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Protein

Alanine--tRNA ligase, cytoplasmic

Gene

AARS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 annotation1 Publication

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion per subunit.UniRule annotation

Kineticsi

kcat is 0.4 sec(-1).1 Publication

  1. KM=3.1 µM for tRNA(Ala) (at 37 Celsius)1 Publication

    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

    GO - Biological processi

    Complete GO annotation...

    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

    ReactomeiR-HSA-379716. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alanine--tRNA ligase, cytoplasmicUniRule annotation (EC:6.1.1.7UniRule annotation1 Publication)
    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
    Proteomesi
    • UP000005640 Componenti: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:20. AARS.

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • cytosol Source: GO_Central
    • extracellular exosome Source: UniProtKB
    • membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Charcot-Marie-Tooth disease 2N (CMT2N)3 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn 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.
    See also OMIM:613287
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711N → Y in CMT2N. 1 Publication
    Corresponds to variant rs387906792 [ dbSNP | Ensembl ].
    VAR_067084
    Natural varianti329 – 3291R → H in CMT2N; severely reduces enzyme activity. 2 Publications
    Corresponds to variant rs267606621 [ dbSNP | Ensembl ].
    VAR_063527
    Epileptic encephalopathy, early infantile, 29 (EIEE29)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. EIEE29 patients manifest severe infantile epileptic encephalopathy, clubfoot, absent deep tendon reflexes, extrapyramidal symptoms, and persistently deficient myelination.
    See also OMIM:616339
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti81 – 811K → T in EIEE29; hypomorphic allele; results in only 2-fold reduction in aminoacylation efficiency. 1 Publication
    Corresponds to variant rs786205157 [ dbSNP | Ensembl ].
    VAR_073719
    Natural varianti751 – 7511R → G in EIEE29; results in 10-fold reduction in aminoacylation efficiency. 1 Publication
    Corresponds to variant rs143370729 [ dbSNP | Ensembl ].
    VAR_073720

    Keywords - Diseasei

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

    Organism-specific databases

    MalaCardsiAARS.
    MIMi613287. phenotype.
    616339. phenotype.
    Orphaneti228174. Autosomal dominant Charcot-Marie-Tooth disease type 2N.
    PharmGKBiPA24367.

    Chemistry

    ChEMBLiCHEMBL3574.
    DrugBankiDB00160. L-Alanine.

    Polymorphism and mutation databases

    BioMutaiAARS.
    DMDMi115502460.

    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-acetylmethionineUniRule annotationCombined sources1 Publication
    Modified residuei3 – 31PhosphoserineCombined sources
    Modified residuei8 – 81PhosphoserineCombined sources
    Modified residuei19 – 191N6-acetyllysineCombined sources
    Modified residuei399 – 3991PhosphoserineCombined sources
    Modified residuei555 – 5551PhosphoserineCombined sources
    Modified residuei876 – 8761N6-acetyllysineCombined sources

    Post-translational modificationi

    ISGylated.UniRule annotation1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    EPDiP49588.
    MaxQBiP49588.
    PaxDbiP49588.
    PeptideAtlasiP49588.
    PRIDEiP49588.

    PTM databases

    iPTMnetiP49588.
    PhosphoSiteiP49588.
    SwissPalmiP49588.

    Expressioni

    Gene expression databases

    BgeeiP49588.
    CleanExiHS_AARS.
    ExpressionAtlasiP49588. baseline and differential.
    GenevisibleiP49588. HS.

    Organism-specific databases

    HPAiCAB034261.
    HPA040870.
    HPA044223.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi106534. 52 interactions.
    IntActiP49588. 6 interactions.
    MINTiMINT-1490092.
    STRINGi9606.ENSP00000261772.

    Chemistry

    BindingDBiP49588.

    Structurei

    Secondary structure

    1
    968
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 2014Combined sources
    Helixi45 – 495Combined sources
    Helixi50 – 534Combined sources
    Helixi62 – 654Combined sources
    Beta strandi68 – 769Combined sources
    Beta strandi78 – 814Combined sources
    Helixi85 – 873Combined sources
    Beta strandi90 – 934Combined sources
    Beta strandi96 – 10914Combined sources
    Helixi111 – 12313Combined sources
    Helixi130 – 1323Combined sources
    Beta strandi133 – 1386Combined sources
    Helixi142 – 1443Combined sources
    Helixi150 – 1589Combined sources
    Helixi163 – 1653Combined sources
    Beta strandi166 – 1694Combined sources
    Helixi171 – 1744Combined sources
    Beta strandi178 – 19518Combined sources
    Helixi201 – 2033Combined sources
    Turni204 – 2074Combined sources
    Beta strandi211 – 22414Combined sources
    Beta strandi230 – 24314Combined sources
    Helixi244 – 2518Combined sources
    Helixi257 – 2593Combined sources
    Turni261 – 2633Combined sources
    Helixi264 – 27411Combined sources
    Helixi284 – 2863Combined sources
    Helixi291 – 31020Combined sources
    Helixi319 – 33921Combined sources
    Turni343 – 3453Combined sources
    Helixi346 – 3494Combined sources
    Helixi350 – 3578Combined sources
    Turni358 – 3603Combined sources
    Helixi362 – 3654Combined sources
    Helixi368 – 38316Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4XEMX-ray1.28A1-455[»]
    4XEOX-ray1.38A/B1-455[»]
    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

    eggNOGiKOG0188. Eukaryota.
    COG0013. LUCA.
    GeneTreeiENSGT00390000016019.
    HOGENOMiHOG000156964.
    HOVERGENiHBG017874.
    InParanoidiP49588.
    KOiK01872.
    OMAiFDFNCPR.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P49588-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MDSTLTASEI RQRFIDFFKR NEHTYVHSSA TIPLDDPTLL FANAGMNQFK
    60 70 80 90 100
    PIFLNTIDPS HPMAKLSRAA NTQKCIRAGG KHNDLDDVGK DVYHHTFFEM
    110 120 130 140 150
    LGSWSFGDYF KELACKMALE LLTQEFGIPI ERLYVTYFGG DEAAGLEADL
    160 170 180 190 200
    ECKQIWQNLG LDDTKILPGN MKDNFWEMGD TGPCGPCSEI HYDRIGGRDA
    210 220 230 240 250
    AHLVNQDDPN VLEIWNLVFI QYNREADGIL KPLPKKSIDT GMGLERLVSV
    260 270 280 290 300
    LQNKMSNYDT DLFVPYFEAI QKGTGARPYT GKVGAEDADG IDMAYRVLAD
    310 320 330 340 350
    HARTITVALA DGGRPDNTGR GYVLRRILRR AVRYAHEKLN ASRGFFATLV
    360 370 380 390 400
    DVVVQSLGDA FPELKKDPDM VKDIINEEEV QFLKTLSRGR RILDRKIQSL
    410 420 430 440 450
    GDSKTIPGDT AWLLYDTYGF PVDLTGLIAE EKGLVVDMDG FEEERKLAQL
    460 470 480 490 500
    KSQGKGAGGE DLIMLDIYAI EELRARGLEV TDDSPKYNYH LDSSGSYVFE
    510 520 530 540 550
    NTVATVMALR REKMFVEEVS TGQECGVVLD KTCFYAEQGG QIYDEGYLVK
    560 570 580 590 600
    VDDSSEDKTE FTVKNAQVRG GYVLHIGTIY GDLKVGDQVW LFIDEPRRRP
    610 620 630 640 650
    IMSNHTATHI LNFALRSVLG EADQKGSLVA PDRLRFDFTA KGAMSTQQIK
    660 670 680 690 700
    KAEEIANEMI EAAKAVYTQD CPLAAAKAIQ GLRAVFDETY PDPVRVVSIG
    710 720 730 740 750
    VPVSELLDDP SGPAGSLTSV EFCGGTHLRN SSHAGAFVIV TEEAIAKGIR
    760 770 780 790 800
    RIVAVTGAEA QKALRKAESL KKCLSVMEAK VKAQTAPNKD VQREIADLGE
    810 820 830 840 850
    ALATAVIPQW QKDELRETLK SLKKVMDDLD RASKADVQKR VLEKTKQFID
    860 870 880 890 900
    SNPNQPLVIL EMESGASAKA LNEALKLFKM HSPQTSAMLF TVDNEAGKIT
    910 920 930 940 950
    CLCQVPQNAA NRGLKASEWV QQVSGLMDGK GGGKDVSAQA TGKNVGCLQE
    960
    ALQLATSFAQ LRLGDVKN
    Length:968
    Mass (Da):106,810
    Last modified:October 3, 2006 - v2
    Checksum:i8683F111CEE42506
    GO
    Isoform 2 (identifier: P49588-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         160-160: G → GTYLYSFVR
         869-869: K → KATQGPGSPPLGLISSL

    Note: No experimental confirmation available.
    Show »
    Length:992
    Mass (Da):109,317
    Checksum:i35B75F8D8FFBA3CD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti82 – 821H → Q in BAA06808 (PubMed:7654687).Curated
    Sequence conflicti334 – 3341Y → C in BAG61157 (PubMed:14702039).Curated
    Sequence conflicti763 – 7631A → T in BAG61157 (PubMed:14702039).Curated
    Sequence conflicti867 – 8671S → T in BAD96544 (Ref. 3) Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti71 – 711N → Y in CMT2N. 1 Publication
    Corresponds to variant rs387906792 [ dbSNP | Ensembl ].
    VAR_067084
    Natural varianti81 – 811K → T in EIEE29; hypomorphic allele; results in only 2-fold reduction in aminoacylation efficiency. 1 Publication
    Corresponds to variant rs786205157 [ dbSNP | Ensembl ].
    VAR_073719
    Natural varianti275 – 2751G → D.
    Corresponds to variant rs11537667 [ dbSNP | Ensembl ].
    VAR_028204
    Natural varianti329 – 3291R → H in CMT2N; severely reduces enzyme activity. 2 Publications
    Corresponds to variant rs267606621 [ dbSNP | Ensembl ].
    VAR_063527
    Natural varianti608 – 6081T → M Found in a patient with distal hereditary motor neuropathy; unknown pathological significance. 1 Publication
    VAR_073293
    Natural varianti751 – 7511R → G in EIEE29; results in 10-fold reduction in aminoacylation efficiency. 1 Publication
    Corresponds to variant rs143370729 [ dbSNP | Ensembl ].
    VAR_073720

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei160 – 1601G → GTYLYSFVR in isoform 2. 1 PublicationVSP_057201
    Alternative sequencei869 – 8691K → KATQGPGSPPLGLISSL in isoform 2. 1 PublicationVSP_057202

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D32050 mRNA. Translation: BAA06808.1.
    AK299098 mRNA. Translation: BAG61157.1.
    AK222824 mRNA. Translation: BAD96544.1.
    AC012184 Genomic DNA. No translation available.
    CH471241 Genomic DNA. Translation: EAW51839.1.
    BC011451 mRNA. Translation: AAH11451.1.
    CCDSiCCDS32474.1. [P49588-1]
    PIRiI60107.
    RefSeqiNP_001596.2. NM_001605.2. [P49588-1]
    UniGeneiHs.315137.

    Genome annotation databases

    EnsembliENST00000261772; ENSP00000261772; ENSG00000090861. [P49588-1]
    GeneIDi16.
    KEGGihsa:16.
    UCSCiuc002eyn.2. human. [P49588-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D32050 mRNA. Translation: BAA06808.1.
    AK299098 mRNA. Translation: BAG61157.1.
    AK222824 mRNA. Translation: BAD96544.1.
    AC012184 Genomic DNA. No translation available.
    CH471241 Genomic DNA. Translation: EAW51839.1.
    BC011451 mRNA. Translation: AAH11451.1.
    CCDSiCCDS32474.1. [P49588-1]
    PIRiI60107.
    RefSeqiNP_001596.2. NM_001605.2. [P49588-1]
    UniGeneiHs.315137.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4XEMX-ray1.28A1-455[»]
    4XEOX-ray1.38A/B1-455[»]
    ProteinModelPortaliP49588.
    SMRiP49588. Positions 6-757.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi106534. 52 interactions.
    IntActiP49588. 6 interactions.
    MINTiMINT-1490092.
    STRINGi9606.ENSP00000261772.

    Chemistry

    BindingDBiP49588.
    ChEMBLiCHEMBL3574.
    DrugBankiDB00160. L-Alanine.

    PTM databases

    iPTMnetiP49588.
    PhosphoSiteiP49588.
    SwissPalmiP49588.

    Polymorphism and mutation databases

    BioMutaiAARS.
    DMDMi115502460.

    Proteomic databases

    EPDiP49588.
    MaxQBiP49588.
    PaxDbiP49588.
    PeptideAtlasiP49588.
    PRIDEiP49588.

    Protocols and materials databases

    DNASUi16.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000261772; ENSP00000261772; ENSG00000090861. [P49588-1]
    GeneIDi16.
    KEGGihsa:16.
    UCSCiuc002eyn.2. human. [P49588-1]

    Organism-specific databases

    CTDi16.
    GeneCardsiAARS.
    GeneReviewsiAARS.
    HGNCiHGNC:20. AARS.
    HPAiCAB034261.
    HPA040870.
    HPA044223.
    MalaCardsiAARS.
    MIMi601065. gene.
    613287. phenotype.
    616339. phenotype.
    neXtProtiNX_P49588.
    Orphaneti228174. Autosomal dominant Charcot-Marie-Tooth disease type 2N.
    PharmGKBiPA24367.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0188. Eukaryota.
    COG0013. LUCA.
    GeneTreeiENSGT00390000016019.
    HOGENOMiHOG000156964.
    HOVERGENiHBG017874.
    InParanoidiP49588.
    KOiK01872.
    OMAiFDFNCPR.
    OrthoDBiEOG7M3HZH.
    PhylomeDBiP49588.
    TreeFamiTF300737.

    Enzyme and pathway databases

    ReactomeiR-HSA-379716. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSiAARS. human.
    GenomeRNAii16.
    PROiP49588.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP49588.
    CleanExiHS_AARS.
    ExpressionAtlasiP49588. baseline and differential.
    GenevisibleiP49588. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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] (ISOFORM 1).
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    3. 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] (ISOFORM 1).
      Tissue: Liver.
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Placenta.
    7. 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.
    8. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    9. Cited for: ISGYLATION.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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].
    12. "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.
    13. "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].
    14. "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.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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].
    17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
      Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
      J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-8 AND SER-555, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma and Erythroleukemia.
    19. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    20. "Loss-of-function alanyl-tRNA synthetase mutations cause an autosomal-recessive early-onset epileptic encephalopathy with persistent myelination defect."
      Simons C., Griffin L.B., Helman G., Golas G., Pizzino A., Bloom M., Murphy J.L., Crawford J., Evans S.H., Topper S., Whitehead M.T., Schreiber J.M., Chapman K.A., Tifft C., Lu K.B., Gamper H., Shigematsu M., Taft R.J.
      , Antonellis A., Hou Y.M., Vanderver A.
      Am. J. Hum. Genet. 96:675-681(2015) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, INVOLVEMENT IN EIEE29, VARIANTS EIEE29 THR-81 AND GLY-751, CHARACTERIZATION OF VARIANTS EIEE29 THR-81 AND GLY-751, CATALYTIC ACTIVITY.
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "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.
    23. "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.
    24. "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.
    25. Cited for: VARIANT MET-608.

    Entry informationi

    Entry nameiSYAC_HUMAN
    AccessioniPrimary (citable) accession number: P49588
    Secondary accession number(s): A6NF14
    , B4DR45, Q53GV7, Q96FA0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: October 3, 2006
    Last modified: July 6, 2016
    This is version 156 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

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.