CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005699
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenylosuccinate synthetase isozyme 1 
Protein Synonyms/Alias
 AMPSase 1; AdSS 1; Adenylosuccinate synthetase, basic isozyme; Adenylosuccinate synthetase, muscle isozyme; M-type adenylosuccinate synthetase; IMP--aspartate ligase 1 
Gene Name
 Adssl1 
Gene Synonyms/Alias
 Adss1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
18PPGTGGVKRGRLQQEubiquitination[1]
48WGDEGKGKVVDLLATubiquitination[1]
158QRQAQEGKNIGTTKKubiquitination[1]
174IGPTYSSKAARTGLRubiquitination[1]
410YETLPGWKADTTGARubiquitination[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
Functional Description
 Component of the purine nucleotide cycle (PNC), which interconverts IMP and AMP to regulate the nucleotide levels in various tissues, and which contributes to glycolysis and ammoniagenesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. 
Sequence Annotation
 NP_BIND 42 48 GTP.
 NP_BIND 70 72 GTP.
 NP_BIND 363 365 GTP.
 NP_BIND 445 448 GTP.
 REGION 43 46 IMP binding.
 REGION 68 71 IMP binding.
 REGION 331 337 Substrate binding.
 ACT_SITE 43 43 Proton acceptor (By similarity).
 ACT_SITE 71 71 Proton donor (By similarity).
 METAL 43 43 Magnesium.
 METAL 70 70 Magnesium; via carbonyl oxygen.
 BINDING 43 43 Substrate.
 BINDING 163 163 IMP.
 BINDING 177 177 IMP; shared with dimeric partner.
 BINDING 256 256 IMP.
 BINDING 271 271 IMP.
 BINDING 335 335 IMP.
 BINDING 337 337 GTP.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium; Membrane; Metal-binding; Nucleotide-binding; Purine biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 457 AA 
Protein Sequence
MSGTRASNDR PPGTGGVKRG RLQQEAAATG SRVTVVLGAQ WGDEGKGKVV DLLATDADIV 60
SRCQGGNNAG HTVVVDGKEY DFHLLPSGII NTKAVSFIGN GVVIHLPGLF EEAEKNEKKG 120
LKDWEKRLII SDRAHLVFDF HQAVDGLQEV QRQAQEGKNI GTTKKGIGPT YSSKAARTGL 180
RICDLLSDFD EFSARFKNLA HQHQSMFPTL EIDVEGQLKR LKGFAERIRP MVRDGVYFMY 240
EALHGPPKKV LVEGANAALL DIDFGTYPFV TSSNCTVGGV CTGLGIPPQN IGDVYGVVKA 300
YTTRVGIGAF PTEQINEIGD LLQNRGHEWG VTTGRKRRCG WLDLMILRYA HMVNGFTALA 360
LTKLDILDVL SEIKVGISYK LNGKRIPYFP ANQEILQKVE VEYETLPGWK ADTTGARKWE 420
DLPPQAQSYV RFVENHMGVA VKWVGVGKSR ESMIQLF 457 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
 GO:0004019; F:adenylosuccinate synthase activity; IDA:MGI.
 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:0006163; P:purine nucleotide metabolic process; IDA:MGI. 
Interpro
 IPR018220; Adenylosuccinate_synthase_AS.
 IPR001114; Adenylosuccinate_synthetase.
 IPR027509; AdSS_1_vert.
 IPR027417; P-loop_NTPase. 
Pfam
 PF00709; Adenylsucc_synt 
SMART
 SM00788; Adenylsucc_synt 
PROSITE
 PS01266; ADENYLOSUCCIN_SYN_1
 PS00513; ADENYLOSUCCIN_SYN_2 
PRINTS