CPLM-002628

Genbank Nucleotide ID

Asparagine synthetase [glutamine-hydrolyzing]

Protein Synonyms/Alias

Cell cycle control protein TS11; Glutamine-dependent asparagine synthetase

Homo sapiens (Human)

Position	Peptide	Type	References
83	GEIYNHKKMQQHFEF	ubiquitination	[1, 2]
132	LLDTANKKVFLGRDT	ubiquitination	[3]
168	AKGLVTLKHSATPFL	ubiquitination	[1, 2, 3, 4, 5]
176	HSATPFLKVEPFLPG	ubiquitination	[1, 2, 3]
191	HYEVLDLKPNGKVAS	ubiquitination	[1, 2, 3]
195	LDLKPNGKVASVEMV	ubiquitination	[3]
203	VASVEMVKYHHCRDV	ubiquitination	[3]
221	ALYDNVEKLFPGFEI	ubiquitination	[1, 6]
232	GFEIETVKNNLRILF	ubiquitination	[2, 3]
244	ILFNNAVKKRLMTDR	ubiquitination	[1, 2, 3, 4, 5]
245	LFNNAVKKRLMTDRR	ubiquitination	[3]
272	LVAATLLKQLKEAQV	ubiquitination	[1, 3]
275	ATLLKQLKEAQVQYP	ubiquitination	[1, 2]
350	VGMYLISKYIRKNTD	ubiquitination	[2, 3]
379	QGYIYFHKAPSPEKA	ubiquitination	[1, 2]
385	HKAPSPEKAEEESER	acetylation	[7]
385	HKAPSPEKAEEESER	ubiquitination	[1, 2]
440	PPEMRIPKNGIEKHL	ubiquitination	[3]
445	IPKNGIEKHLLRETF	ubiquitination	[1, 2, 3]
460	EDSNLIPKEILWRPK	ubiquitination	[1, 2, 3, 4, 5]
467	KEILWRPKEAFSDGI	ubiquitination	[1, 2, 3]
478	SDGITSVKNSWFKIL	ubiquitination	[1, 2, 3, 4, 5, 8]
504	MMANAAQKFPFNTPK	ubiquitination	[1, 2, 3, 4, 5, 6, 9]
511	KFPFNTPKTKEGYYY	ubiquitination	[1]
513	PFNTPKTKEGYYYRQ	ubiquitination	[1, 3]
540	LSHYWMPKWINATDP	ubiquitination	[9]

[1] 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]
[2] 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]
[3] 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]
[4] 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]
[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] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
Xu G, Paige JS, Jaffrey SR.
Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
[7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[8] 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]
[9] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]

Functional Description

DOMAIN 2 191 Glutamine amidotransferase type-2.
DOMAIN 213 536 Asparagine synthetase.
NP_BIND 363 364 ATP (By similarity).
REGION 49 53 Glutamine binding (By similarity).
REGION 75 77 Glutamine binding (By similarity).
ACT_SITE 2 2 For GATase activity.
BINDING 97 97 Glutamine (By similarity).
BINDING 256 256 ATP; via carbonyl oxygen (By similarity).
BINDING 288 288 ATP; via amide nitrogen and carbonyl
MOD_RES 385 385 N6-acetyllysine.

Acetylation; Alternative splicing; Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase; Nucleotide-binding; Polymorphism; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IDA:UniProtKB.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0048037; F:cofactor binding; IEA:Compara.
GO:0006987; P:activation of signaling protein activity involved in unfolded protein response; TAS:Reactome.
GO:0006529; P:asparagine biosynthetic process; IC:UniProtKB.
GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO:0042149; P:cellular response to glucose starvation; IDA:UniProtKB.
GO:0032870; P:cellular response to hormone stimulus; IEA:Compara.
GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway.
GO:0001889; P:liver development; IEA:Compara.
GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO:0045931; P:positive regulation of mitotic cell cycle; IDA:UniProtKB.
GO:0043200; P:response to amino acid stimulus; IEA:Compara.
GO:0032354; P:response to follicle-stimulating hormone stimulus; IEA:Compara.
GO:0009416; P:response to light stimulus; IEA:Compara.
GO:0009612; P:response to mechanical stimulus; IEA:Compara.
GO:0031427; P:response to methotrexate; IEA:Compara.
GO:0009636; P:response to toxic substance; IEA:Compara.

IPR006426; Asn_synth_AEB.
IPR001962; Asn_synthase.
IPR017932; GATase_2_dom.
IPR000583; GATase_dom.
IPR014729; Rossmann-like_a/b/a_fold.

PF00733; Asn_synthase
PF13537; GATase_7

PS51278; GATASE_TYPE_2