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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

    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

    • actin binding 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
    • blood coagulation Source: Reactome
    • canonical glycolysis Source: Reactome
    • carbohydrate metabolic process Source: Reactome
    • fructose 1,6-bisphosphate metabolic process Source: BHF-UCL
    • fructose metabolic process Source: BHF-UCL
    • gluconeogenesis Source: Reactome
    • glucose metabolic process Source: Reactome
    • glycolytic process Source: BHF-UCL
    • muscle cell cellular homeostasis Source: BHF-UCL
    • platelet activation Source: Reactome
    • platelet degranulation Source: Reactome
    • protein homotetramerization Source: UniProtKB
    • regulation of cell shape Source: BHF-UCL
    • small molecule metabolic process Source: Reactome
    • 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.
    BRENDAi4.1.2.13. 2681.
    ReactomeiREACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    REACT_318. Platelet degranulation.
    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
    ProteomesiUP000005640 Componenti: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:414. ALDOA.

    Subcellular locationi

    GO - Cellular componenti

    • actin cytoskeleton 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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti129 – 1291D → G in GSD12; thermolabile. 2 Publications
    VAR_000550
    Natural varianti207 – 2071E → K in GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity. 2 Publications
    VAR_044142
    Natural varianti339 – 3391C → Y in GSD12. 1 Publication
    VAR_044143
    Natural varianti347 – 3471G → S in GSD12; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity. 1 Publication
    Corresponds to variant rs138824667 [ dbSNP | Ensembl ].
    VAR_044144

    Keywords - Diseasei

    Disease mutation, Glycogen storage disease, Hereditary hemolytic anemia

    Organism-specific databases

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

    Polymorphism and mutation databases

    BioMutaiALDOA.
    DMDMi113606.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed5 Publications
    Chaini2 – 364363Fructose-bisphosphate aldolase APRO_0000216936Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei36 – 361Phosphoserine2 Publications
    Modified residuei39 – 391Phosphoserine4 Publications
    Modified residuei42 – 421N6-acetyllysine1 Publication
    Modified residuei46 – 461Phosphoserine3 Publications
    Modified residuei108 – 1081N6-acetyllysine1 Publication
    Modified residuei111 – 1111N6-malonyllysine1 Publication
    Modified residuei272 – 2721Phosphoserine1 Publication
    Modified residuei312 – 3121N6-malonyllysine1 Publication
    Modified residuei330 – 3301N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP04075.
    PaxDbiP04075.
    PRIDEiP04075.

    2D gel databases

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

    PTM databases

    PhosphoSiteiP04075.

    Expressioni

    Gene expression databases

    BgeeiP04075.
    CleanExiHS_ALDOA.
    ExpressionAtlasiP04075. baseline and differential.
    GenevestigatoriP04075.

    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

    Protein-protein interaction databases

    BioGridi106728. 57 interactions.
    IntActiP04075. 28 interactions.
    MINTiMINT-4998828.
    STRINGi9606.ENSP00000336927.

    Structurei

    Secondary structure

    1
    364
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 2314Combined sources
    Beta strandi29 – 335Combined sources
    Helixi37 – 4610Combined sources
    Helixi53 – 6412Combined sources
    Helixi68 – 736Combined sources
    Beta strandi74 – 796Combined sources
    Helixi83 – 853Combined sources
    Helixi94 – 1007Combined sources
    Beta strandi104 – 1085Combined sources
    Beta strandi113 – 1153Combined sources
    Beta strandi119 – 1213Combined sources
    Beta strandi123 – 1253Combined sources
    Helixi131 – 14010Combined sources
    Beta strandi145 – 1528Combined sources
    Beta strandi155 – 1573Combined sources
    Helixi161 – 17919Combined sources
    Turni180 – 1823Combined sources
    Beta strandi184 – 1918Combined sources
    Helixi199 – 21921Combined sources
    Helixi224 – 2263Combined sources
    Helixi246 – 25813Combined sources
    Beta strandi267 – 2704Combined sources
    Helixi277 – 28913Combined sources
    Beta strandi296 – 3038Combined sources
    Helixi304 – 31411Combined sources
    Helixi318 – 3203Combined sources
    Helixi321 – 33818Combined sources
    Turni339 – 3413Combined sources
    Beta strandi348 – 3503Combined sources

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP04075.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG3588.
    GeneTreeiENSGT00390000010235.
    HOVERGENiHBG002386.
    InParanoidiP04075.
    KOiK01623.
    OMAiPNMVIDG.
    OrthoDBiEOG744T94.
    PhylomeDBiP04075.
    TreeFamiTF314203.

    Family and domain databases

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

    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731C → G in CAA30979 (PubMed:3391172).Curated
    Sequence conflicti180 – 1801Q → R in CAG46678 (Ref. 6) Curated
    Sequence conflicti196 – 1961D → A in CAA30979 (PubMed:3391172).Curated
    Sequence conflicti230 – 2301K → N in CAA30979 (PubMed:3391172).Curated
    Sequence conflicti280 – 2801A → S in CAA30979 (PubMed:3391172).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti82 – 821E → Q.
    Corresponds to variant rs11553107 [ dbSNP | Ensembl ].
    VAR_048219
    Natural varianti129 – 1291D → G in GSD12; thermolabile. 2 Publications
    VAR_000550
    Natural varianti142 – 1421G → V.
    Corresponds to variant rs11553108 [ dbSNP | Ensembl ].
    VAR_048220
    Natural varianti207 – 2071E → K in GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity. 2 Publications
    VAR_044142
    Natural varianti339 – 3391C → Y in GSD12. 1 Publication
    VAR_044143
    Natural varianti347 – 3471G → S in GSD12; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity. 1 Publication
    Corresponds to variant rs138824667 [ dbSNP | Ensembl ].
    VAR_044144

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MARRKPEGSSFNMTHLSMAM AFSFPPVASGQLHPQLGNTQ HQTELGKELATTSTM in isoform 2. 1 PublicationVSP_047261

    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]
    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.
    UCSCiuc002dvw.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]
    UniGeneiHs.513490.
    Hs.732822.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi106728. 57 interactions.
    IntActiP04075. 28 interactions.
    MINTiMINT-4998828.
    STRINGi9606.ENSP00000336927.

    Chemistry

    ChEMBLiCHEMBL2106.

    PTM databases

    PhosphoSiteiP04075.

    Polymorphism and mutation databases

    BioMutaiALDOA.
    DMDMi113606.

    2D gel databases

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

    Proteomic databases

    MaxQBiP04075.
    PaxDbiP04075.
    PRIDEiP04075.

    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.
    UCSCiuc002dvw.3. human. [P04075-1]

    Organism-specific databases

    CTDi226.
    GeneCardsiGC16P030064.
    HGNCiHGNC:414. ALDOA.
    HPAiCAB006252.
    HPA004177.
    MIMi103850. gene.
    611881. phenotype.
    neXtProtiNX_P04075.
    Orphaneti57. Glycogen storage disease due to aldolase A deficiency.
    PharmGKBiPA24707.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG3588.
    GeneTreeiENSGT00390000010235.
    HOVERGENiHBG002386.
    InParanoidiP04075.
    KOiK01623.
    OMAiPNMVIDG.
    OrthoDBiEOG744T94.
    PhylomeDBiP04075.
    TreeFamiTF314203.

    Enzyme and pathway databases

    UniPathwayiUPA00109; UER00183.
    BioCyciMetaCyc:HS07647-MONOMER.
    BRENDAi4.1.2.13. 2681.
    ReactomeiREACT_1383. Glycolysis.
    REACT_1520. Gluconeogenesis.
    REACT_318. Platelet degranulation.
    SABIO-RKP04075.

    Miscellaneous databases

    EvolutionaryTraceiP04075.
    GeneWikiiAldolase_A.
    GenomeRNAii226.
    NextBioi920.
    PROiP04075.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP04075.
    CleanExiHS_ALDOA.
    ExpressionAtlasiP04075. baseline and differential.
    GenevestigatoriP04075.

    Family and domain databases

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

    Publicationsi

    « Hide 'large scale' publications
    1. "Nucleotide sequence of a cDNA clone for human aldolase: a messenger RNA in the liver."
      Sakakibara M., Mukai T., Hori K.
      Biochem. Biophys. Res. Commun. 131:413-420(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fibroblast.
    3. "Human aldolase A gene. Structural organization and tissue-specific expression by multiple promoters and alternate mRNA processing."
      Izzo P., Costanzo P., Lupo A., Rippa E., Paolella G., Salvatore F.
      Eur. J. Biochem. 174:569-578(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "An additional promoter functions in the human aldolase A gene, but not in rat."
      Mukai T., Arai Y., Yatsuki H., Joh K., Hori K.
      Eur. J. Biochem. 195:781-787(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Cervix, Eye, Lung, Testis and Uterus.
    10. "Characterization of three optional promoters in the 5' region of the human aldolase A gene."
      Maire P., Gautron S., Hakim V., Gregori C., Mennecier F., Kahn A.
      J. Mol. Biol. 197:425-438(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-108 (ISOFORM 1).
    11. "The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase."
      Freemont P.S., Dunbar B., Fothergill-Gilmore L.A.
      Biochem. J. 249:779-788(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-364.
    12. "Human skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and o-iodosobenzoic acid-cleavage fragments."
      Freemont P.S., Dunbar B., Fothergill L.A.
      Arch. Biochem. Biophys. 228:342-352(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-63 AND 148-358.
    13. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-22.
      Tissue: Platelet.
    14. "Identification of transglutaminase substrates in HT29 colon cancer cells: use of 5-(biotinamido)pentylamine as a transglutaminase-specific probe."
      Lee K.N., Maxwell M.D., Patterson M.K. Jr., Birckbichler P.J., Conway E.
      Biochim. Biophys. Acta 1136:12-16(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-16.
      Tissue: Colon carcinoma.
    15. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-13; 29-42; 44-56; 61-69; 88-99; 154-173; 244-258 AND 332-342, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    16. "Evolutionary implications of the human aldolase-A, -B, -C, and - pseudogene chromosome locations."
      Tolan D.R., Niclas J., Bruce B.D., Lebo R.V.
      Am. J. Hum. Genet. 41:907-924(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 139-364 (ISOFORM 1/2).
    17. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "Evolutionary conserved N-terminal region of human muscle fructose 1,6-bisphosphatase regulates its activity and the interaction with aldolase."
      Gizak A., Maciaszczyk E., Dzugaj A., Eschrich K., Rakus D.
      Proteins 72:209-216(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FBP2.
    20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-108 AND LYS-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    25. Cited for: MALONYLATION AT LYS-111 AND LYS-312.
    26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-46 AND SER-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    30. "The crystal structure of human muscle aldolase at 3.0-A resolution."
      Gamblin S.J., Cooper B., Millar J.R., Davies G.J., Littlechild J.A., Watson H.C.
      FEBS Lett. 262:282-286(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
    31. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    32. "Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications."
      Dalby A., Dauter Z., Littlechild J.A.
      Protein Sci. 8:291-297(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    33. "Human aldolase A deficiency associated with a hemolytic anemia: thermolabile aldolase due to a single base mutation."
      Kishi H., Mukai T., Hirono A., Fujii H., Miwa S., Hori K.
      Proc. Natl. Acad. Sci. U.S.A. 84:8623-8627(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GSD12 GLY-129, CHARACTERIZATION OF VARIANT GSD12 GLY-129.
    34. "Human aldolase A of a hemolytic anemia patient with Asp-128-->Gly substitution: characteristics of an enzyme generated in E. coli transfected with the expression plasmid pHAAD128G."
      Takasaki Y., Takahashi I., Mukai T., Hori K.
      J. Biochem. 108:153-157(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT GSD12 GLY-129.
    35. "Brief report: inherited metabolic myopathy and hemolysis due to a mutation in aldolase A."
      Kreuder J., Borkhardt A., Repp R., Pekrun A., Goettsche B., Gottschalk U., Reichmann H., Schachenmayr W., Schlegel K., Lampert F.
      N. Engl. J. Med. 334:1100-1104(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GSD12 LYS-207.
    36. "Hemolytic anemia and severe rhabdomyolysis caused by compound heterozygous mutations of the gene for erythrocyte/muscle isozyme of aldolase, ALDOA(Arg303X/Cys338Tyr)."
      Yao D.C., Tolan D.R., Murray M.F., Harris D.J., Darras B.T., Geva A., Neufeld E.J.
      Blood 103:2401-2403(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GSD12 TYR-339.
    37. "Human aldolase A natural mutants: relationship between flexibility of the C-terminal region and enzyme function."
      Esposito G., Vitagliano L., Costanzo P., Borrelli L., Barone R., Pavone L., Izzo P., Zagari A., Salvatore F.
      Biochem. J. 380:51-56(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GSD12 SER-347, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS GSD12 LYS-207 AND SER-347.

    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: May 27, 2015
    This is version 187 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

    External Data

    Dasty 3

    Similar proteinsi

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