CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004232
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fructose-bisphosphate aldolase 
Protein Synonyms/Alias
 FBP aldolase; FBPA; Fructose-1,6-bisphosphate aldolase 
Gene Name
 FBA1 
Gene Synonyms/Alias
 YKL060C; YKL320 
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
27HNLFTYAKEHKFAIPacetylation[1]
27HNLFTYAKEHKFAIPubiquitination[2]
30FTYAKEHKFAIPAINacetylation[1]
30FTYAKEHKFAIPAINubiquitination[3]
55LEAARDSKSPIILQTacetylation[1]
73GAAYFAGKGISNEGQacetylation[1]
73GAAYFAGKGISNEGQubiquitination[2, 3]
85EGQNASIKGAIAAAHacetylation[1]
85EGQNASIKGAIAAAHubiquitination[2, 3]
114LHSDHCAKKLLPWFDacetylation[1]
199DKEDLYTKPEQVYNVacetylation[1]
246EILAEHQKYTREQVGubiquitination[3]
255TREQVGCKEEKPLFLubiquitination[2, 3]
258QVGCKEEKPLFLVFHacetylation[1]
258QVGCKEEKPLFLVFHubiquitination[2, 4]
307IRDYVLNKKDYIMSPacetylation[1]
307IRDYVLNKKDYIMSPubiquitination[3]
308RDYVLNKKDYIMSPVacetylation[1]
308RDYVLNKKDYIMSPVubiquitination[2]
323GNPEGPEKPNKKFFDacetylation[1]
323GNPEGPEKPNKKFFDubiquitination[2]
326EGPEKPNKKFFDPRVacetylation[1]
326EGPEKPNKKFFDPRVubiquitination[2, 3]
327GPEKPNKKFFDPRVWacetylation[1]
345GEKTMGAKITKSLETubiquitination[3]
348TMGAKITKSLETFRTacetylation[1]
348TMGAKITKSLETFRTubiquitination[3]
Reference
 [1] 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]
 [2] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047]
 [3] 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, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [4] 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
Functional Description
 Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3- phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis (By similarity). 
Sequence Annotation
 REGION 266 268 Dihydroxyacetone phosphate binding (By
 REGION 287 290 Dihydroxyacetone phosphate binding (By
 ACT_SITE 110 110 Proton donor (By similarity).
 METAL 111 111 Zinc 1; catalytic (By similarity).
 METAL 145 145 Zinc 2 (By similarity).
 METAL 175 175 Zinc 2 (By similarity).
 METAL 227 227 Zinc 1; catalytic (By similarity).
 METAL 265 265 Zinc 1; catalytic (By similarity).
 BINDING 63 63 Glyceraldehyde 3-phosphate (By
 BINDING 228 228 Dihydroxyacetone phosphate; via amide
 MOD_RES 11 11 Phosphothreonine.
 MOD_RES 56 56 Phosphoserine.
 MOD_RES 63 63 Phosphoserine.
 MOD_RES 76 76 Phosphoserine.
 MOD_RES 83 83 Phosphoserine.
 MOD_RES 96 96 Phosphoserine.
 MOD_RES 147 147 Phosphoserine.
 MOD_RES 150 150 Phosphothreonine.
 MOD_RES 179 179 Phosphothreonine.
 MOD_RES 290 290 Phosphothreonine.
 MOD_RES 310 310 Phosphotyrosine.
 MOD_RES 313 313 Phosphoserine.  
Keyword
 Complete proteome; Direct protein sequencing; Glycolysis; Lyase; Metal-binding; Phosphoprotein; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 359 AA 
Protein Sequence
MGVEQILKRK TGVIVGEDVH NLFTYAKEHK FAIPAINVTS SSTAVAALEA ARDSKSPIIL 60
QTSNGGAAYF AGKGISNEGQ NASIKGAIAA AHYIRSIAPA YGIPVVLHSD HCAKKLLPWF 120
DGMLEADEAY FKEHGEPLFS SHMLDLSEET DEENISTCVK YFKRMAAMDQ WLEMEIGITG 180
GEEDGVNNEN ADKEDLYTKP EQVYNVYKAL HPISPNFSIA AAFGNCHGLY AGDIALRPEI 240
LAEHQKYTRE QVGCKEEKPL FLVFHGGSGS TVQEFHTGID NGVVKVNLDT DCQYAYLTGI 300
RDYVLNKKDY IMSPVGNPEG PEKPNKKFFD PRVWVREGEK TMGAKITKSL ETFRTTNTL 359 
Gene Ontology
 GO:0005829; C:cytosol; IDA:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0004332; F:fructose-bisphosphate aldolase activity; IMP:SGD.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006094; P:gluconeogenesis; IMP:SGD.
 GO:0006096; P:glycolysis; IMP:SGD. 
Interpro
 IPR013785; Aldolase_TIM.
 IPR006411; Fruct_bisP_bact.
 IPR000771; Ketose_bisP_aldolase_II. 
Pfam
 PF01116; F_bP_aldolase 
SMART
  
PROSITE
 PS00602; ALDOLASE_CLASS_II_1
 PS00806; ALDOLASE_CLASS_II_2 
PRINTS