UniProt Accession

 SYG_MOUSE; Q9CZD3; Q3TMM4; Q3UK01; Q8VC67 

Genbank Protein ID

 AK146238; AK165857; BC021747 

Genbank Nucleotide ID

 BAE27003.1; BAE38417.1; AAH21747.1 

Protein Name

 Glycine--tRNA ligase 

Protein Synonyms/Alias

 Diadenosine tetraphosphate synthetase; AP-4-A synthetase; Glycyl-tRNA synthetase; GlyRS 

Gene Name

 Gars 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
89	DRAVAELKARKRVLE	acetylation	[1]
89	DRAVAELKARKRVLE	succinylation	[1]
89	DRAVAELKARKRVLE	ubiquitination	[2]
98	RKRVLEAKELALQPK	acetylation	[1, 3, 4]
98	RKRVLEAKELALQPK	succinylation	[1]
98	RKRVLEAKELALQPK	ubiquitination	[2]
187	KTSGHVDKFADFMVK	acetylation	[3]
187	KTSGHVDKFADFMVK	ubiquitination	[2]
194	KFADFMVKDVKNGEC	acetylation	[3, 4]
209	FRADHLLKAHLQKLM	acetylation	[3]
214	LLKAHLQKLMSDKKC	acetylation	[3]
308	LLEFNQGKLPFAAAQ	ubiquitination	[2]
350	HFVDPTEKDHPKFQS	acetylation	[1]
409	RIYLYLTKVGISPDK	ubiquitination	[2]
474	KVPLVAEKPLKEPKT	acetylation	[1]
491	VVQFEPNKGAVGKAY	acetylation	[4]
543	GKTFQLTKDMVSVKR	acetylation	[3]
723	FEGQETGKKETVEE*	ubiquitination	[2]
724	EGQETGKKETVEE**	ubiquitination	[2]

Reference

 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 

Functional Description

 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 (By similarity). 

Sequence Annotation

 DOMAIN 53 109 WHEP-TRS.
 NP_BIND 321 323 ATP (By similarity).
 NP_BIND 331 336 ATP (By similarity).
 NP_BIND 447 448 ATP (By similarity).
 NP_BIND 570 573 ATP (By similarity).
 REGION 336 340 Substrate binding (By similarity).
 REGION 566 570 Substrate binding (By similarity).
 BINDING 203 203 Substrate (By similarity).
 BINDING 289 289 Substrate (By similarity).
 BINDING 425 425 Substrate (By similarity).
 BINDING 425 425 Substrate; via carbonyl oxygen (By
 MOD_RES 194 194 N6-acetyllysine (By similarity).
 MOD_RES 443 443 Phosphotyrosine.
 MOD_RES 491 491 N6-acetyllysine (By similarity).  

Keyword

 Acetylation; Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Mitochondrion; Nucleotide-binding; Phosphoprotein; Protein biosynthesis; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 729 AA 

Protein Sequence

Gene Ontology

 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0030141; C:secretory granule; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004820; F:glycine-tRNA ligase activity; ISS:UniProtKB.
 GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
 GO:0015966; P:diadenosine tetraphosphate biosynthetic process; ISS:UniProtKB.
 GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro. 

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. 

Pfam

 PF03129; HGTP_anticodon
 PF00587; tRNA-synt_2b
 PF00458; WHEP-TRS 

SMART

 SM00991; WHEP-TRS 

PROSITE

 PS50862; AA_TRNA_LIGASE_II
 PS00762; WHEP_TRS_1
 PS51185; WHEP_TRS_2 

PRINTS

 PR01043; TRNASYNTHGLY.