H3BQN4 · H3BQN4_HUMAN

  • Protein
    Fructose-bisphosphate aldolase
  • Gene
    ALDOA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    2/5

Function

Catalytic activity

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular ComponentI band
Cellular ComponentM band
Molecular Functionfructose-bisphosphate aldolase activity
Biological Processglycolytic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Fructose-bisphosphate aldolase
  • EC number

Gene names

    • Name
      ALDOA

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    H3BQN4

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Variants

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The viewer provides 105 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Genetic variation databases

PTM/Processing

Features

Showing features for modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Modified residue (large scale data)3PRIDEPhosphotyrosine
Modified residue (large scale data)5PRIDEPhosphotyrosine
Modified residue (large scale data)9PRIDEPhosphothreonine
Modified residue (large scale data)17PRIDEPhosphoserine
Modified residue (large scale data)36PRIDEPhosphoserine
Modified residue (large scale data)37PRIDEPhosphothreonine
Modified residue (large scale data)39PRIDEPhosphoserine
Modified residue (large scale data)46PRIDEPhosphoserine
Modified residue (large scale data)49PRIDEPhosphothreonine
Modified residue (large scale data)52PRIDEPhosphothreonine
Modified residue (large scale data)100PRIDEPhosphoserine
Modified residue (large scale data)123PRIDEPhosphothreonine
Modified residue (large scale data)124PRIDEPhosphothreonine
Modified residue (large scale data)132PRIDEPhosphoserine
Modified residue (large scale data)158PRIDEPhosphothreonine
Modified residue (large scale data)160PRIDEPhosphoserine
Modified residue (large scale data)176PRIDEPhosphoserine
Modified residue (large scale data)204PRIDEPhosphotyrosine
Modified residue (large scale data)218PRIDEPhosphoserine
Modified residue (large scale data)223PRIDEPhosphotyrosine
Modified residue (large scale data)235PRIDEPhosphothreonine
Modified residue (large scale data)245PRIDEPhosphoserine
Modified residue (large scale data)255PRIDEPhosphothreonine
Modified residue (large scale data)269PRIDEPhosphothreonine
Modified residue (large scale data)272PRIDEPhosphoserine
Modified residue (large scale data)309PRIDEPhosphoserine

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Homotetramer. Interacts with SNX9 and WAS. Interacts with FBP2; the interaction blocks FBP2 inhibition by physiological concentrations of AMP and reduces inhibition by Ca2+.

Structure

Family & Domains

Sequence similarities

Belongs to the class I fructose-bisphosphate aldolase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    361
  • Mass (Da)
    39,340
  • Last updated
    2012-04-18 v1
  • Checksum
    CA08661BBDE6DE36
MPYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKENLKAAQEEYVKRALVRIGRRWAGCLGGWDSEKSPSHSTPLPA

Computationally mapped potential isoform sequences

There are 8 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
P04075ALDOA_HUMANALDOA364
J3KPS3J3KPS3_HUMANALDOA368
H3BU78H3BU78_HUMANALDOA204
H3BUH7H3BUH7_HUMANALDOA155
H3BR04H3BR04_HUMANALDOA162
H3BR68H3BR68_HUMANALDOA130
H3BPS8H3BPS8_HUMANALDOA278
H3BMQ8H3BMQ8_HUMANALDOA140

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC093512
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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