UniProt Accession

 GNMT_MOUSE; Q9QXF8; Q91WN7 

Genbank Protein ID

 D89664; AF325352; AY054408; BC014283 

Genbank Nucleotide ID

 BAA88218.1; AAK00338.1; AAL06142.1; AAH14283.1 

Protein Name

 Glycine N-methyltransferase 

Protein Synonyms/Alias

  

Gene Name

 Gnmt 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
46	RSRTAEYKAWLLGLL	acetylation	[1]
46	RSRTAEYKAWLLGLL	succinylation	[1]
46	RSRTAEYKAWLLGLL	ubiquitination	[2]
93	DASDKMLKYALKERW	ubiquitination	[2]
159	SEHRLALKNIASMVR	ubiquitination	[2]
191	TGCAPPGKNIYYKSD	acetylation	[1, 3, 4]
191	TGCAPPGKNIYYKSD	succinylation	[1]
191	TGCAPPGKNIYYKSD	ubiquitination	[2]
196	PGKNIYYKSDLTKDI	acetylation	[1, 4]
196	PGKNIYYKSDLTKDI	succinylation	[1]
196	PGKNIYYKSDLTKDI	ubiquitination	[2]
201	YYKSDLTKDITTSVL	acetylation	[1, 3, 4, 5, 6]
201	YYKSDLTKDITTSVL	succinylation	[1]
201	YYKSDLTKDITTSVL	ubiquitination	[2]
238	DGSPGFSKFRLSYYP	acetylation	[1, 4, 5]
238	DGSPGFSKFRLSYYP	succinylation	[1]
238	DGSPGFSKFRLSYYP	ubiquitination	[2]
272	HSVLGDFKPYKPGQA	acetylation	[4]
272	HSVLGDFKPYKPGQA	ubiquitination	[2]
290	CYFIHVLKKTD****	acetylation	[4]

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 assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [4] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [5] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [6] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654] 

Functional Description

 Catalyzes the methylation of glycine by using S- adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy). Possible crucial role in the regulation of tissue concentration of AdoMet and of metabolism of methionine (By similarity). 

Sequence Annotation

 REGION 117 118 S-adenosyl-L-methionine binding (By
 BINDING 22 22 S-adenosyl-L-methionine (By similarity).
 BINDING 31 31 S-adenosyl-L-methionine (By similarity).
 BINDING 34 34 Substrate (By similarity).
 BINDING 41 41 S-adenosyl-L-methionine (By similarity).
 BINDING 65 65 S-adenosyl-L-methionine; via carbonyl
 BINDING 86 86 S-adenosyl-L-methionine (By similarity).
 BINDING 137 137 S-adenosyl-L-methionine; via carbonyl
 BINDING 139 139 Substrate (By similarity).
 BINDING 176 176 Substrate (By similarity).
 BINDING 221 221 Substrate (By similarity).
 MOD_RES 2 2 N-acetylvaline (By similarity).
 MOD_RES 233 233 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Complete proteome; Cytoplasm; Folate-binding; Methyltransferase; Phosphoprotein; Reference proteome; S-adenosyl-L-methionine; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 293 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005542; F:folic acid binding; IEA:UniProtKB-KW.
 GO:0016594; F:glycine binding; IDA:UniProtKB.
 GO:0017174; F:glycine N-methyltransferase activity; IDA:UniProtKB.
 GO:0005977; P:glycogen metabolic process; IMP:MGI.
 GO:0006555; P:methionine metabolic process; IMP:MGI.
 GO:0006730; P:one-carbon metabolic process; IMP:MGI.
 GO:0051289; P:protein homotetramerization; IPI:UniProtKB.
 GO:0006111; P:regulation of gluconeogenesis; IMP:MGI.
 GO:0046500; P:S-adenosylmethionine metabolic process; IDA:UniProtKB. 

Interpro

 IPR014369; Gly/Sar_N_MeTrfase.
 IPR025714; Methyltranfer_dom. 

Pfam

 PF13847; Methyltransf_31 

SMART

  

PROSITE

 PS51600; SAM_GNMT 

PRINTS