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Protein

Glycine--tRNA ligase

Gene

GARS

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

Functioni

Catalyzes the attachment of glycine to tRNA(Gly). Is also able produce diadenosine tetraphosphate (Ap4A), a universal pleiotropic signaling molecule needed for cell regulation pathways, by direct condensation of 2 ATPs.2 Publications

Catalytic activityi

ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly).1 Publication
P1,P(4)-bis(5'-guanosyl) tetraphosphate + H2O = GTP + GMP.1 Publication

Kineticsi

  1. KM=1.3 µM for tRNA(Gly(GCC))1 Publication
  2. KM=15 µM for glycine1 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
    • protein dimerization activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Hydrolase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciZFISH:HS02863-MONOMER.
    BRENDAi6.1.1.14. 2681.
    ReactomeiR-HSA-379716. Cytosolic tRNA aminoacylation.
    R-HSA-379726. Mitochondrial tRNA aminoacylation.

    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

    HGNCiHGNC:4162. GARS.

    Subcellular locationi

    GO - Cellular componenti

    • axon Source: UniProtKB
    • cytoplasm Source: HPA
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • mitochondrial matrix Source: Reactome
    • nucleoplasm Source: HPA
    • secretory granule Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Charcot-Marie-Tooth disease 2D (CMT2D)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    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. 1 PublicationCorresponds to variant rs370531212dbSNPEnsembl.1
    Natural variantiVAR_018718125E → G in CMT2D; phenotype overlapping with DSMA-V; complements the defect of the wild-type gene in yeast. 3 PublicationsCorresponds to variant rs28936972dbSNPEnsembl.1
    Natural variantiVAR_073188200D → N in CMT2D; shows a large reduction in aminoacylation activity. 1 Publication1
    Natural variantiVAR_074016200D → Y in CMT2D. 1 Publication1
    Natural variantiVAR_073189265S → F in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in the subcellular location pattern; does not associate with granules. 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. 3 PublicationsCorresponds to variant rs137852643dbSNPEnsembl.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. 1 PublicationCorresponds to variant rs137852648dbSNPEnsembl.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. 1 Publication1
    Natural variantiVAR_073193554D → N in CMT2D; demonstrates no change in subcellular location pattern. 1 PublicationCorresponds to variant rs137852647dbSNPEnsembl.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. 1 Publication1
    Neuronopathy, distal hereditary motor, 5A (HMN5A)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    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. 3 PublicationsCorresponds to variant rs137852644dbSNPEnsembl.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 rs28937323dbSNPEnsembl.1

    Keywords - Diseasei

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

    Organism-specific databases

    DisGeNETi2617.
    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.

    PTM databases

    iPTMnetiP41250.
    PhosphoSitePlusiP41250.
    SwissPalmiP41250.

    Miscellaneous databases

    PMAP-CutDBP41250.

    Expressioni

    Tissue specificityi

    Widely expressed, including 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

    GO - Molecular functioni

    • protein dimerization activity Source: UniProtKB

    Protein-protein interaction databases

    BioGridi108887. 89 interactors.
    DIPiDIP-50471N.
    IntActiP41250. 19 interactors.
    MINTiMINT-1395438.
    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

    Contains 1 WHEP-TRS domain.PROSITE-ProRule annotation

    Phylogenomic databases

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

    Family and domain databases

    CDDicd00774. GlyRS-like_core. 1 hit.
    Gene3Di1.10.287.10. 1 hit.
    3.40.50.800. 1 hit.
    InterProiIPR002314. aa-tRNA-synt_IIb.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR027031. Gly-tRNA_synthase/POLG2.
    IPR033731. GlyRS-like_core.
    IPR009068. S15_NS1_RNA-bd.
    IPR002315. tRNA-synt_gly.
    IPR000738. WHEP-TRS_dom.
    [Graphical view]
    PANTHERiPTHR10745. PTHR10745. 1 hit.
    PfamiPF03129. HGTP_anticodon. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    PF00458. WHEP-TRS. 1 hit.
    [Graphical view]
    PRINTSiPR01043. TRNASYNTHGLY.
    SMARTiSM00991. WHEP-TRS. 1 hit.
    [Graphical view]
    SUPFAMiSSF47060. SSF47060. 1 hit.
    SSF52954. SSF52954. 1 hit.
    TIGRFAMsiTIGR00389. glyS_dimeric. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    PS00762. WHEP_TRS_1. 1 hit.
    PS51185. WHEP_TRS_2. 1 hit.
    [Graphical view]

    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 → A.Combined sources5 PublicationsCorresponds to variant rs1049402dbSNPEnsembl.1
    Natural variantiVAR_073187111A → V in CMT2D; shows a reduction in aminoacylation activity. 1 PublicationCorresponds to variant rs370531212dbSNPEnsembl.1
    Natural variantiVAR_018718125E → G in CMT2D; phenotype overlapping with DSMA-V; complements the defect of the wild-type gene in yeast. 3 PublicationsCorresponds to variant rs28936972dbSNPEnsembl.1
    Natural variantiVAR_018719183L → P in HMN5A; does not complement the defect of the wild-type gene in yeast. 3 PublicationsCorresponds to variant rs137852644dbSNPEnsembl.1
    Natural variantiVAR_073188200D → N in CMT2D; shows a large reduction in aminoacylation activity. 1 Publication1
    Natural variantiVAR_074016200D → Y in CMT2D. 1 Publication1
    Natural variantiVAR_073189265S → F in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in the subcellular location pattern; does not associate with granules. 1 Publication1
    Natural variantiVAR_054866268T → I.Corresponds to variant rs2230310dbSNPEnsembl.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. 3 PublicationsCorresponds to variant rs137852643dbSNPEnsembl.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. 1 PublicationCorresponds to variant rs137852648dbSNPEnsembl.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. 1 Publication1
    Natural variantiVAR_054867388R → Q.Corresponds to variant rs17159287dbSNPEnsembl.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 rs137852647dbSNPEnsembl.1
    Natural variantiVAR_018721580G → R in HMN5A; higher dimerization stability; loss of activity; shows a large reduction in aminoacylation activity. 4 PublicationsCorresponds to variant rs28937323dbSNPEnsembl.1
    Natural variantiVAR_073194635S → L Polymorphism; has no effect on subcellular localization; results in reduced activity. 2 PublicationsCorresponds to variant rs201358272dbSNPEnsembl.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. 1 Publication1

    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.

    Cross-referencesi

    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.
    UniGeneiHs.404321.

    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...

    Protein-protein interaction databases

    BioGridi108887. 89 interactors.
    DIPiDIP-50471N.
    IntActiP41250. 19 interactors.
    MINTiMINT-1395438.
    STRINGi9606.ENSP00000373918.

    Chemistry databases

    DrugBankiDB00145. Glycine.

    PTM databases

    iPTMnetiP41250.
    PhosphoSitePlusiP41250.
    SwissPalmiP41250.

    Polymorphism and mutation databases

    BioMutaiGARS.
    DMDMi313104283.

    Proteomic databases

    EPDiP41250.
    MaxQBiP41250.
    PaxDbiP41250.
    PeptideAtlasiP41250.
    PRIDEiP41250.

    Protocols and materials databases

    DNASUi2617.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi2617.
    DisGeNETi2617.
    GeneCardsiGARS.
    GeneReviewsiGARS.
    H-InvDBHIX0006570.
    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.
    GenAtlasiSearch...

    Phylogenomic databases

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

    Enzyme and pathway databases

    BioCyciZFISH:HS02863-MONOMER.
    BRENDAi6.1.1.14. 2681.
    ReactomeiR-HSA-379716. Cytosolic tRNA aminoacylation.
    R-HSA-379726. Mitochondrial tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSiGARS. human.
    EvolutionaryTraceiP41250.
    GeneWikiiGlycine%E2%80%94tRNA_ligase.
    GenomeRNAii2617.
    PMAP-CutDBP41250.
    PROiP41250.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000106105.
    CleanExiHS_GARS.
    ExpressionAtlasiP41250. baseline and differential.
    GenevisibleiP41250. HS.

    Family and domain databases

    CDDicd00774. GlyRS-like_core. 1 hit.
    Gene3Di1.10.287.10. 1 hit.
    3.40.50.800. 1 hit.
    InterProiIPR002314. aa-tRNA-synt_IIb.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR027031. Gly-tRNA_synthase/POLG2.
    IPR033731. GlyRS-like_core.
    IPR009068. S15_NS1_RNA-bd.
    IPR002315. tRNA-synt_gly.
    IPR000738. WHEP-TRS_dom.
    [Graphical view]
    PANTHERiPTHR10745. PTHR10745. 1 hit.
    PfamiPF03129. HGTP_anticodon. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    PF00458. WHEP-TRS. 1 hit.
    [Graphical view]
    PRINTSiPR01043. TRNASYNTHGLY.
    SMARTiSM00991. WHEP-TRS. 1 hit.
    [Graphical view]
    SUPFAMiSSF47060. SSF47060. 1 hit.
    SSF52954. SSF52954. 1 hit.
    TIGRFAMsiTIGR00389. glyS_dimeric. 1 hit.
    PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
    PS00762. WHEP_TRS_1. 1 hit.
    PS51185. WHEP_TRS_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiSYG_HUMAN
    AccessioniPrimary (citable) accession number: P41250
    Secondary accession number(s): B3KQA2, B4DIA0, Q969Y1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1995
    Last sequence update: November 30, 2010
    Last modified: November 2, 2016
    This is version 176 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    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

    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

    Similar proteinsi

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