NPR1 (Nonexpressor of Pathogenesis-Related Genes 1, also known as NIM1/SAI1) is a transcriptional cofactor that serves as the master regulator of systemic acquired resistance (SAR) and salicylic acid (SA)-mediated plant immunity. NPR1 binds SA only with low affinity, far weaker than its paralog NPR4, and the paralogs NPR3 and NPR4 are the principal SA receptors. Under basal conditions, NPR1 exists as redox-sensitive disulfide-linked oligomers sequestered in the cytoplasm. Upon pathogen challenge and SA accumulation, a biphasic change in cellular reduction potential reduces these oligomers into active dimers and monomers that translocate to the nucleus. In the nucleus, NPR1 functions as both a transcriptional repressor (when unmodified and associated with WRKY70 at W-box elements) and activator (when sumoylated and associated with TGA transcription factors at as-1 elements). The protein contains critical structural domains including BTB/POZ and ankyrin repeats (particularly ANK2 repeat at residues 265-295) that mediate protein-protein interactions. NPR1 forms enhanceosome complexes with TGA factors in a TGA3(2)-NPR1(2)-TGA3(2) stoichiometry to activate defense genes like PR-1 and PR-2. NPR1 is itself a substrate of CUL3-based E3 ubiquitin ligases, in which NPR3 and NPR4 serve as the substrate adaptors; it is recruited for proteasomal turnover after phosphorylation at Ser-11 and Ser-15, and this turnover is required for full target-gene induction. The protein also functions as a key negative regulator of jasmonic acid (JA) signaling, creating essential SA/JA crosstalk that balances defense responses. Additionally, NPR1 controls programmed cell death during effector-triggered immunity, preventing excessive lesion expansion. This multifaceted regulation involves complex post-translational modifications including sumoylation, phosphorylation, and ubiquitination that precisely control NPR1 activity, stability, and subcellular localization.
Definition: The process by which protein oligomers maintained by disulfide bonds are dissociated into active monomers and dimers through reduction of disulfide linkages in response to changes in cellular redox potential
Justification: NPR1's activation mechanism involves a unique redox-dependent dissociation of disulfide-linked oligomers into active forms. This represents a distinct regulatory mechanism not captured by existing GO terms
Parent term: cellular response to oxidative stress
Supporting Evidence:
Definition: The formation of multi-protein transcriptional regulatory complexes where cofactors bridge multiple transcription factors on DNA to coordinately regulate gene expression
Justification: NPR1 forms specific enhanceosome complexes with defined stoichiometry (TGA3(2)-NPR1(2)-TGA3(2)) that represents a distinct mode of transcriptional regulation
Parent term: regulation of protein-containing complex assembly
Supporting Evidence:
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: NPR1 localizes to the nucleus where it functions as a transcriptional co-activator, forming enhanceosome complexes with TGA transcription factors to activate defense gene expression Reason: Nuclear localization is essential for NPR1 function as a transcriptional co-activator. Experimental evidence from IBA indicates this is a core subcellular localization supported by extensive literature [PMID:17172357, PMID:26269953, PMID:35545668] Supporting Evidence: PMID:17172357 The interaction of nucleus-localized NPR1 with TGA transcription factors results in the activation of defense genes, including the SAR marker PATHOGENESIS-RELATED-1 ( PR-1 ), and the deployment of SAR. file:ARATH/NPR1/NPR1-deep-research-falcon.md NPR1 is best described as a **nucleo-cytoplasmic** protein whose function is executed primarily in the **nucleus** (transcriptional co-regulation), but whose activation state is controlled in the **cytosol**. |
| GO:0042742 defense response to bacterium | IBA GO_REF:0000033 | ACCEPT | Summary: NPR1 is a key regulator of bacterial defense responses, activating defense gene expression to confer resistance against bacterial pathogens like Pseudomonas syringae Reason: NPR1 is central to bacterial defense responses through SA-mediated immunity. IBA annotation is well-supported by extensive experimental evidence showing NPR1 role in bacterial resistance [PMID:22699612, PMID:26269953] Supporting Evidence: PMID:26269953 posttranslational modifications enable dynamic but tight and precise control of plant immune responses |
| GO:0050832 defense response to fungus | IBA GO_REF:0000033 | ACCEPT | Summary: NPR1 contributes to antifungal defense responses through SA-mediated immunity pathways, though bacterial defense is more extensively characterized Reason: NPR1 plays a role in fungal defense through broad-spectrum immunity mediated by SA signaling. |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | ACCEPT | Summary: NPR1 is present in the cytoplasm in its oligomeric form under non-induced conditions, and functions there to regulate JA signaling negatively Reason: NPR1 localizes to cytoplasm where it exists as oligomers and regulates JA/SA crosstalk. Upon SA induction, it translocates to nucleus. Cytoplasmic localization is well-documented [PMID:12615947, PMID:35545668] Supporting Evidence: PMID:12615947 NPR1 modulates cross-talk between salicylate- and jasmonate-dependent defense pathways through a novel function in the cytosol. |
| GO:2000022 regulation of jasmonic acid mediated signaling pathway | IBA GO_REF:0000033 | ACCEPT | Summary: NPR1 negatively regulates JA signaling as part of SA-JA crosstalk, suppressing JA-dependent defense responses when SA pathway is activated Reason: NPR1 is a well-established negative regulator of JA signaling, mediating SA-JA antagonism. This is a core function supported by extensive experimental evidence [PMID:12615947, PMID:26269953] Supporting Evidence: PMID:12615947 NPR1 modulates cross-talk between salicylate- and jasmonate-dependent defense pathways through a novel function in the cytosol. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: NPR1 nuclear localization is critical for its transcriptional co-activator function and is well-supported by experimental evidence Reason: Nuclear localization is essential and extensively documented for NPR1, even though this annotation is IEA. Strong experimental support makes this annotation reliable [PMID:17172357, PMID:26269953] Supporting Evidence: PMID:17172357 The interaction of nucleus-localized NPR1 with TGA transcription factors results in the activation of defense genes, including the SAR marker PATHOGENESIS-RELATED-1 ( PR-1 ), and the deployment of SAR. PMID:26269953 NPR1 confers immunity through a transcriptional cascade |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: NPR1 cytoplasmic localization is well-documented, particularly in its oligomeric state before SA induction Reason: Cytoplasmic localization is strongly supported by experimental evidence showing NPR1 exists as cytoplasmic oligomers that are reduced to monomers/dimers upon SA treatment [PMID:12615947, PMID:35545668] Supporting Evidence: PMID:12615947 NPR1 modulates cross-talk between salicylate- and jasmonate-dependent defense pathways through a novel function in the cytosol. |
| GO:0009862 systemic acquired resistance, salicylic acid mediated signaling pathway | IEA GO_REF:0000002 | ACCEPT | Summary: This is the quintessential NPR1 function - NPR1 is the master regulator of systemic acquired resistance mediated by salicylic acid signaling Reason: This represents NPR1s primary and best-characterized function. NPR1 was originally identified as the key regulator of SAR and SA signaling. This annotation captures its core biological role [PMID:9019406, PMID:17172357, PMID:32788727] Supporting Evidence: PMID:9019406 The Arabidopsis NPR1 gene controls the onset of systemic acquired resistance PMID:17172357 NPR1) regulates systemic acquired resistance (SAR) in Arabidopsis thaliana, and current models propose that after treatment with salicylic acid (SA), Cys-82 and Cys-216 of NPR1 are reduced, leading to nuclear import |
| GO:0016604 nuclear body | IEA GO_REF:0000044 | ACCEPT | Summary: NPR1 has been shown to localize to nuclear bodies, which may represent sites of transcriptional activity or protein complex assembly Reason: Nuclear body localization is supported by experimental evidence using IDA methodology, indicating NPR1 forms discrete nuclear structures that may be functionally important [PMID:26269953] |
| GO:0031347 regulation of defense response | IEA GO_REF:0000117 | ACCEPT | Summary: NPR1 is a master regulator of plant defense responses, controlling both positive and negative aspects of immunity signaling Reason: This annotation accurately captures NPR1s regulatory role in defense. NPR1 both positively regulates SA-mediated defenses and negatively regulates JA defenses, making it a key defense regulator [PMID:26269953, PMID:12615947] Supporting Evidence: PMID:26269953 NPR1, a master regulator of basal and systemic acquired resistance in plants PMID:12615947 NPR1 modulates cross-talk between salicylate- and jasmonate-dependent defense pathways |
| GO:0045087 innate immune response | IEA GO_REF:0000117 | ACCEPT | Summary: NPR1 is central to plant innate immunity, regulating both basal and induced immune responses against pathogens Reason: Innate immunity is a core function of NPR1, which regulates both basal defense and systemic acquired resistance. This broad immune term accurately describes NPR1s role [PMID:9019406, PMID:26269953] Supporting Evidence: PMID:9019406 The Arabidopsis NPR1 gene controls the onset of systemic acquired resistance (SAR), a plant immunity, to a broad spectrum of pathogens PMID:26269953 posttranslational modifications enable dynamic but tight and precise control of plant immune responses. |
| GO:2000022 regulation of jasmonic acid mediated signaling pathway | IEA GO_REF:0000002 | ACCEPT | Summary: NPR1 negatively regulates JA signaling, mediating SA-JA antagonism as part of defense pathway crosstalk Reason: JA regulation is a well-established function of NPR1, representing the negative regulatory aspect of SA-JA crosstalk. This is experimentally supported [PMID:12615947, PMID:26269953] Supporting Evidence: PMID:12615947 NPR1 modulates cross-talk between salicylate- and jasmonate-dependent defense pathways |
| GO:2000031 regulation of salicylic acid mediated signaling pathway | IEA GO_REF:0000002 | ACCEPT | Summary: NPR1 is the master positive regulator of SA signaling, essential for SA-mediated defense responses and systemic acquired resistance Reason: This is a core NPR1 function - NPR1 is the key positive regulator of SA signaling pathway. This annotation accurately captures NPR1s primary role [PMID:9019406, PMID:12615947, PMID:32788727] Supporting Evidence: PMID:12615947 NPR1 as a key regulatory factor in the cross-communication between SA and JA signaling |
| GO:0005515 protein binding | IPI PMID:10659709 NPR1 differentially interacts with members of the TGA/OBF fa... | MODIFY | Summary: NPR1 binds TGA transcription factors, but protein binding term is too generic and uninformative Reason: While NPR1 does bind proteins (TGA transcription factors, NPR3/4, NIMIN proteins), the generic protein binding term provides no functional insight. Should be replaced with transcription coregulator activity which better captures NPR1s functional role [PMID:10659709] Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:10659709 NPR1 differentially interacts with members of the TGA/OBF family of transcription factors that bind an element of the PR-1 gene required for induction by salicylic acid |
| GO:0005515 protein binding | IPI PMID:12084833 In vivo interaction between NPR1 and transcription factor TG... | MODIFY | Summary: NPR1 interacts with TGA2 transcription factor for gene activation, but generic protein binding term lacks specificity Reason: This specific publication shows NPR1-TGA2 interaction leading to SA-mediated gene activation. Generic protein binding should be replaced with transcription coregulator activity [PMID:12084833] Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:12084833 In vivo interaction between NPR1 and transcription factor TGA2 leads to salicylic acid-mediated gene activation in Arabidopsis |
| GO:0005515 protein binding | IPI PMID:15634206 An Arabidopsis NPR1-like gene, NPR4, is required for disease... | MODIFY | Summary: NPR1 protein interactions demonstrated through study of NPR4 (NPR1-like protein), but generic protein binding term lacks functional specificity Reason: This study focuses on NPR4 protein interactions with TGA transcription factors, but the generic protein binding term for NPR1 provides no functional insight. Should be replaced with transcription coregulator activity which better captures NPR1s functional role [PMID:15634206] Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:15634206 The NPR4 protein shares 36% identity with NPR1 and interacts with the same spectrum of TGA transcription factors in yeast two-hybrid assays |
| GO:0005515 protein binding | IPI PMID:18571510 NPR1 preferentially binds to the DNA-inactive form of Arabid... | MODIFY | Summary: NPR1 preferentially binds DNA-inactive form of TGA2, demonstrating specific transcription factor interactions, but generic protein binding term lacks specificity Reason: This study demonstrates NPR1s specific interaction with TGA2 in its DNA-unbound state, promoting TGA2 recruitment to active promoter complexes. The generic protein binding term should be replaced with transcription coregulator activity [PMID:18571510] Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:18571510 As shown here, NPR1 appears to preferentially interact with the non-DNA bound fraction of TGA2. |
| GO:0005515 protein binding | IPI PMID:19490895 Proteasome-mediated turnover of the transcription coactivato... | REMOVE | Summary: NPR1 interacts with CUL3A (PMID:19490895), the cullin scaffold of the CUL3 ubiquitin ligase that targets NPR1 for turnover, so NPR1 is the substrate. SAR inducers promote NPR1 phosphorylation at its N-terminal IkB-like phosphodegron (Ser11/Ser15) and its recruitment to the ligase for proteasomal turnover. This is NPR1-ligase binding, not an NPR1-transcription factor interaction, so it does not support transcription coregulator activity; and because NPR3/NPR4, not NPR1, act as the CUL3 substrate adaptors, no adaptor or ubiquitin-ligase MF applies to NPR1 either. The process this interaction serves is captured by the protein ubiquitination row. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. Reconciled with the retired duplicate review genes/ARATH/P93002 (same protein), which had REMOVE; adopted over this file's earlier MARK_AS_OVER_ANNOTATED. Supporting Evidence: PMID:19490895 inducers of SAR promote NPR1 phosphorylation at residues Ser11/Ser15, and then facilitate its recruitment to a Cullin3-based ubiquitin ligase. Turnover of phosphorylated NPR1 is required for full induction of target genes and establishment of SAR |
| GO:0005515 protein binding | IPI PMID:21798944 Evidence for network evolution in an Arabidopsis interactome... | MODIFY | Summary: NPR1 protein interactions identified in large-scale Arabidopsis interactome mapping, but generic protein binding term lacks specificity Reason: This large-scale interactome study identifies NPR1 protein-protein interactions but the generic protein binding term provides no functional context. Should be replaced with transcription coregulator activity [PMID:21798944] Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:21798944 a proteome-wide binary protein-protein interaction map for the interactome network of the plant Arabidopsis thaliana containing about 6200 highly reliable interactions between about 2700 proteins |
| GO:0005515 protein binding | IPI PMID:22699612 NPR3 and NPR4 are receptors for the immune signal salicylic ... | REMOVE | Summary: NPR1 interacts with NPR4 (PMID:22699612), the paralogous SA receptor and CUL3 substrate adaptor that targets NPR1, so NPR1 is the substrate. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. Reconciled with the retired duplicate review genes/ARATH/P93002 (same protein), which had REMOVE; adopted over this file's earlier MODIFY to transcription coregulator activity. Supporting Evidence: PMID:22699612 NPR3 and NPR4 are receptors for the immune signal salicylic acid in plants. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | MODIFY | Summary: NPR1 interactions in phytohormone protein network demonstrating signal integration, but generic protein binding term lacks functional context Reason: This study maps NPR1 within the extensive phytohormone signaling network showing protein interactions for signal integration. Generic protein binding should be replaced with transcription coregulator activity [PMID:32612234] Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions. In the highly interconnected network, we identify pathway communities and hundreds of previously unknown pathway contacts |
| GO:0005634 nucleus | NAS PMID:17172357 The coactivator function of Arabidopsis NPR1 requires the co... | ACCEPT | Summary: NPR1 nuclear localization is essential for transcriptional co-activator function, well-supported by experimental evidence despite NAS code Reason: Nuclear localization is critical for NPR1s transcriptional co-activator role. Even though this is NAS evidence, the nuclear localization is extensively documented experimentally in this and other publications [PMID:17172357, PMID:11148282] Supporting Evidence: PMID:17172357 Activation of PR genes during SAR, which requires the nuclear localization of NPR1 |
| GO:0009862 systemic acquired resistance, salicylic acid mediated signaling pathway | IDA PMID:17172357 The coactivator function of Arabidopsis NPR1 requires the co... | ACCEPT | Summary: This represents NPR1s primary and most well-characterized function - master regulation of SAR through SA signaling pathways Reason: This is NPR1s quintessential function with strong IDA evidence. NPR1 was originally identified as the master regulator of SAR and SA-mediated signaling, making this annotation central to its biological role [PMID:17172357, PMID:9019406] Supporting Evidence: PMID:17172357 NONEXPRESSOR OF PATHOGENESIS-RELATED GENES1 (NPR1) regulates systemic acquired resistance (SAR) in Arabidopsis thaliana PMID:9019406 The Arabidopsis NPR1 gene controls the onset of systemic acquired resistance file:ARATH/NPR1/NPR1-deep-research-falcon.md NPR1 is positioned as a core effector of SA signaling required for PR gene expression and broad-spectrum resistance |
| GO:0045893 positive regulation of DNA-templated transcription | IDA PMID:17172357 The coactivator function of Arabidopsis NPR1 requires the co... | ACCEPT | Summary: NPR1 positively regulates transcription by forming enhanceosome complexes with TGA transcription factors for defense gene activation Reason: Strong IDA evidence demonstrates NPR1s positive regulatory role in transcription. NPR1 forms transcriptional activating complexes with TGA factors to promote defense gene expression [PMID:17172357] Supporting Evidence: PMID:17172357 after stimulation with SA, TGA2 is incorporated into a transactivating complex with NPR1, forming an enhanceosome that requires the core of the NPR1 BTB/POZ domain |
| GO:0090575 RNA polymerase II transcription regulator complex | IPI PMID:12084833 In vivo interaction between NPR1 and transcription factor TG... | ACCEPT | Summary: NPR1 forms transcriptional regulatory complexes with TGA2 for SA-mediated gene activation, representing accurate cellular component annotation Reason: Strong IPI evidence demonstrates NPR1 participation in RNA polymerase II transcription regulatory complexes through its interaction with TGA2. This accurately describes NPR1s cellular context for transcriptional regulation [PMID:12084833] Supporting Evidence: PMID:12084833 In vivo interaction between NPR1 and transcription factor TGA2 leads to salicylic acid-mediated gene activation in Arabidopsis |
| GO:0005515 protein binding | IPI PMID:32788727 Structural basis of salicylic acid perception by Arabidopsis... | REMOVE | Summary: NPR1 interacts with NPR4 (PMID:32788727), the paralogous SA receptor and CUL3 substrate adaptor that targets NPR1, so NPR1 is the substrate. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. Reconciled with the retired duplicate review genes/ARATH/P93002 (same protein), which had REMOVE; adopted over this file's earlier MODIFY to transcription coregulator activity. Supporting Evidence: PMID:32788727 Structural basis of salicylic acid perception by Arabidopsis NPR proteins |
| GO:1901149 salicylic acid binding | IDA PMID:32788727 Structural basis of salicylic acid perception by Arabidopsis... | MARK AS OVER ANNOTATED | Summary: PMID:32788727 maps an SA-binding core (SBC) in NPR1 and detects a weak, Arg432-dependent SA-binding activity, but shows NPR1 has only minimal SA-binding capacity (less than 0.02% of NPR1 competent for binding vs about 8% for NPR4). So NPR1 does bind SA but is not functionally an SA receptor; the SA-receptor role belongs to the paralogues NPR3/NPR4. Reason: The annotation is not technically false - PMID:32788727 confirms NPR1 has a measurable (Arg432-dependent) SA-binding capacity mapped to its SBC, and UniProt records that NPR1 binds SA with low capacity. However, the binding is roughly 400-fold weaker than NPR4 (less than 0.02% vs about 8% occupancy) and NPR1 is not the functional SA receptor. MARK_AS_OVER_ANNOTATED (rather than the prior REMOVE) more accurately reflects the literature - the molecular activity exists but is biologically minor and should not be treated as a core SA-receptor function for NPR1. Supporting Evidence: PMID:32788727 despite the two proteins sharing nearly identical hormone-binding residues, NPR1 displays minimal SA-binding activity compared to NPR4. file:ARATH/NPR1/NPR1-deep-research-falcon.md the 2023 SA-transport/SAR review describes **NPR3/NPR4 as SA receptors and CRL3 substrate adaptors** that can mediate NPR1 polyubiquitination/degradation, with SA disrupting NPR1–NPR4 interaction and thereby stabilizing/activating NPR1 |
| GO:0009617 response to bacterium | IEP PMID:22699612 NPR3 and NPR4 are receptors for the immune signal salicylic ... | ACCEPT | Summary: NPR1 expression patterns consistent with bacterial response, supporting its role in bacterial immunity and defense signaling Reason: IEP evidence demonstrates NPR1 response to bacterial stimuli through expression profiling. NPR1 is well-established in bacterial defense responses and this annotation captures its responsive nature [PMID:22699612] Supporting Evidence: PMID:22699612 NPR3 and NPR4 are receptors for the immune signal salicylic acid in plants. |
| GO:0042742 defense response to bacterium | IMP PMID:22699612 NPR3 and NPR4 are receptors for the immune signal salicylic ... | ACCEPT | Summary: NPR1 mutant phenotypes demonstrate essential role in bacterial defense responses through regulation of immunity signaling pathways Reason: Strong IMP evidence from mutant studies confirms NPR1s critical role in bacterial defense. NPR1 controls both effector-triggered immunity and pathogen-associated molecular pattern responses to bacteria [PMID:22699612] Supporting Evidence: PMID:22699612 NPR3 and NPR4 are receptors for the immune signal salicylic acid in plants. |
| GO:0003712 transcription coregulator activity | IDA PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | ACCEPT | Summary: NPR1 functions as a transcriptional co-activator, forming enhanceosome complexes with TGA transcription factors to activate defense gene expression Reason: This is NPR1s primary molecular function supported by strong IDA evidence. NPR1 serves as transcriptional co-activator bridging TGA transcription factors for defense gene activation [PMID:26269953, PMID:35545668] Supporting Evidence: PMID:26269953 NPR1, a master regulator of basal and systemic acquired resistance in plants, confers immunity through a transcriptional cascade, which includes transcription activators (e.g., TGA3) and repressors (e.g., WRKY70), leading to the massive induction of antimicrobial genes. file:ARATH/NPR1/NPR1-deep-research-falcon.md NPR1 interacts with **TGA transcription factors** to activate SA-inducible promoters such as **PR1**, functioning as a coactivator that enables robust PR gene induction |
| GO:0003712 transcription coregulator activity | IMP PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | ACCEPT | Summary: NPR1 mutant phenotypes demonstrate its essential role as transcriptional co-activator in defense gene regulation Reason: Strong IMP evidence demonstrates NPR1s transcriptional co-activator function is essential for defense responses. Mutant studies confirm this molecular function [PMID:26269953] Supporting Evidence: PMID:26269953 NPR1, a master regulator of basal and systemic acquired resistance in plants, confers immunity through a transcriptional cascade |
| GO:0005515 protein binding | IPI PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | MODIFY | Summary: NPR1 protein interactions with TGA factors and regulatory proteins, but generic term lacks specificity Reason: This study demonstrates NPR1 interactions with multiple proteins (TGA3, NIMIN proteins, NPR3/4), but protein binding is too generic. Should be transcription coregulator activity [PMID:26269953] Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:26269953 Posttranslational Modifications of the Master Transcriptional Regulator NPR1 Enable Dynamic but Tight Control of Plant Immune Responses. |
| GO:0009751 response to salicylic acid | IDA PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | ACCEPT | Summary: NPR1 directly responds to salicylic acid through conformational changes and nuclear translocation, essential for SA-mediated immunity Reason: Response to SA is a fundamental NPR1 function with strong IDA evidence. NPR1 directly senses SA and undergoes conformational changes to activate defense responses [PMID:26269953, PMID:32788727] Supporting Evidence: PMID:26269953 posttranslational modifications enable dynamic but tight and precise control of plant immune responses. |
| GO:0009751 response to salicylic acid | IMP PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | ACCEPT | Summary: NPR1 mutants demonstrate its essential role in salicylic acid responses, confirming SA-dependent function Reason: Strong IMP evidence from mutant studies confirms NPR1s critical role in SA responses. NPR1 mutants are defective in SA-mediated immunity [PMID:26269953] Supporting Evidence: PMID:26269953 Posttranslational Modifications of the Master Transcriptional Regulator NPR1 Enable Dynamic but Tight Control of Plant Immune Responses. |
| GO:1900424 regulation of defense response to bacterium | IMP PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | ACCEPT | Summary: NPR1 mutant studies demonstrate its regulatory control over bacterial defense responses through transcriptional mechanisms Reason: Strong IMP evidence from mutant analysis confirms NPR1s regulatory role in bacterial defense responses. NPR1 functions as master transcriptional regulator of bacterial immunity pathways [PMID:26269953] Supporting Evidence: PMID:26269953 posttranslational modifications enable dynamic but tight and precise control of plant immune responses |
| GO:0005634 nucleus | IDA PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | ACCEPT | Summary: NPR1 nuclear localization is essential for transcriptional co-activator function and is extensively documented with strong IDA evidence Reason: Strong IDA evidence confirms NPR1s nuclear localization required for transcriptional activity. Nuclear accumulation is critical for NPR1s co-activator function in defense gene regulation [PMID:26269953] Supporting Evidence: PMID:26269953 Posttranslational Modifications of the Master Transcriptional Regulator NPR1 Enable Dynamic but Tight Control of Plant Immune Responses. file:ARATH/NPR1/NPR1-deep-research-falcon.md NPR1 is best described as a **nucleo-cytoplasmic** protein whose function is executed primarily in the **nucleus** (transcriptional co-regulation), but whose activation state is controlled in the **cytosol**. |
| GO:0005737 cytoplasm | IDA PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | ACCEPT | Summary: NPR1 cytoplasmic localization is well-documented, existing as oligomers that regulate JA signaling before SA-induced nuclear translocation Reason: Strong IDA evidence supports NPR1s cytoplasmic localization where it exists as oligomers and mediates SA-JA crosstalk. This represents its uninduced state before nuclear translocation [PMID:26269953] Supporting Evidence: PMID:26269953 Posttranslational Modifications of the Master Transcriptional Regulator NPR1 Enable Dynamic but Tight Control of Plant Immune Responses. |
| GO:0016604 nuclear body | IDA PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | ACCEPT | Summary: NPR1 localizes to discrete nuclear bodies which may represent sites of transcriptional complex assembly and activity Reason: Strong IDA evidence demonstrates NPR1s localization to nuclear bodies, which likely represent functional subnuclear compartments for transcriptional regulation. This specific localization may be important for its co-activator activity [PMID:26269953] Supporting Evidence: PMID:26269953 Posttranslational Modifications of the Master Transcriptional Regulator NPR1 Enable Dynamic but Tight Control of Plant Immune Responses. |
| GO:0005515 protein binding | IPI PMID:35545668 Structural basis of NPR1 in activating plant immunity. | MODIFY | Summary: NPR1 structural interactions forming homodimers and complexes with TGA transcription factors, but generic protein binding term lacks specificity Reason: This structural study demonstrates NPR1 homodimer formation and TGA complex assembly, but generic protein binding provides no functional context. Should be replaced with transcription coregulator activity [PMID:35545668] Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:35545668 our structure of the TGA32-NPR12-TGA32 complex, DNA-binding assay and genetic data show that dimeric NPR1 activates transcription by bridging two fatty-acid-bound TGA3 dimers to form an enhanceosome |
| GO:0009751 response to salicylic acid | IMP PMID:35545668 Structural basis of NPR1 in activating plant immunity. | ACCEPT | Summary: NPR1 mutant studies confirm essential role in SA response through structural changes and nuclear translocation upon SA treatment Reason: Strong IMP evidence from mutant analysis demonstrates NPR1s critical role in SA responses. NPR1 undergoes SA-induced conformational changes essential for defense activation [PMID:35545668] Supporting Evidence: PMID:35545668 salicylic-acid-induced folding and docking of the salicylic-acid-binding domain onto ankyrin repeats is required for the transcriptional cofactor activity of NPR1 |
| GO:0016567 protein ubiquitination | IEA GO_REF:0000041 | ACCEPT | Summary: NPR1 undergoes proteasome-mediated ubiquitination for regulatory turnover, though this is computational IEA annotation Reason: Although IEA evidence, NPR1 ubiquitination is well-documented experimentally for its regulated proteolysis by CUL3-based ubiquitin ligase. This process is essential for its transcriptional activity [PMID:19490895] Supporting Evidence: PMID:19490895 inducers of SAR promote NPR1 phosphorylation at residues Ser11/Ser15, and then facilitate its recruitment to a Cullin3-based ubiquitin ligase. Turnover of phosphorylated NPR1 is required for full induction of target genes and establishment of SAR |
| GO:0106167 extracellular ATP signaling | IMP PMID:30630869 Extracellular ATP Shapes a Defense-Related Transcriptome Bot... | KEEP AS NON CORE | Summary: NPR1 involvement in extracellular ATP signaling represents peripheral rather than core function for this transcriptional co-activator Reason: While IMP evidence suggests NPR1 involvement in extracellular ATP signaling, this represents a peripheral function compared to its core role in SA-mediated transcriptional regulation. Should be retained as non-core function [PMID:30630869] Supporting Evidence: PMID:30630869 Extracellular ATP Shapes a Defense-Related Transcriptome Both Independently and along with Other Defense Signaling Pathways |
| GO:0001666 response to hypoxia | IMP PMID:25284079 Arabidopsis acyl-CoA-binding protein ACBP3 participates in p... | KEEP AS NON CORE | Summary: NPR1 involvement in hypoxia response represents peripheral function related to stress responses, but not core transcriptional role Reason: While IMP evidence suggests NPR1 role in hypoxia response, this represents a secondary stress response function compared to its primary role in pathogen defense. Should be retained as non-core function [PMID:25284079] Supporting Evidence: PMID:25284079 Arabidopsis acyl-CoA-binding protein ACBP3 participates in plant response to hypoxia by modulating very-long-chain fatty acid metabolism |
| GO:0005634 nucleus | IDA PMID:23116333 The BLADE-ON-PETIOLE genes of Arabidopsis are essential for ... | ACCEPT | Summary: NPR1 nuclear localization is well-documented and essential for transcriptional co-activator function. In PMID:23116333, wild-type NPR1-GFP transiently expressed in N. benthamiana localized predominantly to the nucleus. Reason: Strong IDA evidence supports NPR1s nuclear localization which is critical for its transcriptional activity. This represents a core cellular component annotation [PMID:23116333] Supporting Evidence: PMID:23116333 But when the wild type and the six alleles of npr1 were expressed in the same conditions, GFP was detected mainly in the nucleus, with no difference existing between the two classes of alleles |
| GO:0009617 response to bacterium | IMP PMID:23073694 Metabolic and transcriptomic changes induced in Arabidopsis ... | ACCEPT | Summary: NPR1 mutant studies demonstrate essential role in bacterial responses through SA-dependent resistance pathways Reason: Strong IMP evidence from mutant analysis confirms NPR1s central role in bacterial response through SA signaling. This represents a core function in plant-microbe interactions [PMID:23073694] Supporting Evidence: PMID:23073694 Pf.SS101-induced resistance response to Pst is dependent on salicylic acid signaling |
| GO:0009682 induced systemic resistance | IMP PMID:23073694 Metabolic and transcriptomic changes induced in Arabidopsis ... | ACCEPT | Summary: NPR1 is required for induced systemic resistance mediated by beneficial rhizobacteria through SA-dependent pathways Reason: Strong IMP evidence demonstrates NPR1s essential role in induced systemic resistance, particularly in SA-dependent ISR responses. This represents an important immune function [PMID:23073694] Supporting Evidence: PMID:23073694 Pf.SS101-induced resistance response to Pst is dependent on salicylic acid signaling |
| GO:0005515 protein binding | IPI PMID:12953119 The Arabidopsis NPR1 disease resistance protein is a novel c... | MODIFY | Summary: NPR1 redox-regulated interaction with the TGA-family bZIP transcription factor TGA4 (partner UniProtKB:Q39162 = TGA4/OBF4), but generic protein binding term lacks functional specificity Reason: This study shows that the reduced forms of TGA1 and TGA4 interact with NPR1 in an SA-regulated, cysteine-dependent manner; this row records the TGA4 partner (the TGA1 partner is the separate Q39237 row). Generic protein binding provides no functional context and should be replaced with transcription coregulator activity [PMID:12953119] Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:12953119 our data provide a mechanistic understanding of how the NPR1–TGA1 and/or the NPR1–TGA4 interaction might be regulated in vivo |
| GO:0005634 nucleus | IDA PMID:11148282 Nuclear localization of NPR1 is required for activation of P... | ACCEPT | Summary: NPR1 nuclear localization is essential for PR gene activation and represents its primary site of transcriptional activity Reason: Strong IDA evidence demonstrating NPR1s nuclear localization requirement for PR gene activation. This is a foundational study establishing nuclear function as essential [PMID:11148282] Supporting Evidence: PMID:11148282 Nuclear localization of NPR1 is required for activation of PR gene expression. |
| GO:0009862 systemic acquired resistance, salicylic acid mediated signaling pathway | IMP PMID:11607555 Arabidopsis signal transduction mutant defective in chemical... | ACCEPT | Summary: This represents NPR1s quintessential function - master regulation of SAR through SA signaling, demonstrated through nim1 mutant studies Reason: Strong IMP evidence from original NPR1/NIM1 mutant characterization demonstrates this as NPR1s primary function. This foundational study established NPR1s role in SAR [PMID:11607555] Supporting Evidence: PMID:11607555 Arabidopsis signal transduction mutant defective in chemically and biologically induced disease resistance. |
| GO:0010112 regulation of systemic acquired resistance | IMP PMID:9002272 Characterization of a salicylic acid-insensitive mutant (sai... | ACCEPT | Summary: NPR1 is the key positive regulator of systemic acquired resistance, demonstrated through sai1 mutant characterization Reason: Strong IMP evidence from sai1 mutant (allelic to npr1) demonstrates NPR1s central regulatory role in SAR. This is a foundational study establishing NPR1s regulatory function [PMID:9002272] Supporting Evidence: PMID:9002272 sai1 is allelic to npr1, a previously identified SA-noninducible mutation. The recessive nature of the noninducible sai1 mutation suggests that the wild-type SAI1 gene acts as a positive regulator in the SA signal transduction pathway |
| GO:2000022 regulation of jasmonic acid mediated signaling pathway | IMP PMID:12615947 NPR1 modulates cross-talk between salicylate- and jasmonate-... | ACCEPT | Summary: NPR1 negatively regulates JA signaling as part of SA-JA crosstalk, demonstrated through mutant analysis Reason: Strong IMP evidence from mutant studies demonstrates NPR1s negative regulatory role in JA signaling, mediating SA-JA antagonism. This represents a core function in defense pathway integration [PMID:12615947] Supporting Evidence: PMID:12615947 NPR1 modulates cross-talk between salicylate- and jasmonate-dependent defense pathways through a novel function in the cytosol. |
| GO:2000031 regulation of salicylic acid mediated signaling pathway | IMP PMID:12615947 NPR1 modulates cross-talk between salicylate- and jasmonate-... | ACCEPT | Summary: NPR1 is the master positive regulator of SA signaling pathway, demonstrated through comprehensive mutant analysis Reason: Strong IMP evidence demonstrates NPR1s central role as positive regulator of SA signaling. This represents NPR1s primary regulatory function in plant immunity [PMID:12615947] Supporting Evidence: PMID:12615947 NPR1 modulates cross-talk between salicylate- and jasmonate-dependent defense pathways through a novel function in the cytosol file:ARATH/NPR1/NPR1-deep-research-falcon.md NPR1)** is currently understood as a central node in **salicylic acid (SA)-mediated immunity**, functioning as a **transcriptional co-regulator** required for induction of SA-responsive defense genes such as **PR1** and for **systemic acquired resistance (SAR)** |
| GO:0009627 systemic acquired resistance | IEP PMID:17419843 Pathogen-associated molecular pattern recognition rather tha... | ACCEPT | Summary: NPR1 expression patterns consistent with SAR induction, supporting its central role in systemic resistance responses Reason: IEP evidence demonstrates NPR1 expression patterns correlating with SAR responses. Although expression-based, this supports NPR1s well-established role in SAR [PMID:17419843] Supporting Evidence: PMID:17419843 Pathogen-associated molecular pattern recognition rather than development of tissue necrosis contributes to bacterial induction of systemic acquired resistance in Arabidopsis |
| GO:0050832 defense response to fungus | IMP PMID:17513501 ABA is an essential signal for plant resistance to pathogens... | ACCEPT | Summary: NPR1 contributes to antifungal defense responses through SA-mediated immunity pathways against fungal pathogens Reason: IMP evidence demonstrates NPR1s role in fungal defense through SA signaling. While bacterial defense is better characterized, NPR1 provides broad-spectrum immunity including fungi [PMID:17513501] Supporting Evidence: PMID:17513501 ABA is an essential signal for plant resistance to pathogens affecting JA biosynthesis and the activation of defenses in Arabidopsis. |
| GO:0031348 negative regulation of defense response | IMP PMID:16732289 Conserved requirement for a plant host cell protein in powde... | UNDECIDED | Summary: The cited publication (PMID:16732289) concerns the requirement for MLO host susceptibility proteins in powdery mildew pathogenesis and explicitly reports that mlo-based resistance does NOT involve salicylic acid signaling; it does not mention NPR1. NPR1 is overwhelmingly a positive regulator of SA-mediated defense, and this annotation is not supported by its reference. Reason: PMID:16732289 is cached abstract-only, and the abstract does not mention NPR1. The TAIR curator's IMP may rest on full-text experiments with npr1 in the mlo background, so the annotation cannot be judged from the cache. The earlier REMOVE, which argued that the paper does not mention NPR1, is withdrawn under the rule against overruling experimental annotations from abstract-only records. Reconciled with the retired duplicate review genes/ARATH/P93002 (same protein), which had KEEP_AS_NON_CORE, likewise without the full text. Supporting Evidence: file:ARATH/NPR1/NPR1-deep-research-falcon.md NPR1 is positioned as a core effector of SA signaling required for PR gene expression and broad-spectrum resistance |
| GO:0009617 response to bacterium | TAS PMID:11418339 Genes controlling expression of defense responses in Arabido... | ACCEPT | Summary: NPR1 response to bacterial stimuli is well-documented in literature reviews and represents core function in plant immunity Reason: TAS evidence from comprehensive review confirms NPR1s central role in bacterial responses. This represents established knowledge of NPR1s function in plant-bacterial interactions [PMID:11418339] Supporting Evidence: PMID:11418339 Genes controlling expression of defense responses in Arabidopsis--2001 status. |
| GO:0005634 nucleus | IDA PMID:10662863 The Arabidopsis NPR1/NIM1 protein enhances the DNA binding a... | ACCEPT | Summary: NPR1 nuclear localization and enhancement of TGA transcription factor DNA binding activity Reason: Strong IDA evidence demonstrates NPR1s nuclear localization where it enhances TGA transcription factor DNA binding activity. This represents its functional nuclear compartment [PMID:10662863] Supporting Evidence: PMID:10662863 The Arabidopsis NPR1/NIM1 protein enhances the DNA binding activity of a subgroup of the TGA family of bZIP transcription factors. |
| GO:0005737 cytoplasm | IDA PMID:10662863 The Arabidopsis NPR1/NIM1 protein enhances the DNA binding a... | ACCEPT | Summary: NPR1 cytoplasmic localization where it exists as oligomers before SA-induced nuclear translocation Reason: Strong IDA evidence demonstrates NPR1s cytoplasmic localization in its uninduced state. NPR1 forms oligomeric complexes in cytoplasm before SA-induced reduction and nuclear translocation [PMID:10662863] Supporting Evidence: PMID:10662863 The Arabidopsis NPR1/NIM1 protein enhances the DNA binding activity of a subgroup of the TGA family of bZIP transcription factors |
| GO:0009408 response to heat | IMP PMID:15923322 Heat stress phenotypes of Arabidopsis mutants implicate mult... | KEEP AS NON CORE | Summary: NPR1 contributes to heat stress tolerance, though this represents peripheral stress function rather than core immunity role Reason: IMP evidence demonstrates NPR1 involvement in heat stress tolerance, but this is a secondary function compared to its primary role in pathogen defense and SA signaling. Should be retained as non-core [PMID:15923322] Supporting Evidence: PMID:15923322 NahG transgenic lines (salicylic acid deficient) showed weaker defects |
| GO:0009611 response to wounding | IMP PMID:11891259 Benzothiadiazole-induced priming for potentiated responses t... | KEEP AS NON CORE | Summary: NPR1 is required for priming responses to wounding, representing a secondary stress function beyond its core pathogen defense role Reason: IMP evidence demonstrates NPR1 requirement for wound-induced priming responses, but this represents a peripheral function compared to its primary role in pathogen defense. Should be retained as non-core [PMID:11891259] Supporting Evidence: PMID:11891259 Benzothiadiazole-induced priming for potentiated responses to pathogen infection, wounding, and infiltration of water into leaves requires the NPR1/NIM1 gene in Arabidopsis |
| GO:0009617 response to bacterium | IMP PMID:15842626 Staphylococcus aureus pathogenicity on Arabidopsis thaliana ... | REMOVE | Summary: PMID:15842626 explicitly demonstrates that Arabidopsis resistance to Staphylococcus aureus is mediated by SA-dependent, NPR1-INDEPENDENT host responses (the npr1-1 mutant did not lose resistance). The paper therefore shows NPR1 is NOT required for this bacterial response, so it cannot support an IMP annotation of NPR1 to "response to bacterium". Reason: The cited reference does not support this annotation. PMID:15842626 tested the npr1-1 mutant and concluded that S. aureus resistance is "SA-dependent, NPR1-independent" - i.e. NPR1 is dispensable for this response. An IMP annotation asserting NPR1 involvement in response to bacterium based on this paper is contradicted by the paper's own conclusion and should be removed. NPR1's genuine bacterial-defense roles remain captured by other annotations such as GO:0042742 IMP PMID:22699612 and GO:0009617 IMP PMID:23073694. Supporting Evidence: PMID:15842626 Arabidopsis thaliana resistance to S. aureus is mediated either by a direct effect of SA on the pathogen, specifically one that affects the attachment/aggregate formation on the root surface and reduces the pathogen's virulence, or by SA-dependent, NPR1-independent host responses. |
| GO:0009625 response to insect | IMP PMID:15923339 Major signaling pathways modulate Arabidopsis glucosinolate ... | KEEP AS NON CORE | Summary: NPR1 modulates glucosinolate accumulation and defensive responses to insect feeding, representing peripheral herbivore defense function Reason: IMP evidence shows NPR1 role in insect defense responses through glucosinolate regulation, but this is secondary to its primary pathogen defense function. Should be retained as non-core [PMID:15923339] Supporting Evidence: PMID:15923339 We found increased GS accumulation in response to insect feeding, which required functional NPR1 |
| GO:0009627 systemic acquired resistance | TAS PMID:11418339 Genes controlling expression of defense responses in Arabido... | ACCEPT | Summary: NPR1s role in SAR is comprehensively documented in literature as its primary and best-characterized function Reason: TAS evidence from comprehensive review establishes NPR1s central role in SAR as fundamental knowledge. This represents the foundational understanding of NPR1 function [PMID:11418339] Supporting Evidence: PMID:11418339 Genes controlling expression of defense responses in Arabidopsis--2001 status. |
| GO:0009862 systemic acquired resistance, salicylic acid mediated signaling pathway | TAS PMID:11418339 Genes controlling expression of defense responses in Arabido... | ACCEPT | Summary: This represents NPR1s quintessential function - well-established in literature as master regulator of SA-mediated SAR Reason: TAS evidence from comprehensive literature review confirms this as NPR1s primary and best-characterized function. This represents fundamental knowledge of NPR1s role [PMID:11418339] Supporting Evidence: PMID:11418339 Genes controlling expression of defense responses in Arabidopsis--2001 status. |
| GO:0009862 systemic acquired resistance, salicylic acid mediated signaling pathway | TAS PMID:9019406 The Arabidopsis NPR1 gene that controls systemic acquired re... | ACCEPT | Summary: This represents the original characterization of NPR1s primary function - controlling SAR through SA signaling pathways Reason: TAS evidence from the foundational NPR1 cloning and characterization paper establishing its role in SAR. This represents the original identification of NPR1s function [PMID:9019406] Supporting Evidence: PMID:9019406 The Arabidopsis NPR1 gene controls the onset of systemic acquired resistance |
| GO:0005515 protein binding | IPI PMID:10659709 NPR1 differentially interacts with members of the TGA/OBF fa... | MODIFY | Summary: NPR1 interacts with the TGA-family bZIP transcription factor TGA6 (PMID:10659709). NPR1 is a coactivator of TGA factors at SA-responsive promoters. Reason: The interaction reflects NPR1's coactivator role with TGA factors, so the uninformative protein binding term is replaced with transcription coregulator activity, matching the verdict on the other TGA rows in this review. Proposed replacements: transcription coregulator activity |
| GO:0005515 protein binding | IPI PMID:10659709 NPR1 differentially interacts with members of the TGA/OBF fa... | MODIFY | Summary: NPR1 interacts with the TGA-family bZIP transcription factor TGA5 (PMID:10659709). NPR1 is a coactivator of TGA factors at SA-responsive promoters. Reason: The interaction reflects NPR1's coactivator role with TGA factors, so the uninformative protein binding term is replaced with transcription coregulator activity, matching the verdict on the other TGA rows in this review. Proposed replacements: transcription coregulator activity |
| GO:0005515 protein binding | IPI PMID:10659709 NPR1 differentially interacts with members of the TGA/OBF fa... | MODIFY | Summary: NPR1 interacts with the TGA-family bZIP transcription factor TGA3 (PMID:10659709). NPR1 is a coactivator of TGA factors at SA-responsive promoters. Reason: The interaction reflects NPR1's coactivator role with TGA factors, so the uninformative protein binding term is replaced with transcription coregulator activity, matching the verdict on the other TGA rows in this review. Proposed replacements: transcription coregulator activity |
| GO:0005515 protein binding | IPI PMID:10659709 NPR1 differentially interacts with members of the TGA/OBF fa... | MODIFY | Summary: NPR1 interacts with the TGA-family bZIP transcription factor TGA1 (PMID:10659709). NPR1 is a coactivator of TGA factors at SA-responsive promoters. Reason: The interaction reflects NPR1's coactivator role with TGA factors, so the uninformative protein binding term is replaced with transcription coregulator activity, matching the verdict on the other TGA rows in this review. Proposed replacements: transcription coregulator activity |
| GO:0005515 protein binding | IPI PMID:12953119 The Arabidopsis NPR1 disease resistance protein is a novel c... | MODIFY | Summary: NPR1 interacts with the TGA-family bZIP transcription factor TGA1 (PMID:12953119). NPR1 is a coactivator of TGA factors at SA-responsive promoters. Reason: The interaction reflects NPR1's coactivator role with TGA factors, so the uninformative protein binding term is replaced with transcription coregulator activity, matching the verdict on the other TGA rows in this review. Proposed replacements: transcription coregulator activity |
| GO:0005515 protein binding | IPI PMID:15634206 An Arabidopsis NPR1-like gene, NPR4, is required for disease... | MODIFY | Summary: NPR1 interacts with the TGA-family bZIP transcription factor TGA6 (PMID:15634206). NPR1 is a coactivator of TGA factors at SA-responsive promoters. Reason: The interaction reflects NPR1's coactivator role with TGA factors, so the uninformative protein binding term is replaced with transcription coregulator activity, matching the verdict on the other TGA rows in this review. Proposed replacements: transcription coregulator activity |
| GO:0005515 protein binding | IPI PMID:15634206 An Arabidopsis NPR1-like gene, NPR4, is required for disease... | MODIFY | Summary: NPR1 interacts with the TGA-family bZIP transcription factor TGA5 (PMID:15634206). NPR1 is a coactivator of TGA factors at SA-responsive promoters. Reason: The interaction reflects NPR1's coactivator role with TGA factors, so the uninformative protein binding term is replaced with transcription coregulator activity, matching the verdict on the other TGA rows in this review. Proposed replacements: transcription coregulator activity |
| GO:0005515 protein binding | IPI PMID:15634206 An Arabidopsis NPR1-like gene, NPR4, is required for disease... | MODIFY | Summary: NPR1 interacts with the TGA-family bZIP transcription factor TGA3 (PMID:15634206). NPR1 is a coactivator of TGA factors at SA-responsive promoters. Reason: The interaction reflects NPR1's coactivator role with TGA factors, so the uninformative protein binding term is replaced with transcription coregulator activity, matching the verdict on the other TGA rows in this review. Proposed replacements: transcription coregulator activity |
| GO:0005515 protein binding | IPI PMID:15634206 An Arabidopsis NPR1-like gene, NPR4, is required for disease... | MODIFY | Summary: NPR1 interacts with the TGA-family bZIP transcription factor TGA7 (PMID:15634206). NPR1 is a coactivator of TGA factors at SA-responsive promoters. Reason: The interaction reflects NPR1's coactivator role with TGA factors, so the uninformative protein binding term is replaced with transcription coregulator activity, matching the verdict on the other TGA rows in this review. Proposed replacements: transcription coregulator activity |
| GO:0005515 protein binding | IPI PMID:15634206 An Arabidopsis NPR1-like gene, NPR4, is required for disease... | REMOVE | Summary: NPR1 interacts with NIMIN-3 (PMID:15634206), an NPR1-interacting protein that dampens NPR1-dependent PR gene activation. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:19490895 Proteasome-mediated turnover of the transcription coactivato... | MODIFY | Summary: NPR1 interacts with the TGA-family bZIP transcription factor TGA2 (PMID:19490895). NPR1 is a coactivator of TGA factors at SA-responsive promoters. Reason: The interaction reflects NPR1's coactivator role with TGA factors, so the uninformative protein binding term is replaced with transcription coregulator activity, matching the verdict on the other TGA rows in this review. Proposed replacements: transcription coregulator activity |
| GO:0005515 protein binding | IPI PMID:21798944 Evidence for network evolution in an Arabidopsis interactome... | REMOVE | Summary: NPR1 interacts with NIMIN-3 (PMID:21798944), an NPR1-interacting protein that dampens NPR1-dependent PR gene activation. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:21798944 Evidence for network evolution in an Arabidopsis interactome... | REMOVE | Summary: NPR1 interacts with NIMIN-1 (PMID:21798944), an NPR1-interacting protein that dampens NPR1-dependent PR gene activation. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:21798944 Evidence for network evolution in an Arabidopsis interactome... | REMOVE | Summary: NPR1 interacts with NIMIN-2 (PMID:21798944), an NPR1-interacting protein. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:22699612 NPR3 and NPR4 are receptors for the immune signal salicylic ... | REMOVE | Summary: NPR1 interacts with NPR3 (PMID:22699612), the paralogous SA receptor and CUL3 substrate adaptor that targets NPR1, so NPR1 is the substrate. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:22699612 NPR3 and NPR4 are receptors for the immune signal salicylic ... | REMOVE | Summary: NPR1 interacts with NPR2 (PMID:22699612), a paralogous NPR protein. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:22699612 NPR3 and NPR4 are receptors for the immune signal salicylic ... | REMOVE | Summary: NPR1 interacts with CUL3A (PMID:22699612), the cullin scaffold of the CUL3 ubiquitin ligase that targets NPR1 for turnover, so NPR1 is the substrate. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | REMOVE | Summary: NPR1 interacts with NPR4 (PMID:26269953), the paralogous SA receptor and CUL3 substrate adaptor that targets NPR1, so NPR1 is the substrate. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | REMOVE | Summary: NPR1 interacts with NPR3 (PMID:26269953), the paralogous SA receptor and CUL3 substrate adaptor that targets NPR1, so NPR1 is the substrate. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | REMOVE | Summary: NPR1 interacts with SUMO3 (PMID:26269953), the SUMO paralog that modifies NPR1, so NPR1 is the substrate. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | REMOVE | Summary: NPR1 interacts with NIMIN-3 (PMID:26269953), an NPR1-interacting protein that dampens NPR1-dependent PR gene activation. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | REMOVE | Summary: NPR1 interacts with NIMIN-1 (PMID:26269953), an NPR1-interacting protein that dampens NPR1-dependent PR gene activation. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | REMOVE | Summary: NPR1 interacts with NIMIN-2 (PMID:26269953), an NPR1-interacting protein. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:26269953 Posttranslational Modifications of the Master Transcriptiona... | MODIFY | Summary: NPR1 interacts with WRKY70 (PMID:26269953), a WRKY transcription factor. Unmodified (non-sumoylated) NPR1 binds WRKY70 at W-box elements and acts as a transcriptional corepressor there, the counterpart of its coactivator role with TGA factors. Reason: The WRKY70 interaction reflects NPR1's corepressor function (UniProt FUNCTION and SUBUNIT, citing PubMed:26269953). Transcription coregulator activity covers corepressor as well as coactivator activity, so the uninformative protein binding term is replaced with it, as on the TGA rows. Proposed replacements: transcription coregulator activity Supporting Evidence: PMID:26269953 at resting state, NPR1 is phosphorylated at Ser55/Ser59, which inhibits sumoylation and promotes interaction with WRKY70 to repress PR1 transcription |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | MODIFY | Summary: NPR1 interacts with the TGA-family bZIP transcription factor TGA6 (PMID:32612234). NPR1 is a coactivator of TGA factors at SA-responsive promoters. Reason: The interaction reflects NPR1's coactivator role with TGA factors, so the uninformative protein binding term is replaced with transcription coregulator activity, matching the verdict on the other TGA rows in this review. Proposed replacements: transcription coregulator activity |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | MODIFY | Summary: NPR1 interacts with the TGA-family bZIP transcription factor TGA5 (PMID:32612234). NPR1 is a coactivator of TGA factors at SA-responsive promoters. Reason: The interaction reflects NPR1's coactivator role with TGA factors, so the uninformative protein binding term is replaced with transcription coregulator activity, matching the verdict on the other TGA rows in this review. Proposed replacements: transcription coregulator activity |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | MODIFY | Summary: NPR1 interacts with the TGA-family bZIP transcription factor TGA3 (PMID:32612234). NPR1 is a coactivator of TGA factors at SA-responsive promoters. Reason: The interaction reflects NPR1's coactivator role with TGA factors, so the uninformative protein binding term is replaced with transcription coregulator activity, matching the verdict on the other TGA rows in this review. Proposed replacements: transcription coregulator activity |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | MODIFY | Summary: NPR1 interacts with the TGA-family bZIP transcription factor TGA1 (PMID:32612234). NPR1 is a coactivator of TGA factors at SA-responsive promoters. Reason: The interaction reflects NPR1's coactivator role with TGA factors, so the uninformative protein binding term is replaced with transcription coregulator activity, matching the verdict on the other TGA rows in this review. Proposed replacements: transcription coregulator activity |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: NPR1 interacts with RFC4 (PMID:32612234), a replication factor C subunit found in a large-scale interaction map. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: NPR1 interacts with MHJ24.13 (PMID:32612234), an RNA methyltransferase-family protein found in a large-scale interaction map. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: NPR1 interacts with NIMIN-3 (PMID:32612234), an NPR1-interacting protein that dampens NPR1-dependent PR gene activation. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: NPR1 interacts with NIMIN-1 (PMID:32612234), an NPR1-interacting protein that dampens NPR1-dependent PR gene activation. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: NPR1 interacts with NIMIN-2 (PMID:32612234), an NPR1-interacting protein. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005515 protein binding | IPI PMID:35545668 Structural basis of NPR1 in activating plant immunity. | REMOVE | Summary: NPR1 interacts with CUL3A (PMID:35545668), the cullin scaffold of the CUL3 ubiquitin ligase that targets NPR1 for turnover, so NPR1 is the substrate. Reason: The interaction is not in doubt. However, under the GO:0005515 policy a bare protein binding row carries no functional information, and transcription coregulator activity does not describe this partner: NPR1 does not coactivate it. REMOVE does not mean the interaction is false. |
| GO:0005634 nucleus | EXP PMID:12837250 Inducers of plant systemic acquired resistance regulate NPR1... | ACCEPT | Summary: UniProt experimental annotation placing NPR1 in the nucleus. NPR1 is held as a cytoplasmic oligomer in uninduced cells and moves to the nucleus as a monomer after SA-induced redox changes. Reason: This matches the many IDA rows for the same compartment in this review. PMID:12837250 is cached abstract-only, so the location is accepted by deference to the curator. |
| GO:0005634 nucleus | ISM GO_REF:0000122 | ACCEPT | Summary: AtSubP prediction of nuclear localization, consistent with the experimental nuclear localization of NPR1. Reason: The prediction agrees with extensive experimental evidence. Reconciled with the retired duplicate review genes/ARATH/P93002 (same protein), which had ACCEPT for this row, which was absent from this file's older GOA snapshot. |
| GO:0005737 cytoplasm | EXP PMID:11148282 Nuclear localization of NPR1 is required for activation of P... | ACCEPT | Summary: UniProt experimental annotation placing NPR1 in the cytoplasm. NPR1 is held as a cytoplasmic oligomer in uninduced cells and moves to the nucleus as a monomer after SA-induced redox changes. Reason: This matches the many IDA rows for the same compartment in this review. Supporting Evidence: PMID:11148282 In guard cells, NPR1-GFP is localized in both the cytoplasm and the nuclei in the absence of an SAR inducer. |
| GO:0005737 cytoplasm | EXP PMID:12837250 Inducers of plant systemic acquired resistance regulate NPR1... | ACCEPT | Summary: UniProt experimental annotation placing NPR1 in the cytoplasm. NPR1 is held as a cytoplasmic oligomer in uninduced cells and moves to the nucleus as a monomer after SA-induced redox changes. Reason: This matches the many IDA rows for the same compartment in this review. PMID:12837250 is cached abstract-only, so the location is accepted by deference to the curator. |
| GO:0042742 defense response to bacterium | IEA GO_REF:0000120 | ACCEPT | Summary: NPR1 is essential for bacterial defense responses, mediating SA-dependent immunity against bacterial pathogens like Pseudomonas syringae Reason: Bacterial defense is one of NPR1s most well-established functions. Even though this is IEA, it is strongly supported by experimental evidence showing NPR1s critical role in bacterial immunity [PMID:22699612, PMID:26269953] (Carried over from the GO_REF:0000117 row for the same term, which GOA now supplies via GO_REF:0000120.) Supporting Evidence: PMID:26269953 posttranslational modifications enable dynamic but tight and precise control of plant immune responses |
| GO:0045893 positive regulation of DNA-templated transcription | IDA PMID:17172357 The coactivator function of Arabidopsis NPR1 requires the co... | ACCEPT | Summary: NPR1 positively regulates transcription by forming enhanceosome complexes with TGA transcription factors for defense gene activation Reason: Same paper and term as the TAIR acts_upstream_of_or_within row, here with the involved_in qualifier from ComplexPortal. Strong IDA evidence demonstrates NPR1s positive regulatory role in transcription. NPR1 forms transcriptional activating complexes with TGA factors to promote defense gene expression [PMID:17172357] Supporting Evidence: PMID:17172357 after stimulation with SA, TGA2 is incorporated into a transactivating complex with NPR1, forming an enhanceosome that requires the core of the NPR1 BTB/POZ domain |
| GO:0050832 defense response to fungus | IEA GO_REF:0000120 | ACCEPT | Summary: NPR1 mediates antifungal defense responses through SA-dependent immunity pathways Reason: NPR1 contributes to broad-spectrum immunity including antifungal responses. While bacterial defense is better characterized, fungal defense is also supported [PMID:17513501] (Carried over from the GO_REF:0000117 row for the same term, which GOA now supplies via GO_REF:0000120.) |
| GO:0080027 response to herbivore | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Ensembl Compara projection from the rice ortholog NH1/OsNPR1 (Q9FDY4). The projection is consistent with direct Arabidopsis evidence (PMID:15923339), where insect-induced glucosinolate accumulation during feeding by two aphids and a caterpillar required functional NPR1 but not SA. Reason: Arabidopsis npr1 mutant data (PMID:15923339, also the IMP basis of the retained GO:0009625 response to insect row) show NPR1 is required for the herbivore-induced glucosinolate response, and the requirement is SA-independent, so it is not merely a side effect of SA-JA antagonism. Herbivore defence is peripheral to NPR1's core role in SA-mediated pathogen immunity, so the term is kept as non-core, matching the GO:0009625 row. Supporting Evidence: PMID:15923339 We found increased GS accumulation in response to insect feeding, which required functional NPR1 and ETR1 but not COI1 or SA. |
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