CPLM-001855

Genbank Nucleotide ID

Argininosuccinate synthase

Protein Synonyms/Alias

Citrulline--aspartate ligase

Homo sapiens (Human)

Position	Peptide	Type	References
41	YLANIGQKEDFEEAR	ubiquitination	[1]
101	ARPCIARKQVEIAQR	ubiquitination	[1]
121	VSHGATGKGNDQVRF	ubiquitination	[1, 2]
140	YSLAPQIKVIAPWRM	ubiquitination	[1, 3]
165	NDLMEYAKQHGIPIP	acetylation	[4, 5]
165	NDLMEYAKQHGIPIP	ubiquitination	[1]
199	AGILENPKNQAPPGL	ubiquitination	[1]
209	APPGLYTKTQDPAKA	acetylation	[6]
209	APPGLYTKTQDPAKA	ubiquitination	[1, 7]
260	YLNEVAGKHGVGRID	ubiquitination	[1]
348	SQERVEGKVQVSVLK	ubiquitination	[1]

[1] 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]
[2] 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]
[3] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[4] 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]
[5] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[6] 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]
[7] 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]

Functional Description

Is indirectly involved in the control of blood pressure (By similarity).

NP_BIND 10 18 ATP (By similarity).
NP_BIND 115 123 ATP (By similarity).
BINDING 36 36 ATP; via amide nitrogen and carbonyl
BINDING 87 87 Citrulline.
BINDING 92 92 Citrulline.
BINDING 119 119 Aspartate.
BINDING 123 123 Aspartate.
BINDING 123 123 Citrulline.
BINDING 124 124 Aspartate.
BINDING 127 127 Citrulline.
BINDING 180 180 Citrulline.
BINDING 189 189 Citrulline.
BINDING 270 270 Citrulline.
BINDING 282 282 Citrulline.
MOD_RES 180 180 Phosphoserine.
MOD_RES 219 219 Phosphothreonine.

3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Complete proteome; Direct protein sequencing; Disease mutation; Ligase; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Urea cycle.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0004055; F:argininosuccinate synthase activity; EXP:Reactome.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
GO:0000050; P:urea cycle; TAS:Reactome.

IPR001518; Arginosuc_synth.
IPR018223; Arginosuc_synth_CS.
IPR023434; Arginosuc_synth_type_1_subfam.
IPR024074; AS_cat/multimer_dom_body.
IPR014729; Rossmann-like_a/b/a_fold.

PF00764; Arginosuc_synth

PS00564; ARGININOSUCCIN_SYN_1
PS00565; ARGININOSUCCIN_SYN_2