CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038357
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Adenylosuccinate lyase 
Protein Synonyms/Alias
  
Gene Name
 Adsl 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
132SRLADFAKDRADLPTacetylation[1]
184ELRFRGVKGTTGTQAubiquitination[2]
203LFEGDHQKVEQLDKMubiquitination[2]
269EMEEPFEKQQIGSSAacetylation[3]
280GSSAMPYKRNPMRSEacetylation[1, 4]
400QQAAAVVKQEGGDNDacetylation[3]
455EEVRPLLKPYGNEMAubiquitination[2]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] 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]
 [3] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [4] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 469 AA 
Protein Sequence
MAASGDPGSA ESYRSPLAAR YASREMCFLF SDRYKFQTWR QLWLWLAEAE QTLGLPITDE 60
QIQEMKSNLN NIDFQMAAEE EKRLRHDVMA HVHTFGHCCP KAAGIIHLGA TSCYVGDNTL 120
ARVISRLADF AKDRADLPTL GFTHFQPAQL TTVGKRCCLW IQDLCMDLQN LKRVRDELRF 180
RGVKGTTGTQ ASFLQLFEGD HQKVEQLDKM VTEKAGFKRA FIITGQTYTR KVDIEVLSVL 240
ASLGASVHKI CTDIRLLANL KEMEEPFEKQ QIGSSAMPYK RNPMRSERCC SLARHLMALT 300
MDPLQTASVQ WFERTLDDSA NRRICLAEAF LTADTILNTL QNISEGLVVY PKVIERRIRQ 360
ELPFMATENI IMAMVKAGGS RQDCHEKIRV LSQQAAAVVK QEGGDNDLIE RIRADAYFSP 420
IHSQLEHLLD PSSFTGRAPQ QVHRFLEEEV RPLLKPYGNE MAVKAELCL 469 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; ISA:MGI.
 GO:0006167; P:AMP biosynthetic process; ISA:MGI. 
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.