TALDO1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0004801 transaldolase activity	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) assignment of transaldolase activity, the defining molecular function of this gene and its orthologs across the transaldolase family. 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. Supporting Evidence: PMID:18687684 we show that a homologous replacement has a similar effect in the human transaldolase Taldo1 (aldolase activity, 14 units/mg). file:human/TALDO1/TALDO1-uniprot.txt Catalyzes the rate-limiting step of the non-oxidative phase
GO:0009052 pentose-phosphate shunt, non-oxidative branch	IBA GO_REF:0000033	ACCEPT	Summary: Phylogenetic (IBA) assignment placing transaldolase in the non-oxidative branch of the pentose phosphate pathway, its core biological process. 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). Supporting Evidence: PMID:8955144 Transaldolase (TAL) is a key enzyme of the reversible nonoxidative branch of the pentose phosphate pathway (PPP) PMID:18498245 Sedoheptulose 7-phosphate was accumulated, whereas G6P (glucose 6-phosphate) was depleted
GO:0005634 nucleus	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: Phylogenetic (IBA) assignment of nuclear localization, reflecting the regulated nucleocytoplasmic shuttling of transaldolase seen in mammalian orthologs. 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. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt The first 10 amino acids are essential for nuclear
GO:0004801 transaldolase activity	IEA GO_REF:0000120	ACCEPT	Summary: Automated (IEA) assignment of transaldolase activity via InterPro/ARBA/EC/RHEA mapping (EC 2.2.1.2, RHEA:17053). Reason: Correct core molecular function, redundant with experimental and IBA annotations. The EC/RHEA/InterPro evidence chain matches the characterized human enzyme. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt EC=2.2.1.2
GO:0005634 nucleus	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: Automated (IEA) nuclear localization from UniProt Subcellular Location keyword mapping (SL-0191). 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. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt Actively transported into the nucleus in an importin
GO:0005737 cytoplasm	IEA GO_REF:0000120	ACCEPT	Summary: Automated (IEA) cytoplasmic localization via InterPro/ARBA and UniProt Subcellular Location mapping (SL-0086). 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. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
GO:0005975 carbohydrate metabolic process	IEA GO_REF:0000002	ACCEPT	Summary: Automated (IEA) assignment of carbohydrate metabolic process from InterPro family membership (TAL/FSA). 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. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt Belongs to the transaldolase family. Type 1 subfamily.
GO:0006098 pentose-phosphate shunt	IEA GO_REF:0000120	ACCEPT	Summary: Automated (IEA) assignment of the pentose phosphate pathway via ARBA/InterPro/UniPathway (UPA00115). 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. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt PATHWAY: Carbohydrate degradation; pentose phosphate pathway
GO:0005515 protein binding	IPI PMID:21044950 Genome-wide YFP fluorescence complementation screen identifi...	MARK AS OVER ANNOTATED	Summary: IPI protein-binding annotation from a genome-wide BiFC telomere-interactome screen; TALDO1 was flagged as interacting with TERF2IP/RAP1 (Q9NYB0). 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. Supporting Evidence: PMID:21044950 we developed an arrayed screening strategy based on protein complementation to systematically investigate protein-protein interactions in live human cells
GO:0005515 protein binding	IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ...	MARK AS OVER ANNOTATED	Summary: IPI protein-binding annotation from a neurodegenerative-disease Y2H interactome map; TALDO1 recorded interacting with HTT (P42858). 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. Supporting Evidence: PMID:32814053 generated by systematic yeast two-hybrid interaction screening of ∼500 ND-related proteins and integration of literature interactions
GO:0005829 cytosol	IEA GO_REF:0000107	ACCEPT	Summary: Automated (IEA, Ensembl Compara orthology) assignment of cytosolic localization/activity. Reason: Cytosol is the primary site of transaldolase catalysis in the PPP, consistent with experimental (IDA) and Reactome annotations. This is a core localization. Supporting Evidence: PMID:18498245 Transaldolase deficiency influences the pentose phosphate pathway
GO:0006002 fructose 6-phosphate metabolic process	IEA GO_REF:0000107	ACCEPT	Summary: Automated (IEA, Ensembl Compara) assignment of fructose-6-phosphate metabolic process. 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. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt erythrose-4-phosphate and beta-D-fructose 6-phosphate
GO:0009052 pentose-phosphate shunt, non-oxidative branch	IEA GO_REF:0000107	ACCEPT	Summary: Automated (IEA, Ensembl Compara) assignment of the non-oxidative branch of the pentose phosphate pathway. Reason: Correct core biological process, redundant with the IBA and IMP annotations to the same term. Supporting Evidence: PMID:8955144 Transaldolase (TAL) is a key enzyme of the reversible nonoxidative branch of the pentose phosphate pathway (PPP)
GO:0019682 glyceraldehyde-3-phosphate metabolic process	IEA GO_REF:0000107	ACCEPT	Summary: Automated (IEA, Ensembl Compara) assignment of glyceraldehyde-3-phosphate metabolic process. 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. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt of sedoheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into
GO:0030246 carbohydrate binding	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: Automated (IEA, Ensembl Compara) assignment of carbohydrate binding. 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. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt /ligand="D-fructose 6-phosphate"
GO:0048029 monosaccharide binding	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: Automated (IEA, Ensembl Compara) assignment of monosaccharide binding. 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. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt /ligand="D-fructose 6-phosphate"
GO:0004801 transaldolase activity	EXP PMID:8955144 Glutathione levels and sensitivity to apoptosis are regulate...	ACCEPT	Summary: Experimental (EXP) evidence for transaldolase activity; Banki et al. characterized human TAL and its role in the non-oxidative PPP branch. 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. Supporting Evidence: PMID:8955144 Transaldolase (TAL) is a key enzyme of the reversible nonoxidative branch of the pentose phosphate pathway (PPP)
GO:0005634 nucleus	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: ISS transfer of nuclear localization from the rat ortholog (Q93092). 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. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt Exported into the cytoplasm by CRM1.
GO:0005737 cytoplasm	ISS GO_REF:0000024	ACCEPT	Summary: ISS transfer of cytoplasmic localization from the rat ortholog (Q93092). Reason: Cytoplasmic localization is the primary site of transaldolase function and is well-supported; a broader parent of the preferred cytosol term. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt Shuttles between the nucleus and
GO:0004801 transaldolase activity	IMP PMID:18498245 Transaldolase deficiency influences the pentose phosphate pa...	ACCEPT	Summary: IMP evidence for transaldolase activity based on the metabolic phenotype of transaldolase-deficient human lymphoblasts (Ser171 deletion). 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. Supporting Evidence: PMID:18498245 Sedoheptulose 7-phosphate was accumulated, whereas G6P (glucose 6-phosphate) was depleted
GO:0005829 cytosol	IDA PMID:18498245 Transaldolase deficiency influences the pentose phosphate pa...	ACCEPT	Summary: Direct assay (IDA) localizing transaldolase to the cytosol. Reason: Direct experimental support for cytosolic localization, the primary site of the enzyme's PPP function. Core localization. Supporting Evidence: PMID:18498245 TAL (transaldolase) was originally described in the yeast as an enzyme of the PPP (pentose phosphate pathway)
GO:0009052 pentose-phosphate shunt, non-oxidative branch	IMP PMID:18498245 Transaldolase deficiency influences the pentose phosphate pa...	ACCEPT	Summary: IMP evidence for involvement in the non-oxidative PPP branch, from the transaldolase-deficiency metabolic phenotype. 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. Supporting Evidence: PMID:18498245 indicating a failure to recycle G6P for the oxidative branch of the PPP
GO:0004801 transaldolase activity	IDA PMID:18687684 Replacement of a phenylalanine by a tyrosine in the active s...	ACCEPT	Summary: Direct assay (IDA) of human transaldolase (Taldo1) activity; the wild-type and F189Y variant were assayed biochemically. Reason: Provides direct biochemical measurement of human TALDO1 transaldolase activity, underpinning the EC 2.2.1.2 assignment. Core molecular function. Supporting Evidence: PMID:18687684 we show that a homologous replacement has a similar effect in the human transaldolase Taldo1 (aldolase activity, 14 units/mg).
GO:0005515 protein binding	IPI PMID:25854864 Interaction between human BAP31 and respiratory syncytial vi...	MARK AS OVER ANNOTATED	Summary: IPI protein-binding annotation associated with a BAP31 (BCAP31) interaction study (recorded with UniProtKB:Q77YB1 in the WITH/FROM field). 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. Supporting Evidence: PMID:25854864 This led to the identification of a membrane protein, B-cell associated protein 31 (BAP31).
GO:0005829 cytosol	TAS Reactome:R-HSA-5659989	ACCEPT	Summary: Reactome traceable-author-statement placing transaldolase in the cytosol (transaldolase-deficiency reaction module). Reason: Consistent with the well-established cytosolic localization of the PPP enzyme. Core localization. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt Distributed under the Creative Commons Attribution (CC BY 4.0) License
GO:0005829 cytosol	TAS Reactome:R-HSA-5659998	ACCEPT	Summary: Reactome TAS placing transaldolase in the cytosol (transaldolase-deficiency reaction module). Reason: Redundant with other cytosol annotations; consistent with the enzyme's established cytosolic PPP function. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt Distributed under the Creative Commons Attribution (CC BY 4.0) License
GO:0070062 extracellular exosome	HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres...	KEEP AS NON CORE	Summary: High-throughput proteomic detection (HDA) of TALDO1 in exosomes isolated from expressed prostatic secretions in urine. 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. Supporting Evidence: PMID:23533145 In pooled EPS-urine exosome samples, ~900 proteins were detected.
GO:0005634 nucleus	HDA PMID:21630459 Proteomic characterization of the human sperm nucleus.	KEEP AS NON CORE	Summary: High-throughput proteomic detection (HDA) of TALDO1 in the human sperm nucleus proteome. 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. Supporting Evidence: PMID:21630459 403 different proteins have been identified from the isolated sperm nuclei.
GO:0070062 extracellular exosome	HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote...	KEEP AS NON CORE	Summary: High-throughput proteomic detection (HDA) of TALDO1 in B-cell-derived exosomes. 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. Supporting Evidence: PMID:20458337 analyzed the total proteome of highly purified B cell-derived exosomes using sensitive and accurate mass spectrometry (MS), and identified 539 proteins
GO:0005829 cytosol	TAS Reactome:R-HSA-163764	ACCEPT	Summary: Reactome TAS placing transaldolase in the cytosol. Reason: Redundant with other cytosol annotations; consistent with the established cytosolic PPP function. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt Distributed under the Creative Commons Attribution (CC BY 4.0) License
GO:0005829 cytosol	TAS Reactome:R-HSA-71334	ACCEPT	Summary: Reactome TAS placing transaldolase in the cytosol (pentose phosphate pathway module). Reason: Redundant with other cytosol annotations; consistent with the established cytosolic PPP function. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt Distributed under the Creative Commons Attribution (CC BY 4.0) License
GO:0005829 cytosol	TAS Reactome:R-HSA-8950367	ACCEPT	Summary: Reactome TAS placing transaldolase in the cytosol. Reason: Redundant with other cytosol annotations; consistent with the established cytosolic PPP function. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt Distributed under the Creative Commons Attribution (CC BY 4.0) License
GO:0005829 cytosol	TAS Reactome:R-HSA-9761858	ACCEPT	Summary: Reactome TAS placing transaldolase in the cytosol. Reason: Redundant with other cytosol annotations; consistent with the established cytosolic PPP function. Supporting Evidence: file:human/TALDO1/TALDO1-uniprot.txt Distributed under the Creative Commons Attribution (CC BY 4.0) License
GO:0005737 cytoplasm	TAS PMID:16130169 Proteomics of human umbilical vein endothelial cells applied...	ACCEPT	Summary: TAS cytoplasmic localization from a HUVEC proteomics study. Reason: Cytoplasm is the correct primary localization for transaldolase; broader parent of the preferred cytosol term. Consistent with all other localization evidence. Supporting Evidence: PMID:16130169 the metabolic capabilities of endothelium
GO:0004801 transaldolase activity	TAS PMID:9524206 Cloning and chromosomal localization of a paralog and a mous...	ACCEPT	Summary: TAS annotation of transaldolase activity from the cloning/characterization paper for the human transaldolase gene and its paralog. Reason: Correct core molecular function; the reference established the human transaldolase gene structure and family. Redundant with the experimental annotations. Supporting Evidence: PMID:9524206 A sequence homologous to the transaldolase gene (TALDO)
GO:0005975 carbohydrate metabolic process	TAS PMID:9524206 Cloning and chromosomal localization of a paralog and a mous...	ACCEPT	Summary: TAS annotation of carbohydrate metabolic process from the transaldolase gene cloning paper. 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. Supporting Evidence: PMID:9524206 To examine the evolutionary conservation of two genes for transaldolase

Gene Description

Existing Annotations Review

Core Functions

References

📚 Additional Documentation

Notes

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