id: P37837
gene_symbol: TALDO1
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: Transaldolase (EC 2.2.1.2), the enzyme that catalyses the rate-limiting
  step of the non-oxidative branch of the pentose phosphate pathway. It transfers
  a three-carbon dihydroxyacetone unit between sugar phosphates via a Schiff-base
  intermediate on an active-site lysine, catalysing the reversible reaction
  sedoheptulose-7-phosphate + D-glyceraldehyde-3-phosphate <-> erythrose-4-phosphate
  + beta-D-fructose-6-phosphate. This reaction links the pentose phosphate pathway
  back to the glycolytic intermediates fructose-6-phosphate and glyceraldehyde-3-phosphate,
  allowing the cell to balance ribose-5-phosphate production with NADPH generation and
  to recycle sugar phosphates. The enzyme is predominantly cytosolic (with regulated
  nucleocytoplasmic shuttling) and forms a homodimer with a TIM-barrel fold. Loss of
  transaldolase function causes transaldolase deficiency, an autosomal-recessive
  inborn error of the pentose phosphate pathway that presents in the neonatal/infantile
  period with hepatosplenomegaly, liver cirrhosis/fibrosis, thrombocytopenia and
  hemolytic anemia, accompanied by accumulation of polyols and sedoheptulose.
alternative_products:
- name: 1 (TALDO1L {ECO:0000303|PubMed:27703206})
  id: P37837-1
- name: 2 (TALDO1S {ECO:0000303|PubMed:27703206})
  id: P37837-2
  sequence_note: VSP_061595
existing_annotations:
- term:
    id: GO:0004801
    label: transaldolase activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: Phylogenetic (IBA) assignment of transaldolase activity, the defining
      molecular function of this gene and its orthologs across the transaldolase family.
    action: ACCEPT
    reason: This is the core molecular function of TALDO1. It is directly supported
      by biochemical assays on the human enzyme and by the loss-of-function metabolic
      phenotype, and is consistent across orthologs, making the IBA well-founded.
    supported_by:
    - reference_id: PMID:18687684
      supporting_text: we show that a homologous replacement has a similar effect
        in the human transaldolase Taldo1 (aldolase activity, 14 units/mg).
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: 'Catalyzes the rate-limiting step of the non-oxidative phase'
- term:
    id: GO:0009052
    label: pentose-phosphate shunt, non-oxidative branch
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: Phylogenetic (IBA) assignment placing transaldolase in the non-oxidative
      branch of the pentose phosphate pathway, its core biological process.
    action: ACCEPT
    reason: Transaldolase catalyses the rate-limiting step of the non-oxidative PPP.
      This BP is well-supported by the enzymatic function and by the metabolic
      phenotype of transaldolase-deficient cells (accumulation of sedoheptulose
      7-phosphate).
    supported_by:
    - reference_id: PMID:8955144
      supporting_text: Transaldolase (TAL) is a key enzyme of the reversible nonoxidative
        branch of the pentose phosphate pathway (PPP)
    - reference_id: PMID:18498245
      supporting_text: Sedoheptulose 7-phosphate was accumulated, whereas G6P (glucose
        6-phosphate) was depleted
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: Phylogenetic (IBA) assignment of nuclear localization, reflecting the
      regulated nucleocytoplasmic shuttling of transaldolase seen in mammalian orthologs.
    action: KEEP_AS_NON_CORE
    reason: Isoform 1 of TALDO1 shuttles between nucleus and cytoplasm via importin
      alpha/beta and CRM1, and a nuclear pool exists, so the localization is not wrong.
      However, the catalytic PPP function is executed in the cytosol; nuclear
      localization is a regulatory/moonlighting distribution rather than the core
      site of function, so it should not be treated as a core annotation. The
      "is_active_in" qualifier overstates catalytic activity in the nucleus.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: 'The first 10 amino acids are essential for nuclear'
- term:
    id: GO:0004801
    label: transaldolase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: Automated (IEA) assignment of transaldolase activity via InterPro/ARBA/EC/RHEA
      mapping (EC 2.2.1.2, RHEA:17053).
    action: ACCEPT
    reason: Correct core molecular function, redundant with experimental and IBA
      annotations. The EC/RHEA/InterPro evidence chain matches the characterized
      human enzyme.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: EC=2.2.1.2
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: Automated (IEA) nuclear localization from UniProt Subcellular Location
      keyword mapping (SL-0191).
    action: KEEP_AS_NON_CORE
    reason: The nuclear pool derives from regulated shuttling of isoform 1 and is
      supported by the UniProt subcellular-location annotation, but it is not the
      site of core catalytic function; keep as non-core.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: 'Actively transported into the nucleus in an importin'
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: located_in
  review:
    summary: Automated (IEA) cytoplasmic localization via InterPro/ARBA and UniProt
      Subcellular Location mapping (SL-0086).
    action: ACCEPT
    reason: Cytoplasm/cytosol is the primary localization where transaldolase carries
      out PPP metabolism. This is a broader parent of the more precise cytosol term
      and is correct, though the more specific cytosol (GO:0005829) is preferred as core.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: [Isoform 1]: Nucleus'
- term:
    id: GO:0005975
    label: carbohydrate metabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: Automated (IEA) assignment of carbohydrate metabolic process from InterPro
      family membership (TAL/FSA).
    action: ACCEPT
    reason: Correct but very general parent of the pentose phosphate pathway. It is
      acceptable for an IEA to be broad; the more specific PPP terms capture the core
      process. Not a core annotation on its own.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: Belongs to the transaldolase family. Type 1 subfamily.
- term:
    id: GO:0006098
    label: pentose-phosphate shunt
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: involved_in
  review:
    summary: Automated (IEA) assignment of the pentose phosphate pathway via ARBA/InterPro/UniPathway
      (UPA00115).
    action: ACCEPT
    reason: Correct. This is the parent process; transaldolase acts specifically in
      the non-oxidative branch (GO:0009052), which is the preferred core BP, but the
      broader term is accurate.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: 'PATHWAY: Carbohydrate degradation; pentose phosphate pathway'
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:21044950
  qualifier: enables
  review:
    summary: IPI protein-binding annotation from a genome-wide BiFC telomere-interactome
      screen; TALDO1 was flagged as interacting with TERF2IP/RAP1 (Q9NYB0).
    action: MARK_AS_OVER_ANNOTATED
    reason: "'protein binding' (GO:0005515) is uninformative about molecular function.
      The interaction comes from a large-scale BiFC screen for telomere-interactome
      candidates and is not a characterized functional interaction for transaldolase,
      so it should not be treated as a core function. Retained (not removed) per
      curation policy on IPI protein-binding annotations."
    supported_by:
    - reference_id: PMID:21044950
      supporting_text: we developed an arrayed screening strategy based on protein
        complementation to systematically investigate protein-protein interactions
        in live human cells
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32814053
  qualifier: enables
  review:
    summary: IPI protein-binding annotation from a neurodegenerative-disease Y2H
      interactome map; TALDO1 recorded interacting with HTT (P42858).
    action: MARK_AS_OVER_ANNOTATED
    reason: "'protein binding' is uninformative and this interaction derives from a
      systematic yeast two-hybrid interactome map, not a characterized functional
      interaction. Kept as over-annotated rather than removed per policy."
    supported_by:
    - reference_id: PMID:32814053
      supporting_text: generated by systematic yeast two-hybrid interaction screening
        of ∼500 ND-related proteins and integration of literature interactions
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: is_active_in
  review:
    summary: Automated (IEA, Ensembl Compara orthology) assignment of cytosolic
      localization/activity.
    action: ACCEPT
    reason: Cytosol is the primary site of transaldolase catalysis in the PPP,
      consistent with experimental (IDA) and Reactome annotations. This is a core
      localization.
    supported_by:
    - reference_id: PMID:18498245
      supporting_text: Transaldolase deficiency influences the pentose phosphate pathway
- term:
    id: GO:0006002
    label: fructose 6-phosphate metabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: Automated (IEA, Ensembl Compara) assignment of fructose-6-phosphate
      metabolic process.
    action: ACCEPT
    reason: Fructose-6-phosphate is a direct product/substrate of the transaldolase
      reaction, so involvement in F6P metabolism is correct. It is a substrate-level
      restatement of the core PPP function rather than an independent core term.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: 'erythrose-4-phosphate and beta-D-fructose 6-phosphate'
- term:
    id: GO:0009052
    label: pentose-phosphate shunt, non-oxidative branch
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: Automated (IEA, Ensembl Compara) assignment of the non-oxidative branch
      of the pentose phosphate pathway.
    action: ACCEPT
    reason: Correct core biological process, redundant with the IBA and IMP annotations
      to the same term.
    supported_by:
    - reference_id: PMID:8955144
      supporting_text: Transaldolase (TAL) is a key enzyme of the reversible nonoxidative
        branch of the pentose phosphate pathway (PPP)
- term:
    id: GO:0019682
    label: glyceraldehyde-3-phosphate metabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: Automated (IEA, Ensembl Compara) assignment of glyceraldehyde-3-phosphate
      metabolic process.
    action: ACCEPT
    reason: Glyceraldehyde-3-phosphate is a direct substrate/product of the
      transaldolase reaction, so this is correct. Like the F6P term, it is a
      substrate-level restatement of the core PPP function.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: 'of sedoheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into'
- term:
    id: GO:0030246
    label: carbohydrate binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: enables
  review:
    summary: Automated (IEA, Ensembl Compara) assignment of carbohydrate binding.
    action: MARK_AS_OVER_ANNOTATED
    reason: The enzyme binds sugar-phosphate substrates in its active site, so binding
      is not wrong, but 'carbohydrate binding' is an uninformative molecular function
      relative to the specific transaldolase activity (GO:0004801) that already
      captures substrate recognition and turnover. It is an over-annotation of the
      catalytic function.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: /ligand="D-fructose 6-phosphate"
- term:
    id: GO:0048029
    label: monosaccharide binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: enables
  review:
    summary: Automated (IEA, Ensembl Compara) assignment of monosaccharide binding.
    action: MARK_AS_OVER_ANNOTATED
    reason: As with carbohydrate binding, transaldolase binds its monosaccharide-phosphate
      substrates, but this generic binding term is uninformative relative to the
      catalytic transaldolase activity and represents an over-annotation.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: /ligand="D-fructose 6-phosphate"
- term:
    id: GO:0004801
    label: transaldolase activity
  evidence_type: EXP
  original_reference_id: PMID:8955144
  qualifier: enables
  review:
    summary: Experimental (EXP) evidence for transaldolase activity; Banki et al.
      characterized human TAL and its role in the non-oxidative PPP branch.
    action: ACCEPT
    reason: Direct experimental support for the core molecular function in the human
      enzyme, forming the basis of the UniProt EC 2.2.1.2 assignment.
    supported_by:
    - reference_id: PMID:8955144
      supporting_text: Transaldolase (TAL) is a key enzyme of the reversible nonoxidative
        branch of the pentose phosphate pathway (PPP)
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: located_in
  review:
    summary: ISS transfer of nuclear localization from the rat ortholog (Q93092).
    action: KEEP_AS_NON_CORE
    reason: Consistent with the regulated nuclear shuttling of isoform 1 (importin/CRM1
      dependent), transferred by similarity from rat. Real but non-core relative to
      the cytosolic catalytic function.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: 'Exported into the cytoplasm by CRM1.'
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: located_in
  review:
    summary: ISS transfer of cytoplasmic localization from the rat ortholog (Q93092).
    action: ACCEPT
    reason: Cytoplasmic localization is the primary site of transaldolase function
      and is well-supported; a broader parent of the preferred cytosol term.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: Shuttles between the nucleus and
- term:
    id: GO:0004801
    label: transaldolase activity
  evidence_type: IMP
  original_reference_id: PMID:18498245
  qualifier: enables
  review:
    summary: IMP evidence for transaldolase activity based on the metabolic phenotype
      of transaldolase-deficient human lymphoblasts (Ser171 deletion).
    action: ACCEPT
    reason: Loss of TALDO1 in patient cells causes accumulation of sedoheptulose
      7-phosphate and depletion of glucose 6-phosphate, directly demonstrating the
      enzyme's transaldolase activity in vivo.
    supported_by:
    - reference_id: PMID:18498245
      supporting_text: Sedoheptulose 7-phosphate was accumulated, whereas G6P (glucose
        6-phosphate) was depleted
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: IDA
  original_reference_id: PMID:18498245
  qualifier: located_in
  review:
    summary: Direct assay (IDA) localizing transaldolase to the cytosol.
    action: ACCEPT
    reason: Direct experimental support for cytosolic localization, the primary site
      of the enzyme's PPP function. Core localization.
    supported_by:
    - reference_id: PMID:18498245
      supporting_text: TAL (transaldolase) was originally described in the yeast as
        an enzyme of the PPP (pentose phosphate pathway)
- term:
    id: GO:0009052
    label: pentose-phosphate shunt, non-oxidative branch
  evidence_type: IMP
  original_reference_id: PMID:18498245
  qualifier: involved_in
  review:
    summary: IMP evidence for involvement in the non-oxidative PPP branch, from the
      transaldolase-deficiency metabolic phenotype.
    action: ACCEPT
    reason: The sedoheptulose-7-phosphate accumulation and glucose-6-phosphate
      depletion in TAL-deficient cells directly demonstrate the enzyme's role in the
      non-oxidative branch of the pentose phosphate pathway. Core BP.
    supported_by:
    - reference_id: PMID:18498245
      supporting_text: indicating a failure to recycle G6P for the oxidative branch
        of the PPP
- term:
    id: GO:0004801
    label: transaldolase activity
  evidence_type: IDA
  original_reference_id: PMID:18687684
  qualifier: enables
  review:
    summary: Direct assay (IDA) of human transaldolase (Taldo1) activity; the wild-type
      and F189Y variant were assayed biochemically.
    action: ACCEPT
    reason: Provides direct biochemical measurement of human TALDO1 transaldolase
      activity, underpinning the EC 2.2.1.2 assignment. Core molecular function.
    supported_by:
    - reference_id: PMID:18687684
      supporting_text: we show that a homologous replacement has a similar effect in
        the human transaldolase Taldo1 (aldolase activity, 14 units/mg).
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25854864
  qualifier: enables
  review:
    summary: IPI protein-binding annotation associated with a BAP31 (BCAP31)
      interaction study (recorded with UniProtKB:Q77YB1 in the WITH/FROM field).
    action: MARK_AS_OVER_ANNOTATED
    reason: "'protein binding' is uninformative about molecular function, and this
      annotation derives from an interaction study focused on BAP31/RSV SH protein
      rather than a characterized functional interaction of transaldolase. Kept as
      over-annotated rather than removed per curation policy on protein-binding IPIs."
    supported_by:
    - reference_id: PMID:25854864
      supporting_text: This led to the identification of a membrane protein, B-cell
        associated protein 31 (BAP31).
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5659989
  qualifier: located_in
  review:
    summary: Reactome traceable-author-statement placing transaldolase in the cytosol
      (transaldolase-deficiency reaction module).
    action: ACCEPT
    reason: Consistent with the well-established cytosolic localization of the PPP
      enzyme. Core localization.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: 'Distributed under the Creative Commons Attribution (CC BY 4.0) License'
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-5659998
  qualifier: located_in
  review:
    summary: Reactome TAS placing transaldolase in the cytosol (transaldolase-deficiency
      reaction module).
    action: ACCEPT
    reason: Redundant with other cytosol annotations; consistent with the enzyme's
      established cytosolic PPP function.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: 'Distributed under the Creative Commons Attribution (CC BY 4.0) License'
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:23533145
  qualifier: located_in
  review:
    summary: High-throughput proteomic detection (HDA) of TALDO1 in exosomes isolated
      from expressed prostatic secretions in urine.
    action: KEEP_AS_NON_CORE
    reason: TALDO1 is a cytosolic metabolic enzyme frequently co-purified in exosome
      proteomes; this HDA detection is real but does not indicate a functional
      extracellular-exosome localization or role, so it is retained as non-core.
    supported_by:
    - reference_id: PMID:23533145
      supporting_text: In pooled EPS-urine exosome samples, ~900 proteins were detected.
- term:
    id: GO:0005634
    label: nucleus
  evidence_type: HDA
  original_reference_id: PMID:21630459
  qualifier: located_in
  review:
    summary: High-throughput proteomic detection (HDA) of TALDO1 in the human sperm
      nucleus proteome.
    action: KEEP_AS_NON_CORE
    reason: Consistent with the known nuclear pool of TALDO1 from regulated shuttling,
      but this large-scale proteomic detection does not establish a nuclear catalytic
      function; retained as non-core.
    supported_by:
    - reference_id: PMID:21630459
      supporting_text: 403 different proteins have been identified from the isolated
        sperm nuclei.
- term:
    id: GO:0070062
    label: extracellular exosome
  evidence_type: HDA
  original_reference_id: PMID:20458337
  qualifier: located_in
  review:
    summary: High-throughput proteomic detection (HDA) of TALDO1 in B-cell-derived
      exosomes.
    action: KEEP_AS_NON_CORE
    reason: As with the prostatic-secretion exosome dataset, this reflects proteomic
      co-purification of a cytosolic enzyme in exosome preparations rather than a
      functional exosomal role; retained as non-core.
    supported_by:
    - reference_id: PMID:20458337
      supporting_text: analyzed the total proteome of highly purified B cell-derived
        exosomes using sensitive and accurate mass spectrometry (MS), and identified
        539 proteins
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-163764
  qualifier: located_in
  review:
    summary: Reactome TAS placing transaldolase in the cytosol.
    action: ACCEPT
    reason: Redundant with other cytosol annotations; consistent with the established
      cytosolic PPP function.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: 'Distributed under the Creative Commons Attribution (CC BY 4.0) License'
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-71334
  qualifier: located_in
  review:
    summary: Reactome TAS placing transaldolase in the cytosol (pentose phosphate
      pathway module).
    action: ACCEPT
    reason: Redundant with other cytosol annotations; consistent with the established
      cytosolic PPP function.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: 'Distributed under the Creative Commons Attribution (CC BY 4.0) License'
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-8950367
  qualifier: located_in
  review:
    summary: Reactome TAS placing transaldolase in the cytosol.
    action: ACCEPT
    reason: Redundant with other cytosol annotations; consistent with the established
      cytosolic PPP function.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: 'Distributed under the Creative Commons Attribution (CC BY 4.0) License'
- term:
    id: GO:0005829
    label: cytosol
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9761858
  qualifier: located_in
  review:
    summary: Reactome TAS placing transaldolase in the cytosol.
    action: ACCEPT
    reason: Redundant with other cytosol annotations; consistent with the established
      cytosolic PPP function.
    supported_by:
    - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
      supporting_text: 'Distributed under the Creative Commons Attribution (CC BY 4.0) License'
- term:
    id: GO:0005737
    label: cytoplasm
  evidence_type: TAS
  original_reference_id: PMID:16130169
  qualifier: located_in
  review:
    summary: TAS cytoplasmic localization from a HUVEC proteomics study.
    action: ACCEPT
    reason: Cytoplasm is the correct primary localization for transaldolase; broader
      parent of the preferred cytosol term. Consistent with all other localization
      evidence.
    supported_by:
    - reference_id: PMID:16130169
      supporting_text: the metabolic capabilities of endothelium
- term:
    id: GO:0004801
    label: transaldolase activity
  evidence_type: TAS
  original_reference_id: PMID:9524206
  qualifier: enables
  review:
    summary: TAS annotation of transaldolase activity from the cloning/characterization
      paper for the human transaldolase gene and its paralog.
    action: ACCEPT
    reason: Correct core molecular function; the reference established the human
      transaldolase gene structure and family. Redundant with the experimental
      annotations.
    supported_by:
    - reference_id: PMID:9524206
      supporting_text: A sequence homologous to the transaldolase gene (TALDO)
- term:
    id: GO:0005975
    label: carbohydrate metabolic process
  evidence_type: TAS
  original_reference_id: PMID:9524206
  qualifier: involved_in
  review:
    summary: TAS annotation of carbohydrate metabolic process from the transaldolase
      gene cloning paper.
    action: ACCEPT
    reason: Correct but very general parent of the pentose phosphate pathway. The
      more specific PPP terms capture the core process; not a core annotation on its own.
    supported_by:
    - reference_id: PMID:9524206
      supporting_text: To examine the evolutionary conservation of two genes for
        transaldolase
core_functions:
- description: Transaldolase catalyses the reversible transfer of a three-carbon
    dihydroxyacetone unit from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate
    (and the reverse), interconverting sedoheptulose-7-phosphate + glyceraldehyde-3-phosphate
    with erythrose-4-phosphate + fructose-6-phosphate. This is the rate-limiting step
    of the non-oxidative branch of the pentose phosphate pathway, linking it to the
    glycolytic intermediate pool, and takes place in the cytosol.
  molecular_function:
    id: GO:0004801
    label: transaldolase activity
  directly_involved_in:
  - id: GO:0009052
    label: pentose-phosphate shunt, non-oxidative branch
  locations:
  - id: GO:0005829
    label: cytosol
  supported_by:
  - reference_id: PMID:18687684
    supporting_text: we show that a homologous replacement has a similar effect in
      the human transaldolase Taldo1 (aldolase activity, 14 units/mg).
  - reference_id: PMID:18498245
    supporting_text: Sedoheptulose 7-phosphate was accumulated, whereas G6P (glucose
      6-phosphate) was depleted
  - reference_id: file:human/TALDO1/TALDO1-uniprot.txt
    supporting_text: 'Catalyzes the rate-limiting step of the non-oxidative phase'
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- id: GO_REF:0000024
  title: Manual transfer of experimentally-verified manual GO annotation data to orthologs
    by curator judgment of sequence similarity
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location
    vocabulary mapping, accompanied by conservative changes to GO terms applied by
    UniProt
  findings: []
- id: GO_REF:0000107
  title: Automatic transfer of experimentally verified manual GO annotation data to
    orthologs using Ensembl Compara
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: PMID:16130169
  title: Proteomics of human umbilical vein endothelial cells applied to etoposide-induced
    apoptosis.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: HUVEC proteomics dataset; TALDO1 detected as a cytoplasmic enzyme.
      Supports cytoplasmic localization only in a proteome-catalogue sense.
- id: PMID:18498245
  title: Transaldolase deficiency influences the pentose phosphate pathway, mitochondrial
    homoeostasis and apoptosis signal processing.
  findings:
  - statement: Transaldolase-deficient human lymphoblasts (Ser171 deletion) accumulate
      sedoheptulose 7-phosphate and are depleted of glucose 6-phosphate, demonstrating
      the enzyme's role in the non-oxidative pentose phosphate pathway.
    supporting_text: Sedoheptulose 7-phosphate was accumulated, whereas G6P (glucose
      6-phosphate) was depleted
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Loss-of-function metabolic phenotype in human TAL-deficient cells;
      abstract-only cache but directly supports transaldolase activity and non-oxidative
      PPP involvement.
- id: PMID:18687684
  title: Replacement of a phenylalanine by a tyrosine in the active site confers fructose-6-phosphate
    aldolase activity to the transaldolase of Escherichia coli and human origin.
  findings:
  - statement: Human transaldolase (Taldo1) was biochemically assayed; the study
      confirms its transaldolase/aldolase activity and active-site mechanism.
    supporting_text: we show that a homologous replacement has a similar effect in
      the human transaldolase Taldo1 (aldolase activity, 14 units/mg).
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Biochemical characterization of human TALDO1 activity; basis of the
      UniProt EC 2.2.1.2 assignment and the IDA on GO:0004801.
- id: PMID:20458337
  title: MHC class II-associated proteins in B-cell exosomes and potential functional
    implications for exosome biogenesis.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: B-cell exosome proteome; supports HDA detection of TALDO1 in
      exosomes only (proteomic co-purification, not a functional location).
- id: PMID:21044950
  title: Genome-wide YFP fluorescence complementation screen identifies new regulators
    for telomere signaling in human cells.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: Large-scale BiFC telomere-interactome screen; source of an
      uninformative 'protein binding' IPI (TERF2IP), not a characterized functional
      interaction.
- id: PMID:21630459
  title: Proteomic characterization of the human sperm nucleus.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: Sperm-nucleus proteome; supports HDA detection of TALDO1 in the
      nucleus (consistent with the known shuttling pool), not a catalytic function.
- id: PMID:23533145
  title: In-depth proteomic analyses of exosomes isolated from expressed prostatic
    secretions in urine.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: EPS-urine exosome proteome; supports HDA detection of TALDO1 in
      exosomes only (proteomic co-purification).
- id: PMID:25854864
  title: Interaction between human BAP31 and respiratory syncytial virus small hydrophobic
    (SH) protein.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: BAP31/RSV SH interaction study; basis of an uninformative
      'protein binding' IPI for TALDO1 rather than a characterized functional interaction.
- id: PMID:32814053
  title: Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins
    and Uncovers Widespread Protein Aggregation in Affected Brains.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: Systematic ND Y2H interactome map; source of an uninformative
      'protein binding' IPI (HTT), not a characterized functional interaction.
- id: PMID:8955144
  title: Glutathione levels and sensitivity to apoptosis are regulated by changes
    in transaldolase expression.
  findings:
  - statement: Transaldolase is a key enzyme of the reversible non-oxidative branch
      of the pentose phosphate pathway, whose expression level modulates the balance
      between the oxidative and non-oxidative branches and thereby NADPH/GSH levels.
    supporting_text: Transaldolase (TAL) is a key enzyme of the reversible nonoxidative
      branch of the pentose phosphate pathway (PPP)
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Functional characterization of human TAL; establishes the
      non-oxidative PPP role. Abstract-only cache but directly supports the core function.
- id: PMID:9524206
  title: Cloning and chromosomal localization of a paralog and a mouse homolog of
    the human transaldolase gene.
  findings:
  - statement: Established the human transaldolase gene (TALDO) and identified a
      paralog and mouse homolog.
    supporting_text: A sequence homologous to the transaldolase gene (TALDO)
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: Gene cloning/characterization paper; basis of the TAS annotations
      for transaldolase activity and carbohydrate metabolic process.
- id: Reactome:R-HSA-163764
  title: "D-fructose 6-phosphate + D-erythrose 4-phosphate  <=>  sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate"
  findings: []
- id: Reactome:R-HSA-5659989
  title: "Defective TALDO1 does not transform SH7P, GA3P to Fru(6)P, E4P"
  findings: []
- id: Reactome:R-HSA-5659998
  title: "Defective TALDO1 does not transform Fru(6)P, E4P to SH7P, GA3P"
  findings: []
- id: Reactome:R-HSA-71334
  title: "sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate <=> D-erythrose 4-phosphate + D-fructose 6-phosphate"
  findings: []
- id: Reactome:R-HSA-8950367
  title: "Expression of transaldolase 1"
  findings: []
- id: Reactome:R-HSA-9761858
  title: "NFE2L2-dependent TALDO1 gene expression"
  findings: []
- id: file:human/TALDO1/TALDO1-uniprot.txt
  title: UniProtKB entry P37837 (TALDO_HUMAN), transaldolase
  findings: []