Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8BIP0 (SYDM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Aspartate--tRNA ligase, mitochondrial

EC=6.1.1.12
Alternative name(s):
Aspartyl-tRNA synthetase
Short name=AspRS
Gene names
Name:Dars2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length653 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtRNA aminoacylation for protein translation

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

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

Transit peptide1 – 4646Mitochondrion Potential
Chain47 – 653607Aspartate--tRNA ligase, mitochondrial
PRO_0000250737

Amino acid modifications

Modified residue2341N6-acetyllysine By similarity
Modified residue6261N6-acetyllysine By similarity

Experimental info

Sequence conflict711I → V in AAH89191. Ref.2
Sequence conflict1041R → G in AAH89191. Ref.2
Sequence conflict5401V → A in AAH89191. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q8BIP0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 8A02D2E62E914E99

FASTA65374,102
        10         20         30         40         50         60 
MYLGFWLSRL CRGLSRPIGK TMRPIWGSLS RNLALSSQRI PEFSSFVART NTCGELRSSH 

        70         80         90        100        110        120 
LGQEVTLCGW IQYRRQNTFL VLRDCHGLVQ ILIPQDESAA SVRRILCEAP VESVVRVSGT 

       130        140        150        160        170        180 
VISRPPGQEN PKMPTGEIEI KVKTAELLNA CKKLPFEIKD FVKKTEALRL QYRYLDLRSF 

       190        200        210        220        230        240 
QMQYNLRLRS QMVMKMREYL CNLHGFVDIE TPTLFKRTPG GAKEFLVPSR EPGKFYSLPQ 

       250        260        270        280        290        300 
SPQQFKQLLM VGGLDRYFQV ARCYRDEGSR PDRQPEFTQI DIEMSFVEQT GIQRLVEGLL 

       310        320        330        340        350        360 
QYSWPGDKDP LVTPFPSMTF AEALATYGTD KPDTRFGMKI VDVSDVFRNT ELRFLQDALA 

       370        380        390        400        410        420 
KPQGTVKAIC VHDGAKYLRK EDIEFIRKFA VHHFSQEVLP IFLNAKKNWS SPFAKFIMEE 

       430        440        450        460        470        480 
ERLELARSME IQEEDIVLLT AGEHEKACSL LGKLRLECAD LLEMRGAVLR DPAVFSFLWV 

       490        500        510        520        530        540 
VDFPLFLAKE ESPTELESAH HPFTAPNSSD IHLLYTEPEK VRGQHYDLVL NGNEIGGGSV 

       550        560        570        580        590        600 
RIHDAQLQRY ILETLLKEDV KLLSHLLQAL DYGAPPHGGI ALGLDRLVCL VTGAPSIRDV 

       610        620        630        640        650 
IAFPKSYRGQ DLMSNAPDSV SPEELKPYHI HVLWPADSEE ESASATPSKH LSS 

« 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.
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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK037337 mRNA. Translation: BAC29789.1.
AK138809 mRNA. Translation: BAE23785.1.
BC076606 mRNA. Translation: AAH76606.1.
BC089191 mRNA. Translation: AAH89191.1.
IPIIPI00273767.
RefSeqNP_766232.1. NM_172644.3.
UniGeneMm.28125.

3D structure databases

HSSPHSSP built from PDB template 1L0W based on UniProtKB P36419.
ProteinModelPortalQ8BIP0.
SMRQ8BIP0. Positions 48-635.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8BIP0.

PTM databases

PhosphoSiteQ8BIP0.

Proteomic databases

PRIDEQ8BIP0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035430; ENSMUSP00000041851; ENSMUSG00000026709.
GeneID226539.
KEGGmmu:226539.
NMPDRfig|10090.3.peg.1326.
UCSCuc007dey.1. mouse.

Organism-specific databases

CTD55157.
MGIMGI:2442510. Dars2.

Phylogenomic databases

eggNOGroNOG07016.
GeneTreeENSGT00550000074971.
HOGENOMHBG396032.
HOVERGENHBG055815.
InParanoidQ8BIP0.
OMAAFPKTQQ.
OrthoDBEOG4M91R5.
PhylomeDBQ8BIP0.

Gene expression databases

ArrayExpressQ8BIP0.
BgeeQ8BIP0.
CleanExMM_DARS2.
GenevestigatorQ8BIP0.
GermOnlineENSMUSG00000026709. Mus musculus.

Family and domain databases

InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004524. Asp-tRNA-synth_IIb_bac/mt.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR004365. NA-bd_OB_tRNA-helicase.
[Graphical view]
Gene3DG3DSA:3.30.1360.30. GAD_dom. 1 hit.
G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
KOK01876.
PANTHERPTHR22594. aa-tRNA-synt_II. 1 hit.
PTHR22594:SF5. AspS_bac. 1 hit.
PfamPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsTIGR00459. AspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio378214.
SOURCESearch...

Entry information

Entry nameSYDM_MOUSE
AccessionPrimary (citable) accession number: Q8BIP0
Secondary accession number(s): Q5FWV4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 85 of the entry and version 1 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