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Protein

Glycine--tRNA ligase

Gene

GARS

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

Functioni

Catalyzes the ligation of glycine to the 3'-end of its cognate tRNA. Also produces diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs.3 Publications

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

Catalytic activityi

ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly).2 Publications
P1,P4-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP.1 Publication

Kineticsi

Kcat is 0.049 (sec-1) for aminoacylation for 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
    Binding sitei213Substrate1 Publication1
    Binding sitei299Substrate1 Publication1
    Binding sitei435Substrate; via carbonyl oxygen1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi331 – 333ATP1 Publication3
    Nucleotide bindingi341 – 346ATP1 Publication6
    Nucleotide bindingi457 – 458ATP1 Publication2
    Nucleotide bindingi580 – 583ATP1 Publication4

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity Source: UniProtKB
    • glycine-tRNA ligase activity Source: UniProtKB
    • identical protein binding Source: IntAct
    • protein dimerization activity Source: UniProtKB

    GO - Biological processi

    • diadenosine tetraphosphate biosynthetic process Source: UniProtKB
    • mitochondrial glycyl-tRNA aminoacylation Source: GO_Central
    • tRNA aminoacylation for protein translation Source: UniProtKB

    Keywordsi

    Molecular functionAminoacyl-tRNA synthetase, Hydrolase, Ligase
    Biological processProtein biosynthesis
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

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

    Protein family/group databases

    MoonProtiP41250

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycine--tRNA ligase (EC:3.6.1.171 Publication, EC:6.1.1.141 Publication)
    Alternative name(s):
    Diadenosine tetraphosphate synthetase
    Short name:
    AP-4-A synthetase
    Glycyl-tRNA synthetase
    Short name:
    GlyRS
    Gene namesi
    Name:GARS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 7

    Organism-specific databases

    EuPathDBiHostDB:ENSG00000106105.13
    HGNCiHGNC:4162 GARS
    MIMi600287 gene
    neXtProtiNX_P41250

    Subcellular locationi

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

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Secreted

    Pathology & Biotechi

    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. Nerve conduction velocities are normal or slightly reduced.
    See also OMIM:601472
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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. 4 PublicationsCorresponds to variant dbSNP:rs137852645EnsemblClinVar.1
    Natural variantiVAR_074016200D → Y in CMT2D. 1 Publication1
    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 Publications1
    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.
    See also OMIM:600794
    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_073192472H → R in HMN5A; shows a large reduction in aminoacylation activity; does not complement the defect of the wild-type gene in yeast. 3 Publications1
    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

    Keywords - Diseasei

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

    Organism-specific databases

    DisGeNETi2617
    GeneReviewsiGARS
    MalaCardsiGARS
    MIMi600794 phenotype
    601472 phenotype
    OpenTargetsiENSG00000106105
    Orphaneti99938 Autosomal dominant Charcot-Marie-Tooth disease type 2D
    139536 Distal hereditary motor neuropathy type 5
    PharmGKBiPA28575

    Chemistry databases

    DrugBankiDB00145 Glycine

    Polymorphism and mutation databases

    BioMutaiGARS
    DMDMi313104283

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000729981 – 739Glycine--tRNA ligaseAdd BLAST739

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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

    EPDiP41250
    MaxQBiP41250
    PaxDbiP41250
    PeptideAtlasiP41250
    PRIDEiP41250
    ProteomicsDBi55453

    PTM databases

    iPTMnetiP41250
    PhosphoSitePlusiP41250
    SwissPalmiP41250

    Miscellaneous databases

    PMAP-CutDBiP41250

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiENSG00000106105
    CleanExiHS_GARS
    ExpressionAtlasiP41250 baseline and differential
    GenevisibleiP41250 HS

    Organism-specific databases

    HPAiHPA017896
    HPA019097

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Binary interactionsi

    Show more details

    GO - Molecular functioni

    • identical protein binding Source: IntAct
    • protein dimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi108887, 91 interactors
    DIPiDIP-50471N
    IntActiP41250, 21 interactors
    MINTiP41250
    STRINGi9606.ENSP00000373918

    Structurei

    Secondary structure

    1739
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni62 – 64Combined sources3
    Helixi65 – 80Combined sources16
    Turni81 – 83Combined sources3
    Helixi95 – 112Combined sources18
    Helixi121 – 130Combined sources10
    Beta strandi133 – 136Combined sources4
    Helixi139 – 141Combined sources3
    Beta strandi148 – 150Combined sources3
    Helixi152 – 168Combined sources17
    Helixi170 – 173Combined sources4
    Beta strandi182 – 185Combined sources4
    Helixi186 – 191Combined sources6
    Helixi194 – 197Combined sources4
    Beta strandi199 – 208Combined sources10
    Beta strandi211 – 213Combined sources3
    Helixi214 – 227Combined sources14
    Beta strandi229 – 231Combined sources3
    Helixi233 – 243Combined sources11
    Turni244 – 248Combined sources5
    Helixi251 – 260Combined sources10
    Beta strandi266 – 268Combined sources3
    Beta strandi276 – 279Combined sources4
    Beta strandi283 – 285Combined sources3
    Beta strandi287 – 296Combined sources10
    Beta strandi298 – 300Combined sources3
    Helixi301 – 305Combined sources5
    Helixi308 – 314Combined sources7
    Turni315 – 317Combined sources3
    Beta strandi321 – 330Combined sources10
    Helixi339 – 341Combined sources3
    Beta strandi344 – 355Combined sources12
    Helixi357 – 359Combined sources3
    Helixi365 – 367Combined sources3
    Turni368 – 370Combined sources3
    Beta strandi372 – 376Combined sources5
    Helixi378 – 382Combined sources5
    Beta strandi388 – 391Combined sources4
    Helixi392 – 397Combined sources6
    Beta strandi400 – 402Combined sources3
    Helixi404 – 420Combined sources17
    Helixi424 – 426Combined sources3
    Beta strandi427 – 431Combined sources5
    Helixi434 – 436Combined sources3
    Beta strandi442 – 451Combined sources10
    Beta strandi454 – 462Combined sources9
    Helixi467 – 476Combined sources10
    Beta strandi482 – 484Combined sources3
    Helixi501 – 507Combined sources7
    Helixi512 – 519Combined sources8
    Helixi524 – 535Combined sources12
    Beta strandi541 – 544Combined sources4
    Beta strandi547 – 550Combined sources4
    Beta strandi552 – 554Combined sources3
    Beta strandi562 – 564Combined sources3
    Turni565 – 567Combined sources3
    Beta strandi568 – 570Combined sources3
    Beta strandi573 – 580Combined sources8
    Helixi581 – 592Combined sources12
    Beta strandi593 – 595Combined sources3
    Beta strandi597 – 600Combined sources4
    Beta strandi603 – 605Combined sources3
    Turni609 – 611Combined sources3
    Beta strandi615 – 621Combined sources7
    Turni625 – 627Combined sources3
    Helixi628 – 640Combined sources13
    Beta strandi645 – 647Combined sources3
    Beta strandi650 – 652Combined sources3
    Helixi654 – 663Combined sources10
    Beta strandi668 – 672Combined sources5
    Helixi674 – 677Combined sources4
    Beta strandi679 – 681Combined sources3
    Beta strandi683 – 688Combined sources6
    Turni689 – 691Combined sources3
    Beta strandi694 – 698Combined sources5
    Turni699 – 701Combined sources3
    Helixi702 – 710Combined sources9
    Beta strandi712 – 714Combined sources3
    Helixi716 – 722Combined sources7

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    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[»]
    ProteinModelPortaliP41250
    SMRiP41250
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP41250

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini63 – 119WHEP-TRSPROSITE-ProRule annotationAdd BLAST57

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni346 – 350Substrate binding5
    Regioni576 – 580Substrate binding5

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG2298 Eukaryota
    COG0423 LUCA
    GeneTreeiENSGT00390000016949
    HOGENOMiHOG000242015
    HOVERGENiHBG036190
    InParanoidiP41250
    KOiK01880
    OMAiEPSYGID
    OrthoDBiEOG091G02U0
    PhylomeDBiP41250
    TreeFamiTF343504

    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

    Sequencei

    Sequence statusi: Complete.

    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
    Checksum:iE4C001CEBF985C59
    GO

    Sequence cautioni

    The sequence AAA57001 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAA86443 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    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. 4 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 Publications1
    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 Publication1
    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 Publications1
    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:rs770924455Ensembl.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 Publications1
    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:
    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
    UniGeneiHs.404321

    Genome annotation databases

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

    Similar proteinsi

    Entry informationi

    Entry nameiGARS_HUMAN
    AccessioniPrimary (citable) accession number: P41250
    Secondary accession number(s): B3KQA2, B4DIA0, Q969Y1
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: November 30, 2010
    Last modified: June 20, 2018
    This is version 192 of the entry and version 3 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

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