Tag | Content |
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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 |
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18 | PPGTGGVKRGRLQQE | ubiquitination | [1] | 48 | WGDEGKGKVVDLLAT | ubiquitination | [1] | 158 | QRQAQEGKNIGTTKK | ubiquitination | [1] | 174 | IGPTYSSKAARTGLR | ubiquitination | [1] | 410 | YETLPGWKADTTGAR | ubiquitination | [1] |
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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. |
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