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Q5JTZ9

- SYAM_HUMAN

UniProt

Q5JTZ9 - SYAM_HUMAN

Protein

Alanine--tRNA ligase, mitochondrial

Gene

AARS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (15 Feb 2005)
      Previous versions | rss
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    Functioni

    Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged tRNA(Ala) via its editing domain.UniRule annotation

    Catalytic activityi

    ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).UniRule annotation

    Cofactori

    Binds 1 zinc ion per subunit.UniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi632 – 6321ZincUniRule annotation
    Metal bindingi636 – 6361ZincUniRule annotation
    Metal bindingi749 – 7491ZincUniRule annotation
    Metal bindingi753 – 7531ZincUniRule annotation

    GO - Molecular functioni

    1. alanine-tRNA ligase activity Source: BHF-UCL
    2. ATP binding Source: UniProtKB-HAMAP
    3. tRNA binding Source: UniProtKB-KW
    4. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mitochondrial alanyl-tRNA aminoacylation Source: BHF-UCL
    3. mitochondrial respiratory chain complex assembly 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, Metal-binding, Nucleotide-binding, RNA-binding, tRNA-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alanine--tRNA ligase, mitochondrialUniRule annotation (EC:6.1.1.7UniRule annotation)
    Alternative name(s):
    Alanyl-tRNA synthetaseUniRule annotation
    Short name:
    AlaRSUniRule annotation
    Gene namesi
    Name:AARS2UniRule annotation
    Synonyms:AARSL, KIAA1270
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:21022. AARS2.

    Subcellular locationi

    Mitochondrion 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Combined oxidative phosphorylation deficiency 8 (COXPD8) [MIM:614096]: A mitochondrial disease characterized by a lethal infantile hypertrophic cardiomyopathy, generalized muscle dysfunction and some neurologic involvement. The liver is not affected.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti155 – 1551L → R in COXPD8. 1 Publication
    VAR_065956
    Natural varianti592 – 5921R → W in COXPD8. 1 Publication
    VAR_065957

    Keywords - Diseasei

    Cardiomyopathy, Disease mutation

    Organism-specific databases

    MIMi614096. phenotype.
    Orphaneti319504. Combined oxidative phosphorylation defect type 8.
    PharmGKBiPA162375129.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2323MitochondrionUniRule annotationAdd
    BLAST
    Chaini24 – 985962Alanine--tRNA ligase, mitochondrialPRO_0000250725Add
    BLAST

    Proteomic databases

    MaxQBiQ5JTZ9.
    PaxDbiQ5JTZ9.
    PeptideAtlasiQ5JTZ9.
    PRIDEiQ5JTZ9.

    PTM databases

    PhosphoSiteiQ5JTZ9.

    Expressioni

    Gene expression databases

    BgeeiQ5JTZ9.
    CleanExiHS_AARS2.
    GenevestigatoriQ5JTZ9.

    Organism-specific databases

    HPAiHPA035636.

    Interactioni

    Subunit structurei

    Monomer.UniRule annotation

    Protein-protein interaction databases

    BioGridi121569. 4 interactions.
    IntActiQ5JTZ9. 2 interactions.
    MINTiMINT-8051598.
    STRINGi9606.ENSP00000244571.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5JTZ9.
    SMRiQ5JTZ9. Positions 37-784.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domaini

    Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.UniRule annotation

    Sequence similaritiesi

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

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0013.
    HOGENOMiHOG000156964.
    HOVERGENiHBG017874.
    InParanoidiQ5JTZ9.
    KOiK01872.
    OMAiWASKGSP.
    OrthoDBiEOG7M3HZH.
    PhylomeDBiQ5JTZ9.
    TreeFamiTF300737.

    Family and domain databases

    HAMAPiMF_00036_B. Ala_tRNA_synth_B.
    InterProiIPR002318. Ala-tRNA-lgiase_IIc.
    IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
    IPR018165. Ala-tRNA-synth_IIc_core.
    IPR018164. Ala-tRNA-synth_IIc_N.
    IPR023033. Ala_tRNA_ligase_euk/bac.
    IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
    IPR009000. Transl_B-barrel.
    IPR012947. tRNA_SAD.
    [Graphical view]
    PfamiPF01411. tRNA-synt_2c. 1 hit.
    PF07973. tRNA_SAD. 1 hit.
    [Graphical view]
    PRINTSiPR00980. TRNASYNTHALA.
    SMARTiSM00863. tRNA_SAD. 1 hit.
    [Graphical view]
    SUPFAMiSSF101353. SSF101353. 1 hit.
    SSF50447. SSF50447. 1 hit.
    SSF55186. SSF55186. 1 hit.
    TIGRFAMsiTIGR00344. alaS. 1 hit.
    PROSITEiPS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q5JTZ9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASVAAAAR RLRRAIRRSP AWRGLSHRPL SSEPPAAKAS AVRAAFLNFF    50
    RDRHGHRLVP SASVRPRGDP SLLFVNAGMN QFKPIFLGTV DPRSEMAGFR 100
    RVANSQKCVR AGGHHNDLED VGRDLSHHTF FEMLGNWAFG GEYFKEEACN 150
    MAWELLTQVY GIPEERLWIS YFDGDPKAGL DPDLETRDIW LSLGVPASRV 200
    LSFGPQENFW EMGDTGPCGP CTEIHYDLAG GVGAPQLVEL WNLVFMQHNR 250
    EADGSLQPLP QRHVDTGMGL ERLVAVLQGK HSTYDTDLFS PLLNAIQQGC 300
    RAPPYLGRVG VADEGRTDTA YRVVADHIRT LSVCISDGIF PGMSGPPLVL 350
    RRILRRAVRF SMEILKAPPG FLGSLVPVVV ETLGDAYPEL QRNSAQIANL 400
    VSEDEAAFLA SLERGRRIID RTLRTLGPSD MFPAEVAWSL SLCGDLGLPL 450
    DMVELMLEEK GVQLDSAGLE RLAQEEAQHR ARQAEPVQKQ GLWLDVHALG 500
    ELQRQGVPPT DDSPKYNYSL RPSGSYEFGT CEAQVLQLYT EDGTAVASVG 550
    KGQRCGLLLD RTNFYAEQGG QASDRGYLVR AGQEDVLFPV ARAQVCGGFI 600
    LHEAVAPECL RLGDQVQLHV DEAWRLGCMA KHTATHLLNW ALRQTLGPGT 650
    EQQGSHLNPE QLRLDVTTQT PLTPEQLRAV ENTVQEAVGQ DEAVYMEEVP 700
    LALTAQVPGL RSLDEVYPDP VRVVSVGVPV AHALDPASQA ALQTSVELCC 750
    GTHLLRTGAV GDLVIIGDRQ LSKGTTRLLA VTGEQAQQAR ELGQSLAQEV 800
    KAATERLSLG SRDVAEALRL SKDIGRLIEA VETAVMPQWQ RRELLATVKM 850
    LQRRANTAIR KLQMGQAAKK TQELLERHSK GPLIVDTVSA ESLSVLVKVV 900
    RQLCEQAPST SVLLLSPQPM GKVLCACQVA QGAMPTFTAE AWALAVCSHM 950
    GGKAWGSRVV AQGTGSTTDL EAALSIAQTY ALSQL 985
    Length:985
    Mass (Da):107,340
    Last modified:February 15, 2005 - v1
    Checksum:i721368BD05474F86
    GO

    Sequence cautioni

    The sequence BAA86584.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti155 – 1551L → R in COXPD8. 1 Publication
    VAR_065956
    Natural varianti339 – 3391I → V.2 Publications
    Corresponds to variant rs324136 [ dbSNP | Ensembl ].
    VAR_027609
    Natural varianti484 – 4841A → D.
    Corresponds to variant rs495294 [ dbSNP | Ensembl ].
    VAR_027610
    Natural varianti592 – 5921R → W in COXPD8. 1 Publication
    VAR_065957
    Natural varianti850 – 8501M → V.
    Corresponds to variant rs35783144 [ dbSNP | Ensembl ].
    VAR_057357

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB033096 mRNA. Translation: BAA86584.1. Different initiation.
    AL353588 Genomic DNA. Translation: CAI40747.1.
    BC013593 mRNA. Translation: AAH13593.1.
    BC033169 mRNA. Translation: AAH33169.1.
    BC131728 mRNA. Translation: AAI31729.1.
    CCDSiCCDS34464.1.
    RefSeqiNP_065796.1. NM_020745.3.
    UniGeneiHs.158381.

    Genome annotation databases

    EnsembliENST00000244571; ENSP00000244571; ENSG00000124608.
    GeneIDi57505.
    KEGGihsa:57505.
    UCSCiuc010jza.1. human.

    Polymorphism databases

    DMDMi74742244.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB033096 mRNA. Translation: BAA86584.1 . Different initiation.
    AL353588 Genomic DNA. Translation: CAI40747.1 .
    BC013593 mRNA. Translation: AAH13593.1 .
    BC033169 mRNA. Translation: AAH33169.1 .
    BC131728 mRNA. Translation: AAI31729.1 .
    CCDSi CCDS34464.1.
    RefSeqi NP_065796.1. NM_020745.3.
    UniGenei Hs.158381.

    3D structure databases

    ProteinModelPortali Q5JTZ9.
    SMRi Q5JTZ9. Positions 37-784.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121569. 4 interactions.
    IntActi Q5JTZ9. 2 interactions.
    MINTi MINT-8051598.
    STRINGi 9606.ENSP00000244571.

    Chemistry

    DrugBanki DB00160. L-Alanine.

    PTM databases

    PhosphoSitei Q5JTZ9.

    Polymorphism databases

    DMDMi 74742244.

    Proteomic databases

    MaxQBi Q5JTZ9.
    PaxDbi Q5JTZ9.
    PeptideAtlasi Q5JTZ9.
    PRIDEi Q5JTZ9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000244571 ; ENSP00000244571 ; ENSG00000124608 .
    GeneIDi 57505.
    KEGGi hsa:57505.
    UCSCi uc010jza.1. human.

    Organism-specific databases

    CTDi 57505.
    GeneCardsi GC06M044266.
    HGNCi HGNC:21022. AARS2.
    HPAi HPA035636.
    MIMi 612035. gene.
    614096. phenotype.
    neXtProti NX_Q5JTZ9.
    Orphaneti 319504. Combined oxidative phosphorylation defect type 8.
    PharmGKBi PA162375129.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0013.
    HOGENOMi HOG000156964.
    HOVERGENi HBG017874.
    InParanoidi Q5JTZ9.
    KOi K01872.
    OMAi WASKGSP.
    OrthoDBi EOG7M3HZH.
    PhylomeDBi Q5JTZ9.
    TreeFami TF300737.

    Enzyme and pathway databases

    Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.

    Miscellaneous databases

    GeneWikii AARS2.
    GenomeRNAii 57505.
    NextBioi 63841.
    PROi Q5JTZ9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q5JTZ9.
    CleanExi HS_AARS2.
    Genevestigatori Q5JTZ9.

    Family and domain databases

    HAMAPi MF_00036_B. Ala_tRNA_synth_B.
    InterProi IPR002318. Ala-tRNA-lgiase_IIc.
    IPR018162. Ala-tRNA-ligase_IIc_anticod-bd.
    IPR018165. Ala-tRNA-synth_IIc_core.
    IPR018164. Ala-tRNA-synth_IIc_N.
    IPR023033. Ala_tRNA_ligase_euk/bac.
    IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
    IPR009000. Transl_B-barrel.
    IPR012947. tRNA_SAD.
    [Graphical view ]
    Pfami PF01411. tRNA-synt_2c. 1 hit.
    PF07973. tRNA_SAD. 1 hit.
    [Graphical view ]
    PRINTSi PR00980. TRNASYNTHALA.
    SMARTi SM00863. tRNA_SAD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF101353. SSF101353. 1 hit.
    SSF50447. SSF50447. 1 hit.
    SSF55186. SSF55186. 1 hit.
    TIGRFAMsi TIGR00344. alaS. 1 hit.
    PROSITEi PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
      DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-339.
      Tissue: Brain.
    2. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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], VARIANT VAL-339.
      Tissue: Lung.
    4. "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: IDENTIFICATION.
    5. "Exome sequencing identifies mitochondrial alanyl-tRNA synthetase mutations in infantile mitochondrial cardiomyopathy."
      Gotz A., Tyynismaa H., Euro L., Ellonen P., Hyotylainen T., Ojala T., Hamalainen R.H., Tommiska J., Raivio T., Oresic M., Karikoski R., Tammela O., Simola K.O., Paetau A., Tyni T., Suomalainen A.
      Am. J. Hum. Genet. 88:635-642(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, VARIANTS COXPD8 ARG-155 AND TRP-592.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSYAM_HUMAN
    AccessioniPrimary (citable) accession number: Q5JTZ9
    Secondary accession number(s): A2RRN5
    , Q8N198, Q96D02, Q9ULF0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: February 15, 2005
    Last modified: October 1, 2014
    This is version 91 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

    Complete proteome, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 6
      Human chromosome 6: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3