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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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	Defects in GARS are the cause of Charcot-Marie-Tooth disease type 2D (CMT2D) [MIM:601472]. CMT2D is a form of Charcot-Marie-Tooth disease, the most common inherited disorder of the peripheral nervous system. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathy or CMT1, and primary peripheral axonal neuropathy or 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. CMT2D is characterized by a more severe phenotype in the upper extremities (severe weakness and atrophy, absence of tendon reflexes) than in the lower limbs. CMT2D inheritance is autosomal dominant. Ref.13 Defects in GARS are the cause of distal spinal muscular neuropathy type 5 (HMN5) [MIM:600794]; also known as distal hereditary motor neuropathy type V (DSMAV). HMN5 is an autosomal dominant distal hereditary motor neuropathy (dHMN) with a phenotype similar to CMTD2. The main characteristic that distinguishes these disorders is the less severe distal sensory involvement in HMN5 patients. 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
Cellular component	cytosol Traceable author statement. Source: Reactome mitochondrial matrix Traceable author statement. Source: Reactome soluble fraction Traceable author statement. Source: ProtInc
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

219

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 HMN5. 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 HMN5; 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 – 173

22

Beta strand

182 – 185

4

Helix

186 – 192

7

Beta strand

195 – 205

11

Turn

206 – 208

3

Beta strand

209 – 213

5

Helix

214 – 226

13

Helix

233 – 243

11

Helix

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 – 291

5

Beta strand

293 – 296

4

Helix

301 – 306

6

Helix

308 – 314

7

Turn

315 – 317

3

Beta strand

321 – 330

10

Beta strand

344 – 355

12

Helix

357 – 359

3

Helix

365 – 367

3

Turn

368 – 370

3

Beta strand

372 – 376

5

Helix

378 – 383

6

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

Beta strand

443 – 451

9

Beta strand

454 – 466

13

Helix

469 – 472

4

Beta strand

573 – 580

8

Helix

581 – 592

12

Beta strand

593 – 595

3

Beta strand

603 – 605

3

Turn

609 – 611

3

Beta strand

615 – 621

7

Helix

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

678 – 681

4

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: 7962006] [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: 7753621] [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: 14702039] [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: 12853948] [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: 15489334] [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: 7961834] [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: 9524218] [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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-204; LYS-219 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: 21269460] [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: 17544401] [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: 17545306] [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: 19710017] [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: 12690580] [Abstract] Cited for: VARIANTS CMT2D GLY-125 AND ARG-294, VARIANTS HMN5 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 65-108, 117-727.

ModBase

Search...

Protein-protein interaction databases

IntAct

P41250. 4 interactions.

MINT

MINT-1395438.

STRING

P41250.

PTM databases

PhosphoSite

P41250.

Polymorphism databases

DMDM

21264523.

Proteomic databases

PRIDE

P41250.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000389266; ENSP00000373918; ENSG00000106105.

GeneID

2617.

KEGG

hsa:2617.

UCSC

uc003tbm.1. 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

prNOG14046.

HOGENOM

HBG319978.

HOVERGEN

HBG036190.

InParanoid

P41250.

OMA

GSITWAD.

OrthoDB

EOG4RV2QV.

PhylomeDB

P41250.

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

InterPro

IPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR009068. S15_NS1_RNA-bd.
IPR002315. tRNA-synt_gly.
IPR000738. WHEP-TRS.
[Graphical view]

Gene3D

G3DSA:3.40.50.800. Anticodon_bd. 1 hit.
G3DSA:1.10.287.10. S15_NS1_RNA_bd. 1 hit.

KO

K01880.

PANTHER

PTHR10745. tRNA-synt_gly. 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

DrugBank

DB00145. Glycine.

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:	January 25, 2012
This is version 125 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.