 653607Aspartate--tRNA ligase, mitochondrialPRO_0000250737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei218 – 2181PhosphothreonineBy similarity
Modified residuei241 – 2411PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BIP0.
MaxQBiQ8BIP0.
PaxDbiQ8BIP0.
PeptideAtlasiQ8BIP0.
PRIDEiQ8BIP0.

PTM databases

iPTMnetiQ8BIP0.
PhosphoSiteiQ8BIP0.

Expressioni

Gene expression databases

BgeeiQ8BIP0.
CleanExiMM_DARS2.
GenevisibleiQ8BIP0. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000041851.

Structurei

3D structure databases

ProteinModelPortaliQ8BIP0.
SMRiQ8BIP0. Positions 41-629.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni243 – 2464AspartateBy similarity

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG2411. Eukaryota.
COG0173. LUCA.
GeneTreeiENSGT00550000074971.
HOGENOMiHOG000275159.
HOVERGENiHBG055815.
InParanoidiQ8BIP0.
KOiK01876.
OMAiYQLDVEM.
OrthoDBiEOG773XFN.
PhylomeDBiQ8BIP0.
TreeFamiTF314827.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.30.1360.30. 1 hit.
HAMAPiMF_00044. Asp_tRNA_synth.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004524. Asp-tRNA-ligase_bac/mit.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD-like.
IPR029351. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 2 hits.
PTHR22594:SF5. PTHR22594:SF5. 2 hits.
PfamiPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsiTIGR00459. aspS_bact. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8BIP0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYLGFWLSRL CRGLSRPIGK TMRPIWGSLS RNLALSSQRI PEFSSFVART
60 70 80 90 100
NTCGELRSSH LGQEVTLCGW IQYRRQNTFL VLRDCHGLVQ ILIPQDESAA
110 120 130 140 150
SVRRILCEAP VESVVRVSGT VISRPPGQEN PKMPTGEIEI KVKTAELLNA
160 170 180 190 200
CKKLPFEIKD FVKKTEALRL QYRYLDLRSF QMQYNLRLRS QMVMKMREYL
210 220 230 240 250
CNLHGFVDIE TPTLFKRTPG GAKEFLVPSR EPGKFYSLPQ SPQQFKQLLM
260 270 280 290 300
VGGLDRYFQV ARCYRDEGSR PDRQPEFTQI DIEMSFVEQT GIQRLVEGLL
310 320 330 340 350
QYSWPGDKDP LVTPFPSMTF AEALATYGTD KPDTRFGMKI VDVSDVFRNT
360 370 380 390 400
ELRFLQDALA KPQGTVKAIC VHDGAKYLRK EDIEFIRKFA VHHFSQEVLP
410 420 430 440 450
IFLNAKKNWS SPFAKFIMEE ERLELARSME IQEEDIVLLT AGEHEKACSL
460 470 480 490 500
LGKLRLECAD LLEMRGAVLR DPAVFSFLWV VDFPLFLAKE ESPTELESAH
510 520 530 540 550
HPFTAPNSSD IHLLYTEPEK VRGQHYDLVL NGNEIGGGSV RIHDAQLQRY
560 570 580 590 600
ILETLLKEDV KLLSHLLQAL DYGAPPHGGI ALGLDRLVCL VTGAPSIRDV
610 620 630 640 650
IAFPKSYRGQ DLMSNAPDSV SPEELKPYHI HVLWPADSEE ESASATPSKH

LSS
Length:653
Mass (Da):74,102
Last modified:March 1, 2003 - v1
Checksum:i8A02D2E62E914E99
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711I → V in AAH89191 (PubMed:15489334).Curated
Sequence conflicti104 – 1041R → G in AAH89191 (PubMed:15489334).Curated
Sequence conflicti540 – 5401V → A in AAH89191 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK037337 mRNA. Translation: BAC29789.1.
AK138809 mRNA. Translation: BAE23785.1.
BC076606 mRNA. Translation: AAH76606.1.
BC089191 mRNA. Translation: AAH89191.1.
CCDSiCCDS15413.1.
RefSeqiNP_766232.1. NM_172644.4.
UniGeneiMm.28125.

Genome annotation databases

EnsembliENSMUST00000035430; ENSMUSP00000041851; ENSMUSG00000026709.
GeneIDi226539.
KEGGimmu:226539.
UCSCiuc007dey.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK037337 mRNA. Translation: BAC29789.1.
AK138809 mRNA. Translation: BAE23785.1.
BC076606 mRNA. Translation: AAH76606.1.
BC089191 mRNA. Translation: AAH89191.1.
CCDSiCCDS15413.1.
RefSeqiNP_766232.1. NM_172644.4.
UniGeneiMm.28125.

3D structure databases

ProteinModelPortaliQ8BIP0.
SMRiQ8BIP0. Positions 41-629.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000041851.

PTM databases

iPTMnetiQ8BIP0.
PhosphoSiteiQ8BIP0.

Proteomic databases

EPDiQ8BIP0.
MaxQBiQ8BIP0.
PaxDbiQ8BIP0.
PeptideAtlasiQ8BIP0.
PRIDEiQ8BIP0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000035430; ENSMUSP00000041851; ENSMUSG00000026709.
GeneIDi226539.
KEGGimmu:226539.
UCSCiuc007dey.1. mouse.

Organism-specific databases

CTDi55157.
MGIiMGI:2442510. Dars2.

Phylogenomic databases

eggNOGiKOG2411. Eukaryota.
COG0173. LUCA.
GeneTreeiENSGT00550000074971.
HOGENOMiHOG000275159.
HOVERGENiHBG055815.
InParanoidiQ8BIP0.
KOiK01876.
OMAiYQLDVEM.
OrthoDBiEOG773XFN.
PhylomeDBiQ8BIP0.
TreeFamiTF314827.

Miscellaneous databases

PROiQ8BIP0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BIP0.
CleanExiMM_DARS2.
GenevisibleiQ8BIP0. MM.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
3.30.1360.30. 1 hit.
HAMAPiMF_00044. Asp_tRNA_synth.
InterProiIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004524. Asp-tRNA-ligase_bac/mit.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD-like.
IPR029351. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERiPTHR22594. PTHR22594. 2 hits.
PTHR22594:SF5. PTHR22594:SF5. 2 hits.
PfamiPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSiPR01042. TRNASYNTHASP.
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsiTIGR00459. aspS_bact. 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.
    Tissue: 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].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver and Spleen.

Entry informationi

Entry nameiSYDM_MOUSE
AccessioniPrimary (citable) accession number: Q8BIP0
Secondary accession number(s): Q5FWV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2003
Last modified: July 6, 2016
This is version 120 of the entry and version 1 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.