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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: glycolysis

    This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase (GPI)
    3. ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase, liver type (PFKL), ATP-dependent 6-phosphofructokinase, platelet type (PFKP), ATP-dependent 6-phosphofructokinase, muscle type (PFKM)
    4. Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase C (ALDOC), Fructose-bisphosphate aldolase (HEL-S-87p), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase B (ALDOB), Fructose-bisphosphate aldolase A (ALDOA), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOC)
    This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei56Substrate1
    Binding sitei147Substrate1
    Active sitei188Proton acceptorBy similarity1
    Active sitei230Schiff-base intermediate with dihydroxyacetone-P1
    Sitei364Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate1

    GO - Molecular functioni

    • ATPase binding Source: BHF-UCL
    • cytoskeletal protein binding Source: BHF-UCL
    • fructose-1-phosphate aldolase activity Source: MGI
    • fructose binding Source: BHF-UCL
    • fructose-bisphosphate aldolase activity Source: BHF-UCL
    • identical protein binding Source: BHF-UCL

    GO - Biological processi

    • canonical glycolysis Source: Reactome
    • fructose 1,6-bisphosphate metabolic process Source: BHF-UCL
    • fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate Source: Reactome
    • fructose metabolic process Source: BHF-UCL
    • gluconeogenesis Source: Reactome
    • glycolytic process Source: BHF-UCL
    • NADH oxidation Source: BHF-UCL
    • positive regulation of ATPase activity Source: BHF-UCL
    • 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.
    ZFISH:HS06234-MONOMER.
    BRENDAi4.1.2.13. 2681.
    ReactomeiR-HSA-70171. Glycolysis.
    R-HSA-70263. Gluconeogenesis.
    R-HSA-70350. 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
    Proteomesi
    • UP000005640 Componenti: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:417. ALDOB.

    Subcellular locationi

    GO - Cellular componenti

    • centriolar satellite Source: BHF-UCL
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • microtubule organizing center Source: BHF-UCL
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Hereditary fructose intolerance (HFI)11 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)DescriptionActionsGraphical viewLength
    Natural variantiVAR_07534846R → W in HFI; reduced enzymatic activity. 1 PublicationCorresponds to variant rs41281039dbSNPEnsembl.1
    Natural variantiVAR_02082274I → T in HFI; affects proper folding. 1 PublicationCorresponds to variant rs781023784dbSNPEnsembl.1
    Natural variantiVAR_020823120 – 121Missing in HFI. 1 Publication2
    Natural variantiVAR_000551135C → R in HFI; America; partial activity. 1 Publication1
    Natural variantiVAR_000553150A → P in HFI; frequent mutation. 6 PublicationsCorresponds to variant rs1800546dbSNPEnsembl.1
    Natural variantiVAR_000554175A → D in HFI; frequent mutation. 6 PublicationsCorresponds to variant rs76917243dbSNPEnsembl.1
    Natural variantiVAR_058211178C → R in HFI. 1 Publication1
    Natural variantiVAR_020824185P → R in HFI. 1 Publication1
    Natural variantiVAR_020826222V → F in HFI; affects proper folding. 1 Publication1
    Natural variantiVAR_020827229L → P in HFI; affects proper folding. 1 Publication1
    Natural variantiVAR_000555257L → P in HFI; Italy. 3 PublicationsCorresponds to variant rs764701775dbSNPEnsembl.1
    Natural variantiVAR_058212284L → P in HFI. 1 Publication1
    Natural variantiVAR_020828304R → Q in HFI; 100-fold decrease in catalytic efficiency for substrates FBP and F1P. 1 PublicationCorresponds to variant rs145078268dbSNPEnsembl.1
    Natural variantiVAR_000556304R → W in HFI; Turkey; 4800-fold decrease in catalytic efficiency for FBP and inactive with F1P. 2 PublicationsCorresponds to variant rs555935217dbSNPEnsembl.1
    Natural variantiVAR_000557335N → K in HFI; frequent mutation. 5 PublicationsCorresponds to variant rs78340951dbSNPEnsembl.1
    Natural variantiVAR_000558338A → V in HFI; Turkey and South Europe. 2 PublicationsCorresponds to variant rs77718928dbSNPEnsembl.1
    Natural variantiVAR_075349343Y → H in HFI; almost no effect on enzymatic activity at 30 degrees Celsius, but reduced activity at higher temperatures. 1 PublicationCorresponds to variant rs369586696dbSNPEnsembl.1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi229.
    MalaCardsiALDOB.
    MIMi229600. phenotype.
    OpenTargetsiENSG00000136872.
    Orphaneti469. Hereditary fructose intolerance.
    PharmGKBiPA24710.

    Polymorphism and mutation databases

    BioMutaiALDOB.
    DMDMi113611.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedBy similarity1 Publication
    ChainiPRO_00002169402 – 364Fructose-bisphosphate aldolase BAdd BLAST363

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylalanineBy similarity1
    Modified residuei13N6-succinyllysineBy similarity1
    Modified residuei36PhosphoserineCombined sources1
    Modified residuei39PhosphothreonineCombined sources1
    Modified residuei89PhosphoserineCombined sources1
    Modified residuei119PhosphothreonineCombined sources1
    Modified residuei121N6-succinyllysineBy similarity1
    Modified residuei132PhosphoserineCombined sources1
    Modified residuei272PhosphoserineCombined sources1
    Modified residuei276PhosphoserineCombined sources1
    Modified residuei299PhosphoserineBy similarity1
    Modified residuei301PhosphoserineBy similarity1
    Modified residuei309PhosphoserineCombined sources1
    Modified residuei317N6-succinyllysineBy similarity1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiP05062.
    MaxQBiP05062.
    PaxDbiP05062.
    PeptideAtlasiP05062.
    PRIDEiP05062.

    PTM databases

    iPTMnetiP05062.
    PhosphoSitePlusiP05062.

    Expressioni

    Gene expression databases

    BgeeiENSG00000136872.
    CleanExiHS_ALDOB.
    ExpressionAtlasiP05062. baseline and differential.
    GenevisibleiP05062. HS.

    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

    GO - Molecular functioni

    • ATPase binding Source: BHF-UCL
    • cytoskeletal protein binding Source: BHF-UCL
    • identical protein binding Source: BHF-UCL

    Protein-protein interaction databases

    BioGridi106730. 13 interactors.
    IntActiP05062. 28 interactors.
    STRINGi9606.ENSP00000363988.

    Structurei

    Secondary structure

    1364
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi10 – 23Combined sources14
    Turni25 – 27Combined sources3
    Beta strandi29 – 33Combined sources5
    Helixi37 – 46Combined sources10
    Helixi53 – 64Combined sources12
    Helixi68 – 72Combined sources5
    Beta strandi74 – 79Combined sources6
    Helixi83 – 85Combined sources3
    Turni89 – 91Combined sources3
    Helixi94 – 100Combined sources7
    Beta strandi104 – 108Combined sources5
    Beta strandi113 – 115Combined sources3
    Beta strandi119 – 121Combined sources3
    Beta strandi123 – 125Combined sources3
    Helixi131 – 140Combined sources10
    Beta strandi145 – 152Combined sources8
    Helixi161 – 179Combined sources19
    Turni180 – 182Combined sources3
    Beta strandi184 – 191Combined sources8
    Helixi199 – 219Combined sources21
    Helixi224 – 226Combined sources3
    Helixi246 – 260Combined sources15
    Beta strandi267 – 271Combined sources5
    Helixi277 – 289Combined sources13
    Beta strandi290 – 292Combined sources3
    Beta strandi296 – 303Combined sources8
    Helixi304 – 306Combined sources3
    Helixi308 – 314Combined sources7
    Helixi318 – 320Combined sources3
    Helixi321 – 338Combined sources18
    Turni339 – 341Combined sources3
    Helixi351 – 354Combined sources4

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05062.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1557. Eukaryota.
    COG3588. LUCA.
    GeneTreeiENSGT00390000010235.
    HOGENOMiHOG000220876.
    HOVERGENiHBG002386.
    InParanoidiP05062.
    KOiK01623.
    OMAiANCQAAQ.
    OrthoDBiEOG091G0A9T.
    PhylomeDBiP05062.
    TreeFamiTF314203.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR029768. Aldolase_I_AS.
    IPR013785. 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

            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)DescriptionActionsGraphical viewLength
    Sequence conflicti54E → D in AAA51691 (PubMed:3016456).Curated1
    Sequence conflicti250A → D in CAA25072 (PubMed:6689266).Curated1
    Sequence conflicti278E → D in BAA00125 (PubMed:2830249).Curated1
    Sequence conflicti309S → V no nucleotide entry (PubMed:6585824).Curated1
    Sequence conflicti348S → C in BAA00125 (PubMed:2830249).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_07534846R → W in HFI; reduced enzymatic activity. 1 PublicationCorresponds to variant rs41281039dbSNPEnsembl.1
    Natural variantiVAR_02082274I → T in HFI; affects proper folding. 1 PublicationCorresponds to variant rs781023784dbSNPEnsembl.1
    Natural variantiVAR_020823120 – 121Missing in HFI. 1 Publication2
    Natural variantiVAR_038429134R → S.Corresponds to variant rs10123355dbSNPEnsembl.1
    Natural variantiVAR_000551135C → R in HFI; America; partial activity. 1 Publication1
    Natural variantiVAR_000552148W → R in one subject with fructose intolerance; rare variant; America. 1 PublicationCorresponds to variant rs118204430dbSNPEnsembl.1
    Natural variantiVAR_000553150A → P in HFI; frequent mutation. 6 PublicationsCorresponds to variant rs1800546dbSNPEnsembl.1
    Natural variantiVAR_000554175A → D in HFI; frequent mutation. 6 PublicationsCorresponds to variant rs76917243dbSNPEnsembl.1
    Natural variantiVAR_058211178C → R in HFI. 1 Publication1
    Natural variantiVAR_020824185P → R in HFI. 1 Publication1
    Natural variantiVAR_020825207E → Q.Corresponds to variant rs3739721dbSNPEnsembl.1
    Natural variantiVAR_020826222V → F in HFI; affects proper folding. 1 Publication1
    Natural variantiVAR_020827229L → P in HFI; affects proper folding. 1 Publication1
    Natural variantiVAR_000555257L → P in HFI; Italy. 3 PublicationsCorresponds to variant rs764701775dbSNPEnsembl.1
    Natural variantiVAR_038430268I → N.Corresponds to variant rs10989495dbSNPEnsembl.1
    Natural variantiVAR_058212284L → P in HFI. 1 Publication1
    Natural variantiVAR_020828304R → Q in HFI; 100-fold decrease in catalytic efficiency for substrates FBP and F1P. 1 PublicationCorresponds to variant rs145078268dbSNPEnsembl.1
    Natural variantiVAR_000556304R → W in HFI; Turkey; 4800-fold decrease in catalytic efficiency for FBP and inactive with F1P. 2 PublicationsCorresponds to variant rs555935217dbSNPEnsembl.1
    Natural variantiVAR_000557335N → K in HFI; frequent mutation. 5 PublicationsCorresponds to variant rs78340951dbSNPEnsembl.1
    Natural variantiVAR_000558338A → V in HFI; Turkey and South Europe. 2 PublicationsCorresponds to variant rs77718928dbSNPEnsembl.1
    Natural variantiVAR_075349343Y → H in HFI; almost no effect on enzymatic activity at 30 degrees Celsius, but reduced activity at higher temperatures. 1 PublicationCorresponds to variant rs369586696dbSNPEnsembl.1

    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.3. human.

    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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi106730. 13 interactors.
    IntActiP05062. 28 interactors.
    STRINGi9606.ENSP00000363988.

    PTM databases

    iPTMnetiP05062.
    PhosphoSitePlusiP05062.

    Polymorphism and mutation databases

    BioMutaiALDOB.
    DMDMi113611.

    Proteomic databases

    EPDiP05062.
    MaxQBiP05062.
    PaxDbiP05062.
    PeptideAtlasiP05062.
    PRIDEiP05062.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000374855; ENSP00000363988; ENSG00000136872.
    GeneIDi229.
    KEGGihsa:229.
    UCSCiuc004bbk.3. human.

    Organism-specific databases

    CTDi229.
    DisGeNETi229.
    GeneCardsiALDOB.
    H-InvDBHIX0125611.
    HGNCiHGNC:417. ALDOB.
    HPAiCAB020827.
    HPA002198.
    MalaCardsiALDOB.
    MIMi229600. phenotype.
    612724. gene.
    neXtProtiNX_P05062.
    OpenTargetsiENSG00000136872.
    Orphaneti469. Hereditary fructose intolerance.
    PharmGKBiPA24710.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1557. Eukaryota.
    COG3588. LUCA.
    GeneTreeiENSGT00390000010235.
    HOGENOMiHOG000220876.
    HOVERGENiHBG002386.
    InParanoidiP05062.
    KOiK01623.
    OMAiANCQAAQ.
    OrthoDBiEOG091G0A9T.
    PhylomeDBiP05062.
    TreeFamiTF314203.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00183.
    BioCyciMetaCyc:HS06234-MONOMER.
    ZFISH:HS06234-MONOMER.
    BRENDAi4.1.2.13. 2681.
    ReactomeiR-HSA-70171. Glycolysis.
    R-HSA-70263. Gluconeogenesis.
    R-HSA-70350. Fructose catabolism.
    SABIO-RKP05062.

    Miscellaneous databases

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

    Gene expression databases

    BgeeiENSG00000136872.
    CleanExiHS_ALDOB.
    ExpressionAtlasiP05062. baseline and differential.
    GenevisibleiP05062. HS.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR029768. Aldolase_I_AS.
    IPR013785. Aldolase_TIM.
    IPR000741. FBA_I.
    [Graphical view]
    PfamiPF00274. Glycolytic. 1 hit.
    [Graphical view]
    PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    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: November 30, 2016
    This is version 190 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

    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 one 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.