CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008904
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenylosuccinate lyase 
Protein Synonyms/Alias
 ASL; Adenylosuccinase; ASase 
Gene Name
 Adsl 
Gene Synonyms/Alias
 Adl 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
199ELRFRGVKGTTGTQAubiquitination[1]
218LFEGDHQKVEQLDKMubiquitination[1]
470EEVRPLLKPYGNEMAubiquitination[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
 Catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D- ribosyl)imidazole-4-carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate (By similarity). 
Sequence Annotation
 REGION 20 21 Substrate binding; shared with
 REGION 85 87 Substrate binding (By similarity).
 REGION 111 112 Substrate binding (By similarity).
 ACT_SITE 159 159 Proton donor/acceptor (By similarity).
 ACT_SITE 289 289 Proton donor/acceptor (By similarity).
 BINDING 241 241 Substrate (By similarity).
 BINDING 303 303 Substrate; shared with neighboring
 BINDING 329 329 Substrate (By similarity).
 BINDING 334 334 Substrate (By similarity).
 BINDING 338 338 Substrate (By similarity).
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 147 147 N6-acetyllysine (By similarity).
 MOD_RES 295 295 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Complete proteome; Lyase; Purine biosynthesis; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 484 AA 
Protein Sequence
MAASGDPGSA ESYRSPLAAR YASREMCFLF SDRYKFQTWR QLWLWLAEAE QTLGLPITDE 60
QIQEMKSNLN NIDFQMAAEE EKRLRHDVMA HVHTFGHCCP KAAGIIHLGA TSCYVGDNTD 120
LIILRNAFDL LLPKLARVIS RLADFAKDRA DLPTLGFTHF QPAQLTTVGK RCCLWIQDLC 180
MDLQNLKRVR DELRFRGVKG TTGTQASFLQ LFEGDHQKVE QLDKMVTEKA GFKRAFIITG 240
QTYTRKVDIE VLSVLASLGA SVHKICTDIR LLANLKEMEE PFEKQQIGSS AMPYKRNPMR 300
SERCCSLARH LMALTMDPLQ TASVQWFERT LDDSANRRIC LAEAFLTADT ILNTLQNISE 360
GLVVYPKVIE RRIRQELPFM ATENIIMAMV KAGGSRQDCH EKIRVLSQQA AAVVKQEGGD 420
NDLIERIRAD AYFSPIHSQL EHLLDPSSFT GRAPQQVHRF LEEEVRPLLK PYGNEMAVKA 480
ELCL 484 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity; IEA:EC.
 GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; ISA:MGI.
 GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0009060; P:aerobic respiration; IEA:Compara.
 GO:0006167; P:AMP biosynthetic process; ISA:MGI.
 GO:0051262; P:protein tetramerization; IEA:Compara.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0014850; P:response to muscle activity; IEA:Compara.
 GO:0007584; P:response to nutrient; IEA:Compara.
 GO:0042594; P:response to starvation; IEA:Compara. 
Interpro
 IPR019468; AdenyloSucc_lyase_C.
 IPR003031; D_crystallin.
 IPR024083; Fumarase/histidase_N.
 IPR000362; Fumarate_lyase.
 IPR020557; Fumarate_lyase_CS.
 IPR022761; Fumarate_lyase_N.
 IPR008948; L-Aspartase-like.
 IPR004769; Pur_lyase. 
Pfam
 PF10397; ADSL_C
 PF00206; Lyase_1 
SMART
 SM00998; ADSL_C 
PROSITE
 PS00163; FUMARATE_LYASES 
PRINTS
 PR00145; ARGSUCLYASE.
 PR00149; FUMRATELYASE.