CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004470
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Argininosuccinate synthase 
Protein Synonyms/Alias
 Citrulline--aspartate ligase 
Gene Name
 Ass1 
Gene Synonyms/Alias
 Ass 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
41YLANIGQKEDFEEARubiquitination[1]
53EARKKALKLGAKKVFacetylation[2]
58ALKLGAKKVFIEDVSubiquitination[1]
112IAQREGAKYVSHGATacetylation[2]
112IAQREGAKYVSHGATubiquitination[1]
121VSHGATGKGNDQVRFacetylation[2]
121VSHGATGKGNDQVRFubiquitination[1]
140YSLAPQIKVIAPWRMubiquitination[1]
155PEFYNRFKGRNDLMEubiquitination[1]
165NDLMEYAKQHGIPIPacetylation[3]
165NDLMEYAKQHGIPIPubiquitination[1]
176IPIPVTPKSPWSMDEubiquitination[1]
199AGILENPKNQAPPGLubiquitination[1]
209APPGLYTKTQDPAKAubiquitination[1]
215TKTQDPAKAPNSPDVacetylation[3]
215TKTQDPAKAPNSPDVubiquitination[1]
228DVLEIEFKKGVPVKVacetylation[2]
228DVLEIEFKKGVPVKVubiquitination[1]
234FKKGVPVKVTNIKDGubiquitination[1]
239PVKVTNIKDGTTRTTacetylation[2]
239PVKVTNIKDGTTRTTubiquitination[1]
260YLNEVAGKHGVGRIDacetylation[2]
260YLNEVAGKHGVGRIDubiquitination[1]
277ENRFIGMKSRGIYETubiquitination[1]
310DREVRKIKQGLGLKFubiquitination[1]
340FVRHCIQKSQERVEGacetylation[2]
340FVRHCIQKSQERVEGubiquitination[1]
408EYHRLQSKVTAK***ubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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
 Is indirectly involved in the control of blood pressure (By similarity). 
Sequence Annotation
 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 (By similarity).
 BINDING 92 92 Citrulline (By similarity).
 BINDING 119 119 Aspartate (By similarity).
 BINDING 123 123 Aspartate (By similarity).
 BINDING 123 123 Citrulline (By similarity).
 BINDING 124 124 Aspartate (By similarity).
 BINDING 127 127 Citrulline (By similarity).
 BINDING 180 180 Citrulline (By similarity).
 BINDING 189 189 Citrulline (By similarity).
 BINDING 270 270 Citrulline (By similarity).
 BINDING 282 282 Citrulline (By similarity).
 MOD_RES 180 180 Phosphoserine (By similarity).  
Keyword
 Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; Nucleotide-binding; Phosphoprotein; Reference proteome; Urea cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 412 AA 
Protein Sequence
MSSKGSVVLA YSGGLDTSCI LVWLKEQGYD VIAYLANIGQ KEDFEEARKK ALKLGAKKVF 60
IEDVSKEFVE EFIWPAVQSS ALYEDRYLLG TSLARPCIAR RQVEIAQREG AKYVSHGATG 120
KGNDQVRFEL TCYSLAPQIK VIAPWRMPEF YNRFKGRNDL MEYAKQHGIP IPVTPKSPWS 180
MDENLMHISY EAGILENPKN QAPPGLYTKT QDPAKAPNSP DVLEIEFKKG VPVKVTNIKD 240
GTTRTTSLEL FMYLNEVAGK HGVGRIDIVE NRFIGMKSRG IYETPAGTIL YHAHLDIEAF 300
TMDREVRKIK QGLGLKFAEL VYTGFWHSPE CEFVRHCIQK SQERVEGKVQ VSVFKGQVYI 360
LGRESPLSLY NEELVSMNVQ GDYEPIDATG FININSLRLK EYHRLQSKVT AK 412 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0004055; F:argininosuccinate synthase activity; IEA:EC.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0000050; P:urea cycle; IEA:UniProtKB-UniPathway. 
Interpro
 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. 
Pfam
 PF00764; Arginosuc_synth 
SMART
  
PROSITE
 PS00564; ARGININOSUCCIN_SYN_1
 PS00565; ARGININOSUCCIN_SYN_2 
PRINTS