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Protein

Fructose-bisphosphate aldolase A

Gene

ALDOA

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

Functioni

Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein (By similarity).By similarity

Catalytic activityi

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

Kineticsi

  1. KM=52 µM for fructose 1,6-bisphosphate (at 30 degrees Celsius)1 Publication

    Temperature dependencei

    Thermal denaturation midpoint (Tm) is 54.4 degrees Celsius.1 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

    • actin binding Source: BHF-UCL
    • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
    • cytoskeletal protein binding Source: BHF-UCL
    • fructose binding Source: BHF-UCL
    • fructose-bisphosphate aldolase activity Source: BHF-UCL
    • identical protein binding Source: BHF-UCL
    • poly(A) RNA binding Source: UniProtKB
    • tubulin binding Source: BHF-UCL

    GO - Biological processi

    • actin filament organization Source: BHF-UCL
    • ATP biosynthetic process Source: BHF-UCL
    • canonical glycolysis Source: Reactome
    • fructose 1,6-bisphosphate metabolic process Source: BHF-UCL
    • fructose metabolic process Source: BHF-UCL
    • gluconeogenesis Source: Reactome
    • glycolytic process Source: BHF-UCL
    • muscle cell cellular homeostasis Source: BHF-UCL
    • platelet degranulation Source: Reactome
    • protein homotetramerization Source: UniProtKB
    • regulation of cell shape Source: BHF-UCL
    • striated muscle contraction Source: BHF-UCL
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07647-MONOMER.
    ZFISH:HS07647-MONOMER.
    BRENDAi4.1.2.13. 2681.
    ReactomeiR-HSA-114608. Platelet degranulation.
    R-HSA-6798695. Neutrophil degranulation.
    R-HSA-70171. Glycolysis.
    R-HSA-70263. Gluconeogenesis.
    SABIO-RKP04075.
    UniPathwayiUPA00109; UER00183.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-bisphosphate aldolase A (EC:4.1.2.13)
    Alternative name(s):
    Lung cancer antigen NY-LU-1
    Muscle-type aldolase
    Gene namesi
    Name:ALDOA
    Synonyms:ALDA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:414. ALDOA.

    Subcellular locationi

    GO - Cellular componenti

    • actin cytoskeleton Source: BHF-UCL
    • cell-cell adherens junction Source: BHF-UCL
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • extracellular region Source: Reactome
    • extracellular space Source: UniProtKB
    • I band Source: BHF-UCL
    • M band Source: UniProtKB-SubCell
    • membrane Source: UniProtKB
    • nucleus Source: UniProtKB
    • platelet alpha granule lumen Source: Reactome
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Glycogen storage disease 12 (GSD12)4 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA metabolic disorder associated with increased hepatic glycogen and hemolytic anemia. It may lead to myopathy with exercise intolerance and rhabdomyolysis.
    See also OMIM:611881
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_000550129D → G in GSD12; thermolabile. 2 PublicationsCorresponds to variant rs121909533dbSNPEnsembl.1
    Natural variantiVAR_044142207E → K in GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity. 2 PublicationsCorresponds to variant rs121909534dbSNPEnsembl.1
    Natural variantiVAR_044143339C → Y in GSD12. 1 Publication1
    Natural variantiVAR_044144347G → S in GSD12; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity. 1 PublicationCorresponds to variant rs138824667dbSNPEnsembl.1

    Keywords - Diseasei

    Disease mutation, Glycogen storage disease, Hereditary hemolytic anemia

    Organism-specific databases

    DisGeNETi226.
    MalaCardsiALDOA.
    MIMi611881. phenotype.
    OpenTargetsiENSG00000149925.
    Orphaneti57. Glycogen storage disease due to aldolase A deficiency.
    PharmGKBiPA24707.

    Chemistry databases

    ChEMBLiCHEMBL2106.

    Polymorphism and mutation databases

    BioMutaiALDOA.
    DMDMi113606.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedCombined sources5 Publications
    ChainiPRO_00002169362 – 364Fructose-bisphosphate aldolase AAdd BLAST363

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei5PhosphotyrosineBy similarity1
    Modified residuei9PhosphothreonineCombined sources1
    Modified residuei36PhosphoserineCombined sources1
    Modified residuei39PhosphoserineCombined sources1
    Modified residuei42N6-acetyllysine; alternateCombined sources1
    Cross-linki42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
    Cross-linki42Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
    Modified residuei46PhosphoserineCombined sources1
    Modified residuei108N6-acetyllysineCombined sources1
    Modified residuei111N6-malonyllysine1 Publication1
    Modified residuei132PhosphoserineBy similarity1
    Modified residuei272PhosphoserineCombined sources1
    Modified residuei312N6-malonyllysine1 Publication1
    Modified residuei330N6-acetyllysineCombined sources1

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    EPDiP04075.
    PaxDbiP04075.
    PeptideAtlasiP04075.
    PRIDEiP04075.
    TopDownProteomicsiP04075-1. [P04075-1]

    2D gel databases

    DOSAC-COBS-2DPAGEP04075.
    OGPiP04075.
    REPRODUCTION-2DPAGEIPI00465439.
    P04075.
    SWISS-2DPAGEP04075.
    UCD-2DPAGEP04075.

    PTM databases

    iPTMnetiP04075.
    PhosphoSitePlusiP04075.
    SwissPalmiP04075.

    Expressioni

    Gene expression databases

    BgeeiENSG00000149925.
    CleanExiHS_ALDOA.
    ExpressionAtlasiP04075. baseline and differential.
    GenevisibleiP04075. HS.

    Organism-specific databases

    HPAiCAB006252.
    HPA004177.

    Interactioni

    Subunit structurei

    Homotetramer. Interacts with SNX9 and WAS (By similarity). Interacts with FBP2; the interaction blocks FBP2 inhibition by physiological concentrations of AMP and reduces inhibition by Ca2+.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ALDOCP099723EBI-10194102,EBI-2952751
    IFNA4P050143EBI-10194102,EBI-10194381
    PCNAP120043EBI-709613,EBI-358311

    GO - Molecular functioni

    • actin binding Source: BHF-UCL
    • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
    • cytoskeletal protein binding Source: BHF-UCL
    • identical protein binding Source: BHF-UCL
    • tubulin binding Source: BHF-UCL

    Protein-protein interaction databases

    BioGridi106728. 111 interactors.
    IntActiP04075. 37 interactors.
    MINTiMINT-4998828.
    STRINGi9606.ENSP00000336927.

    Structurei

    Secondary structure

    1364
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi10 – 23Combined sources14
    Beta strandi29 – 33Combined sources5
    Helixi37 – 46Combined sources10
    Helixi53 – 64Combined sources12
    Helixi68 – 73Combined sources6
    Beta strandi74 – 79Combined sources6
    Helixi83 – 85Combined 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
    Beta strandi155 – 157Combined sources3
    Helixi161 – 179Combined sources19
    Turni180 – 182Combined sources3
    Beta strandi184 – 191Combined sources8
    Helixi199 – 219Combined sources21
    Helixi224 – 226Combined sources3
    Helixi246 – 258Combined sources13
    Beta strandi267 – 270Combined sources4
    Helixi277 – 289Combined sources13
    Beta strandi296 – 303Combined sources8
    Helixi304 – 314Combined sources11
    Helixi318 – 320Combined sources3
    Helixi321 – 338Combined sources18
    Turni339 – 341Combined sources3
    Beta strandi348 – 350Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1ALDX-ray2.00A2-364[»]
    2ALDX-ray2.10A2-364[»]
    4ALDX-ray2.80A2-364[»]
    ProteinModelPortaliP04075.
    SMRiP04075.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04075.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiKOG1557. Eukaryota.
    COG3588. LUCA.
    GeneTreeiENSGT00390000010235.
    HOVERGENiHBG002386.
    InParanoidiP04075.
    KOiK01623.
    OMAiPNMVIDG.
    OrthoDBiEOG091G0A9T.
    PhylomeDBiP04075.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P04075-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE
    60 70 80 90 100
    NTEENRRFYR QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS
    110 120 130 140 150
    KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC
    160 170 180 190 200
    VLKIGEHTPS ALAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK
    210 220 230 240 250
    RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC TQKFSHEEIA
    260 270 280 290 300
    MATVTALRRT VPPAVTGITF LSGGQSEEEA SINLNAINKC PLLKPWALTF
    310 320 330 340 350
    SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG
    360
    AAASESLFVS NHAY
    Length:364
    Mass (Da):39,420
    Last modified:January 23, 2007 - v2
    Checksum:i0AAED80F755A7BE8
    GO
    Isoform 2 (identifier: P04075-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MARRKPEGSSFNMTHLSMAMAFSFPPVASGQLHPQLGNTQHQTELGKELATTSTM

    Show »
    Length:418
    Mass (Da):45,261
    Checksum:iFAE6E6CA84022A8A
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti73C → G in CAA30979 (PubMed:3391172).Curated1
    Sequence conflicti180Q → R in CAG46678 (Ref. 6) Curated1
    Sequence conflicti196D → A in CAA30979 (PubMed:3391172).Curated1
    Sequence conflicti230K → N in CAA30979 (PubMed:3391172).Curated1
    Sequence conflicti280A → S in CAA30979 (PubMed:3391172).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_04821982E → Q.Corresponds to variant rs11553107dbSNPEnsembl.1
    Natural variantiVAR_000550129D → G in GSD12; thermolabile. 2 PublicationsCorresponds to variant rs121909533dbSNPEnsembl.1
    Natural variantiVAR_048220142G → V.Corresponds to variant rs11553108dbSNPEnsembl.1
    Natural variantiVAR_044142207E → K in GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity. 2 PublicationsCorresponds to variant rs121909534dbSNPEnsembl.1
    Natural variantiVAR_044143339C → Y in GSD12. 1 Publication1
    Natural variantiVAR_044144347G → S in GSD12; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity. 1 PublicationCorresponds to variant rs138824667dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0472611M → MARRKPEGSSFNMTHLSMAM AFSFPPVASGQLHPQLGNTQ HQTELGKELATTSTM in isoform 2. 1 Publication1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M11560 mRNA. Translation: AAA51690.1.
    X05236 mRNA. Translation: CAA28861.1.
    X12447 Genomic DNA. Translation: CAA30979.1.
    AK301993 mRNA. Translation: BAG63399.1.
    CR536528 mRNA. Translation: CAG38765.1.
    CR541880 mRNA. Translation: CAG46678.1.
    AC093512 Genomic DNA. No translation available.
    CH471238 Genomic DNA. Translation: EAW79933.1.
    BC000367 mRNA. Translation: AAH00367.2.
    BC004333 mRNA. Translation: AAH04333.1.
    BC010660 mRNA. Translation: AAH10660.1.
    BC012880 mRNA. Translation: AAH12880.1.
    BC013614 mRNA. Translation: AAH13614.1.
    BC015888 mRNA. Translation: AAH15888.1.
    BC016170 mRNA. Translation: AAH16170.1.
    BC016800 mRNA. Translation: AAH16800.1.
    M21190 mRNA. Translation: AAA51697.1.
    CCDSiCCDS10668.1. [P04075-1]
    CCDS58450.1. [P04075-2]
    PIRiS14084. ADHUA.
    RefSeqiNP_000025.1. NM_000034.3. [P04075-1]
    NP_001121089.1. NM_001127617.2. [P04075-1]
    NP_001230106.1. NM_001243177.1. [P04075-2]
    NP_908930.1. NM_184041.2. [P04075-1]
    NP_908932.1. NM_184043.2. [P04075-1]
    XP_011544070.1. XM_011545768.2. [P04075-1]
    UniGeneiHs.513490.
    Hs.732822.

    Genome annotation databases

    EnsembliENST00000338110; ENSP00000336927; ENSG00000149925. [P04075-1]
    ENST00000395248; ENSP00000378669; ENSG00000149925. [P04075-2]
    ENST00000412304; ENSP00000400452; ENSG00000149925. [P04075-1]
    ENST00000563060; ENSP00000455800; ENSG00000149925. [P04075-1]
    ENST00000564546; ENSP00000455917; ENSG00000149925. [P04075-1]
    ENST00000564595; ENSP00000457468; ENSG00000149925. [P04075-2]
    ENST00000566897; ENSP00000455724; ENSG00000149925. [P04075-1]
    ENST00000569545; ENSP00000455700; ENSG00000149925. [P04075-1]
    GeneIDi226.
    KEGGihsa:226.
    UCSCiuc010veg.3. human. [P04075-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M11560 mRNA. Translation: AAA51690.1.
    X05236 mRNA. Translation: CAA28861.1.
    X12447 Genomic DNA. Translation: CAA30979.1.
    AK301993 mRNA. Translation: BAG63399.1.
    CR536528 mRNA. Translation: CAG38765.1.
    CR541880 mRNA. Translation: CAG46678.1.
    AC093512 Genomic DNA. No translation available.
    CH471238 Genomic DNA. Translation: EAW79933.1.
    BC000367 mRNA. Translation: AAH00367.2.
    BC004333 mRNA. Translation: AAH04333.1.
    BC010660 mRNA. Translation: AAH10660.1.
    BC012880 mRNA. Translation: AAH12880.1.
    BC013614 mRNA. Translation: AAH13614.1.
    BC015888 mRNA. Translation: AAH15888.1.
    BC016170 mRNA. Translation: AAH16170.1.
    BC016800 mRNA. Translation: AAH16800.1.
    M21190 mRNA. Translation: AAA51697.1.
    CCDSiCCDS10668.1. [P04075-1]
    CCDS58450.1. [P04075-2]
    PIRiS14084. ADHUA.
    RefSeqiNP_000025.1. NM_000034.3. [P04075-1]
    NP_001121089.1. NM_001127617.2. [P04075-1]
    NP_001230106.1. NM_001243177.1. [P04075-2]
    NP_908930.1. NM_184041.2. [P04075-1]
    NP_908932.1. NM_184043.2. [P04075-1]
    XP_011544070.1. XM_011545768.2. [P04075-1]
    UniGeneiHs.513490.
    Hs.732822.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1ALDX-ray2.00A2-364[»]
    2ALDX-ray2.10A2-364[»]
    4ALDX-ray2.80A2-364[»]
    ProteinModelPortaliP04075.
    SMRiP04075.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi106728. 111 interactors.
    IntActiP04075. 37 interactors.
    MINTiMINT-4998828.
    STRINGi9606.ENSP00000336927.

    Chemistry databases

    ChEMBLiCHEMBL2106.

    PTM databases

    iPTMnetiP04075.
    PhosphoSitePlusiP04075.
    SwissPalmiP04075.

    Polymorphism and mutation databases

    BioMutaiALDOA.
    DMDMi113606.

    2D gel databases

    DOSAC-COBS-2DPAGEP04075.
    OGPiP04075.
    REPRODUCTION-2DPAGEIPI00465439.
    P04075.
    SWISS-2DPAGEP04075.
    UCD-2DPAGEP04075.

    Proteomic databases

    EPDiP04075.
    PaxDbiP04075.
    PeptideAtlasiP04075.
    PRIDEiP04075.
    TopDownProteomicsiP04075-1. [P04075-1]

    Protocols and materials databases

    DNASUi226.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000338110; ENSP00000336927; ENSG00000149925. [P04075-1]
    ENST00000395248; ENSP00000378669; ENSG00000149925. [P04075-2]
    ENST00000412304; ENSP00000400452; ENSG00000149925. [P04075-1]
    ENST00000563060; ENSP00000455800; ENSG00000149925. [P04075-1]
    ENST00000564546; ENSP00000455917; ENSG00000149925. [P04075-1]
    ENST00000564595; ENSP00000457468; ENSG00000149925. [P04075-2]
    ENST00000566897; ENSP00000455724; ENSG00000149925. [P04075-1]
    ENST00000569545; ENSP00000455700; ENSG00000149925. [P04075-1]
    GeneIDi226.
    KEGGihsa:226.
    UCSCiuc010veg.3. human. [P04075-1]

    Organism-specific databases

    CTDi226.
    DisGeNETi226.
    GeneCardsiALDOA.
    HGNCiHGNC:414. ALDOA.
    HPAiCAB006252.
    HPA004177.
    MalaCardsiALDOA.
    MIMi103850. gene.
    611881. phenotype.
    neXtProtiNX_P04075.
    OpenTargetsiENSG00000149925.
    Orphaneti57. Glycogen storage disease due to aldolase A deficiency.
    PharmGKBiPA24707.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1557. Eukaryota.
    COG3588. LUCA.
    GeneTreeiENSGT00390000010235.
    HOVERGENiHBG002386.
    InParanoidiP04075.
    KOiK01623.
    OMAiPNMVIDG.
    OrthoDBiEOG091G0A9T.
    PhylomeDBiP04075.
    TreeFamiTF314203.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00183.
    BioCyciMetaCyc:HS07647-MONOMER.
    ZFISH:HS07647-MONOMER.
    BRENDAi4.1.2.13. 2681.
    ReactomeiR-HSA-114608. Platelet degranulation.
    R-HSA-6798695. Neutrophil degranulation.
    R-HSA-70171. Glycolysis.
    R-HSA-70263. Gluconeogenesis.
    SABIO-RKP04075.

    Miscellaneous databases

    EvolutionaryTraceiP04075.
    GeneWikiiAldolase_A.
    GenomeRNAii226.
    PROiP04075.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000149925.
    CleanExiHS_ALDOA.
    ExpressionAtlasiP04075. baseline and differential.
    GenevisibleiP04075. 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 nameiALDOA_HUMAN
    AccessioniPrimary (citable) accession number: P04075
    Secondary accession number(s): B4DXI7
    , Q6FH76, Q6FI10, Q96B15, Q9BWD9, Q9UCN2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1986
    Last sequence update: January 23, 2007
    Last modified: November 30, 2016
    This is version 204 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, three 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 16
      Human chromosome 16: 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.