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P05062

- ALDOB_HUMAN

UniProt

P05062 - ALDOB_HUMAN

Protein

Fructose-bisphosphate aldolase B

Gene

ALDOB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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 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

    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

    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.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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-acetylalanineBy similarity
    Modified residuei13 – 131N6-succinyllysineBy similarity
    Modified residuei36 – 361PhosphoserineBy similarity
    Modified residuei39 – 391PhosphothreonineBy similarity
    Modified residuei121 – 1211N6-succinyllysineBy similarity
    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.
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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

    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.
    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:
    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

    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: October 1, 2014
    This is version 168 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