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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

Kineticsi

  1. KM=1.3 µM for tRNA(Gly(GCC))1 Publication
  2. KM=15 µM for glycine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei213 – 2131Substrate1 Publication
    Binding sitei299 – 2991Substrate1 Publication
    Binding sitei435 – 4351Substrate; via carbonyl oxygen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi331 – 3333ATP1 Publication
    Nucleotide bindingi341 – 3466ATP1 Publication
    Nucleotide bindingi457 – 4582ATP1 Publication
    Nucleotide bindingi580 – 5834ATP1 Publication

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • glycine-tRNA ligase activity Source: UniProtKB
    • protein dimerization activity Source: UniProtKB

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Aminoacyl-tRNA synthetase, Ligase

    Keywords - Biological processi

    Protein biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi6.1.1.14. 2681.
    ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.
    REACT_15306. Cytosolic tRNA aminoacylation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycine--tRNA ligase (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
    ProteomesiUP000005640 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)1 Publication

    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti111 – 1111A → V in CMT2D; shows a reduction in aminoacylation activity. 1 Publication
    VAR_073187
    Natural varianti125 – 1251E → G in CMT2D; phenotype overlapping with DSMA-V; complements the defect of the wild-type gene in yeast. 3 Publications
    Corresponds to variant rs28936972 [ dbSNP | Ensembl ].
    VAR_018718
    Natural varianti200 – 2001D → N in CMT2D; shows a large reduction in aminoacylation activity. 1 Publication
    VAR_073188
    Natural varianti265 – 2651S → F in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in the subcellular location pattern; does not associate with granules. 1 Publication
    VAR_073189
    Natural varianti294 – 2941G → R in CMT2D; shows a large reduction in aminoacylation activity; does not impair transcription or translation or protein stability. 3 Publications
    VAR_018720
    Natural varianti298 – 2981P → L in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules. 1 Publication
    VAR_073190
    Natural varianti334 – 3341I → F in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules. 1 Publication
    VAR_073191
    Natural varianti554 – 5541D → N in CMT2D; demonstrates no change in subcellular location pattern. 1 Publication
    VAR_073193
    Natural varianti652 – 6521G → A in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules. 1 Publication
    VAR_073195
    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti183 – 1831L → P in HMN5A; does not complement the defect of the wild-type gene in yeast. 3 Publications
    VAR_018719
    Natural varianti472 – 4721H → R in HMN5A; shows a large reduction in aminoacylation activity; does not complement the defect of the wild-type gene in yeast. 3 Publications
    VAR_073192
    Natural varianti580 – 5801G → R in HMN5A; higher dimerization stability; loss of activity; shows a large reduction in aminoacylation activity. 4 Publications
    Corresponds to variant rs28937323 [ dbSNP | Ensembl ].
    VAR_018721

    Keywords - Diseasei

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

    Organism-specific databases

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

    Chemistry

    DrugBankiDB00145. Glycine.

    Polymorphism and mutation databases

    BioMutaiGARS.
    DMDMi313104283.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 739739Glycine--tRNA ligasePRO_0000072998Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei204 – 2041N6-acetyllysine1 Publication
    Modified residuei453 – 4531PhosphotyrosineBy similarity
    Modified residuei501 – 5011N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP41250.
    PaxDbiP41250.
    PRIDEiP41250.

    PTM databases

    PhosphoSiteiP41250.

    Miscellaneous databases

    PMAP-CutDBP41250.

    Expressioni

    Tissue specificityi

    Widely expressed, including brain and spinal cord.1 Publication

    Gene expression databases

    BgeeiP41250.
    CleanExiHS_GARS.
    ExpressionAtlasiP41250. baseline and differential.
    GenevisibleiP41250. HS.

    Organism-specific databases

    HPAiHPA017896.
    HPA019097.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    BioGridi108887. 56 interactions.
    DIPiDIP-50471N.
    IntActiP41250. 7 interactions.
    MINTiMINT-1395438.
    STRINGi9606.ENSP00000373918.

    Structurei

    Secondary structure

    1
    739
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi121 – 13010Combined sources
    Beta strandi133 – 1364Combined sources
    Helixi139 – 1413Combined sources
    Beta strandi148 – 1503Combined sources
    Helixi152 – 16817Combined sources
    Helixi170 – 1734Combined sources
    Beta strandi182 – 1854Combined sources
    Helixi186 – 1916Combined sources
    Helixi194 – 1974Combined sources
    Beta strandi199 – 20810Combined sources
    Beta strandi211 – 2133Combined sources
    Helixi214 – 22714Combined sources
    Beta strandi229 – 2313Combined sources
    Helixi233 – 24311Combined sources
    Turni244 – 2485Combined sources
    Helixi251 – 26010Combined sources
    Beta strandi266 – 2683Combined sources
    Beta strandi276 – 2794Combined sources
    Beta strandi283 – 2853Combined sources
    Beta strandi287 – 29610Combined sources
    Beta strandi298 – 3003Combined sources
    Helixi301 – 3055Combined sources
    Helixi308 – 3147Combined sources
    Turni315 – 3173Combined sources
    Beta strandi321 – 33010Combined sources
    Helixi339 – 3413Combined sources
    Beta strandi344 – 35512Combined sources
    Helixi357 – 3593Combined sources
    Helixi365 – 3673Combined sources
    Turni368 – 3703Combined sources
    Beta strandi372 – 3765Combined sources
    Helixi378 – 3825Combined sources
    Beta strandi388 – 3914Combined sources
    Helixi392 – 3976Combined sources
    Beta strandi400 – 4023Combined sources
    Helixi404 – 42017Combined sources
    Helixi424 – 4263Combined sources
    Beta strandi427 – 4315Combined sources
    Helixi434 – 4363Combined sources
    Beta strandi442 – 45110Combined sources
    Beta strandi454 – 4629Combined sources
    Helixi467 – 47610Combined sources
    Beta strandi482 – 4843Combined sources
    Helixi501 – 5077Combined sources
    Helixi512 – 5198Combined sources
    Helixi524 – 53512Combined sources
    Beta strandi541 – 5444Combined sources
    Beta strandi547 – 5504Combined sources
    Beta strandi552 – 5543Combined sources
    Beta strandi562 – 5643Combined sources
    Turni565 – 5673Combined sources
    Beta strandi568 – 5703Combined sources
    Beta strandi573 – 5808Combined sources
    Helixi581 – 59212Combined sources
    Beta strandi593 – 5953Combined sources
    Beta strandi597 – 6004Combined sources
    Beta strandi603 – 6053Combined sources
    Turni609 – 6113Combined sources
    Beta strandi615 – 6217Combined sources
    Turni625 – 6273Combined sources
    Helixi628 – 64013Combined sources
    Beta strandi645 – 6473Combined sources
    Beta strandi650 – 6523Combined sources
    Helixi654 – 66310Combined sources
    Beta strandi668 – 6725Combined sources
    Helixi674 – 6774Combined sources
    Beta strandi679 – 6813Combined sources
    Beta strandi683 – 6886Combined sources
    Turni689 – 6913Combined sources
    Beta strandi694 – 6985Combined sources
    Turni699 – 7013Combined sources
    Helixi702 – 7109Combined sources
    Beta strandi712 – 7143Combined sources
    Helixi716 – 7227Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliP41250.
    SMRiP41250. Positions 117-728.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP41250.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini63 – 11957WHEP-TRSPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni346 – 3505Substrate binding
    Regioni576 – 5805Substrate binding

    Sequence similaritiesi

    Contains 1 WHEP-TRS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0423.
    GeneTreeiENSGT00390000016949.
    HOGENOMiHOG000242015.
    HOVERGENiHBG036190.
    InParanoidiP41250.
    KOiK01880.
    OMAiFGVTQIG.
    OrthoDBiEOG7FBRH1.
    PhylomeDBiP41250.
    TreeFamiTF343504.

    Family and domain databases

    Gene3Di1.10.287.10. 1 hit.
    3.40.50.800. 1 hit.
    InterProiIPR002314. aa-tRNA-synt_IIb_cons-dom.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR027031. Gly-tRNA_synthase/POLG2.
    IPR009068. S15_NS1_RNA-bd.
    IPR002315. tRNA-synt_gly.
    IPR000738. WHEP-TRS.
    [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 AAA57001.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAA86443.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti9 – 1810Missing in BAG58412 (PubMed:14702039).Curated
    Sequence conflicti205 – 2051D → G in BAG51964 (PubMed:14702039).Curated
    Sequence conflicti530 – 5301M → I in AAA86443 (PubMed:7753621).Curated
    Sequence conflicti634 – 6341L → S in BAG51964 (PubMed:14702039).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti42 – 421P → A.5 Publications
    Corresponds to variant rs1049402 [ dbSNP | Ensembl ].
    VAR_054865
    Natural varianti111 – 1111A → V in CMT2D; shows a reduction in aminoacylation activity. 1 Publication
    VAR_073187
    Natural varianti125 – 1251E → G in CMT2D; phenotype overlapping with DSMA-V; complements the defect of the wild-type gene in yeast. 3 Publications
    Corresponds to variant rs28936972 [ dbSNP | Ensembl ].
    VAR_018718
    Natural varianti183 – 1831L → P in HMN5A; does not complement the defect of the wild-type gene in yeast. 3 Publications
    VAR_018719
    Natural varianti200 – 2001D → N in CMT2D; shows a large reduction in aminoacylation activity. 1 Publication
    VAR_073188
    Natural varianti265 – 2651S → F in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in the subcellular location pattern; does not associate with granules. 1 Publication
    VAR_073189
    Natural varianti268 – 2681T → I.
    Corresponds to variant rs2230310 [ dbSNP | Ensembl ].
    VAR_054866
    Natural varianti294 – 2941G → R in CMT2D; shows a large reduction in aminoacylation activity; does not impair transcription or translation or protein stability. 3 Publications
    VAR_018720
    Natural varianti298 – 2981P → L in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules. 1 Publication
    VAR_073190
    Natural varianti334 – 3341I → F in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules. 1 Publication
    VAR_073191
    Natural varianti388 – 3881R → Q.
    Corresponds to variant rs17159287 [ dbSNP | Ensembl ].
    VAR_054867
    Natural varianti472 – 4721H → R in HMN5A; shows a large reduction in aminoacylation activity; does not complement the defect of the wild-type gene in yeast. 3 Publications
    VAR_073192
    Natural varianti554 – 5541D → N in CMT2D; demonstrates no change in subcellular location pattern. 1 Publication
    VAR_073193
    Natural varianti580 – 5801G → R in HMN5A; higher dimerization stability; loss of activity; shows a large reduction in aminoacylation activity. 4 Publications
    Corresponds to variant rs28937323 [ dbSNP | Ensembl ].
    VAR_018721
    Natural varianti635 – 6351S → L Polymorphism; has no effect on subcellular localization; results in reduced activity. 2 Publications
    VAR_073194
    Natural varianti652 – 6521G → A in CMT2D; shows a large reduction in aminoacylation activity; demonstrates a change in subcellular location pattern; does not associate with granules. 1 Publication
    VAR_073195

    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_002038.2. NM_002047.2.
    UniGeneiHs.404321.

    Genome annotation databases

    EnsembliENST00000389266; ENSP00000373918; ENSG00000106105.
    GeneIDi2617.
    KEGGihsa:2617.
    UCSCiuc003tbm.3. 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_002038.2. NM_002047.2.
    UniGeneiHs.404321.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliP41250.
    SMRiP41250. Positions 117-728.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi108887. 56 interactions.
    DIPiDIP-50471N.
    IntActiP41250. 7 interactions.
    MINTiMINT-1395438.
    STRINGi9606.ENSP00000373918.

    Chemistry

    DrugBankiDB00145. Glycine.

    PTM databases

    PhosphoSiteiP41250.

    Polymorphism and mutation databases

    BioMutaiGARS.
    DMDMi313104283.

    Proteomic databases

    MaxQBiP41250.
    PaxDbiP41250.
    PRIDEiP41250.

    Protocols and materials databases

    DNASUi2617.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000389266; ENSP00000373918; ENSG00000106105.
    GeneIDi2617.
    KEGGihsa:2617.
    UCSCiuc003tbm.3. human.

    Organism-specific databases

    CTDi2617.
    GeneCardsiGC07P030600.
    GeneReviewsiGARS.
    H-InvDBHIX0006570.
    HGNCiHGNC:4162. GARS.
    HPAiHPA017896.
    HPA019097.
    MIMi600287. gene.
    600794. phenotype.
    601472. phenotype.
    neXtProtiNX_P41250.
    Orphaneti99938. Autosomal dominant Charcot-Marie-Tooth disease type 2D.
    139536. Distal hereditary motor neuropathy type 5.
    PharmGKBiPA28575.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG0423.
    GeneTreeiENSGT00390000016949.
    HOGENOMiHOG000242015.
    HOVERGENiHBG036190.
    InParanoidiP41250.
    KOiK01880.
    OMAiFGVTQIG.
    OrthoDBiEOG7FBRH1.
    PhylomeDBiP41250.
    TreeFamiTF343504.

    Enzyme and pathway databases

    BRENDAi6.1.1.14. 2681.
    ReactomeiREACT_15302. Mitochondrial tRNA aminoacylation.
    REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSiGARS. human.
    EvolutionaryTraceiP41250.
    GeneWikiiGlycine%E2%80%94tRNA_ligase.
    GenomeRNAii2617.
    NextBioi10303.
    PMAP-CutDBP41250.
    PROiP41250.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP41250.
    CleanExiHS_GARS.
    ExpressionAtlasiP41250. baseline and differential.
    GenevisibleiP41250. HS.

    Family and domain databases

    Gene3Di1.10.287.10. 1 hit.
    3.40.50.800. 1 hit.
    InterProiIPR002314. aa-tRNA-synt_IIb_cons-dom.
    IPR006195. aa-tRNA-synth_II.
    IPR004154. Anticodon-bd.
    IPR027031. Gly-tRNA_synthase/POLG2.
    IPR009068. S15_NS1_RNA-bd.
    IPR002315. tRNA-synt_gly.
    IPR000738. WHEP-TRS.
    [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...

    Publicationsi

    « Hide 'large scale' publications
    1. "Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation."
      Shiba K., Schimmel P., Motegi H., Noda T.
      J. Biol. Chem. 269:30049-30055(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-42.
    2. "Cloning, sequencing and bacterial expression of human glycine tRNA synthetase."
      Williams J.H., Osvath S.R., Khong T.-F., Pearse M.J., Power D.A.
      Nucleic Acids Res. 23:1307-1310(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-42.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-42.
      Tissue: Embryo and Hippocampus.
    4. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-42.
      Tissue: Eye and Muscle.
    6. "Primary structure and functional expression of human glycyl-tRNA synthetase, an autoantigen in myositis."
      Ge Q., Trieu E.P., Targoff I.N.
      J. Biol. Chem. 269:28790-28797(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-739, VARIANT ALA-42.
    7. "Complex organisation of the 5'-end of the human glycine tRNA synthetase gene."
      Mudge S.J., Williams J.H., Eyre H.J., Sutherland G.R., Cowan P.J., Power D.A.
      Gene 209:45-50(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    8. "Functional analyses of glycyl-tRNA synthetase mutations suggest a key role for tRNA-charging enzymes in peripheral axons."
      Antonellis A., Lee-Lin S.Q., Wasterlain A., Leo P., Quezado M., Goldfarb L.G., Myung K., Burgess S., Fischbeck K.H., Green E.D.
      J. Neurosci. 26:10397-10406(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, VARIANTS CMT2D GLY-125 AND ARG-294, CHARACTERIZATION OF VARIANTS CMT2D GLY-125 AND ARG-294, VARIANTS HMN5A PRO-183; ARG-472 AND ARG-580, CHARACTERIZATION OF VARIANTS HMN5A PRO-183; ARG-472 AND ARG-580.
    9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204 AND LYS-501, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Impaired function is a common feature of neuropathy-associated glycyl-tRNA synthetase mutations."
      Griffin L.B., Sakaguchi R., McGuigan D., Gonzalez M.A., Searby C., Zuchner S., Hou Y.M., Antonellis A.
      Hum. Mutat. 35:1363-1371(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, VARIANTS CMT2D VAL-111; ASN-200; PHE-265; ARG-294; LEU-298; PHE-334; ARG-472; ASN-554; ARG-580 AND ALA-652, VARIANT LEU-635, CHARACTERIZATION OF VARIANTS CMT2D VAL-111; GLY-125; PRO-183; ASN-200; PHE-265; ARG-294; LEU-298; PHE-334; ARG-472; ASN-554; ARG-580 AND ALA-652, CHARACTERIZATION OF VARIANT LEU-635.
    12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "Crystal structure of human wildtype and S581L-mutant glycyl-tRNA synthetase, an enzyme underlying distal spinal muscular atrophy."
      Cader M.Z., Ren J., James P.A., Bird L.E., Talbot K., Stammers D.K.
      FEBS Lett. 581:2959-2964(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 55-739, FUNCTION, SUBUNIT, CHARACTERIZATION OF VARIANT LEU-635, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
    14. "Long-range structural effects of a Charcot-Marie-Tooth disease-causing mutation in human glycyl-tRNA synthetase."
      Xie W., Nangle L.A., Zhang W., Schimmel P., Yang X.-L.
      Proc. Natl. Acad. Sci. U.S.A. 104:9976-9981(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 55-739, VARIANT ARG-580, SUBUNIT.
    15. "Crystal structures and biochemical analyses suggest a unique mechanism and role for human glycyl-tRNA synthetase in Ap4A homeostasis."
      Guo R.-T., Chong Y.E., Guo M., Yang X.-L.
      J. Biol. Chem. 284:28968-28976(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 55-739 IN COMPLEX WITH ATP; SUBSTRATE AND SUBSTRATE ANALOGS, FUNCTION.
    16. Cited for: VARIANTS CMT2D GLY-125 AND ARG-294, VARIANTS HMN5A PRO-183 AND ARG-580, TISSUE SPECIFICITY.
    17. Cited for: VARIANT HMN5A ARG-472.

    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: June 24, 2015
    This is version 161 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

    External Data

    Dasty 3

    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 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.