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Entry version 205 (16 Oct 2019)
Sequence version 3 (30 Nov 2010)
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Protein

Glycine--tRNA ligase

Gene

GARS

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 ATP-dependent ligation of glycine to the 3'-end of its cognate tRNA, via the formation of an aminoacyl-adenylate intermediate (Gly-AMP) (PubMed:17544401, PubMed:28675565, PubMed:24898252). Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs. Thereby, may play a special role in Ap4A homeostasis (PubMed:19710017).4 Publications

Miscellaneous

Human GlyRS uses direct ATP condensation to synthesize Ap4A, a unique amino acid-independent mechanism, in contrast to the classical amino acid-dependent mechanism for synthesis of Ap4A by a tRNA synthetase, that involves the generation of an enzyme-bound aminoacyl-AMP which is then attacked by ATP to form Ap4A.1 Publication

Caution

According to a report, variant Leu-635 induces reduced activity (PubMed:17544401). According to another report, it does not affect function (PubMed:25168514).2 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 <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Ap4A synthesis is inhibited by tRNA, via the disruption of the second ATP-binding site by direct blocking and/or by tRNA-induced conformational change.1 Publication

<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 0.049 sec(-1) for aminoacylation of tRNA(Gly).1 Publication
  1. KM=1.3 µM for tRNA(Gly(GCC))1 Publication
  2. KM=15 µM for glycine1 Publication
  3. KM=0.74 µM for tRNA(Gly)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 sitei299GlycineCombined sources1 Publication2 Publications1
    Binding sitei350GlycineCombined sources1 Publication2 Publications1
    Binding sitei583ATPCombined sources1 Publication1

    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 bindingi331 – 333ATPCombined sources2 Publications1 Publication3
    Nucleotide bindingi342 – 343ATPCombined sources1 Publication2
    Nucleotide bindingi457 – 458ATPCombined sources2 Publications1 Publication2

    <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, Hydrolase, Ligase, Transferase
    Biological processProtein biosynthesis
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    6.1.1.14 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-379716 Cytosolic tRNA aminoacylation
    R-HSA-379726 Mitochondrial tRNA aminoacylation

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P41250

    Protein family/group databases

    MoonProt database of moonlighting proteins

    More...
    MoonProti
    P41250

    <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:
    Glycine--tRNA ligase (EC:6.1.1.143 Publications)
    Alternative name(s):
    Diadenosine tetraphosphate synthetase1 Publication (EC:2.7.7.-1 Publication)
    Short name:
    Ap4A synthetase1 Publication
    Glycyl-tRNA synthetase1 Publication
    Short name:
    GlyRS1 Publication
    <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:GARS
    <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 7

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:4162 GARS

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    600287 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P41250

    <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

    Cell projection, Cytoplasm, Secreted

    <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 2D (CMT2D)9 Publications
    The disease is caused by mutations affecting the gene represented in this entry. Contrary to the wild-type protein, CMT2D variants Gly-125 and Arg-294 strongly interact with NRP1. This interaction may compete out VEGFA binding and inhibits VEGFA-NRP1 signling which is essential for motor neuron survival, as suggested by experiments done in a mouse model.1 Publication
    Disease descriptionA dominant 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_073187111A → V in CMT2D; shows a reduction in aminoacylation activity. 2 PublicationsCorresponds to variant dbSNP:rs370531212Ensembl.1
    Natural variantiVAR_018718125E → G in CMT2D; phenotype overlapping with DSMA-V; complements the defect of the wild-type gene in yeast; contrary to the wild-type protein, strongly binds to NRP1 and competes with VEGFA for NRP1-binding; displays slightly elevated aminoacylation activity over wild-type. 5 PublicationsCorresponds to variant dbSNP:rs137852645EnsemblClinVar.1
    Natural variantiVAR_073188200D → N in CMT2D and HMN5A; shows a large reduction in aminoacylation activity. 2 Publications1
    Natural variantiVAR_074016200D → Y in CMT2D. 1 Publication1
    Natural variantiVAR_073189265S → F in CMT2D and HMN5A; shows a large reduction in aminoacylation activity; demonstrates a change in the subcellular location pattern; does not associate with granules. 2 PublicationsCorresponds to variant dbSNP:rs1554337974EnsemblClinVar.1
    Natural variantiVAR_074017292M → R in CMT2D. 1 Publication1
    Natural variantiVAR_018720294G → R in CMT2D; shows a large reduction in aminoacylation activity; does not impair transcription or translation or protein stability; contrary to the wild-type protein, strongly interacts with NRP1. 4 PublicationsCorresponds to variant dbSNP:rs137852643EnsemblClinVar.1
    Natural variantiVAR_073190298P → L in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules. 2 PublicationsCorresponds to variant dbSNP:rs137852648EnsemblClinVar.1
    Natural variantiVAR_073191334I → F in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules; unknown pathological significance. 3 PublicationsCorresponds to variant dbSNP:rs1554338260EnsemblClinVar.1
    Natural variantiVAR_073193554D → N in CMT2D; demonstrates no change in subcellular location pattern. 1 PublicationCorresponds to variant dbSNP:rs137852647EnsemblClinVar.1
    Natural variantiVAR_073195652G → A in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules. 2 Publications1
    Neuronopathy, distal hereditary motor, 5A (HMN5A)5 Publications
    The disease is caused by mutations affecting the gene represented in this entry. Contrary to the wild-type protein, HMN5A variant Pro-183 strongly interacts with NRP1. This interaction may compete out VEGFA binding and inhibits VEGFA-NRP1 signling which is essential for motor neuron survival, as suggested by experiments done in a mouse model.1 Publication
    Disease descriptionA disorder characterized by distal muscular atrophy mainly affecting the upper extremities, in contrast to other distal motor neuronopathies. These constitute a heterogeneous group of neuromuscular diseases caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_018719183L → P in HMN5A; does not complement the defect of the wild-type gene in yeast; contrary to the wild-type protein, strongly interacts with NRP1. 4 PublicationsCorresponds to variant dbSNP:rs137852644EnsemblClinVar.1
    Natural variantiVAR_073188200D → N in CMT2D and HMN5A; shows a large reduction in aminoacylation activity. 2 Publications1
    Natural variantiVAR_073189265S → F in CMT2D and HMN5A; shows a large reduction in aminoacylation activity; demonstrates a change in the subcellular location pattern; does not associate with granules. 2 PublicationsCorresponds to variant dbSNP:rs1554337974EnsemblClinVar.1
    Natural variantiVAR_073192472H → R in HMN5A; shows a large reduction in aminoacylation activity; does not complement the defect of the wild-type gene in yeast. 3 PublicationsCorresponds to variant dbSNP:rs1060502838EnsemblClinVar.1
    Natural variantiVAR_018721580G → R in HMN5A; higher dimerization stability; loss of activity; shows a large reduction in aminoacylation activity. 4 PublicationsCorresponds to variant dbSNP:rs137852646EnsemblClinVar.1
    Natural variantiVAR_079829598G → A in HMN5A; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs766280100Ensembl.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>Mutagenesisi121R → A: Decrease in catalytic activity by about 10-fold. 1 Publication1
    Mutagenesisi211C → R: Displays 62% of wild-type catalytic activity. Displays 20% of wild-type catalytic activity; when associated with G-125. 1 Publication1
    Mutagenesisi337R → A: Decrease in catalytic activity by more than 10-fold. 1 Publication1
    Mutagenesisi486 – 490Missing : Loss of catalytic activity. 1 Publication5
    Mutagenesisi602R → A: Decrease in catalytic activity by more than 10-fold. 1 Publication1
    Mutagenesisi658Y → F: Decrease in catalytic activity by more than 10-fold. 1 Publication1
    Mutagenesisi729Q → A or N: Decrease in catalytic activity by about 10-fold. 1 Publication1

    Keywords - Diseasei

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

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    2617

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

    More...
    GeneReviewsi
    GARS

    MalaCards human disease database

    More...
    MalaCardsi
    GARS
    MIMi600794 phenotype
    601472 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000106105

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

    More...
    Orphaneti
    99938 Autosomal dominant Charcot-Marie-Tooth disease type 2D
    139536 Distal hereditary motor neuropathy type 5

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA28575

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    P41250

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL4105815

    Drug and drug target database

    More...
    DrugBanki
    DB00145 Glycine

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    GARS

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    313104283

    <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_00000729981 – 739Glycine--tRNA ligaseAdd BLAST739

    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 residuei35PhosphoserineCombined sources1
    Modified residuei204N6-acetyllysineCombined sources1
    Modified residuei453PhosphotyrosineBy similarity1
    Modified residuei501N6-acetyllysineCombined sources1
    Modified residuei700PhosphoserineBy similarity1
    Modified residuei736PhosphothreonineCombined sources1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P41250

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P41250

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    P41250

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P41250

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

    More...
    PaxDbi
    P41250

    PeptideAtlas

    More...
    PeptideAtlasi
    P41250

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P41250

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    55453

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P41250

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

    More...
    PhosphoSitePlusi
    P41250

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P41250

    Miscellaneous databases

    CutDB - Proteolytic event database

    More...
    PMAP-CutDBi
    P41250

    <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

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Widely expressed, including in brain and spinal cord.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000106105 Expressed in 237 organ(s), highest expression level in secondary oocyte

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P41250 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P41250 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA017896
    HPA019097

    <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

    Homodimer.

    2 Publications2 Publications

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    108887, 113 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-50471N

    Protein interaction database and analysis system

    More...
    IntActi
    P41250, 28 interactors

    Molecular INTeraction database

    More...
    MINTi
    P41250

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000373918

    <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

    1739
    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
    P41250

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Protein Data Bank in Europe - Knowledge Base

    More...
    PDBe-KBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P41250

    <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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini63 – 119WHEP-TRSPROSITE-ProRule annotationAdd BLAST57

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni576 – 578Glycine bindingCombined sources2 Publications3

    <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

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG2298 Eukaryota
    COG0423 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000153759

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000242015

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P41250

    KEGG Orthology (KO)

    More...
    KOi
    K01880

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    YDYGQNG

    Database of Orthologous Groups

    More...
    OrthoDBi
    1183820at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P41250

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF343504

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00774 GlyRS-like_core, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.800, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR002314 aa-tRNA-synt_IIb
    IPR006195 aa-tRNA-synth_II
    IPR004154 Anticodon-bd
    IPR036621 Anticodon-bd_dom_sf
    IPR027031 Gly-tRNA_synthase/POLG2
    IPR033731 GlyRS-like_core
    IPR009068 S15_NS1_RNA-bd
    IPR002315 tRNA-synt_gly
    IPR000738 WHEP-TRS_dom

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR10745 PTHR10745, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF03129 HGTP_anticodon, 1 hit
    PF00587 tRNA-synt_2b, 1 hit
    PF00458 WHEP-TRS, 1 hit

    Protein Motif fingerprint database; a protein domain database

    More...
    PRINTSi
    PR01043 TRNASYNTHGLY

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00991 WHEP-TRS, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF47060 SSF47060, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00389 glyS_dimeric, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50862 AA_TRNA_LIGASE_II, 1 hit
    PS00762 WHEP_TRS_1, 1 hit
    PS51185 WHEP_TRS_2, 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>Sequence (1+)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 has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

    P41250-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPSPRPVLLR GARAALLLLL PPRLLARPSL LLRRSLSAAS CPPISLPAAA
    60 70 80 90 100
    SRSSMDGAGA EEVLAPLRLA VRQQGDLVRK LKEDKAPQVD VDKAVAELKA
    110 120 130 140 150
    RKRVLEAKEL ALQPKDDIVD RAKMEDTLKR RFFYDQAFAI YGGVSGLYDF
    160 170 180 190 200
    GPVGCALKNN IIQTWRQHFI QEEQILEIDC TMLTPEPVLK TSGHVDKFAD
    210 220 230 240 250
    FMVKDVKNGE CFRADHLLKA HLQKLMSDKK CSVEKKSEME SVLAQLDNYG
    260 270 280 290 300
    QQELADLFVN YNVKSPITGN DLSPPVSFNL MFKTFIGPGG NMPGYLRPET
    310 320 330 340 350
    AQGIFLNFKR LLEFNQGKLP FAAAQIGNSF RNEISPRSGL IRVREFTMAE
    360 370 380 390 400
    IEHFVDPSEK DHPKFQNVAD LHLYLYSAKA QVSGQSARKM RLGDAVEQGV
    410 420 430 440 450
    INNTVLGYFI GRIYLYLTKV GISPDKLRFR QHMENEMAHY ACDCWDAESK
    460 470 480 490 500
    TSYGWIEIVG CADRSCYDLS CHARATKVPL VAEKPLKEPK TVNVVQFEPS
    510 520 530 540 550
    KGAIGKAYKK DAKLVMEYLA ICDECYITEM EMLLNEKGEF TIETEGKTFQ
    560 570 580 590 600
    LTKDMINVKR FQKTLYVEEV VPNVIEPSFG LGRIMYTVFE HTFHVREGDE
    610 620 630 640 650
    QRTFFSFPAV VAPFKCSVLP LSQNQEFMPF VKELSEALTR HGVSHKVDDS
    660 670 680 690 700
    SGSIGRRYAR TDEIGVAFGV TIDFDTVNKT PHTATLRDRD SMRQIRAEIS
    710 720 730
    ELPSIVQDLA NGNITWADVE ARYPLFEGQE TGKKETIEE
    Length:739
    Mass (Da):83,166
    Last modified:November 30, 2010 - v3
    <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:iE4C001CEBF985C59
    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 are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    F8WCK4F8WCK4_HUMAN
    Glycine--tRNA ligase
    GARS
    79Annotation score:

    Annotation score:1 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>
    H7C443H7C443_HUMAN
    Glycine--tRNA ligase
    GARS
    77Annotation score:

    Annotation score:1 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>

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAA57001 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
    The sequence AAA86443 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

    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 conflicti9 – 18Missing in BAG58412 (PubMed:14702039).Curated10
    Sequence conflicti205D → G in BAG51964 (PubMed:14702039).Curated1
    Sequence conflicti530M → I in AAA86443 (PubMed:7753621).Curated1
    Sequence conflicti634L → S in BAG51964 (PubMed:14702039).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_05486542P → ACombined sources5 PublicationsCorresponds to variant dbSNP:rs1049402EnsemblClinVar.1
    Natural variantiVAR_073187111A → V in CMT2D; shows a reduction in aminoacylation activity. 2 PublicationsCorresponds to variant dbSNP:rs370531212Ensembl.1
    Natural variantiVAR_018718125E → G in CMT2D; phenotype overlapping with DSMA-V; complements the defect of the wild-type gene in yeast; contrary to the wild-type protein, strongly binds to NRP1 and competes with VEGFA for NRP1-binding; displays slightly elevated aminoacylation activity over wild-type. 5 PublicationsCorresponds to variant dbSNP:rs137852645EnsemblClinVar.1
    Natural variantiVAR_018719183L → P in HMN5A; does not complement the defect of the wild-type gene in yeast; contrary to the wild-type protein, strongly interacts with NRP1. 4 PublicationsCorresponds to variant dbSNP:rs137852644EnsemblClinVar.1
    Natural variantiVAR_073188200D → N in CMT2D and HMN5A; shows a large reduction in aminoacylation activity. 2 Publications1
    Natural variantiVAR_074016200D → Y in CMT2D. 1 Publication1
    Natural variantiVAR_073189265S → F in CMT2D and HMN5A; shows a large reduction in aminoacylation activity; demonstrates a change in the subcellular location pattern; does not associate with granules. 2 PublicationsCorresponds to variant dbSNP:rs1554337974EnsemblClinVar.1
    Natural variantiVAR_054866268T → I Found in a patient with mild left ventricular posterior wall hypertrophy, exercise intolerance and lactic acidosis; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs2230310EnsemblClinVar.1
    Natural variantiVAR_074017292M → R in CMT2D. 1 Publication1
    Natural variantiVAR_018720294G → R in CMT2D; shows a large reduction in aminoacylation activity; does not impair transcription or translation or protein stability; contrary to the wild-type protein, strongly interacts with NRP1. 4 PublicationsCorresponds to variant dbSNP:rs137852643EnsemblClinVar.1
    Natural variantiVAR_073190298P → L in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules. 2 PublicationsCorresponds to variant dbSNP:rs137852648EnsemblClinVar.1
    Natural variantiVAR_079827310R → Q Probable disease-associated mutation found in a patient with growth retardation, microcephaly, thinning of the corpus callosum, decreased white matter and brain stem involvement, as well as large calvaria, cerebellar vermis atrophy, dysmorphic features, prominent epicanthal folds, hypotelorism, high-arched palate, delayed motor milestones, apnea and sparse thin scalp hair; reduces to less than 1% aminoacylation activity. 1 PublicationCorresponds to variant dbSNP:rs1135401748EnsemblClinVar.1
    Natural variantiVAR_073191334I → F in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules; unknown pathological significance. 3 PublicationsCorresponds to variant dbSNP:rs1554338260EnsemblClinVar.1
    Natural variantiVAR_054867388R → Q. Corresponds to variant dbSNP:rs17159287EnsemblClinVar.1
    Natural variantiVAR_079828412R → C Found in a patient with mild left ventricular posterior wall hypertrophy, exercise intolerance and lactic acidosis; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs770924455EnsemblClinVar.1
    Natural variantiVAR_073192472H → R in HMN5A; shows a large reduction in aminoacylation activity; does not complement the defect of the wild-type gene in yeast. 3 PublicationsCorresponds to variant dbSNP:rs1060502838EnsemblClinVar.1
    Natural variantiVAR_073193554D → N in CMT2D; demonstrates no change in subcellular location pattern. 1 PublicationCorresponds to variant dbSNP:rs137852647EnsemblClinVar.1
    Natural variantiVAR_018721580G → R in HMN5A; higher dimerization stability; loss of activity; shows a large reduction in aminoacylation activity. 4 PublicationsCorresponds to variant dbSNP:rs137852646EnsemblClinVar.1
    Natural variantiVAR_079829598G → A in HMN5A; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs766280100Ensembl.1
    Natural variantiVAR_073194635S → L Polymorphism; has no effect on subcellular localization; results in reduced activity. 3 PublicationsCorresponds to variant dbSNP:rs201358272EnsemblClinVar.1
    Natural variantiVAR_073195652G → A in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules. 2 Publications1

    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
    D30658 mRNA Translation: BAA06338.1
    U09510 mRNA Translation: AAA86443.1 Different initiation.
    AK074524 mRNA Translation: BAG51964.1
    AK295490 mRNA Translation: BAG58412.1
    AC005154 Genomic DNA No translation available.
    AC006969 Genomic DNA No translation available.
    AC004976 Genomic DNA Translation: AAC71652.1
    BC007722 mRNA Translation: AAH07722.1
    BC007755 mRNA Translation: AAH07755.1
    U09587 mRNA Translation: AAA57001.1 Different initiation.

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS43564.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A55314

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_001303701.1, NM_001316772.1
    NP_002038.2, NM_002047.3

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000389266; ENSP00000373918; ENSG00000106105

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    2617

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:2617

    UCSC genome browser

    More...
    UCSCi
    uc003tbm.4 human

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Inherited peripheral neuropathies mutation db

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D30658 mRNA Translation: BAA06338.1
    U09510 mRNA Translation: AAA86443.1 Different initiation.
    AK074524 mRNA Translation: BAG51964.1
    AK295490 mRNA Translation: BAG58412.1
    AC005154 Genomic DNA No translation available.
    AC006969 Genomic DNA No translation available.
    AC004976 Genomic DNA Translation: AAC71652.1
    BC007722 mRNA Translation: AAH07722.1
    BC007755 mRNA Translation: AAH07755.1
    U09587 mRNA Translation: AAA57001.1 Different initiation.
    CCDSiCCDS43564.1
    PIRiA55314
    RefSeqiNP_001303701.1, NM_001316772.1
    NP_002038.2, NM_002047.3

    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
    2PMEX-ray2.90A55-739[»]
    2PMFX-ray2.85A55-739[»]
    2Q5HX-ray3.00A55-739[»]
    2Q5IX-ray2.80A55-739[»]
    2ZT5X-ray2.50A55-739[»]
    2ZT6X-ray3.08A55-739[»]
    2ZT7X-ray2.70A55-739[»]
    2ZT8X-ray3.35A55-739[»]
    2ZXFX-ray3.40A55-739[»]
    4KQEX-ray2.74A55-739[»]
    4KR2X-ray3.29A114-739[»]
    4KR3X-ray3.24A114-739[»]
    4QEIX-ray2.88A118-739[»]
    5E6MX-ray2.93A/B55-739[»]
    SMRiP41250
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGridi108887, 113 interactors
    DIPiDIP-50471N
    IntActiP41250, 28 interactors
    MINTiP41250
    STRINGi9606.ENSP00000373918

    Chemistry databases

    ChEMBLiCHEMBL4105815
    DrugBankiDB00145 Glycine

    Protein family/group databases

    MoonProtiP41250

    PTM databases

    iPTMnetiP41250
    PhosphoSitePlusiP41250
    SwissPalmiP41250

    Polymorphism and mutation databases

    BioMutaiGARS
    DMDMi313104283

    Proteomic databases

    EPDiP41250
    jPOSTiP41250
    MassIVEiP41250
    MaxQBiP41250
    PaxDbiP41250
    PeptideAtlasiP41250
    PRIDEiP41250
    ProteomicsDBi55453

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    2617

    Genome annotation databases

    EnsembliENST00000389266; ENSP00000373918; ENSG00000106105
    GeneIDi2617
    KEGGihsa:2617
    UCSCiuc003tbm.4 human

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    2617
    DisGeNETi2617

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    GARS
    GeneReviewsiGARS
    HGNCiHGNC:4162 GARS
    HPAiHPA017896
    HPA019097
    MalaCardsiGARS
    MIMi600287 gene
    600794 phenotype
    601472 phenotype
    neXtProtiNX_P41250
    OpenTargetsiENSG00000106105
    Orphaneti99938 Autosomal dominant Charcot-Marie-Tooth disease type 2D
    139536 Distal hereditary motor neuropathy type 5
    PharmGKBiPA28575

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG2298 Eukaryota
    COG0423 LUCA
    GeneTreeiENSGT00940000153759
    HOGENOMiHOG000242015
    InParanoidiP41250
    KOiK01880
    OMAiYDYGQNG
    OrthoDBi1183820at2759
    PhylomeDBiP41250
    TreeFamiTF343504

    Enzyme and pathway databases

    BRENDAi6.1.1.14 2681
    ReactomeiR-HSA-379716 Cytosolic tRNA aminoacylation
    R-HSA-379726 Mitochondrial tRNA aminoacylation
    SABIO-RKiP41250

    Miscellaneous databases

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

    More...
    ChiTaRSi
    GARS human
    EvolutionaryTraceiP41250

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    Glycine%E2%80%94tRNA_ligase

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

    More...
    GenomeRNAii
    2617
    PharosiP41250
    PMAP-CutDBiP41250

    Protein Ontology

    More...
    PROi
    PR:P41250

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000106105 Expressed in 237 organ(s), highest expression level in secondary oocyte
    ExpressionAtlasiP41250 baseline and differential
    GenevisibleiP41250 HS

    Family and domain databases

    CDDicd00774 GlyRS-like_core, 1 hit
    Gene3Di3.40.50.800, 1 hit
    InterProiView protein in InterPro
    IPR002314 aa-tRNA-synt_IIb
    IPR006195 aa-tRNA-synth_II
    IPR004154 Anticodon-bd
    IPR036621 Anticodon-bd_dom_sf
    IPR027031 Gly-tRNA_synthase/POLG2
    IPR033731 GlyRS-like_core
    IPR009068 S15_NS1_RNA-bd
    IPR002315 tRNA-synt_gly
    IPR000738 WHEP-TRS_dom
    PANTHERiPTHR10745 PTHR10745, 1 hit
    PfamiView protein in Pfam
    PF03129 HGTP_anticodon, 1 hit
    PF00587 tRNA-synt_2b, 1 hit
    PF00458 WHEP-TRS, 1 hit
    PRINTSiPR01043 TRNASYNTHGLY
    SMARTiView protein in SMART
    SM00991 WHEP-TRS, 1 hit
    SUPFAMiSSF47060 SSF47060, 1 hit
    TIGRFAMsiTIGR00389 glyS_dimeric, 1 hit
    PROSITEiView protein in PROSITE
    PS50862 AA_TRNA_LIGASE_II, 1 hit
    PS00762 WHEP_TRS_1, 1 hit
    PS51185 WHEP_TRS_2, 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 nameiGARS_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: P41250
    Secondary accession number(s): B3KQA2, B4DIA0, Q969Y1
    <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, 1995
    Last sequence update: November 30, 2010
    Last modified: October 16, 2019
    This is version 205 of the entry and version 3 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, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    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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