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Reviewed, UniProtKB/Swiss-Prot Q6PI48 (SYDM_HUMAN)

Last modified December 16, 2008. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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

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Names and origin

Protein namesRecommended name:
    Aspartyl-tRNA synthetase, mitochondrial
    EC=6.1.1.12
Alternative name(s):
    Aspartate--tRNA ligase
      Short name=AspRS
Gene names
Name: DARS2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length645 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Catalytic activity

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

Subunit structure

Homodimer. Ref.3

Subcellular location

Mitochondrion matrix. Ref.3

Involvement in disease

Defects in DARS2 are a cause of leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation (LBSL) [MIM:611105]. LBSL is an autosomal recessive disease and is defined on the basis of a highly characteristic constellation of abnormalities observed by magnetic resonance imaging and spectroscopy. Affected individuals develop slowly progressive cerebellar ataxia, spasticity, and dorsal column dysfunction, sometimes with a mild cognitive deficit or decline. Ref.4

Sequence similarities

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

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Ontologies

Keywords

   Biological processProtein biosynthesis
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase

Gene Ontology (GO)

   Biological processaspartyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: InterPro

aspartate-tRNA ligase activity

Inferred from electronic annotation. Source: InterPro

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4747Mitochondrion Potential
Chain48 – 645598Aspartyl-tRNA synthetase, mitochondrial
PRO_0000250736

Natural variations

Natural variant101L → V: dbSNP rs4427454.
VAR_027612
Natural variant451S → G in LBSL. Ref.4
VAR_037015
Natural variant1521C → F in LBSL. Ref.4
VAR_037016
Natural variant1791R → H in LBSL. Ref.4
VAR_037017
Natural variant1841Q → K in LBSL. Ref.4
VAR_037018
Natural variant1961K → R: dbSNP rs35515638.
VAR_034525
Natural variant2481Q → K in LBSL. Ref.4
VAR_037019
Natural variant2631R → Q in LBSL. Ref.4
VAR_037020
Natural variant5601D → V in LBSL. Ref.4
VAR_037021
Natural variant6131L → F in LBSL. Ref.4
VAR_037022
Natural variant6261L → Q in LBSL. Ref.4
VAR_037023
Natural variant6261L → V in LBSL. Ref.4
VAR_037024
Natural variant6291Y → C in LBSL. Ref.4
VAR_037025

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Sequences

Sequence LengthMass (Da)Tools
Q6PI48-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 8B668751542F01A1

FASTA64573,563
        10         20         30         40         50         60 
MYFPSWLSQL YRGLSRPIRR TTQPIWGSLY RSLLQSSQRR IPEFSSFVVR TNTCGELRSS 

        70         80         90        100        110        120 
HLGQEVTLCG WIQYRRQNTF LVLRDFDGLV QVIIPQDESA ASVKKILCEA PVESVVQVSG 

       130        140        150        160        170        180 
TVISRPAGQE NPKMPTGEIE IKVKTAELLN ACKKLPFEIK NFVKKTEALR LQYRYLDLRS 

       190        200        210        220        230        240 
FQMQYNLRLR SQMVMKMREY LCNLHGFVDI ETPTLFKRTP GGAKEFLVPS REPGKFYSLP 

       250        260        270        280        290        300 
QSPQQFKQLL MVGGLDRYFQ VARCYRDEGS RPDRQPEFTQ IDIEMSFVDQ TGIQSLIEGL 

       310        320        330        340        350        360 
LQYSWPNDKD PVVVPFPTMT FAEVLATYGT DKPDTRFGMK IIDISDVFRN TEIGFLQDAL 

       370        380        390        400        410        420 
SKPHGTVKAI CIPEGAKYLK RKDIESIRNF AADHFNQEIL PVFLNANRNW NSPVANFIME 

       430        440        450        460        470        480 
SQRLELIRLM ETQEEDVVLL TAGEHNKACS LLGKLRLECA DLLETRGVVL RDPTLFSFLW 

       490        500        510        520        530        540 
VVDFPLFLPK EENPRELESA HHPFTAPHPS DIHLLYTEPK KARSQHYDLV LNGNEIGGGS 

       550        560        570        580        590        600 
IRIHNAELQR YILATLLKED VKMLSHLLQA LDYGAPPHGG IALGLDRLIC LVTGSPSIRD 

       610        620        630        640 
VIAFPKSFRG HDLMSNTPDS VPPEELKPYH IRVSKPTDSK AERAH

« Hide

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References

« Hide 'large scale' references
[1]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Testis.
[3]"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: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
[4]"Mitochondrial aspartyl-tRNA synthetase deficiency causes leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation."
Scheper G.C., van der Klok T., van Andel R.J., van Berkel C.G.M., Sissler M., Smet J., Muravina T.I., Serkov S.V., Uziel G., Bugiani M., Schiffmann R., Kraegeloh-Mann I., Smeitink J.A.M., Florentz C., Van Coster R., Pronk J.C., van der Knaap M.S.
Nat. Genet. 39:534-539(2007) [PubMed: 17384640] [Abstract]
Cited for: VARIANTS LBSL GLY-45; PHE-152; HIS-179; LYS-184; LYS-248; GLN-263; VAL-560; PHE-613; VAL-626; GLN-626 AND CYS-629.

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Cross-references

Sequence databases

AL109921 Genomic DNA. Translation: CAI20380.1.
BC045173 mRNA. Translation: AAH45173.1.
RefSeqNP_060592.2.
UniGeneHs.647707

3D structure databases

HSSPHSSP built from PDB template 1BBW based on UniProtKB P13030.
ModBaseSearch...

PTM databases

PhosphoSiteQ6PI48.

Proteomic databases

PeptideAtlasQ6PI48.
PRIDEQ6PI48.

Genome annotation databases

EnsemblENSG00000117593. Homo sapiens. [Contig view]
GeneID55157.
KEGGhsa:55157.

Organism-specific databases

GeneCardsGC01P172060.
HGNCHGNC:25538. DARS2.
MIM610956. gene.
611105. phenotype.
Orphanet137898. Leukoencephalopathy with brain stem, spinal cord involvement - lactate elevation.
PharmGKBPA142672015.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ6PI48.

Gene expression databases

ArrayExpressQ6PI48.
CleanExHS_DARS2.
GermOnlineENSG00000117593. Homo sapiens.

Family and domain databases

InterProIPR004364. aa-tRNA-synt_II.
IPR006195. aa-tRNA-synth_II.
IPR002312. Asp-tRNA-synth_IIb.
IPR004524. Asp-tRNA-synth_IIb_bac/mito.
IPR004115. GAD.
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.
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.
TIGRFAMsTIGR00459. aspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00128. L-Aspartic Acid.
NextBio58907.
SOURCESearch...

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Entry information

Entry nameSYDM_HUMAN
AccessionPrimary (citable) accession number: Q6PI48
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: July 5, 2004
Last modified: December 16, 2008
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Human chromosome 1

Human chromosome 1: 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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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