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ALDOB (aldolase B, fructose-bisphosphate)

Written2008-11Shian-Yang Peng, Hey-Chi Hsu
Department of General Education, National Taipei College of Nursing, Taipei 100, Taiwan, ROC (SYP); Department of Pathology, National Taiwan University Hospital, 7 Chung-Shan South Road, Taipei 100, Taiwan, ROC (HCH)

(Note : for Links provided by Atlas : click)


HGNC Previous name"aldolase B, fructose-bisphosphate"
LocusID (NCBI) 229
Atlas_Id 44287
Location 9q31.1  [Link to chromosome band 9q31]
Location_base_pair Starts at 101420560 and ends at 101435774 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping ALDOB.png]
Local_order Telomeric to the PRG-3 (plasticity related gene 3), BAAT (bile acid Coenzyme A: amino acid N-acyltransferase), MRPL50 (mitochondrial ribosomal protein L50) and ZNF189 (zinc finger protein 189) genes. Centrimic to C9orf125 (chromosome 9 open reading frame 125), RNF20 (ring finger protein 20), PP3R2 (protein phosphatase 3 regulatory subunit B, beta isoform ) and GRIN3A (glutamate receptor, ionotropic, N-methyl-D-aspartate 3) genes.Those genes are clustered within a genomic region at 102,830K-103,540K bp of chromosome 9q.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
INS-IGF2 (11p15.5) / ALDOB (9q31.1)SERPINA1 (14q32.13) / ALDOB (9q31.1)SNX30 (9q32) / ALDOB (9q31.1)
TXNL4B (16q22.2) / ALDOB (9q31.1)


Note Locus Tag: RP11-490D19.1.
  Genomic organization of ALDOB gene on chromosome 9q21.3 - q22.2. Exons are represented by boxes on the diagram.
Description ALDOB encompasses 14,448 base pairs of genomic DNA on the long arm of chromosome 9 in the telomere- to- centromere orientation. (NCBI Entrez Gene, NC-000009.10, 19-Nov-2008.)
The gene consists of 9 exons, with 115, 122, 212, 55, 161, 84, 193, 200, 526 base pairs, respectively.
Transcription ALDOB encodes a 1669 bp mRNA, the coding region is from 126bp to 1220bp of the mRNA.
Exon 1 and the 3' part of exon 9 of the ALDOB gene are non-coding.
Pseudogene None.


Note Names : aldolase B, Fructose-bisphosphate.
Other Names : aldolase 2, Liver-type aldolase.
Description The 1095 bps open reading frame of ALDOB encodes a 364 amino acids protein with a calculated molecular weight of 39.3kDa.
The functional Aldolase B is a homotetramer. According to the three-dimensional structures of aldolase B homotetramers, the active sites of each monomer locate at the center of the alpha/beta barrels, while the C terminus of the protein is involed in determining the isozyme-specific activity of aldolase. Four isozyme specific regions (ISR) of aldolase B were determined, the first three are expressed by exon 3 of the human aldolase gene, the fourth locates at the C-terminal region.
Expression There are three genetically distinct and tissue-specific isozymes of fructose-biphosphate aldolase (EC-Number ) class-I in mammals. The A isozyme(aldolase A) is expressed mainly in muscle, the B isozyme(aldolase B) in the liver, kidney, stomach and intestine, and the C isozyme (aldolase C) in the brain, heart and ovary. Aldolase B is the only expressed isoform in highly differentiated hepatocytes. The high level of gene expression results from cooperation between a liver-specific promoter and an intronic enhancer.
Localisation Cytoplasm and perinuclear membrane of hepatocytes.
Function All the three aldolase isozymes catalyze the reversible cleavage of fructose-1,6-(bis) phosphate (FBP) or fructose 1-phosphate (F1P) to dihydroxyacetone phosphate and either glyceraldehyde- 3-phosphate or glyceraldehyde, respectively. Aldolase B has equal activity toward substrate F1P and FBP, and is involved in the two opposite metabolic pathways, glycolysis and gluconeogenesis. Aldolase isozymes utilize covalent catalysis through a Schiff base in the active site of the enzyme, but exhibit distinct catalytic properties. The Schiff-base lysine is located in the central cavity of the barrel. The enzymatic active sites at aldolose B protein sequence are: Arg 55 and Lys146 for binding of c-1-phosphate group of the substrate; Lys 299, the Schiff base for dihydroxyacetone-p; Try 363 for enzymatic activity toward fructose 1,6- bisphosphate site; Asp33, Glu187 and Lys229 residues for catalytic function.
Homology The three human aldolase isozymes are similar in sequence with 66% identity between human A and B, 68% identity between B and C, and 78% identity between A and C. Aldolase molecules have seven major conserved common sequence (CCS-1 to -7), that are the constituents forming a basal alpha/beta barrel structure, are conserved in all aldolase molecules beyond isozyme groups. All isozymes have strictly conserved residues in the active site consisting of Asp33, Arg42, Lys107, Lys146, Glu187, Ser271, Arg303, and Lys229.
The identities of aldolase B between human and other animal species are shown bellow. Protein sequences of the mammalian aldolase B are highly conserved.
[Pongo abelii] aldolase B, fructose-bisphosphate (364/364, 100%)
[Pan troglodytes] aldolase B, fructose-bisphosphate (363/364, 99% identity)
[Rattus norvegicus] Aldob, aldolase B fructose-bisphosphate (349/364, 95% identity)
[Mus musculus] Aldob, aldolase B, fructose-bisphosphate (349/364, 95% identity)
[Bos taurus] aldolase B, fructose-bisphosphate (334/364, 91% identity)
[Canis lupus familiaris] aldolase B, fructose-bisphosphate (334/364, 91% identity)
[Ovis aries] aldolase B (333/364, 91% identity)
[Macaca mulatta] aldolase B (333/364, 91% identity)
[Gallus gallus] aldolase B, fructose-bisphosphate (294/364, 80% identity)
[Danio rerio] aldob, aldolase b, fructose-bisphosphate (277/364, 76% identity)
[Salmo salar] aldolase B (266/365, 72% identity)


  Types of mutation related to Hereditary fructose intolerance (HFI).
c. means cDNA coding region mutations, g. means genome mutations and p. refers to protein change after nucleotide mutation. IVS (intervening sequence) refers to introns.
Germinal Recessively inherited mutations in the ALDOB gene, that caused catalytic deficiency of aldolase B, have been found in hereditary fructose intolerance (HFI). Many types of mutation in human ALDOB gene were reported, including missense mutations, nonsense mutations, deletions, insertions and mutation at the splicing regions (list in the diagram above). The mutations bring about reduced enzyme activity and affect structural stability. Mutants that retained tetrameric structure but with altered kinetic properties would reduce its catalytic activity. Mutants with homotetramers dissociated into subunits would have more severe impaired enzymatic activity. The three most common sites are: p.A150P (64%), p.A175D (16%) and p.N335K (5%).
Somatic Human cancer result from the genetic mutation of ALDOB was not reported so far.

Implicated in

Entity Hereditary fructose intolerance (HFI)
Disease An autosomal recessive disease that results in the inability to metabolize fructose and related sugars. When fructose, sucrose, or sorbitol was taken from the diet, affected patients suffer from vomiting, abdominal pain, hypoglycemia. Continued ingestion of noxious sugars leads to hepatic and renal injury, which eventually leads to liver cirrhosis and growth retardation.
Prognosis Complete exclusion of fructose, sucrose, and sorbitol from the diet results in dramatic recovery if liver and kidney damage is not irreversible.
Oncogenesis Not found
Entity Hepatocellular cellular carcinoma (HCC)
Note Aldolase B is the only expressed isoenzymes of aldolase in highly differentiated hepatocytes.
The mRNA of aldolase B was downexpressed in HCC patients detected by northern blot or RT-PCR, and it was also undetectable or expressed at very low levels in the hepatocellular carcinoma (HA22T, SKHep, HCC36, PLC/PLZ/5 and Hep3B) and hepatoblastoma (HepG2) cell lines.
Disease Hepatocellular carcinoma (HCC) is an aggressive malignancy with a poor prognosis.
Down-regulation of ALDOB was detected in patients of HCC and is associated with advanced disease, ETR and poor prognosis. A dramatic down-regulation of ALDOB was found in 116 of 203 HCCs (57%), while 43% of HCCs maintained the expression. The ALDOB down-regulation correlated with high-grade (grade II-IV) HCC (p<0.0001), portal vein invasion ((stage IIIB-IV) (p<1x10-6), early tumor recurrence (ETR) (p<0.001)) and a lower 5-year survival (p=0.000001).
Prognosis In stage II HCC which had no vascular invasion, the ALDOB down-regulation was associated with ETR (p<0.05) and a lower 5-year survival (p=0.015), and ALDOB down-regulation in stage II HCC is a predictive marker of ETR and an unfavorable outcome.


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This paper should be referenced as such :
Peng, SY ; Hsu, HC
ALDOB (aldolase B, fructose-bisphosphate)
Atlas Genet Cytogenet Oncol Haematol. 2009;13(10):704-708.
Free journal version : [ pdf ]   [ DOI ]

Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 1 ]
  t(9;9)(q31;q32) SNX30/ALDOB

External links

HGNC (Hugo)ALDOB   417
Entrez_Gene (NCBI)ALDOB    "aldolase, fructose-bisphosphate B"
AliasesALDB; ALDO2
GeneCards (Weizmann)ALDOB
Ensembl hg19 (Hinxton)ENSG00000136872 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000136872 [Gene_View]  ENSG00000136872 [Sequence]  chr9:101420560-101435774 [Contig_View]  ALDOB [Vega]
ICGC DataPortalENSG00000136872
Genatlas (Paris)ALDOB
Genetics Home Reference (NIH)ALDOB
Genomic and cartography
GoldenPath hg38 (UCSC)ALDOB  -     chr9:101420560-101435774 -  9q31.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)ALDOB  -     9q31.1   [Description]    (hg19-Feb_2009)
GoldenPathALDOB - 9q31.1 [CytoView hg19]  ALDOB - 9q31.1 [CytoView hg38]
genome Data Viewer NCBIALDOB [Mapview hg19]  
OMIM229600   612724   
Gene and transcription
Genbank (Entrez)AK026411 AK290795 AV645373 AV656265 AW242415
RefSeq transcript (Entrez)NM_000035
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)ALDOB
Alternative Splicing GalleryENSG00000136872
Gene Expression Viewer (FireBrowse)ALDOB [ Firebrowse - Broad ]
GenevisibleExpression of ALDOB in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)229
GTEX Portal (Tissue expression)ALDOB
Human Protein AtlasENSG00000136872-ALDOB [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP05062   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP05062  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP05062
Splice isoforms : SwissVarP05062
Catalytic activity : Enzyme4.1.2.13 [ Enzyme-Expasy ] [ IntEnz-EBI ] [ BRENDA ] [ KEGG ]   [ MEROPS ]
Domaine pattern : Prosite (Expaxy)ALDOLASE_CLASS_I (PS00158)   
Domains : Interpro (EBI)Aldolase_I_AS    Aldolase_TIM    FBA_I   
Domain families : Pfam (Sanger)Glycolytic (PF00274)   
Domain families : Pfam (NCBI)pfam00274   
Conserved Domain (NCBI)ALDOB
Blocks (Seattle)ALDOB
PDB (RSDB)1QO5    1XDL    1XDM   
PDB Europe1QO5    1XDL    1XDM   
PDB (PDBSum)1QO5    1XDL    1XDM   
PDB (IMB)1QO5    1XDL    1XDM   
Structural Biology KnowledgeBase1QO5    1XDL    1XDM   
SCOP (Structural Classification of Proteins)1QO5    1XDL    1XDM   
CATH (Classification of proteins structures)1QO5    1XDL    1XDM   
Human Protein Atlas [tissue]ENSG00000136872-ALDOB [tissue]
Peptide AtlasP05062
IPIIPI00218407   IPI00942961   IPI00513830   
Protein Interaction databases
IntAct (EBI)P05062
Ontologies - Pathways
Ontology : AmiGO"fructose-bisphosphate aldolase activity  fructose-bisphosphate aldolase activity  protein binding  microtubule organizing center  cytosol  cytosol  fructose metabolic process  gluconeogenesis  glycolytic process  glycolytic process  NADH oxidation  cytoskeletal protein binding  fructose 1,6-bisphosphate metabolic process  fructose 1,6-bisphosphate metabolic process  positive regulation of ATPase activity  centriolar satellite  identical protein binding  ATPase binding  fructose-1-phosphate aldolase activity  fructose-1-phosphate aldolase activity  canonical glycolysis  fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate  fructose binding  extracellular exosome  vacuolar proton-transporting V-type ATPase complex assembly"  
Ontology : EGO-EBI"fructose-bisphosphate aldolase activity  fructose-bisphosphate aldolase activity  protein binding  microtubule organizing center  cytosol  cytosol  fructose metabolic process  gluconeogenesis  glycolytic process  glycolytic process  NADH oxidation  cytoskeletal protein binding  fructose 1,6-bisphosphate metabolic process  fructose 1,6-bisphosphate metabolic process  positive regulation of ATPase activity  centriolar satellite  identical protein binding  ATPase binding  fructose-1-phosphate aldolase activity  fructose-1-phosphate aldolase activity  canonical glycolysis  fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate  fructose binding  extracellular exosome  vacuolar proton-transporting V-type ATPase complex assembly"  
Pathways : KEGGGlycolysis / Gluconeogenesis    Pentose phosphate pathway    Fructose and mannose metabolism   
REACTOMEP05062 [protein]
REACTOME PathwaysR-HSA-70350 [pathway]   
Atlas of Cancer Signalling NetworkALDOB
Wikipedia pathwaysALDOB
Orthology - Evolution
GeneTree (enSembl)ENSG00000136872
Phylogenetic Trees/Animal Genes : TreeFamALDOB
Homologs : HomoloGeneALDOB
Homology/Alignments : Family Browser (UCSC)ALDOB
Gene fusions - Rearrangements
Fusion : MitelmanSNX30/ALDOB [9q32/9q31.1]  
Fusion PortalSNX30 9q32 ALDOB 9q31.1 PRAD
Fusion : FusionGDB4.1.2.13   
Fusion : QuiverALDOB
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerALDOB [hg38]
Exome Variant ServerALDOB
GNOMAD BrowserENSG00000136872
Varsome BrowserALDOB
Genomic Variants (DGV)ALDOB [DGVbeta]
DECIPHERALDOB [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisALDOB 
ICGC Data PortalALDOB 
TCGA Data PortalALDOB 
Broad Tumor PortalALDOB
OASIS PortalALDOB [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICALDOB  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DALDOB
Mutations and Diseases : HGMDALDOB
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch ALDOB
DgiDB (Drug Gene Interaction Database)ALDOB
DoCM (Curated mutations)ALDOB (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)ALDOB (select a term)
NCG6 (London) select ALDOB
Cancer3DALDOB(select the gene name)
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
OMIM229600    612724   
Genetic Testing Registry ALDOB
NextProtP05062 [Medical]
Target ValidationALDOB
Huge Navigator ALDOB [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTD
Pharm GKB GenePA24710
Clinical trialALDOB
canSAR (ICR)ALDOB (select the gene name)
DataMed IndexALDOB
Other databaseProteinatlas
PubMed65 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Fri Feb 19 17:45:28 CET 2021

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