CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005889
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenylosuccinate synthetase isozyme 2 
Protein Synonyms/Alias
 AMPSase 2; AdSS 2; Adenylosuccinate synthetase, acidic isozyme; Adenylosuccinate synthetase, liver isozyme; L-type adenylosuccinate synthetase; IMP--aspartate ligase 2 
Gene Name
 ADSS 
Gene Synonyms/Alias
 ADSS2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
45WGDEGKGKVVDLLAQubiquitination[1, 2]
118EKNVQKGKGLEGWEKubiquitination[1]
125KGLEGWEKRLIISDRubiquitination[1]
164KNLGTTKKGIGPVYSubiquitination[2]
173IGPVYSSKAARSGLRubiquitination[1, 2, 3]
196DGFSERFKVLANQYKubiquitination[1]
203KVLANQYKSIYPTLEubiquitination[4]
226KLKGYMEKIKPMVRDubiquitination[1]
248ALHGPPKKILVEGANubiquitination[1]
403NKVEVQYKTLPGWNTubiquitination[4, 5, 6]
419ISNARAFKELPVNAQacetylation[2]
419ISNARAFKELPVNAQubiquitination[1, 2, 4, 5, 6, 7]
441DELQIPVKWIGVGKSubiquitination[1, 3, 5, 6]
447VKWIGVGKSRESMIQubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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] 
Functional Description
 Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. 
Sequence Annotation
 NP_BIND 39 45 GTP.
 NP_BIND 67 69 GTP.
 NP_BIND 362 364 GTP.
 NP_BIND 444 447 GTP.
 REGION 40 43 IMP binding (By similarity).
 REGION 65 68 IMP binding (By similarity).
 REGION 330 336 Substrate binding (By similarity).
 ACT_SITE 40 40 Proton acceptor (By similarity).
 ACT_SITE 68 68 Proton donor (By similarity).
 METAL 40 40 Magnesium (By similarity).
 METAL 67 67 Magnesium; via carbonyl oxygen (By
 BINDING 40 40 Substrate (By similarity).
 BINDING 162 162 IMP (By similarity).
 BINDING 176 176 IMP; shared with dimeric partner (By
 BINDING 255 255 IMP (By similarity).
 BINDING 270 270 IMP (By similarity).
 BINDING 334 334 IMP (By similarity).
 BINDING 336 336 GTP (By similarity).  
Keyword
 3D-structure; Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Polymorphism; Purine biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 456 AA 
Protein Sequence
MAFAETYPAA SSLPNGDCGR PRARPGGNRV TVVLGAQWGD EGKGKVVDLL AQDADIVCRC 60
QGGNNAGHTV VVDSVEYDFH LLPSGIINPN VTAFIGNGVV IHLPGLFEEA EKNVQKGKGL 120
EGWEKRLIIS DRAHIVFDFH QAADGIQEQQ RQEQAGKNLG TTKKGIGPVY SSKAARSGLR 180
MCDLVSDFDG FSERFKVLAN QYKSIYPTLE IDIEGELQKL KGYMEKIKPM VRDGVYFLYE 240
ALHGPPKKIL VEGANAALLD IDFGTYPFVT SSNCTVGGVC TGLGMPPQNV GEVYGVVKAY 300
TTRVGIGAFP TEQDNEIGEL LQTRGREFGV TTGRKRRCGW LDLVLLKYAH MINGFTALAL 360
TKLDILDMFT EIKVGVAYKL DGEIIPHIPA NQEVLNKVEV QYKTLPGWNT DISNARAFKE 420
LPVNAQNYVR FIEDELQIPV KWIGVGKSRE SMIQLF 456 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0004019; F:adenylosuccinate synthase activity; IDA:UniProtKB.
 GO:0005525; F:GTP binding; NAS:UniProtKB.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0042301; F:phosphate ion binding; NAS:UniProtKB.
 GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006167; P:AMP biosynthetic process; IDA:UniProtKB.
 GO:0006531; P:aspartate metabolic process; IEA:Compara.
 GO:0071257; P:cellular response to electrical stimulus; IEA:Compara.
 GO:0006184; P:GTP catabolic process; IEA:Compara.
 GO:0002376; P:immune system process; NAS:UniProtKB.
 GO:0046040; P:IMP metabolic process; IEA:Compara.
 GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
 GO:0060359; P:response to ammonium ion; IEA:Compara.
 GO:0014074; P:response to purine-containing compound; IEA:Compara. 
Interpro
 IPR018220; Adenylosuccinate_synthase_AS.
 IPR001114; Adenylosuccinate_synthetase.
 IPR027529; AdSS_2_vert.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00709; Adenylsucc_synt 
SMART
 SM00788; Adenylsucc_synt 
PROSITE
 PS01266; ADENYLOSUCCIN_SYN_1
 PS00513; ADENYLOSUCCIN_SYN_2 
PRINTS