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Entry version 187 (18 Sep 2019)
Sequence version 2 (03 Oct 2006)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi605ZincUniRule annotation1
    Metal bindingi609ZincUniRule annotation1
    Metal bindingi723ZincUniRule annotation1
    Metal bindingi727ZincUniRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi214 – 216ATPCombined sources2 Publications3

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionAminoacyl-tRNA synthetase, Ligase, RNA-binding, tRNA-binding
    Biological processProtein biosynthesis
    LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-379716 Cytosolic tRNA aminoacylation

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:AARSUniRule annotation
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 16

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:20 AARS

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    601065 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P49588

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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.
    Related information in OMIM
    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
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

    DisGeNET

    More...
    DisGeNETi
    16

    GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

    More...
    GeneReviewsi
    AARS

    MalaCards human disease database

    More...
    MalaCardsi
    AARS
    MIMi613287 phenotype
    616339 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000090861

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    228174 Autosomal dominant Charcot-Marie-Tooth disease type 2N
    442835 Undetermined early-onset epileptic encephalopathy

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA24367

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL3574

    Drug and drug target database

    More...
    DrugBanki
    DB00160 L-Alanine

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    AARS

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    115502460

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000752811 – 968Alanine--tRNA ligase, cytoplasmicAdd BLAST968

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>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

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    ISGylated.UniRule annotation1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    The CPTAC Assay portal

    More...
    CPTACi
    CPTAC-1
    CPTAC-2

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P49588

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P49588

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    P49588

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P49588

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P49588

    PeptideAtlas

    More...
    PeptideAtlasi
    P49588

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P49588

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    56022 [P49588-1]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P49588

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    P49588

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P49588

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000090861 Expressed in 239 organ(s), highest expression level in frontal cortex

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P49588 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P49588 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB034261
    HPA040870
    HPA044223

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Monomer (PubMed:27911835).

    Interacts with ANKRD16; the interaction is direct (By similarity).

    UniRule annotation1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    106534, 65 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P49588, 15 interactors

    Molecular INTeraction database

    More...
    MINTi
    P49588

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000261772

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P49588

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

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

    3D structure databases

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P49588

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0188 Eukaryota
    COG0013 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000157335

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000156964

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P49588

    KEGG Orthology (KO)

    More...
    KOi
    K01872

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    YHHTMFE

    Database of Orthologous Groups

    More...
    OrthoDBi
    129373at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P49588

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF300737

    Family and domain databases

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00036_B Ala_tRNA_synth_B, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View 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

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF02272 DHHA1, 1 hit
    PF01411 tRNA-synt_2c, 1 hit
    PF07973 tRNA_SAD, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR00980 TRNASYNTHALA

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00863 tRNA_SAD, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF101353 SSF101353, 1 hit
    SSF50447 SSF50447, 1 hit
    SSF55186 SSF55186, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00344 alaS, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50860 AA_TRNA_LIGASE_II_ALA, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> 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 <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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            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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>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:

    Annotation score:2 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_057201160G → GTYLYSFVR in isoform 2. 1 Publication1
    Alternative sequenceiVSP_057202869K → KATQGPGSPPLGLISSL in isoform 2. 1 Publication1

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS32474.1 [P49588-1]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    I60107

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001596.2, NM_001605.2 [P49588-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000261772; ENSP00000261772; ENSG00000090861 [P49588-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    16

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:16

    UCSC genome browser

    More...
    UCSCi
    uc002eyn.2 human [P49588-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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]

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    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[»]
    SMRiP49588
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi106534, 65 interactors
    IntActiP49588, 15 interactors
    MINTiP49588
    STRINGi9606.ENSP00000261772

    Chemistry databases

    BindingDBiP49588
    ChEMBLiCHEMBL3574
    DrugBankiDB00160 L-Alanine

    PTM databases

    iPTMnetiP49588
    PhosphoSitePlusiP49588
    SwissPalmiP49588

    Polymorphism and mutation databases

    BioMutaiAARS
    DMDMi115502460

    Proteomic databases

    CPTACiCPTAC-1
    CPTAC-2
    EPDiP49588
    jPOSTiP49588
    MassIVEiP49588
    MaxQBiP49588
    PaxDbiP49588
    PeptideAtlasiP49588
    PRIDEiP49588
    ProteomicsDBi56022 [P49588-1]

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    16
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    16
    DisGeNETi16

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    AARS
    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

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0188 Eukaryota
    COG0013 LUCA
    GeneTreeiENSGT00940000157335
    HOGENOMiHOG000156964
    InParanoidiP49588
    KOiK01872
    OMAiYHHTMFE
    OrthoDBi129373at2759
    PhylomeDBiP49588
    TreeFamiTF300737

    Enzyme and pathway databases

    ReactomeiR-HSA-379716 Cytosolic tRNA aminoacylation

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    AARS human

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    16

    Pharos

    More...
    Pharosi
    P49588

    Protein Ontology

    More...
    PROi
    PR:P49588

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000090861 Expressed in 239 organ(s), highest expression level in frontal cortex
    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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiSYAC_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P49588
    Secondary accession number(s): A6NF14
    , B4DR45, Q53GV7, Q96FA0
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: October 3, 2006
    Last modified: September 18, 2019
    This is version 187 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    4. Aminoacyl-tRNA synthetases
      List of aminoacyl-tRNA synthetase entries
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
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