Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P41250

- SYG_HUMAN

UniProt

P41250 - SYG_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Glycine--tRNA ligase

Gene

GARS

Organism
Homo sapiens (Human)
Status
Reviewed - 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.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
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:6.1.1.14)
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
Complete GO annotation...

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

BgeeiP41250.
CleanExiHS_GARS.
ExpressionAtlasiP41250. baseline and differential.
GenevestigatoriP41250.

Organism-specific databases

HPAiHPA017896.
HPA019097.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

BioGridi108887. 56 interactions.
DIPiDIP-50471N.
IntActiP41250. 6 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.
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

        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 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:
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.

Polymorphism databases

DMDMi313104283.

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.
CCDSi CCDS43564.1.
PIRi A55314.
RefSeqi NP_002038.2. NM_002047.2.
UniGenei Hs.404321.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 117-728.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108887. 56 interactions.
DIPi DIP-50471N.
IntActi P41250. 6 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.
GeneTreei ENSGT00390000016949.
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

Bgeei P41250.
CleanExi HS_GARS.
ExpressionAtlasi P41250. baseline and differential.
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

« 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. "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: November 26, 2014
This is version 155 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