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Q6PI48 (SYDM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

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

Leukoencephalopathy with brainstem and spinal cord involvement and lactate elevation (LBSL) [MIM:611105]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4747Mitochondrion Potential
Chain48 – 645598Aspartate--tRNA ligase, mitochondrial
PRO_0000250736

Amino acid modifications

Modified residue2191Phosphothreonine By similarity
Modified residue3821N6-acetyllysine Ref.4

Natural variations

Natural variant101L → V.
Corresponds to variant rs4427454 [ dbSNP | Ensembl ].
VAR_027612
Natural variant451S → G in LBSL. Ref.6
VAR_037015
Natural variant1521C → F in LBSL. Ref.6
VAR_037016
Natural variant1791R → H in LBSL. Ref.6
VAR_037017
Natural variant1841Q → K in LBSL. Ref.6
VAR_037018
Natural variant1961K → R.
Corresponds to variant rs35515638 [ dbSNP | Ensembl ].
VAR_034525
Natural variant2481Q → K in LBSL. Ref.6
VAR_037019
Natural variant2631R → Q in LBSL. Ref.6
VAR_037020
Natural variant5601D → V in LBSL. Ref.6
VAR_037021
Natural variant6131L → F in LBSL. Ref.6
VAR_037022
Natural variant6261L → Q in LBSL. Ref.6
VAR_037023
Natural variant6261L → V in LBSL. Ref.6
VAR_037024
Natural variant6291Y → C in LBSL. Ref.6
VAR_037025

Sequences

Sequence LengthMass (Da)Tools
Q6PI48 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
[4]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-382, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"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] [Europe PMC] [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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL109921 Genomic DNA. Translation: CAI20380.1.
BC045173 mRNA. Translation: AAH45173.1.
RefSeqNP_060592.2. NM_018122.4.
UniGeneHs.647707.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4AH6X-ray3.70A/B/C/D41-645[»]
ProteinModelPortalQ6PI48.
SMRQ6PI48. Positions 42-630.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120459. 7 interactions.
IntActQ6PI48. 3 interactions.
STRING9606.ENSP00000355086.

Chemistry

DrugBankDB00128. L-Aspartic Acid.

PTM databases

PhosphoSiteQ6PI48.

Polymorphism databases

DMDM74758347.

Proteomic databases

PaxDbQ6PI48.
PeptideAtlasQ6PI48.
PRIDEQ6PI48.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361951; ENSP00000355086; ENSG00000117593.
GeneID55157.
KEGGhsa:55157.
UCSCuc001gjh.2. human.

Organism-specific databases

CTD55157.
GeneCardsGC01P173793.
HGNCHGNC:25538. DARS2.
HPAHPA026506.
HPA026528.
MIM610956. gene.
611105. phenotype.
neXtProtNX_Q6PI48.
Orphanet137898. Leukoencephalopathy with brain stem and spinal cord involvement - lactate elevation.
PharmGKBPA142672015.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0173.
HOGENOMHOG000275159.
HOVERGENHBG055815.
InParanoidQ6PI48.
KOK01876.
OMAQLDVEMS.
OrthoDBEOG773XFN.
PhylomeDBQ6PI48.
TreeFamTF314827.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ6PI48.
BgeeQ6PI48.
CleanExHS_DARS2.
GenevestigatorQ6PI48.

Family and domain databases

Gene3D2.40.50.140. 1 hit.
3.30.1360.30. 1 hit.
InterProIPR004364. aa-tRNA-synt_II.
IPR018150. aa-tRNA-synt_II-like.
IPR006195. aa-tRNA-synth_II.
IPR004524. Asp-tRNA-ligase_IIb_bac/mt.
IPR002312. Asp/Asn-tRNA-synth_IIb.
IPR004115. GAD_dom.
IPR012340. NA-bd_OB-fold.
IPR004365. NA-bd_OB_tRNA.
[Graphical view]
PANTHERPTHR22594. PTHR22594. 1 hit.
PTHR22594:SF5. PTHR22594:SF5. 1 hit.
PfamPF02938. GAD. 1 hit.
PF00152. tRNA-synt_2. 1 hit.
PF01336. tRNA_anti-codon. 1 hit.
[Graphical view]
PRINTSPR01042. TRNASYNTHASP.
SUPFAMSSF50249. SSF50249. 1 hit.
SSF55261. SSF55261. 1 hit.
TIGRFAMsTIGR00459. aspS_bact. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDARS2. human.
GenomeRNAi55157.
NextBio58907.
PROQ6PI48.
SOURCESearch...

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: April 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries