CPLM-011375

Genbank Nucleotide ID

Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

Protein Synonyms/Alias

D-fructose-6-phosphate amidotransferase 1; Glutamine:fructose-6-phosphate amidotransferase 1; GFAT 1; GFAT1; Hexosephosphate aminotransferase 1

Homo sapiens (Human)

Position	Peptide	Type	References
25	EILETLIKGLQRLEY	ubiquitination	[1, 2, 3, 4, 5, 6]
48	GFDGGNDKDWEANAC	ubiquitination	[1, 3, 4, 5, 6, 7]
139	LKKFLESKGYDFESE	ubiquitination	[2, 8]
157	ETIAKLVKYMYDNRE	ubiquitination	[4]
216	IGVRSEHKLSTDHIP	ubiquitination	[4]
345	NFSSFMQKEIFEQPE	ubiquitination	[2, 4]
375	TVNLGGLKDHIKEIQ	ubiquitination	[2, 4, 6]
379	GGLKDHIKEIQRCRR	ubiquitination	[4]
694	DFPRNLAKSVTVE**	acetylation	[9]
694	DFPRNLAKSVTVE**	ubiquitination	[2, 4, 10]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[7] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[8] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[9] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
[10] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]

Functional Description

Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.

DOMAIN 2 305 Glutamine amidotransferase type-2.
DOMAIN 377 516 SIS 1.
DOMAIN 548 689 SIS 2.
REGION 313 680 Isomerase.
REGION 394 395 Substrate-binding.
REGION 439 441 Substrate-binding.
ACT_SITE 2 2 For GATase activity (By similarity).
BINDING 444 444 Substrate.
BINDING 584 584 Substrate.
MOD_RES 261 261 Phosphoserine.

3D-structure; Alternative splicing; Aminotransferase; Complete proteome; Congenital myasthenic syndrome; Disease mutation; Glutamine amidotransferase; Phosphoprotein; Reference proteome; Repeat; Transferase.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0016597; F:amino acid binding; IEA:Compara.
GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; TAS:ProtInc.
GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro.
GO:0032869; P:cellular response to insulin stimulus; IEA:Compara.
GO:0006488; P:dolichol-linked oligosaccharide biosynthetic process; TAS:Reactome.
GO:0006112; P:energy reserve metabolic process; TAS:ProtInc.
GO:0006002; P:fructose 6-phosphate metabolic process; TAS:ProtInc.
GO:0006042; P:glucosamine biosynthetic process; IEA:Compara.
GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
GO:0045719; P:negative regulation of glycogen biosynthetic process; IEA:Compara.
GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO:0051289; P:protein homotetramerization; IEA:Compara.
GO:0018279; P:protein N-linked glycosylation via asparagine; TAS:Reactome.
GO:0009744; P:response to sucrose stimulus; IEA:Compara.
GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; TAS:Reactome.

IPR017932; GATase_2_dom.
IPR000583; GATase_dom.
IPR005855; GlmS_trans.
IPR001347; SIS.

PF00310; GATase_2
PF01380; SIS

PS51278; GATASE_TYPE_2
PS51464; SIS