STAT1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding	IBA GO_REF:0000033	ACCEPT	Summary: STAT1 binds to specific DNA regulatory elements including GAS (gamma-activated sites) and ISRE sequences in gene promoters. This IBA annotation accurately reflects STAT1's well-established function as a sequence-specific transcription factor. Reason: IBA annotations represent high-quality phylogenetically-inferred annotations that have undergone extensive review. STAT1's sequence-specific DNA binding to cis-regulatory regions is a core molecular function well-supported by structural and biochemical evidence. Supporting Evidence: PMID:9630226 The crystal structure of the DNA complex of a STAT-1 homodimer has been determined at 2.9 A resolution. STAT-1 utilizes a DNA-binding domain with an immunoglobulin fold, similar to that of NFkappaB and the p53 tumor suppressor protein file:human/STAT1/STAT1-deep-research-falcon.md STAT1 homodimers (historically GAF, gamma-interferon activation factor) bind GAS** (gamma-activated sequence) DNA elements
GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific	IBA GO_REF:0000033	ACCEPT	Summary: This is STAT1's core molecular function. STAT1 is a bona fide transcription factor that activates RNA polymerase II-mediated transcription of interferon-stimulated genes and other cytokine-responsive genes. IBA annotation is well-supported. Reason: This represents STAT1's primary molecular function as established by decades of research. STAT1 directly regulates over 300 interferon-stimulated genes through RNA polymerase II-mediated transcription. IBA evidence reflects phylogenetic conservation of this core function. Supporting Evidence: file:human/STAT1/STAT1-deep-research.md STAT1 regulates a vast network of target genes, with over 300 interferon-stimulated genes (ISGs) identified through experimental validation file:human/STAT1/STAT1-deep-research-falcon.md STAT1’s primary biochemical function is sequence-specific transcriptional regulation as part of IFN-activated transcription factor complexes (GAF and ISGF3), controlling expression of interferon-stimulated genes (ISGs).
GO:0003677 DNA binding	IEA GO_REF:0000120	MARK AS OVER ANNOTATED	Summary: While STAT1 does bind DNA, this term is overly general. STAT1's DNA binding is sequence-specific and is better captured by more specific terms like GO:0000981 or GO:0043565. Reason: Generic DNA binding (GO:0003677) provides insufficient functional specificity for a well-characterized transcription factor like STAT1. The more specific terms 'RNA polymerase II cis-regulatory region sequence-specific DNA binding' and 'DNA-binding transcription factor activity, RNA polymerase II-specific' better capture STAT1's functional specificity.
GO:0003700 DNA-binding transcription factor activity	IEA GO_REF:0000002	ACCEPT	Summary: This is a core function of STAT1 as a transcription factor. However, the more specific term GO:0000981 (DNA-binding transcription factor activity, RNA polymerase II-specific) is more informative. Reason: While GO:0000981 is more specific and preferred, this broader term still accurately describes STAT1's transcriptional function. Both terms can coexist as they represent different levels of annotation granularity, with the specific term providing more mechanistic detail.
GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific	IEA GO_REF:0000117	ACCEPT	Summary: Duplicate of the same term with IBA evidence. This IEA annotation supports the same core function but is redundant with higher-quality IBA annotation.
GO:0005515 protein binding	IPI PMID:11238845 Vaccinia virus blocks gamma interferon signal transduction: ...	MARK AS OVER ANNOTATED	Summary: PMID:11238845 shows STAT1 interaction with vaccinia virus VH1 phosphatase. While STAT1 does bind proteins, this generic term provides limited functional insight. STAT1's critical protein interactions (homodimerization, JAK binding, coactivator binding) are better captured by more specific terms. Supporting Evidence: PMID:11238845 Vaccinia virus blocks gamma interferon signal transduction: viral VH1 phosphatase reverses Stat1 activation.
GO:0005515 protein binding	IPI PMID:12070153 Identification of both positive and negative domains within ...	MARK AS OVER ANNOTATED	Summary: Study shows STAT1 binding to EGFR domains. Generic protein binding term lacks specificity about STAT1's functional protein interactions. Supporting Evidence: PMID:12070153 2002 Jun 17. Identification of both positive and negative domains within the epidermal growth factor receptor COOH-terminal region for signal transducer and activator of transcription (STAT) activation.
GO:0005515 protein binding	IPI PMID:12788789 STAT-1 and c-Fos interaction in nitric oxide synthase-2 gene...	MARK AS OVER ANNOTATED	Summary: Study demonstrates STAT1 interaction with c-Fos in NOS2 gene regulation. While this shows functional protein interaction, the generic term is less informative than specific binding terms. Supporting Evidence: PMID:12788789 STAT-1 and c-Fos interaction in nitric oxide synthase-2 gene activation.
GO:0005515 protein binding	IPI PMID:15780933 Structural bases of unphosphorylated STAT1 association and r...	MARK AS OVER ANNOTATED	Summary: Paper describes structural basis of STAT1 receptor binding interactions. Generic protein binding term lacks functional specificity. Supporting Evidence: PMID:15780933 Structural bases of unphosphorylated STAT1 association and receptor binding.
GO:0005515 protein binding	IPI PMID:15825084 Hepatitis C virus expression suppresses interferon signaling...	MARK AS OVER ANNOTATED	Summary: Shows HCV core protein degrading STAT1 to suppress interferon signaling. Generic term doesn't capture the functional significance of this pathogen-host interaction. Supporting Evidence: PMID:15825084 Hepatitis C virus expression suppresses interferon signaling by degrading STAT1.
GO:0005515 protein binding	IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in...	MARK AS OVER ANNOTATED	Summary: Large-scale proteome interaction mapping study. While it may identify STAT1 interactions, the generic protein binding term provides minimal functional insight. Supporting Evidence: PMID:16189514 Towards a proteome-scale map of the human protein-protein interaction network.
GO:0005515 protein binding	IPI PMID:16273093 A quantitative protein interaction network for the ErbB rece...	MARK AS OVER ANNOTATED	Summary: ErbB receptor protein microarray study. Mass interaction data lacks specific functional context for STAT1. Supporting Evidence: PMID:16273093 A quantitative protein interaction network for the ErbB receptors using protein microarrays.
GO:0005515 protein binding	IPI PMID:16940534 Hepatitis C virus core protein blocks interferon signaling b...	MARK AS OVER ANNOTATED	Summary: HCV core protein blocking STAT1 SH2 domain interactions. While functionally relevant, generic protein binding doesn't capture the mechanistic detail. Supporting Evidence: PMID:16940534 Hepatitis C virus core protein blocks interferon signaling by interaction with the STAT1 SH2 domain.
GO:0005515 protein binding	IPI PMID:17275127 HCV NS5A inhibits interferon-alpha signaling through suppres...	MARK AS OVER ANNOTATED	Summary: HCV NS5A suppressing STAT1 phosphorylation. Generic protein binding term lacks functional specificity for this pathogen-mediated inhibition. Supporting Evidence: PMID:17275127 Dec 14. HCV NS5A inhibits interferon-alpha signaling through suppression of STAT1 phosphorylation in hepatocyte-derived cell lines.
GO:0005515 protein binding	IPI PMID:17596301 Severe acute respiratory syndrome coronavirus ORF6 antagoniz...	MARK AS OVER ANNOTATED	Summary: SARS-CoV ORF6 antagonizing STAT1 nuclear import. While this demonstrates pathogen-host protein interaction, the generic term lacks functional context. Supporting Evidence: PMID:17596301 Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum/Golgi membrane.
GO:0005515 protein binding	IPI PMID:17923090 Acetylation-dependent signal transduction for type I interfe...	MARK AS OVER ANNOTATED	Summary: Study on acetylation-dependent interferon receptor signaling. Generic protein binding term doesn't capture the regulatory complexity of STAT1 interactions. Supporting Evidence: PMID:17923090 Acetylation-dependent signal transduction for type I interferon receptor.
GO:0005515 protein binding	IPI PMID:20195357 A comprehensive resource of interacting protein regions for ...	MARK AS OVER ANNOTATED	Summary: Comprehensive resource of transcription factor interaction networks. Large-scale interaction data lacks specific functional context. Supporting Evidence: PMID:20195357 A comprehensive resource of interacting protein regions for refining human transcription factor networks.
GO:0005515 protein binding	IPI PMID:20576130 Activated networking of platelet activating factor receptor ...	MARK AS OVER ANNOTATED	Summary: PAFR and FAK/STAT1 networking in BRCA1-mutant ovarian epithelium. Context-specific interaction that is better described by more specific terms. Supporting Evidence: PMID:20576130 Activated networking of platelet activating factor receptor and FAK/STAT1 induces malignant potential in BRCA1-mutant at-risk ovarian epithelium.
GO:0005515 protein binding	IPI PMID:21903422 Mapping a dynamic innate immunity protein interaction networ...	MARK AS OVER ANNOTATED	Summary: Mapping innate immunity protein interaction networks regulating type I interferon. While functionally relevant, generic term lacks specificity. Supporting Evidence: PMID:21903422 2011 Sep 8. Mapping a dynamic innate immunity protein interaction network regulating type I interferon production.
GO:0005515 protein binding	IPI PMID:21988832 Toward an understanding of the protein interaction network o...	MARK AS OVER ANNOTATED	Summary: Human liver protein interaction network study. Large-scale proteomic data without specific functional context for STAT1. Supporting Evidence: PMID:21988832 Toward an understanding of the protein interaction network of the human liver.
GO:0005515 protein binding	IPI PMID:24065129 IFNβ-dependent increases in STAT1, STAT2, and IRF9 mediate r...	MARK AS OVER ANNOTATED	Summary: IFN-β increases STAT1/STAT2/IRF9 complex formation for antiviral resistance. While this shows functional protein interactions, generic term doesn't capture the specific complex formation. Supporting Evidence: PMID:24065129 IFNβ-dependent increases in STAT1, STAT2, and IRF9 mediate resistance to viruses and DNA damage.
GO:0005515 protein binding	IPI PMID:24360797 Hepatic RIG-I predicts survival and interferon-α therapeutic...	MARK AS OVER ANNOTATED	Summary: RIG-I interaction with STAT1 in hepatocellular carcinoma interferon response. Generic protein binding lacks mechanistic specificity. Supporting Evidence: PMID:24360797 2013 Dec 19. Hepatic RIG-I predicts survival and interferon-α therapeutic response in hepatocellular carcinoma.
GO:0005515 protein binding	IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ...	MARK AS OVER ANNOTATED	Summary: Mammalian membrane two-hybrid assay for membrane protein interactions. Technical methodology paper with limited functional insight. Supporting Evidence: PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing membrane-protein interactions in human cells.
GO:0005515 protein binding	IPI PMID:25241761 Using an in situ proximity ligation assay to systematically ...	MARK AS OVER ANNOTATED	Summary: In situ proximity ligation assay for pathway protein interactions. Methodological study without specific functional context for STAT1. Supporting Evidence: PMID:25241761 Oct 9. Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	MARK AS OVER ANNOTATED	Summary: Large-scale proteome-scale human interactome network mapping. Generic interaction data without specific functional context. Supporting Evidence: PMID:25416956 A proteome-scale map of the human interactome network.
GO:0005515 protein binding	IPI PMID:25609649 Proteomic analyses reveal distinct chromatin-associated and ...	MARK AS OVER ANNOTATED	Summary: Proteomic analysis of chromatin-associated vs. soluble transcription factor complexes. While relevant to STAT1's transcriptional function, generic protein binding lacks specificity. Supporting Evidence: PMID:25609649 Proteomic analyses reveal distinct chromatin-associated and soluble transcription factor complexes.
GO:0005515 protein binding	IPI PMID:26889034 VP8, the Major Tegument Protein of Bovine Herpesvirus 1, Int...	MARK AS OVER ANNOTATED	Summary: Bovine herpesvirus VP8 protein interacting with STAT1 to inhibit interferon signaling. Pathogen-host interaction better described by more specific terms. Supporting Evidence: PMID:26889034 May 15. VP8, the Major Tegument Protein of Bovine Herpesvirus 1, Interacts with Cellular STAT1 and Inhibits Interferon Beta Signaling.
GO:0005515 protein binding	IPI PMID:26966684 PIPINO: A Software Package to Facilitate the Identification ...	MARK AS OVER ANNOTATED	Summary: PIPINO software for protein-protein interaction identification from mass spectrometry. Computational methodology paper with limited functional context. Supporting Evidence: PMID:26966684 PIPINO: A Software Package to Facilitate the Identification of Protein-Protein Interactions from Affinity Purification Mass Spectrometry Data.
GO:0005515 protein binding	IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ...	MARK AS OVER ANNOTATED	Summary: EGFR network rewiring in KRAS-mutant colorectal cancer cells. Cancer-specific context where generic protein binding lacks functional detail. Supporting Evidence: PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D).
GO:0005515 protein binding	IPI PMID:32953130 SARS-CoV-2 N protein antagonizes type I interferon signaling...	MARK AS OVER ANNOTATED	Summary: SARS-CoV-2 N protein antagonizing STAT1/STAT2 interferon signaling. While functionally relevant pathogen-host interaction, generic term lacks mechanistic detail. Supporting Evidence: PMID:32953130 SARS-CoV-2 N protein antagonizes type I interferon signaling by suppressing phosphorylation and nuclear translocation of STAT1 and STAT2.
GO:0005515 protein binding	IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling...	MARK AS OVER ANNOTATED	Summary: Cell-specific remodeling of human interactome networks. Large-scale proteomic data without specific functional context. Supporting Evidence: PMID:33961781 2021 May 6. Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
GO:0005515 protein binding	IPI PMID:34950606 Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2)...	MARK AS OVER ANNOTATED	Summary: SARS-CoV-2 M and S proteins antagonizing interferon response. Viral interference with STAT1, but generic term lacks mechanistic detail. Supporting Evidence: PMID:34950606 Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Membrane (M) and Spike (S) Proteins Antagonize Host Type I Interferon Response.
GO:0005515 protein binding	IPI PMID:35140242 Human transcription factor protein interaction networks.	MARK AS OVER ANNOTATED	Summary: Human transcription factor protein interaction networks. Large-scale interaction mapping without specific functional context. Supporting Evidence: PMID:35140242 Human transcription factor protein interaction networks.
GO:0005515 protein binding	IPI PMID:8156998 Ligand-induced IFN gamma receptor tyrosine phosphorylation c...	MARK AS OVER ANNOTATED	Summary: IFN-γ receptor tyrosine phosphorylation coupling to STAT1 signal transduction. While this demonstrates functional receptor-STAT1 interaction, generic term lacks specificity. Supporting Evidence: PMID:8156998 Ligand-induced IFN gamma receptor tyrosine phosphorylation couples the receptor to its signal transduction system (p91).
GO:0005515 protein binding	IPI PMID:8605877 The SH2 domains of Stat1 and Stat2 mediate multiple interact...	MARK AS OVER ANNOTATED	Summary: STAT1/STAT2 SH2 domains mediating IFN-α signal transduction. While this shows critical STAT1 protein interactions, the more specific "identical protein binding" term for this paper better captures the homodimerization function. Supporting Evidence: PMID:8605877 The SH2 domains of Stat1 and Stat2 mediate multiple interactions in the transduction of IFN-alpha signals.
GO:0005515 protein binding	IPI PMID:8662591 Differential activation of acute phase response factor/STAT3...	MARK AS OVER ANNOTATED	Summary: Differential STAT3/STAT1 activation via gp130 cytoplasmic domain. Shows STAT1 receptor interactions but generic term lacks functional specificity. Supporting Evidence: PMID:8662591 Differential activation of acute phase response factor/STAT3 and STAT1 via the cytoplasmic domain of the interleukin 6 signal transducer gp130.
GO:0005515 protein binding	IPI PMID:9121453 Functional subdomains of STAT2 required for preassociation w...	MARK AS OVER ANNOTATED	Summary: STAT2 functional subdomains for IFN-α receptor interaction and signaling. Shows STAT1-STAT2 heterodimerization but generic term lacks specificity. Supporting Evidence: PMID:9121453 Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling.
GO:0005515 protein binding	IPI PMID:9881977 Direct suppression of Stat1 function during adenoviral infec...	MARK AS OVER ANNOTATED	Summary: Adenoviral suppression of STAT1 function. Pathogen-host interaction where generic protein binding lacks mechanistic detail. Supporting Evidence: PMID:9881977 Direct suppression of Stat1 function during adenoviral infection.
GO:0042802 identical protein binding	IPI PMID:8605877 The SH2 domains of Stat1 and Stat2 mediate multiple interact...	ACCEPT	Summary: PMID:8605877 demonstrates STAT1 SH2 domain-mediated homodimerization essential for IFN-α signaling. This is a core molecular function of STAT1 - formation of homodimers through reciprocal SH2-phosphotyrosine interactions. Supporting Evidence: PMID:8605877 the SH2 domain of Stat1 and Stat2 can mediate homo- as well as heterodimerization, suggest that a single SH2 domain-phosphotyrosyl interaction is sufficient for dimerization. Moreover, they provide the first direct evidence that the target of the SH2 domain is the STAT tyrosine activation site file:human/STAT1/STAT1-deep-research-falcon.md receptor docking (via SH2), dimerization (via phosphotyrosine–SH2 interactions), DNA binding, and transcriptional activation
GO:0042802 identical protein binding	IPI PMID:9630226 Crystal structure of a tyrosine phosphorylated STAT-1 dimer ...	ACCEPT	Summary: Crystal structure paper showing STAT1 dimer bound to DNA. This provides direct structural evidence for STAT1 homodimerization, which is essential for its transcriptional function. Supporting Evidence: PMID:9630226 The STAT-1 dimer forms a contiguous C-shaped clamp around DNA that is stabilized by reciprocal and highly specific interactions between the SH2 domain of one monomer and the C-terminal segment, phosphorylated on tyrosine, of the other
GO:0031730 CCR5 chemokine receptor binding	IEA GO_REF:0000107	REMOVE	Summary: This is a very specific interaction that is not part of STAT1's core function. STAT1 primarily functions in interferon signaling, not chemokine receptor binding. This appears to be an erroneous computational annotation. Reason: STAT1 is a transcription factor that mediates interferon signaling through JAK-STAT pathway activation. CCR5 chemokine receptor binding is completely unrelated to STAT1's established molecular functions and biological roles. This IEA annotation likely represents a computational error or inappropriate sequence similarity inference.
GO:0043565 sequence-specific DNA binding	IEA GO_REF:0000107	ACCEPT	Summary: STAT1 binds sequence-specifically to GAS elements and ISRE sequences. This is a core molecular function, though the more specific RNA polymerase II terms are preferable. Reason: STAT1 demonstrates sequence-specific DNA binding to GAS (gamma-activated sites) elements as homodimers and to ISRE (interferon-stimulated response elements) as part of ISGF3 complex. This is a well-validated core molecular function. Supporting Evidence: PMID:9630226 The STAT-1 dimer forms a contiguous C-shaped clamp around DNA that is stabilized by reciprocal and highly specific interactions between the SH2 domain of one monomer and the C-terminal segment, phosphorylated on tyrosine, of the other
GO:0051721 protein phosphatase 2A binding	IEA GO_REF:0000107	REMOVE	Summary: While STAT1 may interact with phosphatases for dephosphorylation, PP2A is not a well-established specific regulator of STAT1. This IEA annotation lacks experimental support for a functionally relevant interaction. Reason: STAT1 is primarily regulated by nuclear phosphatases such as TC45/PTPN2 that dephosphorylate Y701, not PP2A. The literature does not support PP2A as a major regulator of STAT1 function. This IEA annotation lacks experimental validation and contradicts established regulatory mechanisms.
GO:0071345 cellular response to cytokine stimulus	IEA GO_REF:0000107	ACCEPT	Summary: This is a core biological process for STAT1. STAT1 mediates cellular responses to multiple cytokines including interferons, IL-6, and others. This is well-supported by extensive literature. Reason: STAT1 is the master regulator of cytokine responses, particularly interferon signaling. This biological process term accurately captures STAT1's primary function in mediating cellular responses to IFN-α/β, IFN-γ, and other cytokines through the JAK-STAT pathway. Supporting Evidence: file:human/STAT1/STAT1-deep-research.md STAT1 functions as a latent cytosolic transcription factor that becomes activated upon extracellular stimulation. The protein undergoes a well-characterized activation cycle through cytokine binding to membrane receptors file:human/STAT1/STAT1-deep-research-falcon.md STAT1 is a signal transducer and transcription factor that is activated downstream of cytokine receptors (classically IFN receptors) via receptor-associated Janus kinases (JAKs), leading to STAT phosphorylation, dimerization, nuclear translocation, and transcriptional regulation of IFN-responsive genes.
GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific	IDA PMID:32209697 Noncanonical STAT1 phosphorylation expands its transcription...	ACCEPT	Summary: Study shows noncanonical STAT1 phosphorylation expanding transcriptional activity to include LPS-induced IL-6 and IL-12p40 production. Strong experimental evidence (IDA) for STAT1's core transcriptional function. Supporting Evidence: PMID:32209697 STAT1 phosphorylated at Thr749 directly enhanced transcription of the gene encoding IL-12p40 (IL12B). Instead of affecting STAT1 nuclear translocation, phosphorylation of Thr749 facilitated the binding of STAT1 to a noncanonical DNA motif (5'-TTTGANNC-3') in the promoter regions of ARID5A and IL12B
GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific	IDA PMID:11972023 Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphoryla...	ACCEPT	Summary: Requirement of Ca2+ and CaMKII for STAT1 Ser-727 phosphorylation in IFN-γ response. Demonstrates STAT1's transcriptional activation function with experimental evidence. Supporting Evidence: PMID:11972023 In response to IFN-γ, the latent cytoplasmic protein signal transducers and activators of transcription 1 (Stat1) becomes phosphorylated on Y701, dimerizes, and accumulates in the nucleus to activate transcription of IFN-γ-responsive genes
GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific	IDA PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Cri...	ACCEPT	Summary: SETD2-mediated methylation of STAT1 critical for interferon antiviral activity. Strong experimental evidence for STAT1's transcription factor function. Supporting Evidence: PMID:28753426 SETD2 directly mediates STAT1 methylation on lysine 525 via its methyltransferase activity, which reinforces IFN-activated STAT1 phosphorylation and antiviral cellular response. In addition, SETD2 selectively catalyzes the tri-methylation of H3K36 on promoters of some ISGs such as ISG15, leading to gene activation
GO:0046427 positive regulation of receptor signaling pathway via JAK-STAT	IDA PMID:16257975 The conserved Leu-724 residue is required for both serine ph...	MODIFY	Summary: Study shows conserved Leu-724 required for STAT1 serine phosphorylation and coactivator recruitment for IFN-γ mediated transcription, reflecting STAT1's role in promoting JAK-STAT pathway signaling. This annotation is flagged retired:true in GOA. Per PR #831 review feedback, a retired annotation should not be ACCEPTed as-is; changed to MODIFY pointing at the current active form of the term (GO:0046427 was relabeled from "positive regulation of JAK-STAT cascade" to "positive regulation of receptor signaling pathway via JAK-STAT"). Proposed replacements: positive regulation of receptor signaling pathway via JAK-STAT Supporting Evidence: PMID:16257975 the conserved Leu-724 residue is also essential for gene activation mediated by Stat1.
GO:0003700 DNA-binding transcription factor activity	IDA PMID:9535918 Heteromerization of the gammac chain with the interleukin-9 ...	ACCEPT	Summary: IL-9 receptor leads to STAT activation and apoptosis prevention. While this shows STAT1's transcriptional activity, the more specific RNA polymerase II term is preferable for precision. Supporting Evidence: PMID:9535918 Heteromerization of the gammac chain with the interleukin-9 receptor alpha subunit leads to STAT activation and prevention of apoptosis
GO:0000977 RNA polymerase II transcription regulatory region sequence-specific DNA binding	IDA PMID:22002246 A novel disrupter of telomere silencing 1-like (DOT1L) inter...	ACCEPT	Summary: DOT1L interaction required for STAT1-activated gene expression. This demonstrates STAT1's sequence-specific binding to regulatory regions, which is a core molecular function. Supporting Evidence: PMID:22002246 STAT1 binding to its DNA recognition element near the IRF1 promoter is diminished 2-fold in the DOT1L-depleted cell line. In vivo and in vitro protein interaction assays reveal a DOT1L-STAT1 interaction
GO:0001223 transcription coactivator binding	IPI PMID:22002246 A novel disrupter of telomere silencing 1-like (DOT1L) inter...	ACCEPT	Summary: STAT1 interaction with DOT1L coactivator for gene expression. This reflects STAT1's ability to recruit transcriptional machinery, which is essential for its transcriptional activation function. Supporting Evidence: PMID:22002246 Domain mapping identifies the middle region of DOT1L (amino acids 580–1183) as the STAT1 interaction domain.
GO:0001222 transcription corepressor binding	IPI PMID:23386060 hCAF1/CNOT7 regulates interferon signalling by targeting STA...	KEEP AS NON CORE	Summary: hCAF1/CNOT7 regulates interferon signaling by targeting STAT1. While STAT1 may interact with corepressors as part of regulatory mechanisms, this is not a core function and may represent context-specific regulation. Reason: Transcription corepressor binding represents a regulatory mechanism for fine-tuning STAT1 activity rather than a core molecular function. While functionally relevant for STAT1 regulation, this interaction is context-dependent and not part of STAT1's primary interferon signaling functions. Supporting Evidence: PMID:23386060 hcaf1/cnot7 regulates interferon signalling by targeting stat1
GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific	ISA GO_REF:0000113	ACCEPT	Summary: Annotation based on sequence similarity to known transcription factors. While ISA evidence is less strong than experimental evidence, this accurately reflects STAT1's core function. Reason: ISA (Inferred from Sequence Alignment) annotation is supported by STAT1's well-characterized DNA-binding domain structure and sequence similarity to other transcription factors. The annotation accurately reflects STAT1's core transcriptional function despite being computationally inferred.
GO:0000979 RNA polymerase II core promoter sequence-specific DNA binding	IDA PMID:23386060 hCAF1/CNOT7 regulates interferon signalling by targeting STA...	KEEP AS NON CORE	Summary: hCAF1/CNOT7 regulation of STAT1 interferon signaling. While STAT1 can bind core promoter regions, it more commonly binds to enhancer regions (GAS elements). This may be context-specific. Reason: STAT1 primarily binds to enhancer elements (GAS sites) and distal regulatory regions rather than core promoters. While it may occasionally bind core promoter sequences in specific contexts, this represents a minority of STAT1's DNA binding activity and is not a core molecular function. Supporting Evidence: PMID:23386060 Consistently, hCAF1 silencing enhances STAT1 basal promoter occupancy associated with increased expression of a subset of STAT1-regulated genes
GO:0045296 cadherin binding	HDA PMID:25468996 E-cadherin interactome complexity and robustness resolved by...	REMOVE	Summary: E-cadherin interactome study using high-throughput methods. Cadherin binding is not a known or relevant function of STAT1, which is a cytokine-responsive transcription factor. This appears to be a false positive from proteomic screening. Reason: STAT1 functions as a cytosolic/nuclear transcription factor in interferon signaling pathways. Cadherin binding is completely unrelated to STAT1's established molecular functions and likely represents a false positive from high-throughput proteomics screening (HDA evidence). No mechanistic rationale exists for STAT1-cadherin interactions. Supporting Evidence: PMID:25468996 E-cadherin interactome complexity and robustness resolved by quantitative proteomics
GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding	IDA PMID:21268089 Molecular mechanisms underlying the inhibition of IFN-γ-indu...	ACCEPT	Summary: STAT1-mediated gene transcription inhibition by simvastatin and PPAR/LXR agonists. This demonstrates STAT1's binding to cis-regulatory elements, which is a core function. Supporting Evidence: PMID:21268089 Simvastatin and PPAR agonists had no effect on the IFN-γ-induced, phosphorylation-mediated activation of STAT1 and its DNA binding but attenuated its ability to activate gene transcription.
GO:0000981 DNA-binding transcription factor activity, RNA polymerase II-specific	IDA PMID:21268089 Molecular mechanisms underlying the inhibition of IFN-γ-indu...	ACCEPT	Summary: Another duplicate of STAT1's core transcription factor function with strong experimental evidence. Consistent with previous assessments. Supporting Evidence: PMID:21268089 Simvastatin and PPAR agonists had no effect on the IFN-γ-induced, phosphorylation-mediated activation of STAT1 and its DNA binding but attenuated its ability to activate gene transcription.
GO:0005515 protein binding	IPI PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	MARK AS OVER ANNOTATED	Summary: PARP9-DTX3L targeting histone H2BJ and viral protease to enhance interferon signaling. While this shows STAT1 in regulatory complexes, generic protein binding lacks functional specificity. Supporting Evidence: PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection.
GO:0005634 nucleus	IDA PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	ACCEPT	Summary: STAT1 translocates to the nucleus upon activation where it functions as a transcription factor. Nuclear localization is a key aspect of STAT1's function cycle. Supporting Evidence: PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection
GO:0019899 enzyme binding	IPI PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	ACCEPT	Summary: STAT1 interactions with various enzymes (kinases, phosphatases, methyltransferases) are critical for its regulation. This is more informative than generic protein binding but still quite broad. Supporting Evidence: PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection
GO:0035035 histone acetyltransferase binding	IPI PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	ACCEPT	Summary: STAT1 interacts with histone-modifying enzymes as part of transcriptional activation complexes. This reflects STAT1's role in chromatin regulation during gene activation. Supporting Evidence: PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection
GO:0042393 histone binding	IPI PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	MARK AS OVER ANNOTATED	Summary: The IPI histone-binding annotation derives from PMID:26479788, which shows the PARP9-DTX3L ubiquitin ligase (not STAT1) directly targets histone H2BJ. STAT1 forms a complex with PARP9, so the histone co-recovery most likely reflects indirect association via the PARP9 complex rather than a direct STAT1-histone interaction. Per PR #831 review feedback, downgraded ACCEPT → MARK_AS_OVER_ANNOTATED to reflect the indirect nature. (The companion GO:0035035 histone acetyltransferase binding annotation, supported by STAT1 recruiting p300/CBP, remains ACCEPT.) Reason: Direct STAT1-histone binding is not demonstrated; PMID:26479788 shows PARP9-DTX3L targeting histone H2BJ, with STAT1 present in the complex. The histone-binding IPI most plausibly reflects indirect complex co-recovery, not a direct STAT1 molecular function. Supporting Evidence: PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection
GO:0044389 ubiquitin-like protein ligase binding	IPI PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	ACCEPT	Summary: STAT1 regulation involves ubiquitin-like modifications and interactions with ligases for protein stability and localization control. This is a relevant regulatory mechanism. Supporting Evidence: PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection
GO:0000979 RNA polymerase II core promoter sequence-specific DNA binding	IDA PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Cri...	KEEP AS NON CORE	Summary: SETD2 methylation study showing STAT1 binding to core promoter regions. While STAT1 primarily binds enhancer regions, it can also bind promoter regions depending on gene context. Supporting Evidence: PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Critical for Interferon Antiviral Activity.
GO:0005515 protein binding	IPI PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Cri...	MARK AS OVER ANNOTATED	Summary: SETD2 methyltransferase interaction with STAT1. While this is a functionally important interaction for STAT1 regulation, the generic protein binding term lacks specificity. Supporting Evidence: PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Critical for Interferon Antiviral Activity.
GO:0042803 protein homodimerization activity	IDA PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Cri...	ACCEPT	Summary: Demonstrates STAT1 homodimerization essential for transcriptional function. This is a more specific and accurate term than "identical protein binding" for describing STAT1's dimerization. Supporting Evidence: PMID:28753426 SETD2 directly mediates STAT1 methylation on lysine 525 via its methyltransferase activity, which reinforces IFN-activated STAT1 phosphorylation and antiviral cellular response file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus
GO:0003700 DNA-binding transcription factor activity	IDA PMID:23386060 hCAF1/CNOT7 regulates interferon signalling by targeting STA...	ACCEPT	Summary: hCAF1/CNOT7 regulation of STAT1. Strong experimental evidence for STAT1's transcriptional function, though RNA polymerase II-specific terms are more precise. Supporting Evidence: PMID:23386060 Consistently, hCAF1 silencing enhances STAT1 basal promoter occupancy associated with increased expression of a subset of STAT1-regulated genes.
GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding	IDA PMID:18035482 Regulation of XAF1 expression in human colon cancer cell by ...	ACCEPT	Summary: STAT1 regulation of XAF1 expression in colon cancer cells by IFN-β. Demonstrates STAT1's sequence-specific binding to regulatory regions, which is a core function. Supporting Evidence: PMID:18035482 Regulation of XAF1 expression in human colon cancer cell by interferon beta: activation by the transcription regulator STAT1
GO:0005515 protein binding	IPI PMID:12867595 The cell death regulator GRIM-19 is an inhibitor of signal t...	MARK AS OVER ANNOTATED	Summary: GRIM-19 as inhibitor of STAT3, may also interact with STAT1. Generic protein binding term lacks functional specificity. Supporting Evidence: PMID:12867595 The cell death regulator GRIM-19 is an inhibitor of signal transducer and activator of transcription 3.
GO:0043542 endothelial cell migration	IMP NOT PMID:16585190 Signal transducer and activator of transcription 1 activatio...	ACCEPT	Summary: PMID:16585190 reports STAT1 activation inhibits angiogenesis and tube formation; GOA captures this PMID as NOT involved in endothelial cell migration. Reason: GOA marks this PMID as NOT involved_in endothelial cell migration. The study shows STAT1-driven inhibition of angiogenic responses in endothelial cells rather than promoting migration, so the negated annotation is appropriate. Supporting Evidence: PMID:16585190 Signal transducer and activator of transcription 1 activation in endothelial cells is a negative regulator of angiogenesis
GO:0003700 DNA-binding transcription factor activity	IDA PMID:10973496 Nucleocytoplasmic translocation of Stat1 is regulated by a l...	ACCEPT	Summary: Nucleocytoplasmic translocation of STAT1 regulated by leucine-rich export signal. Strong experimental evidence for STAT1's transcriptional function. Supporting Evidence: PMID:10973496 Signal transducer and activator of transcription (Stat) proteins are latent transcription factors that reside in the cytoplasm before activation. On cytokine-induced tyrosine phosphorylation, these molecules dimerize and accumulate transiently in the nucleus
GO:0005164 tumor necrosis factor receptor binding	IPI PMID:10848577 Stat1 as a component of tumor necrosis factor alpha receptor...	KEEP AS NON CORE	Summary: STAT1 as component of TNFR1-TRADD signaling complex to inhibit NF-κB. While this shows STAT1 in TNF signaling context, this is not a core function compared to interferon signaling. Reason: While STAT1 can participate in TNF receptor signaling complexes, this represents cross-pathway interactions rather than STAT1's core function. STAT1's primary role is as an interferon-responsive transcription factor in JAK-STAT signaling, not TNF receptor binding. This interaction may be functionally relevant in specific contexts but is not a central molecular function. Supporting Evidence: PMID:10848577 Stat1 as a component of tumor necrosis factor alpha receptor 1-TRADD signaling complex to inhibit NF-kappaB activation
GO:0005515 protein binding	IPI PMID:10848577 Stat1 as a component of tumor necrosis factor alpha receptor...	MARK AS OVER ANNOTATED	Summary: STAT1-TNFR interaction. Generic protein binding lacks functional specificity for this cross-pathway interaction. Supporting Evidence: PMID:10848577 Stat1 as a component of tumor necrosis factor alpha receptor 1-TRADD signaling complex to inhibit NF-kappaB activation.
GO:0003690 double-stranded DNA binding	IDA PMID:9630226 Crystal structure of a tyrosine phosphorylated STAT-1 dimer ...	ACCEPT	Summary: Crystal structure of STAT1 dimer bound to DNA shows double-stranded DNA binding. While accurate, the sequence-specific DNA binding terms are more informative for STAT1's function. Supporting Evidence: PMID:9630226 The crystal structure of the DNA complex of a STAT-1 homodimer has been determined at 2.9 A resolution. STAT-1 utilizes a DNA-binding domain with an immunoglobulin fold, similar to that of NFkappaB and the p53 tumor suppressor protein
GO:0042803 protein homodimerization activity	IDA PMID:9630226 Crystal structure of a tyrosine phosphorylated STAT-1 dimer ...	ACCEPT	Summary: Crystal structure provides definitive evidence for STAT1 homodimerization through reciprocal SH2-phosphotyrosine interactions. This is a core molecular function. Supporting Evidence: PMID:9630226 The STAT-1 dimer forms a contiguous C-shaped clamp around DNA that is stabilized by reciprocal and highly specific interactions between the SH2 domain of one monomer and the C-terminal segment, phosphorylated on tyrosine, of the other
GO:0005515 protein binding	IPI PMID:16531398 Tid1 isoforms are mitochondrial DnaJ-like chaperones with un...	MARK AS OVER ANNOTATED	Summary: Tid1 isoforms as mitochondrial DnaJ-like chaperones interacting with STAT1. Generic protein binding lacks functional context for this chaperone interaction. Supporting Evidence: PMID:16531398 Epub 2006 Mar 10. Tid1 isoforms are mitochondrial DnaJ-like chaperones with unique carboxyl termini that determine cytosolic fate.
GO:0005515 protein binding	IPI PMID:16306601 Respiratory syncytial virus-inducible BCL-3 expression antag...	MARK AS OVER ANNOTATED	Summary: RSV-inducible BCL-3 antagonizing STAT/IRF and NF-κB signaling. Pathogen-mediated interference with STAT1 signaling, but generic term lacks specificity. Supporting Evidence: PMID:16306601 Respiratory syncytial virus-inducible BCL-3 expression antagonizes the STAT/IRF and NF-kappaB signaling pathways by inducing histone deacetylase 1 recruitment to the interleukin-8 promoter.
GO:0005515 protein binding	IPI PMID:34521819 Could not retrieve title - publication not available	UNDECIDED	Summary: The generic protein binding annotation is supported by PMID:34521819, which could not be retrieved and verified. Per the schema convention ("ALWAYS USE UNDECIDED IF YOU ARE UNABLE TO ACCESS RELEVANT PUBLICATIONS") and PR #831 review feedback, the action is set to UNDECIDED rather than MARK_AS_OVER_ANNOTATED until the underlying publication can be accessed and the interaction assessed. Reason: The supporting publication PMID:34521819 could not be retrieved or verified, so the annotation cannot be evaluated. Although generic GO:0005515 protein binding is uninformative in general, the schema requires UNDECIDED when the relevant publication is inaccessible.
GO:0005634 nucleus	IBA GO_REF:0000033	ACCEPT	Summary: STAT1 translocates to the nucleus upon activation to act as a transcription factor at GAS/ISRE elements. Nuclear localization is a core, well-established site of STAT1 action. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 executes its transcriptional role in the nucleus at IFN-responsive promoters/enhancers.
GO:0006357 regulation of transcription by RNA polymerase II	IBA GO_REF:0000033	ACCEPT	Summary: STAT1 directly regulates RNA polymerase II-dependent transcription of interferon-stimulated genes. Core function. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1’s primary biochemical function is sequence-specific transcriptional regulation as part of IFN-activated transcription factor complexes (GAF and ISGF3), controlling expression of interferon-stimulated genes (ISGs).
GO:0007259 cell surface receptor signaling pathway via JAK-STAT	IBA GO_REF:0000033	ACCEPT	Summary: STAT1 is the canonical signal transducer of the JAK-STAT cell surface receptor signaling pathway, activated by interferon and other cytokine receptors via receptor-associated Janus kinases. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 is a signal transducer and transcription factor that is activated downstream of cytokine receptors (classically IFN receptors) via receptor-associated Janus kinases (JAKs), leading to STAT phosphorylation, dimerization, nuclear translocation, and transcriptional regulation of IFN-responsive genes.
GO:0006952 defense response	IBA GO_REF:0000033	ACCEPT	Summary: STAT1 is essential for host defense, particularly via interferon-driven antiviral, antibacterial and antifungal gene expression. AR complete STAT1 deficiency abolishes IFN responses with severe infection susceptibility. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md A 2024 review summarizes autosomal recessive complete STAT1 deficiency as abolishing type I/II/III IFN and IL-27 signaling
GO:0005737 cytoplasm	IBA GO_REF:0000033	ACCEPT	Summary: Latent STAT1 is cytoplasmic and acts in the cytoplasm to receive cytokine-receptor-driven JAK phosphorylation prior to nuclear translocation. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md In resting cells, STAT1 is largely cytoplasmic or shuttling in unphosphorylated/preassociated forms; after tyrosine phosphorylation it forms dimers that translocate to the nucleus.
GO:0042127 regulation of cell population proliferation	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: STAT1 generally exerts antiproliferative effects downstream of interferon signaling (e.g. induction of p21 and cell-cycle inhibitors), consistent with this phylogenetically inferred role in regulating cell population proliferation. Reason: Regulation of cell proliferation is a downstream physiological consequence of STAT1-driven gene expression rather than its core molecular activity; the IBA term is biologically sound but represents a non-core pleiotropic output. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1's primary biochemical function is sequence-specific transcriptional regulation as part of IFN-activated transcription factor complexes (GAF and ISGF3), controlling expression of interferon-stimulated genes (ISGs).
GO:0043434 response to peptide hormone	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: STAT1 can be activated downstream of peptide-hormone receptors (e.g. growth hormone, leptin, insulin-related signaling) that engage the JAK-STAT pathway, supporting a response to peptide hormone. Reason: STAT1 participation in peptide-hormone responses reflects the broad use of the JAK-STAT module by many receptors; it is a peripheral, context-dependent role rather than STAT1's core interferon function.
GO:0060337 type I interferon-mediated signaling pathway	IBA GO_REF:0000033	ACCEPT	Summary: STAT1, with STAT2 and IRF9, forms ISGF3 to mediate type I (IFN-alpha/beta) signaling and binds ISRE elements in target genes. Core function. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1–STAT2 heterodimers plus IRF9 form ISGF3, which binds ISRE** (interferon-stimulated response element) DNA elements.
GO:0005634 nucleus	IEA GO_REF:0000044	ACCEPT	Summary: STAT1 translocates to the nucleus upon activation to act as a transcription factor; nuclear localization is well established. Reason: Nuclear localization is a core, experimentally validated aspect of STAT1 biology; the IEA term is correct.
GO:0005654 nucleoplasm	IEA GO_REF:0000117	ACCEPT	Summary: Activated STAT1 dimers/ISGF3 act in the nucleoplasm at target-gene promoters. Reason: Nucleoplasmic localization is consistent with STAT1's role as a nuclear transcription factor and is supported by experimental nuclear/nucleoplasm annotations.
GO:0006355 regulation of DNA-templated transcription	IEA GO_REF:0000002	ACCEPT	Summary: STAT1 regulates transcription of its target genes; this broad term is subsumed by the more specific RNA Pol II transcription-factor annotations. Reason: A correct but general transcription-regulation term; acceptable as a broad parent of STAT1's specific transcriptional roles.
GO:0007165 signal transduction	IEA GO_REF:0000002	ACCEPT	Summary: STAT1 is a signal transducer in the JAK-STAT pathway; the generic signal transduction term is correct but less informative than the specific JAK-STAT terms. Reason: Generic signal transduction is a true parent of STAT1's JAK-STAT signaling role; acceptable though more specific terms are preferred.
GO:0042981 regulation of apoptotic process	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: STAT1 regulates apoptosis, chiefly by inducing pro-apoptotic genes (caspases, Fas/TRAIL) downstream of interferon signaling. Reason: Regulation of apoptosis is a downstream consequence of STAT1 transcriptional output rather than a core molecular function; biologically valid but non-core.
GO:0051093 negative regulation of developmental process	IEA GO_REF:0000117	KEEP AS NON CORE	Summary: STAT1 can negatively regulate certain developmental processes (e.g. angiogenesis, mesenchymal-to-epithelial transitions), consistent with this broad term. Reason: Negative regulation of developmental processes reflects context-specific, pleiotropic outputs of STAT1, not its core interferon-signaling function.
GO:0051607 defense response to virus	IEA GO_REF:0000120	ACCEPT	Summary: STAT1 drives interferon-induced antiviral gene programs (ISGs); STAT1 LOF abolishes IFN responses with severe viral disease. Core function. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md A 2024 review summarizes autosomal recessive complete STAT1 deficiency as abolishing type I/II/III IFN and IL-27 signaling and reports 24 patients described "so far" in that review; it notes severe early-life infections
GO:0060333 type II interferon-mediated signaling pathway	IEA GO_REF:0000117	ACCEPT	Summary: STAT1 homodimers form GAF and bind GAS DNA elements, mediating the type II (IFN-gamma) signaling pathway. Core function. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 homodimers (historically GAF, gamma-interferon activation factor) bind GAS** (gamma-activated sequence) DNA elements.
GO:0060337 type I interferon-mediated signaling pathway	IEA GO_REF:0000117	ACCEPT	Summary: STAT1 (with STAT2 and IRF9) forms ISGF3 to mediate type I IFN signaling and binds ISRE elements; central, well-established function. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1–STAT2 heterodimers plus IRF9 form ISGF3, which binds ISRE** (interferon-stimulated response element) DNA elements.
GO:0007259 cell surface receptor signaling pathway via JAK-STAT	NAS PMID:24058793 STAT heterodimers in immunity: A mixed message or a unique s...	ACCEPT	Summary: STAT1 is activated as the signal transducer of the JAK-STAT pathway in this study, downstream of cytokine/interferon receptors. Reason: JAK-STAT signal transduction is a core STAT1 function directly supported here. Supporting Evidence: PMID:24058793 STAT heterodimers in immunity: A mixed message or a unique signal? Delgoffe GM(1), Vignali DA.
GO:0045944 positive regulation of transcription by RNA polymerase II	NAS PMID:24058793 STAT heterodimers in immunity: A mixed message or a unique s...	ACCEPT	Summary: STAT1 directly drives positive transcription of interferon/cytokine target genes by RNA polymerase II (e.g. XAF1, IL12B, antiviral ISGs). Reason: Positive regulation of RNA Pol II transcription is a core STAT1 function with strong direct and structural support. Supporting Evidence: PMID:24058793 STAT heterodimers in immunity: A mixed message or a unique signal? Delgoffe GM(1), Vignali DA.
GO:0045944 positive regulation of transcription by RNA polymerase II	IDA PMID:24065129 IFNβ-dependent increases in STAT1, STAT2, and IRF9 mediate r...	ACCEPT	Summary: STAT1 (as ISGF3 component) drives positive transcriptional regulation of antiviral genes by RNA polymerase II. Core function supported by direct experimental evidence. Supporting Evidence: PMID:24065129 IFNβ-dependent increases in STAT1, STAT2, and IRF9 mediate resistance to viruses and DNA damage. file:human/STAT1/STAT1-deep-research-falcon.md STAT1’s primary biochemical function is sequence-specific transcriptional regulation as part of IFN-activated transcription factor complexes (GAF and ISGF3), controlling expression of interferon-stimulated genes (ISGs).
GO:0007259 cell surface receptor signaling pathway via JAK-STAT	IEA GO_REF:0000120	ACCEPT	Summary: STAT1 is the canonical signal transducer of the JAK-STAT cell surface receptor signaling pathway. Reason: This is a core function of STAT1, well supported across the literature; the IEA term is correct. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 is a signal transducer and transcription factor that is activated downstream of cytokine receptors (classically IFN receptors) via receptor-associated Janus kinases (JAKs), leading to STAT phosphorylation, dimerization, nuclear translocation, and transcriptional regulation of IFN-responsive genes.
GO:0007584 response to nutrient	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA orthology transfer (Ensembl Compara) of 'response to nutrient'. STAT1 can be engaged in this response in specific contexts via JAK-STAT signaling, but it is a peripheral, non- core role transferred computationally without direct human evidence. Reason: Context-specific physiological-stimulus response transferred by orthology; biologically plausible as a downstream/secondary STAT1 role but not part of its core interferon function and lacking direct human experimental support.
GO:0008015 blood circulation	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA orthology transfer (Ensembl Compara) of 'blood circulation'. STAT1 can be engaged in this response in specific contexts via JAK-STAT signaling, but it is a peripheral, non- core role transferred computationally without direct human evidence. Reason: Context-specific physiological-stimulus response transferred by orthology; biologically plausible as a downstream/secondary STAT1 role but not part of its core interferon function and lacking direct human experimental support.
GO:0008284 positive regulation of cell population proliferation	IEA GO_REF:0000107	MARK AS OVER ANNOTATED	Summary: IEA orthology transfer of 'positive regulation of cell population proliferation'. STAT1 is predominantly antiproliferative downstream of interferon; a positive proliferation role is at best highly context-specific and not characteristic of STAT1. Reason: This Ensembl-Compara orthology transfer conflicts with STAT1's well-documented antiproliferative/tumor-suppressive activity and lacks direct human evidence; likely an over-annotation.
GO:0009410 response to xenobiotic stimulus	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA orthology transfer (Ensembl Compara) of 'response to xenobiotic stimulus'. STAT1 can be engaged in this response in specific contexts via JAK-STAT signaling, but it is a peripheral, non-core role transferred computationally without direct human evidence. Reason: Context-specific physiological-stimulus response transferred by orthology; biologically plausible as a downstream/secondary STAT1 role but not part of its core interferon function and lacking direct human experimental support.
GO:0009612 response to mechanical stimulus	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA orthology transfer (Ensembl Compara) of 'response to mechanical stimulus'. STAT1 can be engaged in this response in specific contexts via JAK-STAT signaling, but it is a peripheral, non-core role transferred computationally without direct human evidence. Reason: Context-specific physiological-stimulus response transferred by orthology; biologically plausible as a downstream/secondary STAT1 role but not part of its core interferon function and lacking direct human experimental support.
GO:0032869 cellular response to insulin stimulus	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA orthology transfer (Ensembl Compara) of 'cellular response to insulin stimulus'. STAT1 can be engaged in this response in specific contexts via JAK-STAT signaling, but it is a peripheral, non-core role transferred computationally without direct human evidence. Reason: Context-specific physiological-stimulus response transferred by orthology; biologically plausible as a downstream/secondary STAT1 role but not part of its core interferon function and lacking direct human experimental support.
GO:0034097 response to cytokine	IEA GO_REF:0000107	ACCEPT	Summary: STAT1 mediates cellular responses to numerous cytokines through the JAK-STAT pathway. Reason: Response to cytokine is a core aspect of STAT1 function and is well supported.
GO:0042542 response to hydrogen peroxide	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA orthology transfer (Ensembl Compara) of 'response to hydrogen peroxide'. STAT1 can be engaged in this response in specific contexts via JAK-STAT signaling, but it is a peripheral, non-core role transferred computationally without direct human evidence. Reason: Context-specific physiological-stimulus response transferred by orthology; biologically plausible as a downstream/secondary STAT1 role but not part of its core interferon function and lacking direct human experimental support.
GO:0043434 response to peptide hormone	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: STAT1 can be activated downstream of peptide-hormone receptors (e.g. growth hormone, leptin, insulin-related signaling) that engage the JAK-STAT pathway, supporting a response to peptide hormone. Reason: STAT1 participation in peptide-hormone responses reflects the broad use of the JAK-STAT module by many receptors; it is a peripheral, context-dependent role rather than STAT1's core interferon function.
GO:0045429 positive regulation of nitric oxide biosynthetic process	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA orthology transfer (Ensembl Compara) of 'positive regulation of nitric oxide biosynthetic process'. STAT1 can be engaged in this response in specific contexts via JAK- STAT signaling, but it is a peripheral, non-core role transferred computationally without direct human evidence. Reason: Context-specific physiological-stimulus response transferred by orthology; biologically plausible as a downstream/secondary STAT1 role but not part of its core interferon function and lacking direct human experimental support.
GO:0048661 positive regulation of smooth muscle cell proliferation	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA orthology transfer (Ensembl Compara) of 'positive regulation of smooth muscle cell proliferation'. STAT1 can be engaged in this response in specific contexts via JAK-STAT signaling, but it is a peripheral, non-core role transferred computationally without direct human evidence. Reason: Context-specific physiological-stimulus response transferred by orthology; biologically plausible as a downstream/secondary STAT1 role but not part of its core interferon function and lacking direct human experimental support.
GO:0051591 response to cAMP	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA orthology transfer (Ensembl Compara) of 'response to cAMP'. STAT1 can be engaged in this response in specific contexts via JAK-STAT signaling, but it is a peripheral, non- core role transferred computationally without direct human evidence. Reason: Context-specific physiological-stimulus response transferred by orthology; biologically plausible as a downstream/secondary STAT1 role but not part of its core interferon function and lacking direct human experimental support.
GO:0097696 cell surface receptor signaling pathway via STAT	IDA PMID:18035482 Regulation of XAF1 expression in human colon cancer cell by ...	ACCEPT	Summary: STAT1 mediates cell surface receptor signaling via STAT, activating XAF1 expression downstream of IFN-beta in colon cancer cells. Reason: STAT-mediated receptor signaling is core to STAT1; directly supported. Supporting Evidence: PMID:18035482 Epub 2007 Nov 26. Regulation of XAF1 expression in human colon cancer cell by interferon beta: activation by the transcription regulator STAT1.
GO:0007259 cell surface receptor signaling pathway via JAK-STAT	NAS PMID:9630226 Crystal structure of a tyrosine phosphorylated STAT-1 dimer ...	ACCEPT	Summary: STAT1 is activated as the signal transducer of the JAK-STAT pathway in this study, downstream of cytokine/interferon receptors. Reason: JAK-STAT signal transduction is a core STAT1 function directly supported here. Supporting Evidence: PMID:9630226 Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA.
GO:0045944 positive regulation of transcription by RNA polymerase II	NAS PMID:9630226 Crystal structure of a tyrosine phosphorylated STAT-1 dimer ...	ACCEPT	Summary: STAT1 directly drives positive transcription of interferon/cytokine target genes by RNA polymerase II (e.g. XAF1, IL12B, antiviral ISGs). Reason: Positive regulation of RNA Pol II transcription is a core STAT1 function with strong direct and structural support. Supporting Evidence: PMID:9630226 Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA.
GO:0005654 nucleoplasm	IDA GO_REF:0000052	ACCEPT	Summary: Immunofluorescence localizes STAT1 to the nucleoplasm, consistent with its active nuclear form. Reason: Nucleoplasmic localization is consistent with STAT1's core nuclear transcription-factor function.
GO:0005634 nucleus	IDA PMID:32209697 Noncanonical STAT1 phosphorylation expands its transcription...	ACCEPT	Summary: STAT1 localizes to the nucleus upon activation, where it functions as a transcription factor; directly observed in this study. Reason: Nuclear localization is a core, repeatedly validated feature of activated STAT1. Supporting Evidence: PMID:32209697 Noncanonical STAT1 phosphorylation expands its transcriptional activity into promoting LPS-induced IL-6 and IL-12p40 production.
GO:0045944 positive regulation of transcription by RNA polymerase II	IDA PMID:32209697 Noncanonical STAT1 phosphorylation expands its transcription...	ACCEPT	Summary: STAT1 directly drives positive transcription of interferon/cytokine target genes by RNA polymerase II (e.g. XAF1, IL12B, antiviral ISGs). Reason: Positive regulation of RNA Pol II transcription is a core STAT1 function with strong direct and structural support. Supporting Evidence: PMID:32209697 Noncanonical STAT1 phosphorylation expands its transcriptional activity into promoting LPS-induced IL-6 and IL-12p40 production.
GO:0038111 interleukin-7-mediated signaling pathway	IDA PMID:29202461 IL-7-dependent STAT1 activation limits homeostatic CD4+ T ce...	KEEP AS NON CORE	Summary: Under lymphopenic conditions, IL-7 induces STAT1 activation that limits homeostatic CD4+ T cell expansion, placing STAT1 in the IL-7-mediated signaling pathway. Reason: IL-7-mediated STAT1 signaling is a context-specific (lymphopenia) role; biologically supported but peripheral to STAT1's core interferon function. Supporting Evidence: PMID:29202461 under lymphopenic conditions, there is a modulation of STAT1 expression resulting in an IL-7-dependent STAT1 and STAT5 activation
GO:0005634 nucleus	IC PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Cri...	ACCEPT	Summary: STAT1 localizes to the nucleus upon activation, where it functions as a transcription factor; directly observed in this study. Reason: Nuclear localization is a core, repeatedly validated feature of activated STAT1. Supporting Evidence: PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Critical for Interferon Antiviral Activity.
GO:0005634 nucleus	IDA PMID:18035482 Regulation of XAF1 expression in human colon cancer cell by ...	ACCEPT	Summary: STAT1 localizes to the nucleus upon activation, where it functions as a transcription factor; directly observed in this study. Reason: Nuclear localization is a core, repeatedly validated feature of activated STAT1. Supporting Evidence: PMID:18035482 Epub 2007 Nov 26. Regulation of XAF1 expression in human colon cancer cell by interferon beta: activation by the transcription regulator STAT1.
GO:0060337 type I interferon-mediated signaling pathway	IDA PMID:23386060 hCAF1/CNOT7 regulates interferon signalling by targeting STA...	ACCEPT	Summary: STAT1 directly mediates 'type I interferon-mediated signaling pathway', a core interferon- response function demonstrated experimentally in this study. Reason: Interferon signaling/antiviral response is the central, non-redundant function of STAT1; directly supported. Supporting Evidence: PMID:23386060 hCAF1/CNOT7 regulates interferon signalling by targeting STAT1.
GO:0007259 cell surface receptor signaling pathway via JAK-STAT	IDA PMID:11972023 Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphoryla...	ACCEPT	Summary: STAT1 is activated as the signal transducer of the JAK-STAT pathway in this study, downstream of cytokine/interferon receptors. Reason: JAK-STAT signal transduction is a core STAT1 function directly supported here. Supporting Evidence: PMID:11972023 Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphorylation in response to IFN-gamma.
GO:0034341 response to type II interferon	IDA PMID:11972023 Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphoryla...	ACCEPT	Summary: STAT1 directly mediates 'response to type II interferon', a core interferon-response function demonstrated experimentally in this study. Reason: Interferon signaling/antiviral response is the central, non-redundant function of STAT1; directly supported. Supporting Evidence: PMID:11972023 Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphorylation in response to IFN-gamma.
GO:0005634 nucleus	IDA PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Cri...	ACCEPT	Summary: STAT1 localizes to the nucleus upon activation, where it functions as a transcription factor; directly observed in this study. Reason: Nuclear localization is a core, repeatedly validated feature of activated STAT1. Supporting Evidence: PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Critical for Interferon Antiviral Activity.
GO:0007259 cell surface receptor signaling pathway via JAK-STAT	IDA PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Cri...	ACCEPT	Summary: STAT1 is activated as the signal transducer of the JAK-STAT pathway in this study, downstream of cytokine/interferon receptors. Reason: JAK-STAT signal transduction is a core STAT1 function directly supported here. Supporting Evidence: PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Critical for Interferon Antiviral Activity.
GO:0035458 cellular response to interferon-beta	IDA PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Cri...	ACCEPT	Summary: STAT1 directly mediates 'cellular response to interferon-beta', a core interferon-response function demonstrated experimentally in this study. Reason: Interferon signaling/antiviral response is the central, non-redundant function of STAT1; directly supported. Supporting Evidence: PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Critical for Interferon Antiviral Activity.
GO:0071346 cellular response to type II interferon	IDA PMID:11972023 Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphoryla...	ACCEPT	Summary: STAT1 directly mediates 'cellular response to type II interferon', a core interferon- response function demonstrated experimentally in this study. Reason: Interferon signaling/antiviral response is the central, non-redundant function of STAT1; directly supported. Supporting Evidence: PMID:11972023 Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphorylation in response to IFN-gamma.
GO:0006357 regulation of transcription by RNA polymerase II	IDA PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Cri...	ACCEPT	Summary: SETD2-mediated methylation of STAT1 modulates STAT1-dependent transcription of ISGs by RNA Pol II. Reason: Regulation of RNA Pol II transcription is core to STAT1; directly supported. Supporting Evidence: PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Critical for Interferon Antiviral Activity.
GO:0005634 nucleus	IDA PMID:15322115 Protein kinase Cdelta regulates apoptosis via activation of ...	ACCEPT	Summary: STAT1 localizes to the nucleus upon activation, where it functions as a transcription factor; directly observed in this study. Reason: Nuclear localization is a core, repeatedly validated feature of activated STAT1. Supporting Evidence: PMID:15322115 2004 Aug 20. Protein kinase Cdelta regulates apoptosis via activation of STAT1.
GO:0007259 cell surface receptor signaling pathway via JAK-STAT	IDA PMID:22002246 A novel disrupter of telomere silencing 1-like (DOT1L) inter...	ACCEPT	Summary: STAT1 is activated as the signal transducer of the JAK-STAT pathway in this study, downstream of cytokine/interferon receptors. Reason: JAK-STAT signal transduction is a core STAT1 function directly supported here. Supporting Evidence: PMID:22002246 Epub 2011 Oct 15. A novel disrupter of telomere silencing 1-like (DOT1L) interaction is required for signal transducer and activator of transcription 1 (STAT1)-activated gene expression.
GO:0005634 nucleus	IC PMID:9535918 Heteromerization of the gammac chain with the interleukin-9 ...	ACCEPT	Summary: STAT1 localizes to the nucleus upon activation, where it functions as a transcription factor; directly observed in this study. Reason: Nuclear localization is a core, repeatedly validated feature of activated STAT1. Supporting Evidence: PMID:9535918 Heteromerization of the gammac chain with the interleukin-9 receptor alpha subunit leads to STAT activation and prevention of apoptosis.
GO:0038113 interleukin-9-mediated signaling pathway	IDA PMID:9535918 Heteromerization of the gammac chain with the interleukin-9 ...	KEEP AS NON CORE	Summary: STAT1 is activated downstream of the IL-9 receptor (gammac/IL-9Ralpha), participating in IL-9-mediated signaling and apoptosis prevention. Reason: IL-9-mediated STAT1 signaling is a specific cytokine-context role, peripheral to STAT1's core interferon function. Supporting Evidence: PMID:9535918 Heteromerization of the gammac chain with the interleukin-9 receptor alpha subunit leads to STAT activation and prevention of apoptosis
GO:0070106 interleukin-27-mediated signaling pathway	IDA PMID:32270034 IL-27 signaling activates skin cells to induce innate antivi...	KEEP AS NON CORE	Summary: IL-27 activates STAT1 in skin cells to induce innate antiviral proteins, placing STAT1 in the IL-27-mediated signaling pathway. Reason: IL-27-mediated STAT1 signaling is a specific cytokine-context antiviral role; supported but non-core relative to interferon signaling. Supporting Evidence: PMID:32270034 IL-27 signaling activates skin cells to induce innate antiviral proteins and protects against Zika virus infection.
GO:1990841 promoter-specific chromatin binding	IDA PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	ACCEPT	Summary: STAT1 binds specific gene promoters (promoter-specific chromatin binding) to activate ISGs, consistent with its sequence-specific transcription-factor function. Reason: Promoter-specific chromatin binding is a core molecular feature of STAT1 as a DNA-binding transcription factor. Supporting Evidence: PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection.
GO:0000785 chromatin	ISA GO_REF:0000113	ACCEPT	Summary: As a DNA-binding transcription factor, STAT1 localizes to chromatin at target-gene promoters. Reason: Chromatin localization is consistent with STAT1's core transcription-factor function and is additionally supported by promoter-occupancy/ChIP data.
GO:0002230 positive regulation of defense response to virus by host	IMP PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	ACCEPT	Summary: STAT1, via PARP9-DTX3L-enhanced interferon signaling, positively regulates the host antiviral defense response. Reason: Positive regulation of host antiviral defense is central to STAT1 function and is directly supported. Supporting Evidence: PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection.
GO:0002230 positive regulation of defense response to virus by host	IGI PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	ACCEPT	Summary: STAT1, via PARP9-DTX3L-enhanced interferon signaling, positively regulates the host antiviral defense response. Reason: Positive regulation of host antiviral defense is central to STAT1 function and is directly supported. Supporting Evidence: PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection.
GO:0045893 positive regulation of DNA-templated transcription	IMP PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	ACCEPT	Summary: STAT1 positively regulates transcription of its target genes; directly supported (e.g. PARP9-DTX3L/STAT1 enhancing ISG expression; Stat1 export-signal mutants altering target- gene activation). Reason: Positive regulation of DNA-templated transcription is a core STAT1 activity; the broad term is correct and complementary to the RNA Pol II-specific terms. Supporting Evidence: PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection.
GO:0045893 positive regulation of DNA-templated transcription	IGI PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	ACCEPT	Summary: STAT1 positively regulates transcription of its target genes; directly supported (e.g. PARP9-DTX3L/STAT1 enhancing ISG expression; Stat1 export-signal mutants altering target- gene activation). Reason: Positive regulation of DNA-templated transcription is a core STAT1 activity; the broad term is correct and complementary to the RNA Pol II-specific terms. Supporting Evidence: PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection.
GO:0060333 type II interferon-mediated signaling pathway	IMP PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	ACCEPT	Summary: STAT1 directly mediates 'type II interferon-mediated signaling pathway', a core interferon-response function demonstrated experimentally in this study. Reason: Interferon signaling/antiviral response is the central, non-redundant function of STAT1; directly supported. Supporting Evidence: PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection.
GO:0032727 positive regulation of interferon-alpha production	IDA PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Cri...	KEEP AS NON CORE	Summary: SETD2-methylated STAT1 reinforces interferon antiviral responses including IFN-alpha production in a positive feedback loop. Reason: Positive regulation of IFN-alpha production reflects STAT1's feed-forward amplification of the interferon system; a genuine but secondary output relative to its core transcription- factor role. Supporting Evidence: PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Critical for Interferon Antiviral Activity.
GO:0051607 defense response to virus	IDA PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Cri...	ACCEPT	Summary: STAT1 directly mediates 'defense response to virus', a core interferon-response function demonstrated experimentally in this study. Reason: Interferon signaling/antiviral response is the central, non-redundant function of STAT1; directly supported. Supporting Evidence: PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Critical for Interferon Antiviral Activity.
GO:0005634 nucleus	IDA PMID:23386060 hCAF1/CNOT7 regulates interferon signalling by targeting STA...	ACCEPT	Summary: STAT1 localizes to the nucleus upon activation, where it functions as a transcription factor; directly observed in this study. Reason: Nuclear localization is a core, repeatedly validated feature of activated STAT1. Supporting Evidence: PMID:23386060 hCAF1/CNOT7 regulates interferon signalling by targeting STAT1.
GO:0071346 cellular response to type II interferon	IDA PMID:23386060 hCAF1/CNOT7 regulates interferon signalling by targeting STA...	ACCEPT	Summary: STAT1 directly mediates 'cellular response to type II interferon', a core interferon- response function demonstrated experimentally in this study. Reason: Interferon signaling/antiviral response is the central, non-redundant function of STAT1; directly supported. Supporting Evidence: PMID:23386060 hCAF1/CNOT7 regulates interferon signalling by targeting STAT1.
GO:0045648 positive regulation of erythrocyte differentiation	IMP PMID:28283061 Functional Selectivity in Cytokine Signaling Revealed Throug...	KEEP AS NON CORE	Summary: A pathogenic EPO mutation study implicates STAT1 (alongside STAT5) in cytokine signaling affecting erythroid differentiation. Reason: Erythrocyte differentiation is a specialized, context-dependent role downstream of cytokine receptor signaling, peripheral to STAT1's core interferon function. Supporting Evidence: PMID:28283061 Functional Selectivity in Cytokine Signaling Revealed Through a Pathogenic EPO Mutation.
GO:0005634 nucleus	IDA PMID:15825084 Hepatitis C virus expression suppresses interferon signaling...	ACCEPT	Summary: STAT1 localizes to the nucleus upon activation, where it functions as a transcription factor; directly observed in this study. Reason: Nuclear localization is a core, repeatedly validated feature of activated STAT1. Supporting Evidence: PMID:15825084 Hepatitis C virus expression suppresses interferon signaling by degrading STAT1.
GO:0035456 response to interferon-beta	IMP PMID:24882218 Unanchored K48-linked polyubiquitin synthesized by the E3-ub...	ACCEPT	Summary: STAT1 directly mediates 'response to interferon-beta', a core interferon-response function demonstrated experimentally in this study. Reason: Interferon signaling/antiviral response is the central, non-redundant function of STAT1; directly supported. Supporting Evidence: PMID:24882218 2014 May 29. Unanchored K48-linked polyubiquitin synthesized by the E3-ubiquitin ligase TRIM6 stimulates the interferon-IKKε kinase-mediated antiviral response.
GO:0046725 negative regulation by virus of viral protein levels in host cell	IMP PMID:15825084 Hepatitis C virus expression suppresses interferon signaling...	KEEP AS NON CORE	Summary: In the HCV system, STAT1-driven interferon signaling restricts viral protein levels; HCV core counteracts this by degrading STAT1. Reason: This term captures STAT1's antiviral restriction of viral protein accumulation in a specific host-pathogen context; biologically valid but non-core and somewhat contorted. Supporting Evidence: PMID:15825084 Hepatitis C virus expression suppresses interferon signaling by degrading STAT1.
GO:0035458 cellular response to interferon-beta	IMP PMID:18035482 Regulation of XAF1 expression in human colon cancer cell by ...	ACCEPT	Summary: STAT1 directly mediates 'cellular response to interferon-beta', a core interferon-response function demonstrated experimentally in this study. Reason: Interferon signaling/antiviral response is the central, non-redundant function of STAT1; directly supported. Supporting Evidence: PMID:18035482 Epub 2007 Nov 26. Regulation of XAF1 expression in human colon cancer cell by interferon beta: activation by the transcription regulator STAT1.
GO:0045944 positive regulation of transcription by RNA polymerase II	IMP PMID:18035482 Regulation of XAF1 expression in human colon cancer cell by ...	ACCEPT	Summary: STAT1 directly drives positive transcription of interferon/cytokine target genes by RNA polymerase II (e.g. XAF1, IL12B, antiviral ISGs). Reason: Positive regulation of RNA Pol II transcription is a core STAT1 function with strong direct and structural support. Supporting Evidence: PMID:18035482 Epub 2007 Nov 26. Regulation of XAF1 expression in human colon cancer cell by interferon beta: activation by the transcription regulator STAT1.
GO:0060333 type II interferon-mediated signaling pathway	ISS GO_REF:0000024	ACCEPT	Summary: STAT1 homodimers (GAF) mediate the type II (IFN-gamma) signaling pathway. Reason: Core STAT1 function; the ISS annotation duplicates the well-supported type II IFN signaling role. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md * STAT1 homodimers (historically GAF, gamma-interferon activation factor) bind GAS (gamma-activated sequence) DNA elements.
GO:0060337 type I interferon-mediated signaling pathway	ISS GO_REF:0000024	ACCEPT	Summary: STAT1 (with STAT2/IRF9 as ISGF3) mediates the type I IFN signaling pathway. Reason: Core STAT1 function; ISS annotation duplicates the well-supported type I IFN signaling role. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1–STAT2 heterodimers plus IRF9 form ISGF3, which binds ISRE (interferon-stimulated response element) DNA elements.
GO:0000785 chromatin	IDA PMID:18035482 Regulation of XAF1 expression in human colon cancer cell by ...	ACCEPT	Summary: STAT1 binds chromatin at the ISRE of the XAF1 promoter (quantitative ChIP), directly demonstrating chromatin localization. Reason: Direct ChIP evidence supports STAT1 chromatin localization, consistent with its core DNA- binding transcription-factor function. Supporting Evidence: PMID:18035482 Epub 2007 Nov 26. Regulation of XAF1 expression in human colon cancer cell by interferon beta: activation by the transcription regulator STAT1.
GO:0000122 negative regulation of transcription by RNA polymerase II	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: STAT1 can act as a transcriptional repressor at specific targets (e.g. repressing ULK1 and certain pro-angiogenic/proliferative genes), supporting negative regulation of RNA Pol II transcription. Reason: While STAT1 is primarily a transcriptional activator, context-specific repression is documented; this ISS term captures a real but non-core, gene-specific repressive activity.
GO:0001937 negative regulation of endothelial cell proliferation	IMP PMID:16585190 Signal transducer and activator of transcription 1 activatio...	KEEP AS NON CORE	Summary: IFN-gamma-activated STAT1 in endothelial cells inhibits proliferation and tube formation, negatively regulating endothelial cell proliferation. Reason: Endothelial antiproliferative/antiangiogenic activity is a context-specific downstream output of STAT1 signaling, peripheral to its core interferon transcription-factor role. Supporting Evidence: PMID:16585190 IFN-gamma inhibited cell growth and tube formation of HUVECs
GO:0002053 positive regulation of mesenchymal cell proliferation	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Sequence-similarity-based transfer of a kidney/metanephros developmental role ('positive regulation of mesenchymal cell proliferation'). STAT1 has a documented role in renal tubule (re)differentiation, so a developmental kidney role is plausible, but these specific metanephric terms are non-core developmental annotations. Reason: These curator-judgment ISS transfers describe specialized kidney-developmental roles that are peripheral to STAT1's core interferon/transcription-factor function; retained as non- core. Supporting Evidence: PMID:20861313 STAT1 is required for redifferentiation during Madin-Darby canine kidney tubulogenesis.
GO:0003340 negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Sequence-similarity-based transfer of a kidney/metanephros developmental role ('negative regulation of mesenchymal to epithelial transition involved in metanephros morphogenesis'). STAT1 has a documented role in renal tubule (re)differentiation, so a developmental kidney role is plausible, but these specific metanephric terms are non-core developmental annotations. Reason: These curator-judgment ISS transfers describe specialized kidney-developmental roles that are peripheral to STAT1's core interferon/transcription-factor function; retained as non- core. Supporting Evidence: PMID:20861313 STAT1 is required for redifferentiation during Madin-Darby canine kidney tubulogenesis.
GO:0016525 negative regulation of angiogenesis	IMP PMID:16585190 Signal transducer and activator of transcription 1 activatio...	KEEP AS NON CORE	Summary: STAT1 activation in endothelial cells is a negative regulator of angiogenesis, suppressing VEGF-driven growth and tube formation. Reason: Negative regulation of angiogenesis is a documented but context-specific downstream effect of STAT1; retained as non-core. Supporting Evidence: PMID:16585190 Signal transducer and activator of transcription 1 activation in endothelial cells is a negative regulator of angiogenesis.
GO:0042981 regulation of apoptotic process	TAS PMID:12108949 The role of STATs in apoptosis.	KEEP AS NON CORE	Summary: STAT1 regulates apoptosis, predominantly transducing pro-apoptotic signals by inducing genes such as caspases, Fas and TRAIL. Reason: Regulation of apoptosis is a downstream transcriptional output of STAT1 rather than a core molecular function; supported as a non-core role. Supporting Evidence: PMID:12108949 STAT1 and, under some circums-tances. STAT3 are important for transducing pro-apoptotic signals
GO:0061326 renal tubule development	IMP PMID:20861313 STAT1 is required for redifferentiation during Madin-Darby c...	KEEP AS NON CORE	Summary: STAT1 is required for epithelial redifferentiation during MDCK kidney tubulogenesis, supporting a role in renal tubule development. Reason: Renal tubule development is a specialized morphogenetic role, peripheral to STAT1's core interferon function; supported but non-core. Supporting Evidence: PMID:20861313 STAT1 is required for redifferentiation during Madin-Darby canine kidney tubulogenesis.
GO:0072136 metanephric mesenchymal cell proliferation involved in metanephros development	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Sequence-similarity-based transfer of a kidney/metanephros developmental role ('metanephric mesenchymal cell proliferation involved in metanephros development'). STAT1 has a documented role in renal tubule (re)differentiation, so a developmental kidney role is plausible, but these specific metanephric terms are non-core developmental annotations. Reason: These curator-judgment ISS transfers describe specialized kidney-developmental roles that are peripheral to STAT1's core interferon/transcription-factor function; retained as non- core. Supporting Evidence: PMID:20861313 STAT1 is required for redifferentiation during Madin-Darby canine kidney tubulogenesis.
GO:0072162 metanephric mesenchymal cell differentiation	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Sequence-similarity-based transfer of a kidney/metanephros developmental role ('metanephric mesenchymal cell differentiation'). STAT1 has a documented role in renal tubule (re)differentiation, so a developmental kidney role is plausible, but these specific metanephric terms are non-core developmental annotations. Reason: These curator-judgment ISS transfers describe specialized kidney-developmental roles that are peripheral to STAT1's core interferon/transcription-factor function; retained as non- core. Supporting Evidence: PMID:20861313 STAT1 is required for redifferentiation during Madin-Darby canine kidney tubulogenesis.
GO:0072308 negative regulation of metanephric nephron tubule epithelial cell differentiation	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: Sequence-similarity-based transfer of a kidney/metanephros developmental role ('negative regulation of metanephric nephron tubule epithelial cell differentiation'). STAT1 has a documented role in renal tubule (re)differentiation, so a developmental kidney role is plausible, but these specific metanephric terms are non-core developmental annotations. Reason: These curator-judgment ISS transfers describe specialized kidney-developmental roles that are peripheral to STAT1's core interferon/transcription-factor function; retained as non- core. Supporting Evidence: PMID:20861313 STAT1 is required for redifferentiation during Madin-Darby canine kidney tubulogenesis.
GO:0005634 nucleus	IDA PMID:10692450 Thrombin inhibits tumor cell growth in association with up-r...	ACCEPT	Summary: STAT1 localizes to the nucleus upon activation, where it functions as a transcription factor; directly observed in this study. Reason: Nuclear localization is a core, repeatedly validated feature of activated STAT1. Supporting Evidence: PMID:10692450 Thrombin inhibits tumor cell growth in association with up-regulation of p21(waf/cip1) and caspases via a p53-independent, STAT-1-dependent pathway.
GO:0045893 positive regulation of DNA-templated transcription	IDA PMID:10973496 Nucleocytoplasmic translocation of Stat1 is regulated by a l...	ACCEPT	Summary: STAT1 positively regulates transcription of its target genes; directly supported (e.g. PARP9-DTX3L/STAT1 enhancing ISG expression; Stat1 export-signal mutants altering target- gene activation). Reason: Positive regulation of DNA-templated transcription is a core STAT1 activity; the broad term is correct and complementary to the RNA Pol II-specific terms. Supporting Evidence: PMID:10973496 Nucleocytoplasmic translocation of Stat1 is regulated by a leucine-rich export signal in the coiled-coil domain.
GO:0005634 nucleus	IDA PMID:10973496 Nucleocytoplasmic translocation of Stat1 is regulated by a l...	ACCEPT	Summary: STAT1 localizes to the nucleus upon activation, where it functions as a transcription factor; directly observed in this study. Reason: Nuclear localization is a core, repeatedly validated feature of activated STAT1. Supporting Evidence: PMID:10973496 Nucleocytoplasmic translocation of Stat1 is regulated by a leucine-rich export signal in the coiled-coil domain.
GO:0033209 tumor necrosis factor-mediated signaling pathway	IDA PMID:10848577 Stat1 as a component of tumor necrosis factor alpha receptor...	KEEP AS NON CORE	Summary: STAT1 is a component of the TNFR1-TRADD signaling complex, participating in TNF-alpha- mediated signaling. Reason: STAT1's role in TNF signaling (inhibiting NF-kappaB) is a specific, non-canonical function distinct from its core interferon-driven transcription; retained as non-core. Supporting Evidence: PMID:10848577 Stat1 as a component of tumor necrosis factor alpha receptor 1-TRADD signaling complex to inhibit NF-kappaB activation.
GO:0043124 negative regulation of canonical NF-kappaB signal transduction	IMP PMID:10848577 Stat1 as a component of tumor necrosis factor alpha receptor...	KEEP AS NON CORE	Summary: STAT1 negatively regulates canonical NF-kappaB signaling as part of the TNFR1-TRADD complex. Reason: Negative regulation of NF-kappaB is a specific, non-canonical STAT1 activity in TNF signaling; biologically supported but peripheral to STAT1's core function. Supporting Evidence: PMID:10848577 Stat1 as a component of tumor necrosis factor alpha receptor 1-TRADD signaling complex to inhibit NF-kappaB activation.
GO:0005634 nucleus	IDA PMID:21268089 Molecular mechanisms underlying the inhibition of IFN-γ-indu...	ACCEPT	Summary: STAT1 localizes to the nucleus upon activation, where it functions as a transcription factor; directly observed in this study. Reason: Nuclear localization is a core, repeatedly validated feature of activated STAT1. Supporting Evidence: PMID:21268089 Molecular mechanisms underlying the inhibition of IFN-γ-induced, STAT1-mediated gene transcription in human macrophages by simvastatin and agonists of PPARs and LXRs.
GO:0060333 type II interferon-mediated signaling pathway	IDA PMID:21268089 Molecular mechanisms underlying the inhibition of IFN-γ-indu...	ACCEPT	Summary: STAT1 directly mediates 'type II interferon-mediated signaling pathway', a core interferon-response function demonstrated experimentally in this study. Reason: Interferon signaling/antiviral response is the central, non-redundant function of STAT1; directly supported. Supporting Evidence: PMID:21268089 Molecular mechanisms underlying the inhibition of IFN-γ-induced, STAT1-mediated gene transcription in human macrophages by simvastatin and agonists of PPARs and LXRs.
GO:0005634 nucleus	IDA PMID:16306601 Respiratory syncytial virus-inducible BCL-3 expression antag...	ACCEPT	Summary: STAT1 localizes to the nucleus upon activation, where it functions as a transcription factor; directly observed in this study. Reason: Nuclear localization is a core, repeatedly validated feature of activated STAT1. Supporting Evidence: PMID:16306601 Respiratory syncytial virus-inducible BCL-3 expression antagonizes the STAT/IRF and NF-kappaB signaling pathways by inducing histone deacetylase 1 recruitment to the interleukin-8 promoter.
GO:0070721 ISGF3 complex	IBA GO_REF:0000033	ACCEPT	Summary: STAT1 is a defining component of the ISGF3 transcription factor complex, together with STAT2 and IRF9, that drives type I/III IFN responses by binding ISRE elements. Core complex assignment. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1–STAT2 heterodimers plus IRF9 form ISGF3, which binds ISRE** (interferon-stimulated response element) DNA elements.
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: Latent STAT1 resides in the cytoplasm prior to cytokine-induced phosphorylation and nuclear import. Reason: Cytoplasmic localization of the latent pool is a core, well-established feature of STAT1 signaling.
GO:0005829 cytosol	IEA GO_REF:0000117	ACCEPT	Summary: STAT1's latent pool is cytosolic; this cytosol localization is consistent with established biology. Reason: Cytosolic localization of latent STAT1 is well supported; the IEA term is appropriate.
GO:0090575 RNA polymerase II transcription regulator complex	IEA GO_REF:0000117	ACCEPT	Summary: As a sequence-specific RNA Pol II transcription factor, STAT1 is part of RNA polymerase II transcription regulator complexes (e.g. GAF/ISGF3 assembled on promoters). Reason: Membership in an RNA Pol II transcription regulator complex is consistent with STAT1's core transcription-factor function.
GO:0090575 RNA polymerase II transcription regulator complex	IPI PMID:8662591 Differential activation of acute phase response factor/STAT3...	ACCEPT	Summary: STAT1 assembles into RNA polymerase II transcription regulator complexes (e.g. STAT dimers and ISGF3) on target promoters. Reason: Membership in an RNA Pol II transcription regulator complex is consistent with STAT1's core transcription-factor function. Supporting Evidence: PMID:8662591 Differential activation of acute phase response factor/STAT3 and STAT1 via the cytoplasmic domain of the interleukin 6 signal transducer gp130.
GO:0070721 ISGF3 complex	IPI PMID:24065129 IFNβ-dependent increases in STAT1, STAT2, and IRF9 mediate r...	ACCEPT	Summary: Direct IPI evidence for STAT1's role in the ISGF3 complex (with STAT2 and IRF9). Core complex assignment. Supporting Evidence: PMID:24065129 IFNβ-dependent increases in STAT1, STAT2, and IRF9 mediate resistance to viruses and DNA damage. file:human/STAT1/STAT1-deep-research-falcon.md STAT1–STAT2 heterodimers plus IRF9 form ISGF3, which binds ISRE** (interferon-stimulated response element) DNA elements.
GO:0090575 RNA polymerase II transcription regulator complex	NAS PMID:24058793 STAT heterodimers in immunity: A mixed message or a unique s...	ACCEPT	Summary: STAT1 assembles into RNA polymerase II transcription regulator complexes (e.g. STAT dimers and ISGF3) on target promoters. Reason: Membership in an RNA Pol II transcription regulator complex is consistent with STAT1's core transcription-factor function. Supporting Evidence: PMID:24058793 STAT heterodimers in immunity: A mixed message or a unique signal? Delgoffe GM(1), Vignali DA.
GO:0030424 axon	IEA GO_REF:0000107	REMOVE	Summary: STAT1 is a cytoplasmic/nuclear transcription factor that translocates to the nucleus upon IFN-driven phosphorylation. Axonal localization is not a documented STAT1 compartment; this IEA annotation (Ensembl Compara ortholog transfer, GO_REF:0000107) is most likely an erroneous transfer. Per PR #831 review feedback, resolved PENDING → REMOVE. Reason: Axon localization is inconsistent with STAT1's well-established cytoplasmic-to-nuclear transcription-factor biology and is not supported by direct evidence; the IEA orthology transfer is an over-prediction.
GO:0030425 dendrite	IEA GO_REF:0000107	REMOVE	Summary: As with the axon annotation, dendritic localization is not a documented STAT1 compartment. STAT1 is a cytoplasmic/nuclear transcription factor; this IEA orthology transfer (GO_REF:0000107) is most likely erroneous. Per PR #831 review feedback, resolved PENDING → REMOVE. Reason: Dendrite localization is inconsistent with STAT1's cytoplasmic-to- nuclear transcription-factor biology and lacks direct supporting evidence; the IEA orthology transfer is an over-prediction.
GO:0090575 RNA polymerase II transcription regulator complex	IPI PMID:9630226 Crystal structure of a tyrosine phosphorylated STAT-1 dimer ...	ACCEPT	Summary: STAT1 assembles into RNA polymerase II transcription regulator complexes (e.g. STAT dimers and ISGF3) on target promoters. Reason: Membership in an RNA Pol II transcription regulator complex is consistent with STAT1's core transcription-factor function. Supporting Evidence: PMID:9630226 Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA.
GO:0005730 nucleolus	IDA GO_REF:0000052	MARK AS OVER ANNOTATED	Summary: HPA immunofluorescence reports a nucleolar signal for STAT1. STAT1 is a nucleoplasmic/cytoplasmic transcription factor; a dedicated nucleolar role is not part of its characterized biology and this single high-throughput localization is not corroborated by functional data. Reason: Nucleolar localization rests on a single high-throughput immunofluorescence dataset and is not supported by STAT1's established nucleoplasmic transcription-factor function; likely over-annotation.
GO:0005829 cytosol	IDA GO_REF:0000052	ACCEPT	Summary: Immunofluorescence localizes STAT1 to the cytosol, consistent with its latent cytosolic pool. Reason: Cytosolic localization of latent STAT1 is well established; the IDA (HPA immunofluorescence) annotation is appropriate.
GO:0005737 cytoplasm	IDA PMID:32209697 Noncanonical STAT1 phosphorylation expands its transcription...	ACCEPT	Summary: STAT1 resides in the cytoplasm in its inactive state and becomes activated upon phosphorylation by JAK kinases. It must be present in the cytoplasm to receive signals from cytokine receptors and before translocating to the nucleus. Reason: Cytoplasmic localization is essential for STAT1's signaling mechanism, as it must be available in the cytoplasm to be phosphorylated by activated JAK kinases and to form dimers before nuclear translocation for transcriptional regulation. Supporting Evidence: PMID:32209697 Noncanonical STAT1 phosphorylation expands its transcriptional activity into promoting LPS-induced IL-6 and IL-12p40 production.
GO:0005829 cytosol	TAS Reactome:R-HSA-9851142	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-8985981	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-8985983	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-9865524	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8985900	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8985943	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8985966	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8985981	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8985983	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8985988	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-9865511	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005737 cytoplasm	IDA PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	ACCEPT	Summary: STAT1 is observed in the cytoplasm, consistent with its latent cytoplasmic pool prior to nuclear translocation. Reason: Cytoplasmic localization of latent STAT1 is core and well supported. Supporting Evidence: PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection.
GO:0005737 cytoplasm	IDA PMID:27796300 PARP9 and PARP14 cross-regulate macrophage activation via ST...	ACCEPT	Summary: STAT1 is observed in the cytoplasm, consistent with its latent cytoplasmic pool prior to nuclear translocation. Reason: Cytoplasmic localization of latent STAT1 is core and well supported. Supporting Evidence: PMID:27796300 PARP9 and PARP14 cross-regulate macrophage activation via STAT1 ADP-ribosylation.
GO:0032991 protein-containing complex	IDA PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	KEEP AS NON CORE	Summary: STAT1 is part of protein-containing complexes (e.g. with PARP9-DTX3L) during interferon signaling. Reason: Generic protein-containing complex is uninformative relative to STAT1's specific transcription-factor complexes (GAF/ISGF3); retained as non-core. Supporting Evidence: PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection.
GO:0005737 cytoplasm	IDA PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Cri...	ACCEPT	Summary: STAT1 is observed in the cytoplasm, consistent with its latent cytoplasmic pool prior to nuclear translocation. Reason: Cytoplasmic localization of latent STAT1 is core and well supported. Supporting Evidence: PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Critical for Interferon Antiviral Activity.
GO:0005737 cytoplasm	IDA PMID:23386060 hCAF1/CNOT7 regulates interferon signalling by targeting STA...	ACCEPT	Summary: STAT1 is observed in the cytoplasm, consistent with its latent cytoplasmic pool prior to nuclear translocation. Reason: Cytoplasmic localization of latent STAT1 is core and well supported. Supporting Evidence: PMID:23386060 hCAF1/CNOT7 regulates interferon signalling by targeting STAT1.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-8987218	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-1112565	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-1112602	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-1169406	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-1433456	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-1470009	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-1678841	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-1888198	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-380782	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-6788571	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-6788582	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-6790041	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8950441	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8950453	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8950485	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8950518	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8950522	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8983835	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8983841	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8983845	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8983983	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8983996	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8984014	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8984021	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8984023	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8985929	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8986985	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8987007	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8987033	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8987080	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8987097	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8987150	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8987218	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8987230	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8987255	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8987266	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8987270	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-9006870	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-9006873	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-9670412	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-9670416	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-9672159	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-9672176	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-9729454	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-9835443	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-1112587	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-6788623	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-8950522	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-8950733	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-9021334	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0048471 perinuclear region of cytoplasm	IDA PMID:17275127 HCV NS5A inhibits interferon-alpha signaling through suppres...	KEEP AS NON CORE	Summary: STAT1 was detected in the perinuclear region in hepatocytes where HCV NS5A suppresses STAT1 phosphorylation; this perinuclear pool is a context-specific observation. Reason: Perinuclear localization is a context-specific observation (HCV-infected hepatocytes) rather than a core STAT1 compartment; retained as non-core. Supporting Evidence: PMID:17275127 Dec 14. HCV NS5A inhibits interferon-alpha signaling through suppression of STAT1 phosphorylation in hepatocyte-derived cell lines.
GO:0005737 cytoplasm	IDA PMID:17275127 HCV NS5A inhibits interferon-alpha signaling through suppres...	ACCEPT	Summary: STAT1 is observed in the cytoplasm, consistent with its latent cytoplasmic pool prior to nuclear translocation. Reason: Cytoplasmic localization of latent STAT1 is core and well supported. Supporting Evidence: PMID:17275127 Dec 14. HCV NS5A inhibits interferon-alpha signaling through suppression of STAT1 phosphorylation in hepatocyte-derived cell lines.
GO:0005737 cytoplasm	IDA PMID:15825084 Hepatitis C virus expression suppresses interferon signaling...	ACCEPT	Summary: STAT1 is observed in the cytoplasm, consistent with its latent cytoplasmic pool prior to nuclear translocation. Reason: Cytoplasmic localization of latent STAT1 is core and well supported. Supporting Evidence: PMID:15825084 Hepatitis C virus expression suppresses interferon signaling by degrading STAT1.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-1015699	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-1031713	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-1470012	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-873917	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-877281	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-909721	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-913529	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-9670426	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005654 nucleoplasm	TAS Reactome:R-HSA-997326	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the nucleoplasm. STAT1 is genuinely present in the nucleoplasm as an active dimer/ISGF3, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The nucleoplasm localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported nucleoplasm annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-1112727	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-1470010	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-1470012	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-873917	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-873921	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-873922	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-873927	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-909552	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-909718	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-909721	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-909722	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-909725	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-909726	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-913529	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-9670417	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-9670426	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-9710959	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-9710963	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-997309	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-1112538	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-1112587	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-1112604	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-6788622	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-6788623	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-6788628	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8950733	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005829 cytosol	TAS Reactome:R-HSA-8950782	ACCEPT	Summary: Bulk Reactome reaction-participant annotation placing STAT1 in the cytosol. STAT1 is genuinely a latent cytosolic factor before activation, so the localization is correct, but this is one of many redundant per-reaction Reactome TAS rows for the same compartment. Reason: The cytosol localization is consistent with STAT1 biology (latent cytosolic pool / nuclear active form), but this specific row is a bulk Reactome reaction-participant annotation that adds no functional specificity beyond the experimentally supported cytosol annotation already accepted; a redundant per-reaction Reactome participant record. Supporting Evidence: file:human/STAT1/STAT1-deep-research-falcon.md STAT1 exists in unphosphorylated/preassociated states at baseline and, upon tyrosine phosphorylation, forms dimers that translocate to the nucleus, where they bind regulatory DNA elements (GAS/ISRE) and regulate transcription.
GO:0005737 cytoplasm	IDA PMID:10692450 Thrombin inhibits tumor cell growth in association with up-r...	ACCEPT	Summary: STAT1 is observed in the cytoplasm, consistent with its latent cytoplasmic pool prior to nuclear translocation. Reason: Cytoplasmic localization of latent STAT1 is core and well supported. Supporting Evidence: PMID:10692450 Thrombin inhibits tumor cell growth in association with up-regulation of p21(waf/cip1) and caspases via a p53-independent, STAT-1-dependent pathway.
GO:0005737 cytoplasm	IDA PMID:10973496 Nucleocytoplasmic translocation of Stat1 is regulated by a l...	ACCEPT	Summary: STAT1 is observed in the cytoplasm, consistent with its latent cytoplasmic pool prior to nuclear translocation. Reason: Cytoplasmic localization of latent STAT1 is core and well supported. Supporting Evidence: PMID:10973496 Nucleocytoplasmic translocation of Stat1 is regulated by a leucine-rich export signal in the coiled-coil domain.
GO:0045087 innate immune response	IEA	NEW	Summary: Essential mediator of innate immune responses through interferon signaling pathway activation and antimicrobial gene expression Reason: STAT1 is a central component of the innate immune response, serving as the key transcriptional mediator for both type I (IFN-α/β) and type II (IFN-γ) interferon signaling pathways. Upon pathogen recognition, STAT1 is activated by JAK kinases and translocates to the nucleus to induce expression of interferon-stimulated genes (ISGs) that establish antiviral and antimicrobial states. STAT1 knockout studies demonstrate its non-redundant role in host defense against viruses, bacteria, and fungi, making it essential for innate immunity. Supporting Evidence: PMID:21903422 Mapping a dynamic innate immunity protein interaction network regulating type I interferon production. PMID:23386060 hCAF1/CNOT7 regulates interferon signalling by targeting STAT1.
GO:0005634 nucleus	IDA PMID:26479788 PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and v...	ACCEPT	Summary: STAT1 localizes to the nucleus upon activation, where it functions as a transcription factor; directly observed in this study. Reason: Nuclear localization is a core, repeatedly validated feature of activated STAT1.
GO:0005634 nucleus	IDA PMID:28753426 Methyltransferase SETD2-Mediated Methylation of STAT1 Is Cri...	ACCEPT	Summary: STAT1 localizes to the nucleus upon activation, where it functions as a transcription factor; directly observed in this study. Reason: Nuclear localization is a core, repeatedly validated feature of activated STAT1.

Gene Description

Existing Annotations Review

Core Functions

Master transcriptional regulator of interferon responses and cytokine signaling

SH2 domain-mediated homodimerization and heterodimerization essential for transcriptional activation

Sequence-specific DNA binding to interferon-responsive regulatory elements (GAS and ISRE)

References

Suggested Questions for Experts

Suggested Experiments

Deep Research

Falcon

Deep Research Report: STAT1 (human)

📚 Additional Documentation

Notes

Pn Notes

📄 View Raw YAML

🔗 Related Resources