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P41250

- SYG_HUMAN

UniProt

P41250 - SYG_HUMAN

Protein

Glycine--tRNA ligase

Gene

GARS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (30 Nov 2010)
      Previous versions | rss
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    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.1 Publication

    Catalytic activityi

    ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly).

    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

    1. ATP binding Source: UniProtKB-KW
    2. glycine-tRNA ligase activity Source: UniProtKB
    3. protein dimerization activity Source: UniProtKB

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. diadenosine tetraphosphate biosynthetic process Source: UniProtKB
    3. gene expression Source: Reactome
    4. glycyl-tRNA aminoacylation Source: InterPro
    5. tRNA aminoacylation for protein translation Source: Reactome

    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:6.1.1.14)
    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: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:4162. GARS.

    Subcellular locationi

    Cytoplasm 1 Publication. Mitochondrion 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. mitochondrial matrix Source: Reactome
    5. nucleus Source: HPA
    6. secretory granule Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Charcot-Marie-Tooth disease 2D (CMT2D) [MIM:601472]: A 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti125 – 1251E → G in CMT2D; phenotype overlapping with DSMA-V. 1 Publication
    Corresponds to variant rs28936972 [ dbSNP | Ensembl ].
    VAR_018718
    Natural varianti294 – 2941G → R in CMT2D. 1 Publication
    VAR_018720
    Neuronopathy, distal hereditary motor, 5A (HMN5A) [MIM:600794]: A 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti183 – 1831L → P in HMN5A. 1 Publication
    VAR_018719
    Natural varianti580 – 5801G → R in HMN5A; higher dimerization stability but loss of activity. 2 Publications
    Corresponds to variant rs28937323 [ dbSNP | Ensembl ].
    VAR_018721

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi635 – 6351S → L: Reduced activity. 1 Publication

    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.

    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

    ArrayExpressiP41250.
    BgeeiP41250.
    CleanExiHS_GARS.
    GenevestigatoriP41250.

    Organism-specific databases

    HPAiHPA017896.
    HPA019097.

    Interactioni

    Subunit structurei

    Homodimer.3 Publications

    Protein-protein interaction databases

    BioGridi108887. 54 interactions.
    DIPiDIP-50471N.
    IntActiP41250. 5 interactions.
    MINTiMINT-1395438.
    STRINGi9606.ENSP00000373918.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 117-727.
    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.
    HOGENOMiHOG000242015.
    HOVERGENiHBG036190.
    InParanoidiP41250.
    KOiK01880.
    OMAiLMFQTTI.
    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

    MPSPRPVLLR GARAALLLLL PPRLLARPSL LLRRSLSAAS CPPISLPAAA    50
    SRSSMDGAGA EEVLAPLRLA VRQQGDLVRK LKEDKAPQVD VDKAVAELKA 100
    RKRVLEAKEL ALQPKDDIVD RAKMEDTLKR RFFYDQAFAI YGGVSGLYDF 150
    GPVGCALKNN IIQTWRQHFI QEEQILEIDC TMLTPEPVLK TSGHVDKFAD 200
    FMVKDVKNGE CFRADHLLKA HLQKLMSDKK CSVEKKSEME SVLAQLDNYG 250
    QQELADLFVN YNVKSPITGN DLSPPVSFNL MFKTFIGPGG NMPGYLRPET 300
    AQGIFLNFKR LLEFNQGKLP FAAAQIGNSF RNEISPRSGL IRVREFTMAE 350
    IEHFVDPSEK DHPKFQNVAD LHLYLYSAKA QVSGQSARKM RLGDAVEQGV 400
    INNTVLGYFI GRIYLYLTKV GISPDKLRFR QHMENEMAHY ACDCWDAESK 450
    TSYGWIEIVG CADRSCYDLS CHARATKVPL VAEKPLKEPK TVNVVQFEPS 500
    KGAIGKAYKK DAKLVMEYLA ICDECYITEM EMLLNEKGEF TIETEGKTFQ 550
    LTKDMINVKR FQKTLYVEEV VPNVIEPSFG LGRIMYTVFE HTFHVREGDE 600
    QRTFFSFPAV VAPFKCSVLP LSQNQEFMPF VKELSEALTR HGVSHKVDDS 650
    SGSIGRRYAR TDEIGVAFGV TIDFDTVNKT PHTATLRDRD SMRQIRAEIS 700
    ELPSIVQDLA NGNITWADVE ARYPLFEGQE TGKKETIEE 739
    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.
    The sequence AAA86443.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    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 varianti125 – 1251E → G in CMT2D; phenotype overlapping with DSMA-V. 1 Publication
    Corresponds to variant rs28936972 [ dbSNP | Ensembl ].
    VAR_018718
    Natural varianti183 – 1831L → P in HMN5A. 1 Publication
    VAR_018719
    Natural varianti268 – 2681T → I.
    Corresponds to variant rs2230310 [ dbSNP | Ensembl ].
    VAR_054866
    Natural varianti294 – 2941G → R in CMT2D. 1 Publication
    VAR_018720
    Natural varianti388 – 3881R → Q.
    Corresponds to variant rs17159287 [ dbSNP | Ensembl ].
    VAR_054867
    Natural varianti580 – 5801G → R in HMN5A; higher dimerization stability but loss of activity. 2 Publications
    Corresponds to variant rs28937323 [ dbSNP | Ensembl ].
    VAR_018721

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi313104283.

    Cross-referencesi

    Web resourcesi

    Inherited peripheral neuropathies mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSi CCDS43564.1.
    PIRi A55314.
    RefSeqi NP_002038.2. NM_002047.2.
    UniGenei Hs.404321.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2PME X-ray 2.90 A 55-739 [» ]
    2PMF X-ray 2.85 A 55-739 [» ]
    2Q5H X-ray 3.00 A 55-739 [» ]
    2Q5I X-ray 2.80 A 55-739 [» ]
    2ZT5 X-ray 2.50 A 55-739 [» ]
    2ZT6 X-ray 3.08 A 55-739 [» ]
    2ZT7 X-ray 2.70 A 55-739 [» ]
    2ZT8 X-ray 3.35 A 55-739 [» ]
    2ZXF X-ray 3.40 A 55-739 [» ]
    4KQE X-ray 2.74 A 55-739 [» ]
    4KR2 X-ray 3.29 A 114-739 [» ]
    4KR3 X-ray 3.24 A 114-739 [» ]
    ProteinModelPortali P41250.
    SMRi P41250. Positions 117-727.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108887. 54 interactions.
    DIPi DIP-50471N.
    IntActi P41250. 5 interactions.
    MINTi MINT-1395438.
    STRINGi 9606.ENSP00000373918.

    Chemistry

    DrugBanki DB00145. Glycine.

    PTM databases

    PhosphoSitei P41250.

    Polymorphism databases

    DMDMi 313104283.

    Proteomic databases

    MaxQBi P41250.
    PaxDbi P41250.
    PRIDEi P41250.

    Protocols and materials databases

    DNASUi 2617.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389266 ; ENSP00000373918 ; ENSG00000106105 .
    GeneIDi 2617.
    KEGGi hsa:2617.
    UCSCi uc003tbm.3. human.

    Organism-specific databases

    CTDi 2617.
    GeneCardsi GC07P030600.
    GeneReviewsi GARS.
    H-InvDB HIX0006570.
    HGNCi HGNC:4162. GARS.
    HPAi HPA017896.
    HPA019097.
    MIMi 600287. gene.
    600794. phenotype.
    601472. phenotype.
    neXtProti NX_P41250.
    Orphaneti 99938. Autosomal dominant Charcot-Marie-Tooth disease type 2D.
    139536. Distal hereditary motor neuropathy type 5.
    PharmGKBi PA28575.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0423.
    HOGENOMi HOG000242015.
    HOVERGENi HBG036190.
    InParanoidi P41250.
    KOi K01880.
    OMAi LMFQTTI.
    OrthoDBi EOG7FBRH1.
    PhylomeDBi P41250.
    TreeFami TF343504.

    Enzyme and pathway databases

    BRENDAi 6.1.1.14. 2681.
    Reactomei REACT_15302. Mitochondrial tRNA aminoacylation.
    REACT_15306. Cytosolic tRNA aminoacylation.

    Miscellaneous databases

    ChiTaRSi GARS. human.
    EvolutionaryTracei P41250.
    GeneWikii Glycine%E2%80%94tRNA_ligase.
    GenomeRNAii 2617.
    NextBioi 10303.
    PMAP-CutDB P41250.
    PROi P41250.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P41250.
    Bgeei P41250.
    CleanExi HS_GARS.
    Genevestigatori P41250.

    Family and domain databases

    Gene3Di 1.10.287.10. 1 hit.
    3.40.50.800. 1 hit.
    InterProi IPR002314. 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 ]
    PANTHERi PTHR10745. PTHR10745. 1 hit.
    Pfami PF03129. HGTP_anticodon. 1 hit.
    PF00587. tRNA-synt_2b. 1 hit.
    PF00458. WHEP-TRS. 1 hit.
    [Graphical view ]
    PRINTSi PR01043. TRNASYNTHGLY.
    SMARTi SM00991. WHEP-TRS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47060. SSF47060. 1 hit.
    SSF52954. SSF52954. 1 hit.
    TIGRFAMsi TIGR00389. glyS_dimeric. 1 hit.
    PROSITEi PS50862. AA_TRNA_LIGASE_II. 1 hit.
    PS00762. WHEP_TRS_1. 1 hit.
    PS51185. WHEP_TRS_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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, SUBUNIT, MUTAGENESIS OF SER-635, BIOPHYSICOCHEMICAL PROPERTIES.
    12. "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.
    13. "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.
    14. Cited for: VARIANTS CMT2D GLY-125 AND ARG-294, VARIANTS HMN5A PRO-183 AND ARG-580, TISSUE SPECIFICITY.

    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: October 1, 2014
    This is version 153 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

    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