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Q6PI48

- SYDM_HUMAN

UniProt

Q6PI48 - SYDM_HUMAN

Protein

Aspartate--tRNA ligase, mitochondrial

Gene

DARS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei266 – 2661AspartateBy similarity
    Binding sitei535 – 5351ATPBy similarity
    Binding sitei542 – 5421AspartateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi266 – 2683ATPBy similarity
    Nucleotide bindingi584 – 5874ATPBy similarity

    GO - Molecular functioni

    1. aspartate-tRNA(Asn) ligase activity Source: BHF-UCL
    2. aspartate-tRNA ligase activity Source: Reactome
    3. ATP binding Source: BHF-UCL
    4. protein binding Source: BHF-UCL
    5. protein homodimerization activity Source: BHF-UCL
    6. tRNA binding Source: BHF-UCL

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mitochondrial asparaginyl-tRNA aminoacylation Source: BHF-UCL
    3. tRNA aminoacylation Source: BHF-UCL
    4. tRNA aminoacylation for protein translation Source: Reactome

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:25538. DARS2.

    Subcellular locationi

    Mitochondrion matrix 1 Publication

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: BHF-UCL
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti45 – 451S → G in LBSL. 1 Publication
    VAR_037015
    Natural varianti152 – 1521C → F in LBSL. 1 Publication
    VAR_037016
    Natural varianti179 – 1791R → H in LBSL. 1 Publication
    VAR_037017
    Natural varianti184 – 1841Q → K in LBSL. 1 Publication
    VAR_037018
    Natural varianti248 – 2481Q → K in LBSL. 1 Publication
    VAR_037019
    Natural varianti263 – 2631R → Q in LBSL. 1 Publication
    VAR_037020
    Natural varianti560 – 5601D → V in LBSL. 1 Publication
    VAR_037021
    Natural varianti613 – 6131L → F in LBSL. 1 Publication
    VAR_037022
    Natural varianti626 – 6261L → Q in LBSL. 1 Publication
    VAR_037023
    Natural varianti626 – 6261L → V in LBSL. 1 Publication
    VAR_037024
    Natural varianti629 – 6291Y → C in LBSL. 1 Publication
    VAR_037025

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi611105. phenotype.
    Orphaneti137898. Leukoencephalopathy with brain stem and spinal cord involvement - high lactate.
    PharmGKBiPA142672015.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4747MitochondrionSequence AnalysisAdd
    BLAST
    Chaini48 – 645598Aspartate--tRNA ligase, mitochondrialPRO_0000250736Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei219 – 2191PhosphothreonineBy similarity
    Modified residuei382 – 3821N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ6PI48.
    PaxDbiQ6PI48.
    PeptideAtlasiQ6PI48.
    PRIDEiQ6PI48.

    PTM databases

    PhosphoSiteiQ6PI48.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6PI48.
    BgeeiQ6PI48.
    CleanExiHS_DARS2.
    GenevestigatoriQ6PI48.

    Organism-specific databases

    HPAiHPA026506.
    HPA026528.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi120459. 10 interactions.
    IntActiQ6PI48. 3 interactions.
    STRINGi9606.ENSP00000355086.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AH6X-ray3.70A/B/C/D41-645[»]
    ProteinModelPortaliQ6PI48.
    SMRiQ6PI48. Positions 42-630.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni244 – 2474AspartateBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0173.
    HOGENOMiHOG000275159.
    HOVERGENiHBG055815.
    InParanoidiQ6PI48.
    KOiK01876.
    OMAiFVEQNDV.
    OrthoDBiEOG773XFN.
    PhylomeDBiQ6PI48.
    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_IIb_bac/mt.
    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. 1 hit.
    PTHR22594:SF5. PTHR22594:SF5. 1 hit.
    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.

    Q6PI48-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYFPSWLSQL YRGLSRPIRR TTQPIWGSLY RSLLQSSQRR IPEFSSFVVR    50
    TNTCGELRSS HLGQEVTLCG WIQYRRQNTF LVLRDFDGLV QVIIPQDESA 100
    ASVKKILCEA PVESVVQVSG TVISRPAGQE NPKMPTGEIE IKVKTAELLN 150
    ACKKLPFEIK NFVKKTEALR LQYRYLDLRS FQMQYNLRLR SQMVMKMREY 200
    LCNLHGFVDI ETPTLFKRTP GGAKEFLVPS REPGKFYSLP QSPQQFKQLL 250
    MVGGLDRYFQ VARCYRDEGS RPDRQPEFTQ IDIEMSFVDQ TGIQSLIEGL 300
    LQYSWPNDKD PVVVPFPTMT FAEVLATYGT DKPDTRFGMK IIDISDVFRN 350
    TEIGFLQDAL SKPHGTVKAI CIPEGAKYLK RKDIESIRNF AADHFNQEIL 400
    PVFLNANRNW NSPVANFIME SQRLELIRLM ETQEEDVVLL TAGEHNKACS 450
    LLGKLRLECA DLLETRGVVL RDPTLFSFLW VVDFPLFLPK EENPRELESA 500
    HHPFTAPHPS DIHLLYTEPK KARSQHYDLV LNGNEIGGGS IRIHNAELQR 550
    YILATLLKED VKMLSHLLQA LDYGAPPHGG IALGLDRLIC LVTGSPSIRD 600
    VIAFPKSFRG HDLMSNTPDS VPPEELKPYH IRVSKPTDSK AERAH 645
    Length:645
    Mass (Da):73,563
    Last modified:July 5, 2004 - v1
    Checksum:i8B668751542F01A1
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti10 – 101L → V.
    Corresponds to variant rs4427454 [ dbSNP | Ensembl ].
    VAR_027612
    Natural varianti45 – 451S → G in LBSL. 1 Publication
    VAR_037015
    Natural varianti152 – 1521C → F in LBSL. 1 Publication
    VAR_037016
    Natural varianti179 – 1791R → H in LBSL. 1 Publication
    VAR_037017
    Natural varianti184 – 1841Q → K in LBSL. 1 Publication
    VAR_037018
    Natural varianti196 – 1961K → R.
    Corresponds to variant rs35515638 [ dbSNP | Ensembl ].
    VAR_034525
    Natural varianti248 – 2481Q → K in LBSL. 1 Publication
    VAR_037019
    Natural varianti263 – 2631R → Q in LBSL. 1 Publication
    VAR_037020
    Natural varianti560 – 5601D → V in LBSL. 1 Publication
    VAR_037021
    Natural varianti613 – 6131L → F in LBSL. 1 Publication
    VAR_037022
    Natural varianti626 – 6261L → Q in LBSL. 1 Publication
    VAR_037023
    Natural varianti626 – 6261L → V in LBSL. 1 Publication
    VAR_037024
    Natural varianti629 – 6291Y → C in LBSL. 1 Publication
    VAR_037025

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL109921 Genomic DNA. Translation: CAI20380.1.
    BC045173 mRNA. Translation: AAH45173.1.
    CCDSiCCDS1311.1.
    RefSeqiNP_060592.2. NM_018122.4.
    UniGeneiHs.647707.

    Genome annotation databases

    EnsembliENST00000361951; ENSP00000355086; ENSG00000117593.
    GeneIDi55157.
    KEGGihsa:55157.
    UCSCiuc001gjh.2. human.

    Polymorphism databases

    DMDMi74758347.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL109921 Genomic DNA. Translation: CAI20380.1 .
    BC045173 mRNA. Translation: AAH45173.1 .
    CCDSi CCDS1311.1.
    RefSeqi NP_060592.2. NM_018122.4.
    UniGenei Hs.647707.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4AH6 X-ray 3.70 A/B/C/D 41-645 [» ]
    ProteinModelPortali Q6PI48.
    SMRi Q6PI48. Positions 42-630.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120459. 10 interactions.
    IntActi Q6PI48. 3 interactions.
    STRINGi 9606.ENSP00000355086.

    Chemistry

    DrugBanki DB00128. L-Aspartic Acid.

    PTM databases

    PhosphoSitei Q6PI48.

    Polymorphism databases

    DMDMi 74758347.

    Proteomic databases

    MaxQBi Q6PI48.
    PaxDbi Q6PI48.
    PeptideAtlasi Q6PI48.
    PRIDEi Q6PI48.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361951 ; ENSP00000355086 ; ENSG00000117593 .
    GeneIDi 55157.
    KEGGi hsa:55157.
    UCSCi uc001gjh.2. human.

    Organism-specific databases

    CTDi 55157.
    GeneCardsi GC01P173793.
    GeneReviewsi DARS2.
    HGNCi HGNC:25538. DARS2.
    HPAi HPA026506.
    HPA026528.
    MIMi 610956. gene.
    611105. phenotype.
    neXtProti NX_Q6PI48.
    Orphaneti 137898. Leukoencephalopathy with brain stem and spinal cord involvement - high lactate.
    PharmGKBi PA142672015.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0173.
    HOGENOMi HOG000275159.
    HOVERGENi HBG055815.
    InParanoidi Q6PI48.
    KOi K01876.
    OMAi FVEQNDV.
    OrthoDBi EOG773XFN.
    PhylomeDBi Q6PI48.
    TreeFami TF314827.

    Enzyme and pathway databases

    Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi DARS2. human.
    GenomeRNAii 55157.
    NextBioi 58907.
    PROi Q6PI48.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6PI48.
    Bgeei Q6PI48.
    CleanExi HS_DARS2.
    Genevestigatori Q6PI48.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    3.30.1360.30. 1 hit.
    HAMAPi MF_00044. Asp_tRNA_synth.
    InterProi IPR004364. 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-like.
    IPR029351. GAD_dom.
    IPR012340. NA-bd_OB-fold.
    IPR004365. NA-bd_OB_tRNA.
    [Graphical view ]
    PANTHERi PTHR22594. PTHR22594. 1 hit.
    PTHR22594:SF5. PTHR22594:SF5. 1 hit.
    Pfami PF02938. GAD. 1 hit.
    PF00152. tRNA-synt_2. 1 hit.
    PF01336. tRNA_anti-codon. 1 hit.
    [Graphical view ]
    PRINTSi PR01042. TRNASYNTHASP.
    SUPFAMi SSF50249. SSF50249. 1 hit.
    SSF55261. SSF55261. 1 hit.
    TIGRFAMsi TIGR00459. aspS_bact. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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.

    Entry informationi

    Entry nameiSYDM_HUMAN
    AccessioniPrimary (citable) accession number: Q6PI48
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3