CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-029202
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fructose-bisphosphate aldolase 
Protein Synonyms/Alias
  
Gene Name
 Aldoa 
Gene Synonyms/Alias
 mCG_22383 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
68ALTPEQKKELSDIAHacetylation[1]
68ALTPEQKKELSDIAHubiquitination[2]
82HRIVAPGKGILAADEubiquitination[2]
96ESTGSIAKRLQSIGTacetylation[1, 3, 4, 5, 6]
96ESTGSIAKRLQSIGTsuccinylation[6]
96ESTGSIAKRLQSIGTubiquitination[2]
141FHETLYQKADDGRPFubiquitination[2]
153RPFPQVIKSKGGVVGacetylation[6]
153RPFPQVIKSKGGVVGsuccinylation[6]
153RPFPQVIKSKGGVVGubiquitination[2]
155FPQVIKSKGGVVGIKubiquitination[2]
162KGGVVGIKVDKGVVPacetylation[6]
162KGGVVGIKVDKGVVPubiquitination[2]
165VVGIKVDKGVVPLAGacetylation[5, 6]
165VVGIKVDKGVVPLAGubiquitination[2]
194ERCAQYKKDGADFAKubiquitination[2]
201KDGADFAKWRCVLKIacetylation[1, 4, 5, 6]
201KDGADFAKWRCVLKIubiquitination[2]
207AKWRCVLKIGEHTPSacetylation[1, 7]
207AKWRCVLKIGEHTPSubiquitination[2]
254PDGDHDLKRCQYVTEacetylation[5]
254PDGDHDLKRCQYVTEphosphoglycerylation[8]
254PDGDHDLKRCQYVTEubiquitination[2]
262RCQYVTEKVLAAVYKubiquitination[2]
284YLEGTLLKPNMVTPGacetylation[4, 6]
284YLEGTLLKPNMVTPGubiquitination[2]
348INKCPLLKPWALTFSacetylation[1, 6]
348INKCPLLKPWALTFSsuccinylation[6]
366ALQASALKAWGGKKEacetylation[4, 6]
366ALQASALKAWGGKKEsuccinylation[6]
366ALQASALKAWGGKKEubiquitination[2]
371ALKAWGGKKENLKAAubiquitination[2]
372LKAWGGKKENLKAAQubiquitination[2]
376GGKKENLKAAQEEYIacetylation[5, 6]
376GGKKENLKAAQEEYIsuccinylation[6]
376GGKKENLKAAQEEYIubiquitination[2]
384AAQEEYIKRALANSLacetylation[1, 4, 6]
384AAQEEYIKRALANSLsuccinylation[6]
384AAQEEYIKRALANSLubiquitination[2]
396NSLACQGKYTPSGQSubiquitination[2]
Reference
 [1] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [7] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [8] Functional lysine modification by an intrinsically reactive primary glycolytic metabolite.
 Moellering RE, Cravatt BF.
 Science. 2013 Aug 2;341(6145):549-53. [PMID: 23908237
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Glycolysis; Lyase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 418 AA 
Protein Sequence
MATRRPDGSS FNMTRLSLAL AFSFPPVASE QPHSELGNTQ QQTELGKEST ATGTMPHPYP 60
ALTPEQKKEL SDIAHRIVAP GKGILAADES TGSIAKRLQS IGTENTEENR RFYRQLLLTA 120
DDRVNPCIGG VILFHETLYQ KADDGRPFPQ VIKSKGGVVG IKVDKGVVPL AGTNGETTTQ 180
GLDGLSERCA QYKKDGADFA KWRCVLKIGE HTPSALAIME NANVLARYAS ICQQNGIVPI 240
VEPEILPDGD HDLKRCQYVT EKVLAAVYKA LSDHHVYLEG TLLKPNMVTP GHACTQKFSN 300
EEIAMATVTA LRRTVPPAVT GVTFLSGGQS EEEASINLNA INKCPLLKPW ALTFSYGRAL 360
QASALKAWGG KKENLKAAQE EYIKRALANS LACQGKYTPS GQSGAAASES LFISNHAY 418 
Gene Ontology
 GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:EC.
 GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway. 
Interpro
 IPR000741; Aldolase_I.
 IPR013785; Aldolase_TIM. 
Pfam
 PF00274; Glycolytic 
SMART
  
PROSITE
 PS00158; ALDOLASE_CLASS_I 
PRINTS