P41250 (SYG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

GARS

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	739 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.12
Catalytic activity	ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly).
Subunit structure	Homodimer. Ref.10 Ref.11
Subcellular location	Cytoplasm. Mitochondrion Ref.7.
Tissue specificity	Widely expressed, including brain and spinal cord. Ref.13
Involvement in disease	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 regeneration 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Distal hereditary motor neuronopathy 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. Contains 1 WHEP-TRS domain.
Biophysicochemical properties	Kinetic parameters: KM=1.3 µM for tRNA(Gly(GCC)) Ref.10 KM=15 µM for glycine
Sequence caution	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.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm Mitochondrion
Disease	Charcot-Marie-Tooth disease Disease mutation Neurodegeneration Neuropathy
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell death Inferred from electronic annotation. Source: UniProtKB-KW diadenosine tetraphosphate biosynthetic process Inferred from direct assay Ref.12. Source: UniProtKB glycyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro tRNA aminoacylation for protein translation Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome mitochondrial matrix Traceable author statement. Source: Reactome secretory granule Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glycine-tRNA ligase activity Inferred from direct assay Ref.10Ref.11Ref.12. Source: UniProtKB protein dimerization activity Inferred from direct assay Ref.10Ref.11. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 739

739

Glycine--tRNA ligase

PRO_0000072998

Regions

Domain

63 – 119

57

WHEP-TRS

Nucleotide binding

331 – 333

3

ATP

Nucleotide binding

341 – 346

6

ATP

Nucleotide binding

457 – 458

2

ATP

Nucleotide binding

580 – 583

4

ATP

Region

346 – 350

5

Substrate binding

Region

576 – 580

5

Substrate binding

Sites

Binding site

213

1

Substrate

Binding site

299

1

Substrate

Binding site

435

1

Substrate; via carbonyl oxygen

Amino acid modifications

Modified residue

204

1

N6-acetyllysine Ref.8

Modified residue

453

1

Phosphotyrosine By similarity

Modified residue

501

1

N6-acetyllysine Ref.8

Natural variations

Natural variant

42

1

P → A. Ref.1 Ref.2 Ref.3 Ref.5 Ref.6
Corresponds to variant rs1049402 [ dbSNP | Ensembl ].

VAR_054865

Natural variant

125

1

E → G in CMT2D; phenotype overlapping with DSMA-V. Ref.13
Corresponds to variant rs28936972 [ dbSNP | Ensembl ].

VAR_018718

Natural variant

183

1

L → P in HMN5A. Ref.13

VAR_018719

Natural variant

268

1

T → I.
Corresponds to variant rs2230310 [ dbSNP | Ensembl ].

VAR_054866

Natural variant

294

1

G → R in CMT2D. Ref.13

VAR_018720

Natural variant

388

1

R → Q.
Corresponds to variant rs17159287 [ dbSNP | Ensembl ].

VAR_054867

Natural variant

580

1

G → R in HMN5A; higher dimerization stability but loss of activity. Ref.11 Ref.13
Corresponds to variant rs28937323 [ dbSNP | Ensembl ].

VAR_018721

Experimental info

Mutagenesis

635

1

S → L: Reduced activity. Ref.10

Sequence conflict

9 – 18

10

Missing in BAG58412. Ref.3

Sequence conflict

205

1

D → G in BAG51964. Ref.3

Sequence conflict

530

1

M → I in AAA86443. Ref.2

Sequence conflict

634

1

L → S in BAG51964. Ref.3

Secondary structure

1

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739

Helix Strand Turn

Details...

Helix

121 – 130

10

Beta strand

133 – 136

4

Helix

139 – 141

3

Beta strand

148 – 150

3

Helix

152 – 168

17

Helix

170 – 173

4

Beta strand

182 – 185

4

Helix

186 – 191

6

Helix

194 – 197

4

Beta strand

199 – 208

10

Beta strand

211 – 213

3

Helix

214 – 227

14

Beta strand

229 – 231

3

Helix

233 – 243

11

Turn

244 – 248

5

Helix

251 – 260

10

Beta strand

266 – 268

3

Beta strand

276 – 279

4

Beta strand

283 – 285

3

Beta strand

287 – 296

10

Beta strand

298 – 300

3

Helix

301 – 305

5

Helix

308 – 314

7

Turn

315 – 317

3

Beta strand

321 – 330

10

Helix

339 – 341

3

Beta strand

344 – 355

12

Helix

357 – 359

3

Helix

365 – 367

3

Turn

368 – 370

3

Beta strand

372 – 376

5

Helix

378 – 382

5

Beta strand

388 – 391

4

Helix

392 – 397

6

Beta strand

400 – 402

3

Helix

404 – 420

17

Helix

424 – 426

3

Beta strand

427 – 431

5

Helix

434 – 436

3

Beta strand

442 – 451

10

Beta strand

454 – 462

9

Helix

467 – 476

10

Beta strand

482 – 484

3

Beta strand

562 – 564

3

Turn

565 – 567

3

Beta strand

568 – 570

3

Beta strand

573 – 580

8

Helix

581 – 592

12

Beta strand

593 – 595

3

Beta strand

597 – 600

4

Beta strand

603 – 605

3

Turn

609 – 611

3

Beta strand

615 – 621

7

Turn

625 – 627

3

Helix

628 – 640

13

Beta strand

645 – 647

3

Helix

654 – 663

10

Beta strand

668 – 672

5

Helix

674 – 677

4

Beta strand

679 – 681

3

Beta strand

683 – 688

6

Turn

689 – 691

3

Beta strand

694 – 698

5

Turn

699 – 701

3

Helix

702 – 710

9

Helix

716 – 722

7

Sequences

	Sequence		Length	Mass (Da)
	P41250 [UniParc]. Last modified November 30, 2010. Version 3. Checksum: E4C001CEBF985C59	FASTA	739	83,166
	10 20 30 40 50 60 MPSPRPVLLR GARAALLLLL PPRLLARPSL LLRRSLSAAS CPPISLPAAA SRSSMDGAGA 70 80 90 100 110 120 EEVLAPLRLA VRQQGDLVRK LKEDKAPQVD VDKAVAELKA RKRVLEAKEL ALQPKDDIVD 130 140 150 160 170 180 RAKMEDTLKR RFFYDQAFAI YGGVSGLYDF GPVGCALKNN IIQTWRQHFI QEEQILEIDC 190 200 210 220 230 240 TMLTPEPVLK TSGHVDKFAD FMVKDVKNGE CFRADHLLKA HLQKLMSDKK CSVEKKSEME 250 260 270 280 290 300 SVLAQLDNYG QQELADLFVN YNVKSPITGN DLSPPVSFNL MFKTFIGPGG NMPGYLRPET 310 320 330 340 350 360 AQGIFLNFKR LLEFNQGKLP FAAAQIGNSF RNEISPRSGL IRVREFTMAE IEHFVDPSEK 370 380 390 400 410 420 DHPKFQNVAD LHLYLYSAKA QVSGQSARKM RLGDAVEQGV INNTVLGYFI GRIYLYLTKV 430 440 450 460 470 480 GISPDKLRFR QHMENEMAHY ACDCWDAESK TSYGWIEIVG CADRSCYDLS CHARATKVPL 490 500 510 520 530 540 VAEKPLKEPK TVNVVQFEPS KGAIGKAYKK DAKLVMEYLA ICDECYITEM EMLLNEKGEF 550 560 570 580 590 600 TIETEGKTFQ LTKDMINVKR FQKTLYVEEV VPNVIEPSFG LGRIMYTVFE HTFHVREGDE 610 620 630 640 650 660 QRTFFSFPAV VAPFKCSVLP LSQNQEFMPF VKELSEALTR HGVSHKVDDS SGSIGRRYAR 670 680 690 700 710 720 TDEIGVAFGV TIDFDTVNKT PHTATLRDRD SMRQIRAEIS ELPSIVQDLA NGNITWADVE 730 ARYPLFEGQE TGKKETIEE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, MASS SPECTROMETRY.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V." Antonellis A., Ellsworth R.E., Sambuughin N., Puls I., Abel A., Lee-Lin S.Q., Jordanova A., Kremensky I., Christodoulou K., Middleton L.T., Sivakumar K., Ionasescu V., Funalot B., Vance J.M., Goldfarb L.G., Fischbeck K.H., Green E.D. Am. J. Hum. Genet. 72:1293-1299(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS CMT2D GLY-125 AND ARG-294, VARIANTS HMN5A PRO-183 AND ARG-580, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Web resources

Inherited peripheral neuropathies mutation db

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00783097.

PIR

A55314.

RefSeq

NP_002038.2. NM_002047.2.

UniGene

Hs.404321.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P41250.

SMR

P41250. Positions 117-727.

ModBase

Search...

Protein-protein interaction databases

IntAct

P41250. 4 interactions.

MINT

MINT-1395438.

STRING

9606.ENSP00000373918.

PTM databases

PhosphoSite

P41250.

Polymorphism databases

DMDM

21264523.

Proteomic databases

PaxDb

P41250.

PRIDE

P41250.

Protocols and materials databases

DNASU

2617.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000389266; ENSP00000373918; ENSG00000106105.

GeneID

2617.

KEGG

hsa:2617.

UCSC

uc003tbm.3. human.

Organism-specific databases

CTD

2617.

GeneCards

GC07P030600.

H-InvDB

HIX0006570.

HGNC

HGNC:4162. GARS.

HPA

HPA017896.
HPA019097.

MIM

600287. gene.
600794. phenotype.
601472. phenotype.

neXtProt

NX_P41250.

Orphanet

99938. Autosomal dominant Charcot-Marie-Tooth disease type 2D.
139536. Distal hereditary motor neuropathy type 5.

PharmGKB

PA28575.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0423.

HOGENOM

HOG000242015.

HOVERGEN

HBG036190.

InParanoid

P41250.

KO

K01880.

OMA

VFIASGH.

OrthoDB

EOG4RV2QV.

Enzyme and pathway databases

BRENDA

6.1.1.14. 2681.

Reactome

REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P41250.

Bgee

P41250.

CleanEx

HS_GARS.

Genevestigator

P41250.

GermOnline

ENSG00000106105. Homo sapiens.

Family and domain databases

Gene3D

1.10.287.10. 1 hit.
3.40.50.800. 1 hit.

InterPro

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]

PANTHER

PTHR10745. PTHR10745. 1 hit.

Pfam

PF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF00458. WHEP-TRS. 1 hit.
[Graphical view]

PRINTS

PR01043. TRNASYNTHGLY.

SMART

SM00991. WHEP-TRS. 1 hit.
[Graphical view]

SUPFAM

SSF52954. Anticodon_bd. 1 hit.

TIGRFAMs

TIGR00389. glyS_dimeric. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
PS00762. WHEP_TRS_1. 1 hit.
PS51185. WHEP_TRS_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

GARS. human.

DrugBank

DB00145. Glycine.

EvolutionaryTrace

P41250.

GenomeRNAi

2617.

NextBio

10303.

PMAP-CutDB

P41250.

SOURCE

Search...

Entry information

Entry name

SYG_HUMAN

Accession

Primary (citable) accession number: P41250
Secondary accession number(s): B3KQA2, B4DIA0, Q969Y1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	November 30, 2010
Last modified:	May 1, 2013
This is version 138 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.