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Protein

Alanine--tRNA ligase, cytoplasmic

Gene

AARS

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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) (PubMed:27622773, PubMed:27911835, PubMed:28493438). Also edits incorrectly charged tRNA(Ala) via its editing domain (PubMed:27622773, PubMed:27911835, PubMed:28493438).UniRule annotation3 Publications

Catalytic activityi

ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala).UniRule annotation4 Publications

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)DescriptionActionsGraphical viewLength
    Binding sitei77ATPCombined sources2 Publications1
    Binding sitei95ATP; via amide nitrogen and carbonyl oxygenCombined sources2 Publications1
    Binding sitei176ATPCombined sources2 Publications1
    Binding sitei216L-alanineCombined sources2 Publications1
    Binding sitei239L-alanineCombined sources2 Publications1
    Binding sitei243ATP; via amide nitrogenCombined sources2 Publications1
    Metal bindingi605ZincUniRule annotation1
    Metal bindingi609ZincUniRule annotation1
    Metal bindingi723ZincUniRule annotation1
    Metal bindingi727ZincUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi214 – 216ATPCombined sources2 Publications3

    GO - Molecular functioni

    • alanine-tRNA ligase activity Source: UniProtKB
    • amino acid binding Source: GO_Central
    • aminoacyl-tRNA editing activity Source: UniProtKB
    • ATP binding Source: GO_Central
    • Ser-tRNA(Ala) hydrolase activity Source: UniProtKB
    • translation regulator activity Source: Ensembl
    • tRNA binding Source: GO_Central
    • zinc ion binding Source: UniProtKB-UniRule

    GO - Biological processi

    Keywordsi

    Molecular functionAminoacyl-tRNA synthetase, Ligase, RNA-binding, tRNA-binding
    Biological processProtein biosynthesis
    LigandATP-binding, Metal-binding, Nucleotide-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 annotation4 Publications)
    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

    EuPathDBiHostDB:ENSG00000090861.15
    HGNCiHGNC:20 AARS
    MIMi601065 gene
    neXtProtiNX_P49588

    Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    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.
    See also OMIM:613287
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_06708471N → Y in CMT2N. 1 PublicationCorresponds to variant dbSNP:rs387906792EnsemblClinVar.1
    Natural variantiVAR_063527329R → H in CMT2N; severely reduces enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs267606621EnsemblClinVar.1
    Epileptic encephalopathy, early infantile, 29 (EIEE29)2 Publications
    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)DescriptionActionsGraphical viewLength
    Natural variantiVAR_07371981K → T in EIEE29; hypomorphic allele; results in only 2-fold reduction in aminoacylation efficiency. 1 PublicationCorresponds to variant dbSNP:rs786205157EnsemblClinVar.1
    Natural variantiVAR_073720751R → G in EIEE29; results in 10-fold reduction in aminoacylation efficiency. 1 PublicationCorresponds to variant dbSNP:rs143370729EnsemblClinVar.1
    Natural variantiVAR_079703913G → D in EIEE29; decreases protein abundance; decreases aminoacylation activity; no effect on the editing activity. 1 PublicationCorresponds to variant dbSNP:rs369774476EnsemblClinVar.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi448A → Q: Decreases misincorporation of Cys instead of Ala. 1 Publication1
    Mutagenesisi723C → A: Decreases editing activity. 1 Publication1

    Keywords - Diseasei

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

    Organism-specific databases

    DisGeNETi16
    GeneReviewsiAARS
    MalaCardsiAARS
    MIMi613287 phenotype
    616339 phenotype
    OpenTargetsiENSG00000090861
    Orphaneti228174 Autosomal dominant Charcot-Marie-Tooth disease type 2N
    442835 Undetermined early-onset epileptic encephalopathy
    PharmGKBiPA24367

    Chemistry databases

    ChEMBLiCHEMBL3574
    DrugBankiDB00160 L-Alanine

    Polymorphism and mutation databases

    BioMutaiAARS
    DMDMi115502460

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000752811 – 968Alanine--tRNA ligase, cytoplasmicAdd BLAST968

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei1N-acetylmethionineUniRule annotationCombined sources1 Publication1
    Modified residuei3PhosphoserineCombined sources1
    Modified residuei8PhosphoserineCombined sources1
    Modified residuei19N6-acetyllysineCombined sources1
    Modified residuei399PhosphoserineCombined sources1
    Modified residuei555PhosphoserineCombined sources1
    Modified residuei876N6-acetyllysineCombined sources1

    Post-translational modificationi

    ISGylated.UniRule annotation1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    EPDiP49588
    MaxQBiP49588
    PaxDbiP49588
    PeptideAtlasiP49588
    PRIDEiP49588
    ProteomicsDBi56022

    PTM databases

    iPTMnetiP49588
    PhosphoSitePlusiP49588
    SwissPalmiP49588

    Expressioni

    Gene expression databases

    BgeeiENSG00000090861 Expressed in 239 organ(s), highest expression level in frontal cortex
    CleanExiHS_AARS
    ExpressionAtlasiP49588 baseline and differential
    GenevisibleiP49588 HS

    Organism-specific databases

    HPAiCAB034261
    HPA040870
    HPA044223

    Interactioni

    Subunit structurei

    Monomer (PubMed:27911835). Interacts with ANKRD16; the interaction is direct (By similarity).UniRule annotation1 Publication

    Protein-protein interaction databases

    BioGridi106534, 57 interactors
    IntActiP49588, 8 interactors
    MINTiP49588
    STRINGi9606.ENSP00000261772

    Chemistry databases

    BindingDBiP49588

    Structurei

    Secondary structure

    1968
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    ProteinModelPortaliP49588
    SMRiP49588
    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) is not required for catalytic activity and can bind DNA (in vitro) (PubMed:27911835). 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 (PubMed:19661429).2 Publications

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiKOG0188 Eukaryota
    COG0013 LUCA
    GeneTreeiENSGT00390000016019
    HOGENOMiHOG000156964
    HOVERGENiHBG017874
    InParanoidiP49588
    KOiK01872
    OMAiFEMMAHH
    OrthoDBiEOG091G00Z9
    PhylomeDBiP49588
    TreeFamiTF300737

    Family and domain databases

    HAMAPiMF_00036_B Ala_tRNA_synth_B, 1 hit
    InterProiView protein in InterPro
    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_sf
    IPR012947 tRNA_SAD
    PfamiView protein in Pfam
    PF02272 DHHA1, 1 hit
    PF01411 tRNA-synt_2c, 1 hit
    PF07973 tRNA_SAD, 1 hit
    PRINTSiPR00980 TRNASYNTHALA
    SMARTiView protein in SMART
    SM00863 tRNA_SAD, 1 hit
    SUPFAMiSSF101353 SSF101353, 1 hit
    SSF50447 SSF50447, 1 hit
    SSF55186 SSF55186, 1 hit
    TIGRFAMsiTIGR00344 alaS, 1 hit
    PROSITEiView protein in PROSITE
    PS50860 AA_TRNA_LIGASE_II_ALA, 1 hit

    Sequences (2+)i

    Sequence statusi: Complete.

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

    This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

    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

    Computationally mapped potential isoform sequencesi

    There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    H3BPK7H3BPK7_HUMAN
    Alanine--tRNA ligase, cytoplasmic
    AARS
    280Annotation score:

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti82H → Q in BAA06808 (PubMed:7654687).Curated1
    Sequence conflicti334Y → C in BAG61157 (PubMed:14702039).Curated1
    Sequence conflicti763A → T in BAG61157 (PubMed:14702039).Curated1
    Sequence conflicti867S → T in BAD96544 (Ref. 3) Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_06708471N → Y in CMT2N. 1 PublicationCorresponds to variant dbSNP:rs387906792EnsemblClinVar.1
    Natural variantiVAR_07371981K → T in EIEE29; hypomorphic allele; results in only 2-fold reduction in aminoacylation efficiency. 1 PublicationCorresponds to variant dbSNP:rs786205157EnsemblClinVar.1
    Natural variantiVAR_028204275G → D. Corresponds to variant dbSNP:rs11537667EnsemblClinVar.1
    Natural variantiVAR_063527329R → H in CMT2N; severely reduces enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs267606621EnsemblClinVar.1
    Natural variantiVAR_073293608T → M Found in a patient with distal hereditary motor neuropathy; unknown pathological significance. 1 Publication1
    Natural variantiVAR_073720751R → G in EIEE29; results in 10-fold reduction in aminoacylation efficiency. 1 PublicationCorresponds to variant dbSNP:rs143370729EnsemblClinVar.1
    Natural variantiVAR_079703913G → D in EIEE29; decreases protein abundance; decreases aminoacylation activity; no effect on the editing activity. 1 PublicationCorresponds to variant dbSNP:rs369774476EnsemblClinVar.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_057201160G → GTYLYSFVR in isoform 2. 1 Publication1
    Alternative sequenceiVSP_057202869K → KATQGPGSPPLGLISSL in isoform 2. 1 Publication1

    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

    Similar proteinsi

    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
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    4XEMX-ray1.28A1-455[»]
    4XEOX-ray1.38A/B1-455[»]
    5KNNX-ray2.68A/B/C/D/E/F/G/H4-453[»]
    5T5SX-ray2.20A757-965[»]
    5T76X-ray2.00A757-965[»]
    5V59X-ray2.03A1-455[»]
    ProteinModelPortaliP49588
    SMRiP49588
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi106534, 57 interactors
    IntActiP49588, 8 interactors
    MINTiP49588
    STRINGi9606.ENSP00000261772

    Chemistry databases

    BindingDBiP49588
    ChEMBLiCHEMBL3574
    DrugBankiDB00160 L-Alanine

    PTM databases

    iPTMnetiP49588
    PhosphoSitePlusiP49588
    SwissPalmiP49588

    Polymorphism and mutation databases

    BioMutaiAARS
    DMDMi115502460

    Proteomic databases

    EPDiP49588
    MaxQBiP49588
    PaxDbiP49588
    PeptideAtlasiP49588
    PRIDEiP49588
    ProteomicsDBi56022

    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
    DisGeNETi16
    EuPathDBiHostDB:ENSG00000090861.15
    GeneCardsiAARS
    GeneReviewsiAARS
    HGNCiHGNC:20 AARS
    HPAiCAB034261
    HPA040870
    HPA044223
    MalaCardsiAARS
    MIMi601065 gene
    613287 phenotype
    616339 phenotype
    neXtProtiNX_P49588
    OpenTargetsiENSG00000090861
    Orphaneti228174 Autosomal dominant Charcot-Marie-Tooth disease type 2N
    442835 Undetermined early-onset epileptic encephalopathy
    PharmGKBiPA24367
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0188 Eukaryota
    COG0013 LUCA
    GeneTreeiENSGT00390000016019
    HOGENOMiHOG000156964
    HOVERGENiHBG017874
    InParanoidiP49588
    KOiK01872
    OMAiFEMMAHH
    OrthoDBiEOG091G00Z9
    PhylomeDBiP49588
    TreeFamiTF300737

    Enzyme and pathway databases

    ReactomeiR-HSA-379716 Cytosolic tRNA aminoacylation

    Miscellaneous databases

    ChiTaRSiAARS human
    GenomeRNAii16
    PROiPR:P49588
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000090861 Expressed in 239 organ(s), highest expression level in frontal cortex
    CleanExiHS_AARS
    ExpressionAtlasiP49588 baseline and differential
    GenevisibleiP49588 HS

    Family and domain databases

    HAMAPiMF_00036_B Ala_tRNA_synth_B, 1 hit
    InterProiView protein in InterPro
    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_sf
    IPR012947 tRNA_SAD
    PfamiView protein in Pfam
    PF02272 DHHA1, 1 hit
    PF01411 tRNA-synt_2c, 1 hit
    PF07973 tRNA_SAD, 1 hit
    PRINTSiPR00980 TRNASYNTHALA
    SMARTiView protein in SMART
    SM00863 tRNA_SAD, 1 hit
    SUPFAMiSSF101353 SSF101353, 1 hit
    SSF50447 SSF50447, 1 hit
    SSF55186 SSF55186, 1 hit
    TIGRFAMsiTIGR00344 alaS, 1 hit
    PROSITEiView protein in PROSITE
    PS50860 AA_TRNA_LIGASE_II_ALA, 1 hit
    ProtoNetiSearch...

    Entry informationi

    Entry nameiSYAC_HUMAN
    AccessioniPrimary (citable) accession number: P49588
    Secondary accession number(s): A6NF14
    , B4DR45, Q53GV7, Q96FA0
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: October 3, 2006
    Last modified: November 7, 2018
    This is version 179 of the entry and version 2 of the sequence. See 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. SIMILARITY comments
      Index of protein domains and families
    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. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
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