CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011324
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Adenylosuccinate lyase 
Protein Synonyms/Alias
 ASL; Adenylosuccinase; ASase 
Gene Name
 ADE13 
Gene Synonyms/Alias
 YLR359W; L8039.12 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
196DIGLRGVKGTTGTQAubiquitination[1, 2, 3]
231TELLGFDKVYPVTGQacetylation[4]
273IRLLANLKEVEEPFEubiquitination[5]
281EVEEPFEKSQIGSSAacetylation[4]
292GSSAMAYKRNPMRCEacetylation[4]
456RAPQQVEKFVQKDVNacetylation[4]
471NALQPFQKYLNDEQVacetylation[4]
Reference
 [1] A proteomics approach to understanding protein ubiquitination.
 Peng J, Schwartz D, Elias JE, Thoreen CC, Cheng D, Marsischky G, Roelofs J, Finley D, Gygi SP.
 Nat Biotechnol. 2003 Aug;21(8):921-6. [PMID: 12872131]
 [2] Computational identification of ubiquitylation sites from protein sequences.
 Tung CW, Ho SY.
 BMC Bioinformatics. 2008 Jul 15;9:310. [PMID: 18625080]
 [3] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269]
 [4] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [5] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
  
Sequence Annotation
 REGION 14 15 Substrate binding; shared with
 REGION 82 84 Substrate binding (By similarity).
 REGION 108 109 Substrate binding (By similarity).
 ACT_SITE 156 156 Proton donor/acceptor (By similarity).
 ACT_SITE 286 286 Proton donor/acceptor (By similarity).
 BINDING 238 238 Substrate (By similarity).
 BINDING 300 300 Substrate; shared with neighboring
 BINDING 326 326 Substrate (By similarity).
 BINDING 331 331 Substrate (By similarity).
 BINDING 335 335 Substrate (By similarity).
 CROSSLNK 196 196 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Complete proteome; Isopeptide bond; Lyase; Purine biosynthesis; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 482 AA 
Protein Sequence
MPDYDNYTTP LSSRYASKEM SATFSLRNRF STWRKLWLNL AIAEKELGLT VVTDEAIEQM 60
RKHVEITDDE IAKASAQEAI VRHDVMAHVH TFGETCPAAA GIIHLGATSC FVTDNADLIF 120
IRDAYDIIIP KLVNVINRLA KFAMEYKDLP VLGWTHFQPA QLTTLGKRAT LWIQELLWDL 180
RNFERARNDI GLRGVKGTTG TQASFLALFH GNHDKVEALD ERVTELLGFD KVYPVTGQTY 240
SRKIDIDVLA PLSSFAATAH KMATDIRLLA NLKEVEEPFE KSQIGSSAMA YKRNPMRCER 300
VCSLARHLGS LFSDAVQTAS VQWFERTLDD SAIRRISLPS AFLTADILLS TLLNISSGLV 360
VYPKVIERRI KGELPFMATE NIIMAMVEKN ASRQEVHERI RVLSHQAAAV VKEEGGENDL 420
IERVKRDEFF KPIWEELDSL LEPSTFVGRA PQQVEKFVQK DVNNALQPFQ KYLNDEQVKL 480
NV 482 
Gene Ontology
 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; IMP:SGD.
 GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0006189; P:'de novo' IMP biosynthetic process; IMP:SGD. 
Interpro
 IPR019468; AdenyloSucc_lyase_C.
 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
 PR00149; FUMRATELYASE.