CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-035837
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; IMP--aspartate ligase 2 
Gene Name
 Adss 
Gene Synonyms/Alias
 Adss2; Adss_predicted; rCG_20425 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
419ISNARTFKELPVNAQacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405
Functional Description
 Plays an important role in the de novo pathway and in the salvage pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP (By similarity). 
Sequence Annotation
 NP_BIND 39 45 GTP (By similarity).
 NP_BIND 67 69 GTP (By similarity).
 NP_BIND 362 364 GTP (By similarity).
 NP_BIND 444 447 GTP (By similarity).
 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
 Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium; Metal-binding; Nucleotide-binding; Purine biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 456 AA 
Protein Sequence
MSISESSPAA TSLPNGDCGR PRARPGGNRV TVVLGAQWGD EGKGKVVDLL AQDADIVCRC 60
QGGNNAGHTV VVDSVEYDFH LLPSGIINPN VTAFIGNGVV IHLPGLFEEA EKNVQKGKGL 120
DGWEKRLIIS DRAHIVFDFH QAADGIQEQQ RQEQAGKNLG TTKKGIGPVY SSKAARSGLR 180
MCDLVSDFDG FSERFKVLAN QYKSIYPTLE IDIEGELQQL KGYMERIKPM VRDGVYFLYE 240
ALHGPPKKIL VEGANAALLD IDFGTYPFVT SSNCTVGGVC TGLGMPPQNV GEVYGVVKAY 300
TTRVGIGAFP TEQDNEIGEL LQTRGREFGV TTGRKRRCGW LDLVLLKYAH MINGFTALAL 360
TKLDILDMFT EIKVGVAYKL DGETIPHFPA NQEVLNKVEV QYKTLPGWNT DISNARTFKE 420
LPVNAQNYVR FIEDELQIPV KWIGVGKSRE SMIQLF 456 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0004019; F:adenylosuccinate synthase activity; IDA:RGD.
 GO:0005525; F:GTP binding; IEA:HAMAP.
 GO:0000287; F:magnesium ion binding; IEA:HAMAP.
 GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006531; P:aspartate metabolic process; IDA:RGD.
 GO:0071257; P:cellular response to electrical stimulus; IEP:RGD.
 GO:0006184; P:GTP catabolic process; IDA:RGD.
 GO:0046040; P:IMP metabolic process; IDA:RGD.
 GO:0060359; P:response to ammonium ion; IEP:RGD.
 GO:0014074; P:response to purine-containing compound; IEP:RGD. 
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