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Protein

Fructose-bisphosphate aldolase B

Gene

ALDOB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Kineticsi

  1. KM=1.6 µM for fructose 1,6-bisphosphate1 Publication
  2. KM=2.3 mM for fructose 1-phosphate1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561Substrate
Binding sitei147 – 1471Substrate
Active sitei188 – 1881Proton acceptorBy similarity
Active sitei230 – 2301Schiff-base intermediate with dihydroxyacetone-P
Sitei364 – 3641Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

GO - Molecular functioni

  1. ATPase binding Source: BHF-UCL
  2. cytoskeletal protein binding Source: BHF-UCL
  3. fructose-1-phosphate aldolase activity Source: MGI
  4. fructose binding Source: BHF-UCL
  5. fructose-bisphosphate aldolase activity Source: BHF-UCL
  6. identical protein binding Source: BHF-UCL

GO - Biological processi

  1. carbohydrate metabolic process Source: Reactome
  2. fructose 1,6-bisphosphate metabolic process Source: BHF-UCL
  3. fructose catabolic process Source: Reactome
  4. fructose metabolic process Source: BHF-UCL
  5. gluconeogenesis Source: Reactome
  6. glucose metabolic process Source: Reactome
  7. glycolytic process Source: BHF-UCL
  8. NADH oxidation Source: BHF-UCL
  9. pathogenesis Source: Reactome
  10. positive regulation of ATPase activity Source: BHF-UCL
  11. small molecule metabolic process Source: Reactome
  12. vacuolar proton-transporting V-type ATPase complex assembly Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciMetaCyc:HS06234-MONOMER.
BRENDAi4.1.2.13. 2681.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
REACT_1571. Fructose catabolism.
SABIO-RKP05062.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase B (EC:4.1.2.13)
Alternative name(s):
Liver-type aldolase
Gene namesi
Name:ALDOB
Synonyms:ALDB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:417. ALDOB.

Subcellular locationi

Cytoplasmcytoskeletonmicrotubule organizing centercentrosomecentriolar satellite 1 Publication

GO - Cellular componenti

  1. centriolar satellite Source: BHF-UCL
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. microtubule organizing center Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Hereditary fructose intolerance (HFI)10 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAutosomal recessive disease that results in an inability to metabolize fructose and related sugars. Complete exclusion of fructose results in dramatic recovery; however, if not treated properly, HFI subjects suffer episodes of hypoglycemia, general ill condition, and risk of death the remainder of life.

See also OMIM:229600
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 741I → T in HFI; affects proper folding. 1 Publication
VAR_020822
Natural varianti120 – 1212Missing in HFI. 1 Publication
VAR_020823
Natural varianti135 – 1351C → R in HFI; America; partial activity. 1 Publication
VAR_000551
Natural varianti150 – 1501A → P in HFI; frequent mutation. 5 Publications
Corresponds to variant rs1800546 [ dbSNP | Ensembl ].
VAR_000553
Natural varianti175 – 1751A → D in HFI; frequent mutation. 5 Publications
Corresponds to variant rs76917243 [ dbSNP | Ensembl ].
VAR_000554
Natural varianti178 – 1781C → R in HFI. 1 Publication
VAR_058211
Natural varianti185 – 1851P → R in HFI. 1 Publication
VAR_020824
Natural varianti222 – 2221V → F in HFI; affects proper folding. 1 Publication
VAR_020826
Natural varianti229 – 2291L → P in HFI; affects proper folding. 1 Publication
VAR_020827
Natural varianti257 – 2571L → P in HFI; Italy. 3 Publications
VAR_000555
Natural varianti284 – 2841L → P in HFI. 1 Publication
VAR_058212
Natural varianti304 – 3041R → Q in HFI; 100-fold decrease in catalytic efficiency for substrates FBP and F1P. 1 Publication
Corresponds to variant rs145078268 [ dbSNP | Ensembl ].
VAR_020828
Natural varianti304 – 3041R → W in HFI; Turkey; 4800-fold decrease in catalytic efficiency for FBP and inactive with F1P. 2 Publications
VAR_000556
Natural varianti335 – 3351N → K in HFI; frequent mutation. 5 Publications
VAR_000557
Natural varianti338 – 3381A → V in HFI; Turkey and South Europe. 2 Publications
VAR_000558

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi229600. phenotype.
Orphaneti469. Hereditary fructose intolerance.
PharmGKBiPA24710.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity1 Publication
Chaini2 – 364363Fructose-bisphosphate aldolase BPRO_0000216940Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei13 – 131N6-succinyllysineBy similarity
Modified residuei36 – 361Phosphoserine1 Publication
Modified residuei39 – 391Phosphothreonine1 Publication
Modified residuei89 – 891Phosphoserine1 Publication
Modified residuei119 – 1191Phosphothreonine1 Publication
Modified residuei121 – 1211N6-succinyllysineBy similarity
Modified residuei132 – 1321Phosphoserine1 Publication
Modified residuei272 – 2721Phosphoserine1 Publication
Modified residuei276 – 2761Phosphoserine1 Publication
Modified residuei309 – 3091Phosphoserine1 Publication
Modified residuei317 – 3171N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP05062.
PaxDbiP05062.
PeptideAtlasiP05062.
PRIDEiP05062.

PTM databases

PhosphoSiteiP05062.

Expressioni

Gene expression databases

BgeeiP05062.
CleanExiHS_ALDOB.
ExpressionAtlasiP05062. baseline and differential.
GenevestigatoriP05062.

Organism-specific databases

HPAiCAB020827.
HPA002198.

Interactioni

Subunit structurei

Homotetramer. Interacts with BBS1, BBS2, BBS4 and BBS7.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BBS1Q8NFJ94EBI-1045507,EBI-1805484
BBS2Q9BXC94EBI-1045507,EBI-748297
BBS4Q96RK44EBI-1045507,EBI-1805814
BBS7Q8IWZ64EBI-1045507,EBI-1806001

Protein-protein interaction databases

BioGridi106730. 12 interactions.
IntActiP05062. 28 interactions.
STRINGi9606.ENSP00000363988.

Structurei

Secondary structure

1
364
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2314Combined sources
Turni25 – 273Combined sources
Beta strandi29 – 335Combined sources
Helixi37 – 4610Combined sources
Helixi53 – 6412Combined sources
Helixi68 – 725Combined sources
Beta strandi74 – 796Combined sources
Helixi83 – 853Combined sources
Turni89 – 913Combined sources
Helixi94 – 1007Combined sources
Beta strandi104 – 1085Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi123 – 1253Combined sources
Helixi131 – 14010Combined sources
Beta strandi145 – 1528Combined sources
Helixi161 – 17919Combined sources
Turni180 – 1823Combined sources
Beta strandi184 – 1918Combined sources
Helixi199 – 21921Combined sources
Helixi224 – 2263Combined sources
Helixi246 – 26015Combined sources
Beta strandi267 – 2715Combined sources
Helixi277 – 28913Combined sources
Beta strandi290 – 2923Combined sources
Beta strandi296 – 3038Combined sources
Helixi304 – 3063Combined sources
Helixi308 – 3147Combined sources
Helixi318 – 3203Combined sources
Helixi321 – 33818Combined sources
Turni339 – 3413Combined sources
Helixi351 – 3544Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QO5X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R2-364[»]
1XDLX-ray3.00A/B/C/D/W/X/Y/Z2-364[»]
1XDMX-ray3.00A/B/C/D/W/X/Y/Z2-364[»]
ProteinModelPortaliP05062.
SMRiP05062. Positions 2-361.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05062.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP05062.
KOiK01623.
OMAiRAMANCQ.
OrthoDBiEOG744T94.
PhylomeDBiP05062.
TreeFamiTF314203.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05062-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAHRFPALTQ EQKKELSEIA QSIVANGKGI LAADESVGTM GNRLQRIKVE
60 70 80 90 100
NTEENRRQFR EILFSVDSSI NQSIGGVILF HETLYQKDSQ GKLFRNILKE
110 120 130 140 150
KGIVVGIKLD QGGAPLAGTN KETTIQGLDG LSERCAQYKK DGVDFGKWRA
160 170 180 190 200
VLRIADQCPS SLAIQENANA LARYASICQQ NGLVPIVEPE VIPDGDHDLE
210 220 230 240 250
HCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC TKKYTPEQVA
260 270 280 290 300
MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF
310 320 330 340 350
SYGRALQASA LAAWGGKAAN KEATQEAFMK RAMANCQAAK GQYVHTGSSG
360
AASTQSLFTA CYTY
Length:364
Mass (Da):39,473
Last modified:January 23, 2007 - v2
Checksum:iDCE314E7AC5586CA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541E → D in AAA51691 (PubMed:3016456).Curated
Sequence conflicti250 – 2501A → D in CAA25072 (PubMed:6689266).Curated
Sequence conflicti278 – 2781E → D in BAA00125 (PubMed:2830249).Curated
Sequence conflicti309 – 3091S → V no nucleotide entry (PubMed:6585824).Curated
Sequence conflicti348 – 3481S → C in BAA00125 (PubMed:2830249).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 741I → T in HFI; affects proper folding. 1 Publication
VAR_020822
Natural varianti120 – 1212Missing in HFI. 1 Publication
VAR_020823
Natural varianti134 – 1341R → S.
Corresponds to variant rs10123355 [ dbSNP | Ensembl ].
VAR_038429
Natural varianti135 – 1351C → R in HFI; America; partial activity. 1 Publication
VAR_000551
Natural varianti148 – 1481W → R in one subject with fructose intolerance; rare variant; America. 1 Publication
VAR_000552
Natural varianti150 – 1501A → P in HFI; frequent mutation. 5 Publications
Corresponds to variant rs1800546 [ dbSNP | Ensembl ].
VAR_000553
Natural varianti175 – 1751A → D in HFI; frequent mutation. 5 Publications
Corresponds to variant rs76917243 [ dbSNP | Ensembl ].
VAR_000554
Natural varianti178 – 1781C → R in HFI. 1 Publication
VAR_058211
Natural varianti185 – 1851P → R in HFI. 1 Publication
VAR_020824
Natural varianti207 – 2071E → Q.
Corresponds to variant rs3739721 [ dbSNP | Ensembl ].
VAR_020825
Natural varianti222 – 2221V → F in HFI; affects proper folding. 1 Publication
VAR_020826
Natural varianti229 – 2291L → P in HFI; affects proper folding. 1 Publication
VAR_020827
Natural varianti257 – 2571L → P in HFI; Italy. 3 Publications
VAR_000555
Natural varianti268 – 2681I → N.
Corresponds to variant rs10989495 [ dbSNP | Ensembl ].
VAR_038430
Natural varianti284 – 2841L → P in HFI. 1 Publication
VAR_058212
Natural varianti304 – 3041R → Q in HFI; 100-fold decrease in catalytic efficiency for substrates FBP and F1P. 1 Publication
Corresponds to variant rs145078268 [ dbSNP | Ensembl ].
VAR_020828
Natural varianti304 – 3041R → W in HFI; Turkey; 4800-fold decrease in catalytic efficiency for FBP and inactive with F1P. 2 Publications
VAR_000556
Natural varianti335 – 3351N → K in HFI; frequent mutation. 5 Publications
VAR_000557
Natural varianti338 – 3381A → V in HFI; Turkey and South Europe. 2 Publications
VAR_000558

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02747 mRNA. Translation: CAA26526.1.
D00183 Genomic DNA. Translation: BAA00125.1.
M15656, M15657 Genomic DNA. Translation: AAA51691.1.
AL353621 Genomic DNA. Translation: CAI14614.1.
CH471105 Genomic DNA. Translation: EAW58951.1.
X00270 mRNA. Translation: CAA25072.1.
X01098 mRNA. Translation: CAA25572.1.
CCDSiCCDS6756.1.
PIRiA41505. ADHUB.
RefSeqiNP_000026.2. NM_000035.3.
UniGeneiHs.530274.

Genome annotation databases

EnsembliENST00000374855; ENSP00000363988; ENSG00000136872.
GeneIDi229.
KEGGihsa:229.
UCSCiuc004bbk.2. human.

Polymorphism databases

DMDMi113611.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X02747 mRNA. Translation: CAA26526.1.
D00183 Genomic DNA. Translation: BAA00125.1.
M15656, M15657 Genomic DNA. Translation: AAA51691.1.
AL353621 Genomic DNA. Translation: CAI14614.1.
CH471105 Genomic DNA. Translation: EAW58951.1.
X00270 mRNA. Translation: CAA25072.1.
X01098 mRNA. Translation: CAA25572.1.
CCDSiCCDS6756.1.
PIRiA41505. ADHUB.
RefSeqiNP_000026.2. NM_000035.3.
UniGeneiHs.530274.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QO5X-ray2.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R2-364[»]
1XDLX-ray3.00A/B/C/D/W/X/Y/Z2-364[»]
1XDMX-ray3.00A/B/C/D/W/X/Y/Z2-364[»]
ProteinModelPortaliP05062.
SMRiP05062. Positions 2-361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106730. 12 interactions.
IntActiP05062. 28 interactions.
STRINGi9606.ENSP00000363988.

PTM databases

PhosphoSiteiP05062.

Polymorphism databases

DMDMi113611.

Proteomic databases

MaxQBiP05062.
PaxDbiP05062.
PeptideAtlasiP05062.
PRIDEiP05062.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374855; ENSP00000363988; ENSG00000136872.
GeneIDi229.
KEGGihsa:229.
UCSCiuc004bbk.2. human.

Organism-specific databases

CTDi229.
GeneCardsiGC09M104182.
H-InvDBHIX0125611.
HGNCiHGNC:417. ALDOB.
HPAiCAB020827.
HPA002198.
MIMi229600. phenotype.
612724. gene.
neXtProtiNX_P05062.
Orphaneti469. Hereditary fructose intolerance.
PharmGKBiPA24710.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP05062.
KOiK01623.
OMAiRAMANCQ.
OrthoDBiEOG744T94.
PhylomeDBiP05062.
TreeFamiTF314203.

Enzyme and pathway databases

UniPathwayiUPA00109; UER00183.
BioCyciMetaCyc:HS06234-MONOMER.
BRENDAi4.1.2.13. 2681.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
REACT_1571. Fructose catabolism.
SABIO-RKP05062.

Miscellaneous databases

ChiTaRSiALDOB. human.
EvolutionaryTraceiP05062.
GeneWikiiAldolase_B.
GenomeRNAii229.
NextBioi930.
PROiP05062.
SOURCEiSearch...

Gene expression databases

BgeeiP05062.
CleanExiHS_ALDOB.
ExpressionAtlasiP05062. baseline and differential.
GenevestigatoriP05062.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and nucleotide sequence of a full-length cDNA coding for aldolase B from human liver."
    Paolella G., Santamaria R., Izzo P., Costanzo P., Salvatore F.
    Nucleic Acids Res. 12:7401-7410(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Human aldolase isozyme gene: the structure of multispecies aldolase B mRNAs."
    Sakakibara M., Mukai T., Yatsuki H., Hori K.
    Nucleic Acids Res. 13:5055-5069(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Complete amino acid sequence for human aldolase B derived from cDNA and genomic clones."
    Rottmann W.H., Tolan D.R., Penhoet E.E.
    Proc. Natl. Acad. Sci. U.S.A. 81:2738-2742(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  4. "Human aldolase B gene: characterization of the genomic aldolase B gene and analysis of sequences required for multiple polyadenylations."
    Mukai T., Yatsuki H., Arai Y., Joh K., Matsuhashi S., Hori K.
    J. Biochem. 102:1043-1051(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Characterization of the human aldolase B gene."
    Tolan D.R., Penhoet E.E.
    Mol. Biol. Med. 3:245-264(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "Construction and expression of human aldolase A and B expression plasmids in Escherichia coli host."
    Sakakibara M., Takahashi I., Takasaki Y., Mukai T., Hori K.
    Biochim. Biophys. Acta 1007:334-342(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-33 AND 357-364.
  9. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 238-364.
  10. Cited for: INTERACTION WITH BBS1; BBS2; BBS4 AND BBS7, SUBCELLULAR LOCATION.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-39; SER-89; THR-119; SER-132; SER-272; SER-276 AND SER-309, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "The structure of human liver fructose-1,6-bisphosphate aldolase."
    Dalby A.R., Tolan D.R., Littlechild J.A.
    Acta Crystallogr. D 57:1526-1533(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  13. "Molecular basis of hereditary fructose intolerance: mutations and polymorphisms in the human aldolase B gene."
    Tolan D.R.
    Hum. Mutat. 6:210-218(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  14. "Catalytic deficiency of human aldolase B in hereditary fructose intolerance caused by a common missense mutation."
    Cross N.C.P., Tolan D.R., Cox T.M.
    Cell 53:881-885(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HFI PRO-150.
  15. Cited for: VARIANT HFI ASP-175.
  16. "A partially active mutant aldolase B from a patient with hereditary fructose intolerance."
    Brooks C.C., Tolan D.R.
    FASEB J. 8:107-113(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HFI ARG-135.
  17. "Diverse mutations in the aldolase B gene that underlie the prevalence of hereditary fructose intolerance."
    Ali M., Cox T.M.
    Am. J. Hum. Genet. 56:1002-1005(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-148.
  18. "Identification of a novel mutation (Leu 256-->Pro) in the human aldolase B gene associated with hereditary fructose intolerance."
    Ali M., Sebastio G., Cox T.M.
    Hum. Mol. Genet. 3:203-204(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HFI PRO-257.
  19. "A new aldolase B variant, N334K, is a common cause of hereditary fructose intolerance in Yugoslavia."
    Cross N.C.P., Stojanov L.M., Cox T.M.
    Nucleic Acids Res. 18:1925-1925(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HFI LYS-335.
  20. "Screening for hereditary fructose intolerance mutations by reverse dot-blot."
    Lau J., Tolan D.R.
    Mol. Cell. Probes 13:35-40(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HFI PRO-150; ASP-175; PRO-257; TRP-304; LYS-335 AND VAL-338.
  21. "Functional and molecular modelling studies of two hereditary fructose intolerance-causing mutations at arginine 303 in human liver aldolase."
    Santamaria R., Esposito G., Vitagliano L., Race V., Paglionico I., Zancan L., Zagari A., Salvatore F.
    Biochem. J. 350:823-828(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HFI GLN-304 AND TRP-304, CHARACTERIZATION OF VARIANTS HFI GLN-304 AND TRP-304, KINETIC PARAMETERS.
  22. "Molecular analysis of the aldolase B gene in patients with hereditary fructose intolerance from Spain."
    Sanchez-Gutierrez J.C., Benlloch T., Leal M.A., Samper B., Garcia-Ripoll I., Feliu J.E.
    J. Med. Genet. 39:E56-E56(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HFI PRO-150; ASP-175; ARG-185 AND LYS-335.
  23. "Six novel alleles identified in Italian hereditary fructose intolerance patients enlarge the mutation spectrum of the aldolase B gene."
    Esposito G., Santamaria R., Vitagliano L., Ieno L., Viola A., Fiori L., Parenti G., Zancan L., Zagari A., Salvatore F.
    Hum. Mutat. 24:534-534(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HFI THR-74; 120-ASN-LYS-121 DEL; PRO-150; ASP-175; PHE-222; PRO-229; PRO-257; LYS-335 AND VAL-338, CHARACTERIZATION OF VARIANTS HFI THR-74; PHE-222 AND PRO-229.
  24. "The spectrum of aldolase B (ALDOB) mutations and the prevalence of hereditary fructose intolerance in Central Europe."
    Santer R., Rischewski J., von Weihe M., Niederhaus M., Schneppenheim S., Baerlocher K., Kohlschuetter A., Muntau A., Posselt H.-G., Steinmann B., Schneppenheim R.
    Hum. Mutat. 25:594-594(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HFI PRO-150; ASP-175; ARG-178; PRO-284 AND LYS-335.

Entry informationi

Entry nameiALDOB_HUMAN
AccessioniPrimary (citable) accession number: P05062
Secondary accession number(s): Q13741, Q13742, Q5T7D6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 173 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

In vertebrates, 3 forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.