tpx1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0005829 cytosol	IBA GO_REF:0000033	ACCEPT	Summary: Tpx1 is predominantly cytosolic before and after H2O2 exposure, consistent with its roles in controlling cytosolic thioredoxins and transcription-factor signaling. A minor mitochondrial intermembrane-space pool is also reported under oxidative conditions, but the cytosol is the principal site of function. Reason: Supported by phylogenetic inference and corroborated by falcon deep research and experimental localization data. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 is primarily described as cytosolic before and after H2O2 exposure, consistent with its roles in controlling cytosolic thioredoxins and transcription factor signaling.
GO:0006979 response to oxidative stress	IBA GO_REF:0000033	ACCEPT	Summary: Response to oxidative stress is a central biological process for Tpx1, which is the major peroxide-detoxifying enzyme during aerobic growth; tpx1 deletion causes extreme peroxide sensitivity. This is a true core function rather than a peripheral context, though the more specific term hydrogen peroxide catabolic process is preferred for the MF/process pairing. Reason: Falcon deep research and primary literature establish oxidative stress defense as a central, not peripheral, role for Tpx1. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 is central to peroxide defense during aerobic growth: loss of Tpx1 yields strong peroxide sensitivity and evidence of increased oxidative damage, consistent with a major antioxidant role.
GO:0008379 thioredoxin peroxidase activity	IBA GO_REF:0000033	ACCEPT	Summary: Core molecular function. Tpx1 is a thioredoxin-dependent peroxidase that detoxifies hydrogen peroxide and organic peroxides, recycled primarily by the cytosolic thioredoxin system (Trx1 main donor), consistent with its classification as the single typical 2-Cys peroxiredoxin of S. pombe. Reason: Supported by phylogenetic inference and corroborated by experimental literature and falcon deep research. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 functions as a thioredoxin-dependent peroxidase that detoxifies hydrogen peroxide and can also reduce organic peroxides, consistent with its classification as a typical 2‑Cys peroxiredoxin. file:SCHPO/tpx1/tpx1-deep-research-falcon.md Trx1 is described as the main electron donor for Tpx1, with Trx3 reported as partially compensatory when Trx1 is absent; thioredoxin reductase (Trr1) maintains the thioredoxin pool using NADPH.
GO:0042744 hydrogen peroxide catabolic process	IBA GO_REF:0000033	ACCEPT	Summary: Core biological process. As the major 2-Cys peroxiredoxin, Tpx1 reduces hydrogen peroxide to water; tpx1 deletion causes extreme peroxide sensitivity and increased oxidative damage markers, directly supporting this catabolic role in vivo. Reason: Supported by phylogenetic inference and corroborated by falcon deep research and primary literature. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Experimentally, tpx1 deletion causes extreme peroxide sensitivity and increased oxidative damage markers (e.g., protein carbonylation), supporting a central peroxide-detoxifying role in vivo.
GO:0045454 cell redox homeostasis	IBA GO_REF:0000033	ACCEPT	Summary: Core process. Tpx1 maintains cellular redox balance via the thioredoxin-coupled peroxidatic cycle (Cys48 peroxidatic / Cys169 resolving), the reducing equivalents being supplied by the thioredoxin system (Trx1/Trr1/NADPH). Reason: Supported by phylogenetic inference and corroborated by falcon deep research. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Trx1 is described as the main electron donor for Tpx1, with Trx3 reported as partially compensatory when Trx1 is absent; thioredoxin reductase (Trr1) maintains the thioredoxin pool using NADPH.
GO:0000165 MAPK cascade	IEA GO_REF:0000108	KEEP AS NON CORE	Summary: Tpx1 acts as a redox transducer in the Sty1 (p38/SAPK) MAPK pathway, promoting Sty1 activation in response to H2O2. This is a genuine signaling role of the gene, though this generic IEA term is less specific than the experimentally supported positive regulation of p38MAPK cascade (GO:1900745) annotation retained elsewhere. Reason: Genuine but generic; the experimentally supported p38MAPK regulation term is preferred for the core signaling role. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Underwood (2019) describes Tpx1 as a direct redox transducer promoting Sty1 activation, and other mechanistic discussion links Tpx1 to Sty1 regulation and oxidation events, including interactions/disulfide formation with Sty1.
GO:0004601 peroxidase activity	IEA GO_REF:0000043	ACCEPT	Summary: Correct but generic. Peroxidase activity is the parent of the specific thioredoxin-dependent peroxiredoxin activity (GO:0140824) that captures the actual mechanism; retained as a true but less informative grouping term. Reason: Accurate parent term; the more specific thioredoxin-dependent peroxiredoxin activity is the core MF. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 functions as a thioredoxin-dependent peroxidase that detoxifies hydrogen peroxide and can also reduce organic peroxides, consistent with its classification as a typical 2‑Cys peroxiredoxin.
GO:0005634 nucleus	IEA GO_REF:0000044	KEEP AS NON CORE	Summary: Nuclear localization is reported from large-scale localization analysis (also annotated HDA from PMID:16823372). Plausible given Tpx1 influence on transcription-factor (Pap1) activation, but Tpx1 is predominantly cytosolic and the bulk of its function is executed in the cytosol. Retained as non-core. Reason: Supported by localization screens but secondary to the predominant cytosolic site of function per falcon deep research. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 is primarily described as cytosolic before and after H2O2 exposure, consistent with its roles in controlling cytosolic thioredoxins and transcription factor signaling.
GO:0005737 cytoplasm	IEA GO_REF:0000120	ACCEPT	Summary: Consistent with the predominant cytosolic localization of Tpx1. Cytosol (GO:0005829) is the more precise term and is also annotated; cytoplasm is the accurate parent. Reason: Supported by experimental localization and falcon deep research; cytosol is the more specific term. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 is primarily described as cytosolic before and after H2O2 exposure, consistent with its roles in controlling cytosolic thioredoxins and transcription factor signaling.
GO:0016209 antioxidant activity	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: High-level grouping term that is correct (Tpx1 is a major antioxidant enzyme) but uninformative relative to the specific thioredoxin-dependent peroxiredoxin activity. Retained as non-core. Reason: Correct but generic grouping term superseded by the specific peroxiredoxin MF.
GO:0016491 oxidoreductase activity	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: Very high-level grouping term. Correct (Tpx1 is a thiol-based oxidoreductase, EC 1.11.1.24) but far less informative than the specific peroxiredoxin activity term. Retained as non-core. Reason: Accurate but uninformative root-level term superseded by the specific peroxiredoxin MF.
GO:0034599 cellular response to oxidative stress	IEA GO_REF:0000117	ACCEPT	Summary: Consistent with Tpx1 acting as both the major peroxide scavenger and a H2O2 sensor/transducer that routes oxidative-stress information to the Pap1 and Sty1 response pathways. Reason: Supported by falcon deep research and primary literature on Tpx1-mediated oxidative stress signaling. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md A defining feature of S. pombe Tpx1 is that it is not only an antioxidant enzyme but also a central peroxide sensor/transducer that routes H2O2 information to at least two major oxidative stress response branches: Pap1 (AP‑1-like) and the Sty1/Atf1 stress-activated MAPK pathway.
GO:0051920 peroxiredoxin activity	IEA GO_REF:0000002	ACCEPT	Summary: Accurate. Tpx1 is the single typical 2-Cys peroxiredoxin of S. pombe, using a peroxidatic Cys48 and resolving Cys169. The more specific thioredoxin-dependent peroxiredoxin activity (GO:0140824) is preferred as core MF. Reason: Supported by InterPro/family inference and corroborated by falcon deep research. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md catalytic cycle in S. pombe involves a peroxidatic cysteine (Cys48) and resolving cysteine (Cys169), consistent with typical 2‑Cys Prx chemistry.
GO:0140824 thioredoxin-dependent peroxiredoxin activity	IEA GO_REF:0000120	ACCEPT	Summary: Core molecular function. Tpx1 reduces peroxides using the thioredoxin system as electron donor (Trx1 main donor, Trr1/NADPH recycling), matching the EC 1.11.1.24 catalytic activity in UniProt. This is the most specific MF term and is duplicated by an IDA-supported annotation below. Reason: Supported by IEA and corroborated by experimental IDA evidence and falcon deep research. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Trx1 is described as the main electron donor for Tpx1, with Trx3 reported as partially compensatory when Trx1 is absent; thioredoxin reductase (Trr1) maintains the thioredoxin pool using NADPH.
GO:0005078 MAP kinase scaffold activity	EXP PMID:37572670 A peroxiredoxin-P38 MAPK scaffold increases MAPK activity by...	MARK AS OVER ANNOTATED	Summary: The scaffold-activity annotation rests on an artificial, genetically encoded peroxiredoxin-P38 fusion protein that substitutes for the Mcs4 scaffold and MAP3K activity in driving cells into mitosis "by a mechanism that does not require the H2O2-sensing cysteine of the Prdx." This demonstrates what a covalent Prdx-MAPK fusion can do, but assigning native Tpx1 a dedicated MAP kinase scaffold molecular function on this basis is an over-extension: the native redox-transducer role for the Sty1/p38 pathway is more accurately captured by the positive regulation of p38MAPK cascade (GO:1900745) process term retained elsewhere. Reason: Evidence is from an engineered Prdx-P38 fusion construct (cysteine-independent), not native Tpx1; the genuine signaling role is captured by the p38MAPK regulation process term, so a dedicated scaffold MF over-annotates the native protein. Supporting Evidence: PMID:37572670 We demonstrate that a P38-Prdx fusion protein compensates for loss of the yeast scaffold protein Mcs4 and MAP3K activity, driving yeast into mitosis file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 contributes to activation and signaling context for the S. pombe stress-activated MAPK Sty1 and downstream transcription factor Atf1, functioning as a redox transducer/scaffold in peroxide signaling.
GO:0015035 protein-disulfide reductase activity	EXP PMID:37572670 A peroxiredoxin-P38 MAPK scaffold increases MAPK activity by...	KEEP AS NON CORE	Summary: Reflects Tpx1 redox-relay chemistry: as a 2-Cys peroxiredoxin it forms transient mixed disulfides with partner proteins (e.g., Pap1, Pka1, Csn5, thioredoxins), exchanging thiol-disulfide redox equivalents. Captures the relay/disulfide-exchange aspect of Tpx1 function rather than its primary peroxidase activity; retained as non-core. Reason: Captures the disulfide-relay aspect of Tpx1; secondary to the core peroxidase function and reinforced by falcon redox-relay evidence. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Pka1 and Csn5 form protein–protein disulfide complexes with Tpx1 in response to 0.2 mM H2O2, consistent with Tpx1 functioning as a redox relay to regulatory proteins.
GO:1900745 positive regulation of p38MAPK cascade	IMP PMID:37572670 A peroxiredoxin-P38 MAPK scaffold increases MAPK activity by...	KEEP AS NON CORE	Summary: Experimentally supported (IMP). Tpx1 positively regulates the Sty1/p38 MAPK cascade, acting as a direct redox transducer promoting Sty1 activation. This signaling role can be genetically separated from the peroxidase activity (e.g., tpx1C169S retains Sty1 regulation), establishing it as a bona fide second function of the gene. Reason: Bona fide signaling function supported by IMP evidence and falcon deep research; non-core relative to the primary detoxification role. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md role in Sty1 pathway signaling can be genetically separated from its thioredoxin peroxidase activity using alleles such as tpx1C169S, described as disrupting thioredoxin peroxidase activity while leaving Sty1 regulation intact.
GO:0061692 cellular detoxification of hydrogen peroxide	IMP PMID:24521463 A genetic approach to study H2O2 scavenging in fission yeast...	ACCEPT	Summary: Core process, experimentally supported (IMP). Genetic dissection establishes Tpx1 (with catalase) as a principal H2O2-scavenging enzyme; tpx1 deletion causes extreme peroxide sensitivity, directly demonstrating its role in cellular H2O2 detoxification. Reason: Strong IMP evidence corroborated by falcon deep research; a core function of the gene. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Experimentally, tpx1 deletion causes extreme peroxide sensitivity and increased oxidative damage markers (e.g., protein carbonylation), supporting a central peroxide-detoxifying role in vivo.
GO:0005737 cytoplasm	IDA PMID:22344694 The transcription factors Pap1 and Prr1 collaborate to activ...	ACCEPT	Summary: Cytoplasmic localization, consistent with Tpx1 acting in the cytosol as the upstream redox transmitter for the cytosolic Pap1 transcription factor. The more specific cytosol term is also annotated. Reason: Direct localization evidence corroborated by falcon deep research; cytosol is the more specific term. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 is primarily described as cytosolic before and after H2O2 exposure, consistent with its roles in controlling cytosolic thioredoxins and transcription factor signaling.
GO:0051082 unfolded protein binding	IDA PMID:20356456 Distinct functional roles of peroxiredoxin isozymes and glut...	MODIFY	Summary: Recombinant TPx (Tpx1) inhibited thermal aggregation of citrate synthase, demonstrating molecular chaperone (holdase) activity in vitro, a known moonlighting property of typical 2-Cys peroxiredoxins. The activity is better captured by the MF term protein folding chaperone (GO:0044183) than by the binding-only term unfolded protein binding. Both terms are molecular function, so this is a within-aspect refinement. Reason: In-vitro chaperone (anti-aggregation) activity is more precisely a protein folding chaperone MF than a binding term; supported by the original IDA reference. Proposed replacements: protein folding chaperone Supporting Evidence: PMID:20356456 to inhibit the aggregation. The chaperone activities of PMP20 and GPx were
GO:0140824 thioredoxin-dependent peroxiredoxin activity	IDA PMID:20356456 Distinct functional roles of peroxiredoxin isozymes and glut...	ACCEPT	Summary: Core molecular function, directly demonstrated (IDA): recombinant TPx reduces peroxides using the thioredoxin system, matching EC 1.11.1.24. This is the most specific and best-supported MF term for Tpx1. Reason: Direct in-vitro demonstration corroborated by falcon deep research; the primary core MF of the gene. Supporting Evidence: PMID:20356456 TPx (thioredoxin peroxidase) exhibited a capacity for peroxide reduction with the thioredoxin system. file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 functions as a thioredoxin-dependent peroxidase that detoxifies hydrogen peroxide and can also reduce organic peroxides, consistent with its classification as a typical 2‑Cys peroxiredoxin.
GO:0008379 thioredoxin peroxidase activity	IMP PMID:24268782 A peroxiredoxin promotes H2O2 signaling and oxidative stress...	ACCEPT	Summary: Core molecular function supported by mutational/genetic evidence. Tpx1 reduces peroxides via its thioredoxin-coupled cycle; the catalytic mechanism uses peroxidatic Cys48 and resolving Cys169. Notably, Brown et al. show the only essential function of this thioredoxin peroxidase activity in H2O2 resistance is to inhibit the thioredoxin family protein Txl1 by oxidizing it, i.e. the peroxidase activity also drives an oxidative redox relay rather than acting purely as a reductive detoxifier. Reason: Supported by IMP evidence and falcon deep research; a core function of the gene. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md catalytic cycle in S. pombe involves a peroxidatic cysteine (Cys48) and resolving cysteine (Cys169), consistent with typical 2‑Cys Prx chemistry.
GO:0045944 positive regulation of transcription by RNA polymerase II	IMP PMID:24268782 A peroxiredoxin promotes H2O2 signaling and oxidative stress...	KEEP AS NON CORE	Summary: Reflects the Tpx1->Pap1 redox relay: under mild H2O2, Tpx1 is required for Pap1 oxidation/activation, driving Pap1-dependent antioxidant gene transcription. Mechanistically this relay operates by Tpx1 transferring oxidizing equivalents to partner proteins (Brown et al. show the essential relay in H2O2 resistance is oxidation/inhibition of the thioredoxin family protein Txl1), amplifying the H2O2 signal. This is an indirect, signaling-mediated effect on transcription (Tpx1 is not itself a transcription factor), so it is kept as a non-core consequence of the H2O2-sensor role. Reason: Genuine but indirect/signaling-mediated effect on transcription via Pap1; non-core relative to the primary peroxidase function. Reinforced by falcon deep research. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 is reported to be required for Pap1 oxidation/activation under mild peroxide stress, acting as the primary peroxide sensor/transducer for this pathway; Pap1 nuclear accumulation and downstream gene induction depend on Tpx1-mediated redox control.
GO:0042744 hydrogen peroxide catabolic process	IMP PMID:24521463 A genetic approach to study H2O2 scavenging in fission yeast...	ACCEPT	Summary: Core process, IMP-supported. Genetic dissection of H2O2 scavenging shows Tpx1 is a principal peroxide-catabolizing enzyme during aerobic growth alongside catalase. Reason: Strong IMP evidence corroborated by falcon deep research; a core function of the gene. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 is central to peroxide defense during aerobic growth: loss of Tpx1 yields strong peroxide sensitivity and evidence of increased oxidative damage, consistent with a major antioxidant role.
GO:0045454 cell redox homeostasis	IMP PMID:24521463 A genetic approach to study H2O2 scavenging in fission yeast...	ACCEPT	Summary: Core process, IMP-supported. By scavenging peroxides through the thioredoxin-coupled cycle, Tpx1 maintains intracellular redox balance during aerobic growth and peroxide stress. Reason: Supported by IMP evidence and falcon deep research; a core function of the gene. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Trx1 is described as the main electron donor for Tpx1, with Trx3 reported as partially compensatory when Trx1 is absent; thioredoxin reductase (Trr1) maintains the thioredoxin pool using NADPH.
GO:0000122 negative regulation of transcription by RNA polymerase II	IMP PMID:22245228 Inactivation of a peroxiredoxin by hydrogen peroxide is crit...	KEEP AS NON CORE	Summary: Reflects signal gating by Tpx1 hyperoxidation: at high H2O2, Tpx1 is hyperoxidized (Cys-sulfinic acid) and inactivated, which redirects thioredoxin reducing capacity to repair oxidized proteins and reset the transcriptional response. The effect on transcription is indirect and signaling-mediated, so it is kept as non-core. Reason: Indirect, signaling-mediated transcriptional effect via the hyperoxidation switch; non-core relative to the primary peroxidase function. Reinforced by falcon deep research. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md which inactivates thioredoxin-dependent peroxidase activity because thioredoxin cannot directly reduce the sulfinic form. Hyperoxidized typical 2‑Cys Prxs can be repaired by sulfiredoxin (Srx) via an ATP-dependent reaction, restoring catalytic competence and changing signaling capacity over time.
GO:0042744 hydrogen peroxide catabolic process	IMP PMID:22245228 Inactivation of a peroxiredoxin by hydrogen peroxide is crit...	ACCEPT	Summary: Core process. Confirms Tpx1 as a major H2O2-catabolizing enzyme whose peroxidase activity (and its reversible inactivation by hyperoxidation) governs cellular peroxide levels. Reason: Supported by IMP evidence and falcon deep research; a core function of the gene. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Experimentally, tpx1 deletion causes extreme peroxide sensitivity and increased oxidative damage markers (e.g., protein carbonylation), supporting a central peroxide-detoxifying role in vivo.
GO:0005737 cytoplasm	IDA PMID:22245228 Inactivation of a peroxiredoxin by hydrogen peroxide is crit...	ACCEPT	Summary: Directly observed cytoplasmic localization, consistent with the predominantly cytosolic site where Tpx1 detoxifies peroxides and controls cytosolic thioredoxin/Pap1 signaling. Reason: Direct localization evidence corroborated by falcon deep research. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 is primarily described as cytosolic before and after H2O2 exposure, consistent with its roles in controlling cytosolic thioredoxins and transcription factor signaling.
GO:0004601 peroxidase activity	IDA PMID:17409354 The peroxiredoxin Tpx1 is essential as a H2O2 scavenger duri...	ACCEPT	Summary: Directly demonstrated peroxidase activity. Tpx1 is essential as the H2O2 scavenger during aerobic growth. The specific thioredoxin-dependent peroxiredoxin activity term is the preferred core MF; this is the accurate parent. Reason: Direct experimental evidence; accurate parent of the specific peroxiredoxin MF. Corroborated by falcon deep research. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 functions as a thioredoxin-dependent peroxidase that detoxifies hydrogen peroxide and can also reduce organic peroxides, consistent with its classification as a typical 2‑Cys peroxiredoxin.
GO:0005515 protein binding	IPI PMID:17409354 The peroxiredoxin Tpx1 is essential as a H2O2 scavenger duri...	MARK AS OVER ANNOTATED	Summary: Uninformative per curation guidelines. Tpx1 does form functionally meaningful interactions (homodimer, transient mixed disulfides with thioredoxins, Pap1, Pka1, Csn5, and Srx1), but these are captured by more specific MF terms such as thioredoxin-dependent peroxiredoxin activity and protein-disulfide reductase activity. The bare protein binding term adds no information. Reason: Generic protein binding is uninformative; specific MF terms (peroxiredoxin/disulfide-relay activities) capture the actual interactions.
GO:0045454 cell redox homeostasis	IMP PMID:17409354 The peroxiredoxin Tpx1 is essential as a H2O2 scavenger duri...	ACCEPT	Summary: Core process. As the essential H2O2 scavenger during aerobic growth, Tpx1 is central to maintaining cellular redox balance. Reason: Supported by IMP evidence and falcon deep research; a core function of the gene. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 is central to peroxide defense during aerobic growth: loss of Tpx1 yields strong peroxide sensitivity and evidence of increased oxidative damage, consistent with a major antioxidant role.
GO:0051920 peroxiredoxin activity	IDA PMID:17409354 The peroxiredoxin Tpx1 is essential as a H2O2 scavenger duri...	ACCEPT	Summary: Directly demonstrated peroxiredoxin activity. The more specific thioredoxin-dependent peroxiredoxin activity (GO:0140824) term is the preferred core MF. Reason: Direct experimental evidence corroborated by falcon deep research; specific peroxiredoxin MF is preferred. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md catalytic cycle in S. pombe involves a peroxidatic cysteine (Cys48) and resolving cysteine (Cys169), consistent with typical 2‑Cys Prx chemistry.
GO:0005634 nucleus	HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ...	KEEP AS NON CORE	Summary: Nuclear signal from a genome-wide GFP localization screen. Plausible given Tpx1 influence on Pap1 activation, but Tpx1 is predominantly cytosolic and executes its core function in the cytosol; retained as non-core. Reason: High-throughput localization signal; secondary to the predominant cytosolic site of function per falcon deep research. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 is primarily described as cytosolic before and after H2O2 exposure, consistent with its roles in controlling cytosolic thioredoxins and transcription factor signaling.
GO:0005829 cytosol	HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ...	ACCEPT	Summary: Cytosolic localization from a genome-wide GFP localization screen, concordant with the predominant cytosolic site where Tpx1 detoxifies peroxides and controls thioredoxin/Pap1 signaling. This is the principal site of function. Reason: High-throughput localization consistent with the predominant cytosolic site of function per falcon deep research. Supporting Evidence: file:SCHPO/tpx1/tpx1-deep-research-falcon.md Tpx1 is primarily described as cytosolic before and after H2O2 exposure, consistent with its roles in controlling cytosolic thioredoxins and transcription factor signaling.
GO:0005515 protein binding	IPI PMID:15824112 Oxidation of a eukaryotic 2-Cys peroxiredoxin is a molecular...	MARK AS OVER ANNOTATED	Summary: Uninformative per curation guidelines. This IPI derives from the Tpx1-Srx1 interaction (sulfiredoxin-mediated repair of hyperoxidized Tpx1) and the Tpx1-Pap1 redox switch, but the bare protein binding term conveys none of this. The specific redox-relay/peroxidase MF terms and the regulatory process terms capture the biology. Reason: Generic protein binding is uninformative; the Srx1/Pap1 interactions are better captured by specific MF/process terms.

Gene Description

Existing Annotations Review

Core Functions

Thioredoxin-dependent peroxiredoxin activity that detoxifies H2O2 and maintains cellular redox balance during aerobic growth and peroxide stress.

References

Deep Research

Falcon

📚 Additional Documentation

Bioreason Rl Predictions

Bioreason Rl Review

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