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P49588

- SYAC_HUMAN

UniProt

P49588 - SYAC_HUMAN

Protein

Alanine--tRNA ligase, cytoplasmic

Gene

AARS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (03 Oct 2006)
      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 bindingi605 – 6051ZincUniRule annotation
    Metal bindingi609 – 6091ZincUniRule annotation
    Metal bindingi723 – 7231ZincUniRule annotation
    Metal bindingi727 – 7271ZincUniRule annotation

    GO - Molecular functioni

    1. alanine-tRNA ligase activity Source: UniProtKB-HAMAP
    2. amino acid binding Source: Ensembl
    3. aminoacyl-tRNA editing activity Source: Ensembl
    4. ATP binding Source: UniProtKB-HAMAP
    5. tRNA binding Source: ProtInc
    6. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. alanyl-tRNA aminoacylation Source: ProtInc
    2. cell death Source: UniProtKB-KW
    3. cerebellar Purkinje cell layer development Source: Ensembl
    4. endoplasmic reticulum unfolded protein response Source: Ensembl
    5. gene expression Source: Reactome
    6. hair follicle development Source: Ensembl
    7. negative regulation of neuron apoptotic process Source: Ensembl
    8. neuromuscular process controlling balance Source: Ensembl
    9. protein folding Source: Ensembl
    10. response to amino acid Source: Ensembl
    11. tRNA aminoacylation for protein translation Source: Reactome
    12. tRNA modification Source: Ensembl
    13. tRNA processing Source: ProtInc

    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_15306. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alanine--tRNA ligase, cytoplasmicUniRule annotation (EC:6.1.1.7UniRule annotation)
    Alternative name(s):
    Alanyl-tRNA synthetaseUniRule annotation
    Short name:
    AlaRSUniRule annotation
    Renal carcinoma antigen NY-REN-42
    Gene namesi
    Name:AARSUniRule annotation
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:20. AARS.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Charcot-Marie-Tooth disease 2N (CMT2N) [MIM:613287]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711N → Y in CMT2N. 1 Publication
    VAR_067084
    Natural varianti329 – 3291R → H in CMT2N; severely reduces enzyme activity. 2 Publications
    VAR_063527

    Keywords - Diseasei

    Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

    Organism-specific databases

    MIMi613287. phenotype.
    Orphaneti228174. Autosomal dominant Charcot-Marie-Tooth disease type 2N.
    PharmGKBiPA24367.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 968968Alanine--tRNA ligase, cytoplasmicPRO_0000075281Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine4 PublicationsUniRule annotation
    Modified residuei19 – 191N6-acetyllysine1 Publication
    Modified residuei399 – 3991Phosphoserine1 Publication
    Modified residuei555 – 5551Phosphoserine1 Publication
    Modified residuei876 – 8761N6-acetyllysine1 Publication

    Post-translational modificationi

    ISGylated.1 PublicationUniRule annotation

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP49588.
    PaxDbiP49588.
    PRIDEiP49588.

    PTM databases

    PhosphoSiteiP49588.

    Expressioni

    Gene expression databases

    BgeeiP49588.
    CleanExiHS_AARS.
    GenevestigatoriP49588.

    Organism-specific databases

    HPAiCAB034261.
    HPA040870.
    HPA044223.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi106534. 42 interactions.
    IntActiP49588. 4 interactions.
    MINTiMINT-1490092.
    STRINGi9606.ENSP00000261772.

    Structurei

    3D structure databases

    ProteinModelPortaliP49588.
    SMRiP49588. Positions 6-757.
    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
    The C-terminal C-Ala domain (residues 756 to 968), along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs. The human domain can be used in vitro to replace the corresponding domain in E.coli.1 Publication

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0013.
    HOGENOMiHOG000156964.
    HOVERGENiHBG017874.
    InParanoidiP49588.
    KOiK01872.
    OMAiYFEGDAK.
    OrthoDBiEOG7M3HZH.
    PhylomeDBiP49588.
    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.
    IPR003156. DHHA1_dom.
    IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
    IPR009000. Transl_B-barrel.
    IPR012947. tRNA_SAD.
    [Graphical view]
    PfamiPF02272. DHHA1. 1 hit.
    PF01411. 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.

    P49588-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDSTLTASEI RQRFIDFFKR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK    50
    PIFLNTIDPS HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM 100
    LGSWSFGDYF KELACKMALE LLTQEFGIPI ERLYVTYFGG DEAAGLEADL 150
    ECKQIWQNLG LDDTKILPGN MKDNFWEMGD TGPCGPCSEI HYDRIGGRDA 200
    AHLVNQDDPN VLEIWNLVFI QYNREADGIL KPLPKKSIDT GMGLERLVSV 250
    LQNKMSNYDT DLFVPYFEAI QKGTGARPYT GKVGAEDADG IDMAYRVLAD 300
    HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYAHEKLN ASRGFFATLV 350
    DVVVQSLGDA FPELKKDPDM VKDIINEEEV QFLKTLSRGR RILDRKIQSL 400
    GDSKTIPGDT AWLLYDTYGF PVDLTGLIAE EKGLVVDMDG FEEERKLAQL 450
    KSQGKGAGGE DLIMLDIYAI EELRARGLEV TDDSPKYNYH LDSSGSYVFE 500
    NTVATVMALR REKMFVEEVS TGQECGVVLD KTCFYAEQGG QIYDEGYLVK 550
    VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GDLKVGDQVW LFIDEPRRRP 600
    IMSNHTATHI LNFALRSVLG EADQKGSLVA PDRLRFDFTA KGAMSTQQIK 650
    KAEEIANEMI EAAKAVYTQD CPLAAAKAIQ GLRAVFDETY PDPVRVVSIG 700
    VPVSELLDDP SGPAGSLTSV EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR 750
    RIVAVTGAEA QKALRKAESL KKCLSVMEAK VKAQTAPNKD VQREIADLGE 800
    ALATAVIPQW QKDELRETLK SLKKVMDDLD RASKADVQKR VLEKTKQFID 850
    SNPNQPLVIL EMESGASAKA LNEALKLFKM HSPQTSAMLF TVDNEAGKIT 900
    CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDVSAQA TGKNVGCLQE 950
    ALQLATSFAQ LRLGDVKN 968
    Length:968
    Mass (Da):106,810
    Last modified:October 3, 2006 - v2
    Checksum:i8683F111CEE42506
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti82 – 821H → Q in BAA06808. (PubMed:7654687)Curated
    Sequence conflicti867 – 8671S → T in BAD96544. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711N → Y in CMT2N. 1 Publication
    VAR_067084
    Natural varianti275 – 2751G → D.
    Corresponds to variant rs11537667 [ dbSNP | Ensembl ].
    VAR_028204
    Natural varianti329 – 3291R → H in CMT2N; severely reduces enzyme activity. 2 Publications
    VAR_063527

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D32050 mRNA. Translation: BAA06808.1.
    AK222824 mRNA. Translation: BAD96544.1.
    AC012184 Genomic DNA. No translation available.
    CH471241 Genomic DNA. Translation: EAW51839.1.
    BC011451 mRNA. Translation: AAH11451.1.
    CCDSiCCDS32474.1.
    PIRiI60107.
    RefSeqiNP_001596.2. NM_001605.2.
    UniGeneiHs.315137.

    Genome annotation databases

    EnsembliENST00000261772; ENSP00000261772; ENSG00000090861.
    GeneIDi16.
    KEGGihsa:16.
    UCSCiuc002eyn.1. human.

    Polymorphism databases

    DMDMi115502460.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D32050 mRNA. Translation: BAA06808.1 .
    AK222824 mRNA. Translation: BAD96544.1 .
    AC012184 Genomic DNA. No translation available.
    CH471241 Genomic DNA. Translation: EAW51839.1 .
    BC011451 mRNA. Translation: AAH11451.1 .
    CCDSi CCDS32474.1.
    PIRi I60107.
    RefSeqi NP_001596.2. NM_001605.2.
    UniGenei Hs.315137.

    3D structure databases

    ProteinModelPortali P49588.
    SMRi P49588. Positions 6-757.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106534. 42 interactions.
    IntActi P49588. 4 interactions.
    MINTi MINT-1490092.
    STRINGi 9606.ENSP00000261772.

    Chemistry

    BindingDBi P49588.
    ChEMBLi CHEMBL3574.
    DrugBanki DB00160. L-Alanine.

    PTM databases

    PhosphoSitei P49588.

    Polymorphism databases

    DMDMi 115502460.

    Proteomic databases

    MaxQBi P49588.
    PaxDbi P49588.
    PRIDEi P49588.

    Protocols and materials databases

    DNASUi 16.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261772 ; ENSP00000261772 ; ENSG00000090861 .
    GeneIDi 16.
    KEGGi hsa:16.
    UCSCi uc002eyn.1. human.

    Organism-specific databases

    CTDi 16.
    GeneCardsi GC16M070286.
    GeneReviewsi AARS.
    HGNCi HGNC:20. AARS.
    HPAi CAB034261.
    HPA040870.
    HPA044223.
    MIMi 601065. gene.
    613287. phenotype.
    neXtProti NX_P49588.
    Orphaneti 228174. Autosomal dominant Charcot-Marie-Tooth disease type 2N.
    PharmGKBi PA24367.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0013.
    HOGENOMi HOG000156964.
    HOVERGENi HBG017874.
    InParanoidi P49588.
    KOi K01872.
    OMAi YFEGDAK.
    OrthoDBi EOG7M3HZH.
    PhylomeDBi P49588.
    TreeFami TF300737.

    Enzyme and pathway databases

    Reactomei REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi AARS. human.
    GenomeRNAii 16.
    NextBioi 39.
    PROi P49588.
    SOURCEi Search...

    Gene expression databases

    Bgeei P49588.
    CleanExi HS_AARS.
    Genevestigatori P49588.

    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.
    IPR003156. DHHA1_dom.
    IPR018163. Thr/Ala-tRNA-synth_IIc_edit.
    IPR009000. Transl_B-barrel.
    IPR012947. tRNA_SAD.
    [Graphical view ]
    Pfami PF02272. DHHA1. 1 hit.
    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. "Human alanyl-tRNA synthetase: conservation in evolution of catalytic core and microhelix recognition."
      Shiba K., Ripmaster T.L., Suzuki N., Nichols R., Plotz P., Noda T., Schimmel P.
      Biochemistry 34:10340-10349(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Liver.
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Placenta.
    6. Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 1-11; 304-320 AND 684-695, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Osteosarcoma.
    7. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    8. Cited for: ISGYLATION.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "The C-Ala domain brings together editing and aminoacylation functions on one tRNA."
      Guo M., Chong Y.E., Beebe K., Shapiro R., Yang X.-L., Schimmel P.
      Science 325:744-747(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN EXCHANGE EXPERIMENTS.
    12. "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-19 AND LYS-876, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease."
      Latour P., Thauvin-Robinet C., Baudelet-Mery C., Soichot P., Cusin V., Faivre L., Locatelli M.C., Mayencon M., Sarcey A., Broussolle E., Camu W., David A., Rousson R.
      Am. J. Hum. Genet. 86:77-82(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMT2N HIS-329.
    18. "The mutational spectrum in a cohort of Charcot-Marie-Tooth disease type 2 among the Han Chinese in Taiwan."
      Lin K.P., Soong B.W., Yang C.C., Huang L.W., Chang M.H., Lee I.H., Antonellis A., Lee Y.C.
      PLoS ONE 6:E29393-E29393(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMT2N TYR-71.
    19. "A recurrent loss-of-function alanyl-tRNA synthetase (AARS) mutation in patients with Charcot-Marie-Tooth disease type 2N (CMT2N)."
      McLaughlin H.M., Sakaguchi R., Giblin W., Wilson T.E., Biesecker L., Lupski J.R., Talbot K., Vance J.M., Zuchner S., Lee Y.C., Kennerson M., Hou Y.M., Nicholson G., Antonellis A.
      Hum. Mutat. 33:244-253(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMT2N HIS-329, CHARACTERIZATION OF VARIANT CMT2N HIS-329.

    Entry informationi

    Entry nameiSYAC_HUMAN
    AccessioniPrimary (citable) accession number: P49588
    Secondary accession number(s): A6NF14, Q53GV7, Q96FA0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 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, Direct protein sequencing, Reference proteome

    Documents

    1. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    2. Human chromosome 16
      Human chromosome 16: 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