CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018562
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fructose-bisphosphate aldolase B 
Protein Synonyms/Alias
 Aldolase 2; Liver-type aldolase 
Gene Name
 Aldob 
Gene Synonyms/Alias
 Aldo2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
13PALTPEQKKELSEIAacetylation[1]
13PALTPEQKKELSEIAsuccinylation[1]
13PALTPEQKKELSEIAubiquitination[2]
14ALTPEQKKELSEIAQacetylation[3, 4]
14ALTPEQKKELSEIAQubiquitination[2]
28QRIVANGKGILAADEubiquitination[2]
48GNRLQRIKVENTEENacetylation[5, 6]
48GNRLQRIKVENTEENubiquitination[2]
99NLFRNVLKEKGIVVGacetylation[5, 6]
101FRNVLKEKGIVVGIKubiquitination[2]
108KGIVVGIKLDQGGAPacetylation[3]
108KGIVVGIKLDQGGAPubiquitination[2]
121APLAGTNKETTIQGLacetylation[1, 3, 4, 5]
121APLAGTNKETTIQGLsuccinylation[1]
121APLAGTNKETTIQGLubiquitination[2]
140ERCAQYKKDGVDFGKubiquitination[2]
147KDGVDFGKWRAVLRIacetylation[3, 5, 6, 7]
147KDGVDFGKWRAVLRIphosphoglycerylation[8]
147KDGVDFGKWRAVLRIubiquitination[2]
230YLEGTLLKPNMVTAGacetylation[5]
230YLEGTLLKPNMVTAGubiquitination[2]
242TAGHACTKKYTPEQVubiquitination[2]
243AGHACTKKYTPEQVAphosphoglycerylation[8]
243AGHACTKKYTPEQVAubiquitination[2]
317ALAAWGGKAANKKATacetylation[1]
317ALAAWGGKAANKKATsuccinylation[1]
317ALAAWGGKAANKKATubiquitination[2]
322GGKAANKKATQEAFMubiquitination[2]
330ATQEAFMKRAMANCQacetylation[1, 5, 9]
330ATQEAFMKRAMANCQsuccinylation[1]
330ATQEAFMKRAMANCQubiquitination[2]
Reference
 [1] 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]
 [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] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [5] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [6] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [7] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [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]
 [9] 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
Functional Description
  
Sequence Annotation
 ACT_SITE 188 188 Proton acceptor (By similarity).
 ACT_SITE 230 230 Schiff-base intermediate with
 BINDING 56 56 Substrate.
 BINDING 147 147 Substrate.
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 36 36 Phosphoserine.  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; Glycolysis; Lyase; Phosphoprotein; Reference proteome; Schiff base. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 364 AA 
Protein Sequence
MAHRFPALTP EQKKELSEIA QRIVANGKGI LAADESVGTM GNRLQRIKVE NTEENRRQFR 60
ELLFSVDNSI SQSIGGVILF HETLYQKDSQ GNLFRNVLKE KGIVVGIKLD QGGAPLAGTN 120
KETTIQGLDG LSERCAQYKK DGVDFGKWRA VLRIADQCPS SLAIQENANA LARYASICQQ 180
NGLVPIVEPE VLPDGDHDLE HCQYVSEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC 240
TKKYTPEQVA MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINRC PLPRPWKLSF 300
SYGRALQASA LAAWGGKAAN KKATQEAFMK RAMANCQAAQ GQYVHTGSSG AAATQSLFTA 360
SYTY 364 
Gene Ontology
 GO:0034451; C:centriolar satellite; IEA:Compara.
 GO:0070061; F:fructose binding; IEA:Compara.
 GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:EC.
 GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:Compara.
 GO:0006000; P:fructose metabolic process; IEA:Compara.
 GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway.
 GO:0006116; P:NADH oxidation; IEA:Compara.
 GO:0032781; P:positive regulation of ATPase activity; IEA:Compara.
 GO:0070072; P:vacuolar proton-transporting V-type ATPase complex assembly; IEA:Compara. 
Interpro
 IPR000741; Aldolase_I.
 IPR013785; Aldolase_TIM. 
Pfam
 PF00274; Glycolytic 
SMART
  
PROSITE
 PS00158; ALDOLASE_CLASS_I 
PRINTS