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P05062

- ALDOB_HUMAN

UniProt

P05062 - ALDOB_HUMAN

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Protein

Fructose-bisphosphate aldolase B

Gene
ALDOB, ALDB
Organism
Homo sapiens (Human)
Status
Reviewed - 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-phosphate

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561Substrate
Binding sitei147 – 1471Substrate
Active sitei188 – 1881Proton acceptor By 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 binding Source: BHF-UCL
  4. fructose-bisphosphate aldolase activity Source: BHF-UCL
  5. identical protein binding Source: BHF-UCL
  6. protein binding Source: IntAct

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. positive regulation of ATPase activity Source: BHF-UCL
  10. small molecule metabolic process Source: Reactome
  11. 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.
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: 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: UniProt
  4. microtubule organizing center Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Hereditary fructose intolerance (HFI) [MIM:229600]: Autosomal 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.10 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti74 – 741I → T in HFI; affects proper folding. 1 Publication
VAR_020822
Natural varianti120 – 1212Missing in HFI.
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 – 11Removed1 Publication
Chaini2 – 364363Fructose-bisphosphate aldolase BPRO_0000216940Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei13 – 131N6-succinyllysine By similarity
Modified residuei36 – 361Phosphoserine By similarity
Modified residuei39 – 391Phosphothreonine By similarity
Modified residuei121 – 1211N6-succinyllysine By similarity
Modified residuei317 – 3171N6-succinyllysine By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP05062.
PaxDbiP05062.
PeptideAtlasiP05062.
PRIDEiP05062.

PTM databases

PhosphoSiteiP05062.

Expressioni

Gene expression databases

BgeeiP05062.
CleanExiHS_ALDOB.
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. 14 interactions.
STRINGi9606.ENSP00000363988.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP05062.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
HOGENOMiHOG000220876.
HOVERGENiHBG002386.
InParanoidiP05062.
KOiK01623.
OMAiDMEHCQY.
OrthoDBiEOG744T94.
PhylomeDBiP05062.
TreeFamiTF314203.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
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

MAHRFPALTQ EQKKELSEIA QSIVANGKGI LAADESVGTM GNRLQRIKVE    50
NTEENRRQFR EILFSVDSSI NQSIGGVILF HETLYQKDSQ GKLFRNILKE 100
KGIVVGIKLD QGGAPLAGTN KETTIQGLDG LSERCAQYKK DGVDFGKWRA 150
VLRIADQCPS SLAIQENANA LARYASICQQ NGLVPIVEPE VIPDGDHDLE 200
HCQYVTEKVL AAVYKALNDH HVYLEGTLLK PNMVTAGHAC TKKYTPEQVA 250
MATVTALHRT VPAAVPGICF LSGGMSEEDA TLNLNAINLC PLPKPWKLSF 300
SYGRALQASA LAAWGGKAAN KEATQEAFMK RAMANCQAAK GQYVHTGSSG 350
AASTQSLFTA CYTY 364
Length:364
Mass (Da):39,473
Last modified:January 23, 2007 - v2
Checksum:iDCE314E7AC5586CA
GO

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.
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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti54 – 541E → D in AAA51691. 1 Publication
Sequence conflicti250 – 2501A → D in CAA25072. 1 Publication
Sequence conflicti278 – 2781E → D in BAA00125. 1 Publication
Sequence conflicti309 – 3091S → V no nucleotide entry 1 Publication
Sequence conflicti348 – 3481S → C in BAA00125. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS6756.1.
PIRi A41505. ADHUB.
RefSeqi NP_000026.2. NM_000035.3.
UniGenei Hs.530274.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QO5 X-ray 2.50 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R 2-364 [» ]
1XDL X-ray 3.00 A/B/C/D/W/X/Y/Z 2-364 [» ]
1XDM X-ray 3.00 A/B/C/D/W/X/Y/Z 2-364 [» ]
ProteinModelPortali P05062.
SMRi P05062. Positions 2-361.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106730. 12 interactions.
IntActi P05062. 14 interactions.
STRINGi 9606.ENSP00000363988.

PTM databases

PhosphoSitei P05062.

Polymorphism databases

DMDMi 113611.

Proteomic databases

MaxQBi P05062.
PaxDbi P05062.
PeptideAtlasi P05062.
PRIDEi P05062.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374855 ; ENSP00000363988 ; ENSG00000136872 .
GeneIDi 229.
KEGGi hsa:229.
UCSCi uc004bbk.2. human.

Organism-specific databases

CTDi 229.
GeneCardsi GC09M104182.
H-InvDB HIX0125611.
HGNCi HGNC:417. ALDOB.
HPAi CAB020827.
HPA002198.
MIMi 229600. phenotype.
612724. gene.
neXtProti NX_P05062.
Orphaneti 469. Hereditary fructose intolerance.
PharmGKBi PA24710.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3588.
HOGENOMi HOG000220876.
HOVERGENi HBG002386.
InParanoidi P05062.
KOi K01623.
OMAi DMEHCQY.
OrthoDBi EOG744T94.
PhylomeDBi P05062.
TreeFami TF314203.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .
BioCyci MetaCyc:HS06234-MONOMER.
Reactomei REACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
REACT_1571. Fructose catabolism.
SABIO-RK P05062.

Miscellaneous databases

ChiTaRSi ALDOB. human.
EvolutionaryTracei P05062.
GeneWikii Aldolase_B.
GenomeRNAii 229.
NextBioi 930.
PROi P05062.
SOURCEi Search...

Gene expression databases

Bgeei P05062.
CleanExi HS_ALDOB.
Genevestigatori P05062.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view ]
Pfami PF00274. Glycolytic. 1 hit.
[Graphical view ]
PROSITEi PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(1984) [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(1985) [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(1984) [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(1987) [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(1986) [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(2004) [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(1989) [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. "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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
  12. "Molecular basis of hereditary fructose intolerance: mutations and polymorphisms in the human aldolase B gene."
    Tolan D.R.
    Hum. Mutat. 6:210-218(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  13. "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(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HFI PRO-150.
  14. Cited for: VARIANT HFI ASP-175.
  15. "A partially active mutant aldolase B from a patient with hereditary fructose intolerance."
    Brooks C.C., Tolan D.R.
    FASEB J. 8:107-113(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HFI ARG-135.
  16. "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(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ARG-148.
  17. "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(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HFI PRO-257.
  18. "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(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HFI LYS-335.
  19. "Screening for hereditary fructose intolerance mutations by reverse dot-blot."
    Lau J., Tolan D.R.
    Mol. Cell. Probes 13:35-40(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HFI PRO-150; ASP-175; PRO-257; TRP-304; LYS-335 AND VAL-338.
  20. "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(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HFI GLN-304 AND TRP-304, CHARACTERIZATION OF VARIANTS HFI GLN-304 AND TRP-304, KINETIC PARAMETERS.
  21. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HFI PRO-150; ASP-175; ARG-185 AND LYS-335.
  22. "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(2004) [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.
  23. "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(2005) [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: September 3, 2014
This is version 167 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

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