Gene Ontology annotation through association of InterPro records with GO terms.
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara.
Gene Ontology annotation of human sequence-specific DNA binding transcription factors (DbTFs) based on the TFClass database
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods.
Stat1 as a component of tumor necrosis factor alpha receptor 1-TRADD signaling complex to inhibit NF-kappaB activation.
Nucleocytoplasmic translocation of Stat1 is regulated by a leucine-rich export signal in the coiled-coil domain.
Vaccinia virus blocks gamma interferon signal transduction: viral VH1 phosphatase reverses Stat1 activation.
Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphorylation in response to IFN-gamma.
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.
STAT-1 and c-Fos interaction in nitric oxide synthase-2 gene activation.
The cell death regulator GRIM-19 is an inhibitor of signal transducer and activator of transcription 3.
Structural bases of unphosphorylated STAT1 association and receptor binding.
Hepatitis C virus expression suppresses interferon signaling by degrading STAT1.
Towards a proteome-scale map of the human protein-protein interaction network.
The conserved Leu-724 residue is required for both serine phosphorylation and co-activator recruitment for Stat1-mediated transcription activation in response to interferon-gamma.
A quantitative protein interaction network for the ErbB receptors using protein microarrays.
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.
Tid1 isoforms are mitochondrial DnaJ-like chaperones with unique carboxyl termini that determine cytosolic fate.
Signal transducer and activator of transcription 1 activation in endothelial cells is a negative regulator of angiogenesis.
Hepatitis C virus core protein blocks interferon signaling by interaction with the STAT1 SH2 domain.
HCV NS5A inhibits interferon-alpha signaling through suppression of STAT1 phosphorylation in hepatocyte-derived cell lines.
Severe acute respiratory syndrome coronavirus ORF6 antagonizes STAT1 function by sequestering nuclear import factors on the rough endoplasmic reticulum/Golgi membrane.
Acetylation-dependent signal transduction for type I interferon receptor.
Regulation of XAF1 expression in human colon cancer cell by interferon beta: activation by the transcription regulator STAT1.
A comprehensive resource of interacting protein regions for refining human transcription factor networks.
Activated networking of platelet activating factor receptor and FAK/STAT1 induces malignant potential in BRCA1-mutant at-risk ovarian epithelium.
Molecular mechanisms underlying the inhibition of IFN-γ-induced, STAT1-mediated gene transcription in human macrophages by simvastatin and agonists of PPARs and LXRs.
Mapping a dynamic innate immunity protein interaction network regulating type I interferon production.
Toward an understanding of the protein interaction network of the human liver.
A novel disrupter of telomere silencing 1-like (DOT1L) interaction is required for signal transducer and activator of transcription 1 (STAT1)-activated gene expression.
hCAF1/CNOT7 regulates interferon signalling by targeting STAT1.
IFNβ-dependent increases in STAT1, STAT2, and IRF9 mediate resistance to viruses and DNA damage.
Hepatic RIG-I predicts survival and interferon-α therapeutic response in hepatocellular carcinoma.
The mammalian-membrane two-hybrid assay (MaMTH) for probing membrane-protein interactions in human cells.
Using an in situ proximity ligation assay to systematically profile endogenous protein-protein interactions in a pathway network.
A proteome-scale map of the human interactome network.
E-cadherin interactome complexity and robustness resolved by quantitative proteomics.
Proteomic analyses reveal distinct chromatin-associated and soluble transcription factor complexes.
PARP9-DTX3L ubiquitin ligase targets host histone H2BJ and viral 3C protease to enhance interferon signaling and control viral infection.
VP8, the Major Tegument Protein of Bovine Herpesvirus 1, Interacts with Cellular STAT1 and Inhibits Interferon Beta Signaling.
PIPINO: A Software Package to Facilitate the Identification of Protein-Protein Interactions from Affinity Purification Mass Spectrometry Data.
Methyltransferase SETD2-Mediated Methylation of STAT1 Is Critical for Interferon Antiviral Activity.
Extensive rewiring of the EGFR network in colorectal cancer cells expressing transforming levels of KRAS(G13D).
Noncanonical STAT1 phosphorylation expands its transcriptional activity into promoting LPS-induced IL-6 and IL-12p40 production.
SARS-CoV-2 N protein antagonizes type I interferon signaling by suppressing phosphorylation and nuclear translocation of STAT1 and STAT2.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) Membrane (M) and Spike (S) Proteins Antagonize Host Type I Interferon Response.
Human transcription factor protein interaction networks.
Ligand-induced IFN gamma receptor tyrosine phosphorylation couples the receptor to its signal transduction system (p91).
The SH2 domains of Stat1 and Stat2 mediate multiple interactions in the transduction of IFN-alpha signals.
Differential activation of acute phase response factor/STAT3 and STAT1 via the cytoplasmic domain of the interleukin 6 signal transducer gp130. I. Definition of a novel phosphotyrosine motif mediating STAT1 activation.
Functional subdomains of STAT2 required for preassociation with the alpha interferon receptor and for signaling.
Heteromerization of the gammac chain with the interleukin-9 receptor alpha subunit leads to STAT activation and prevention of apoptosis.
Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA.
Could not retrieve title - publication not available
Direct suppression of Stat1 function during adenoviral infection.
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity.
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt.
Gene Ontology annotation based on curation of immunofluorescence data
Thrombin inhibits tumor cell growth in association with up-regulation of p21(waf/cip1) and caspases via a p53-independent, STAT-1-dependent pathway.
The role of STATs in apoptosis.
Protein kinase Cdelta regulates apoptosis via activation of STAT1.
STAT1 is required for redifferentiation during Madin-Darby canine kidney tubulogenesis.
STAT heterodimers in immunity: A mixed message or a unique signal?
Unanchored K48-linked polyubiquitin synthesized by the E3-ubiquitin ligase TRIM6 stimulates the interferon-IKKε kinase-mediated antiviral response.
Functional Selectivity in Cytokine Signaling Revealed Through a Pathogenic EPO Mutation.
IL-7-dependent STAT1 activation limits homeostatic CD4+ T cell expansion.
IL-27 signaling activates skin cells to induce innate antiviral proteins and protects against Zika virus infection.
PARP9 and PARP14 cross-regulate macrophage activation via STAT1 ADP-ribosylation.
ISGF3 binds the ISRE promoter elements in IFN-stimulated genes
GAF binds the GAS promoter elements in the IFNG-regulated genes
Phosphorylated STAT1, STAT3 form dimers
Tyrosine phosphorylated IL6ST binds STAT1,STAT3
STAT1 and STAT3 dimers translocate to the nucleus
Tyrosine phosphorylation of STAT1, STAT3 by IL6 receptor
Phosphorylated STATs are released
Serine phosphorylation of STATs
ISGylation of host proteins
Disassociation and translocation of STATs to the nucleus
Regulation of protein ISGylation by ISG15 deconjugating enzyme USP18
FGFR1OP-FGFR1 phosphorylates STAT1 and STAT3
STAT binds to the active receptor
STAT1,STAT3,STAT6 bind IL13:IL13R type II
STAT1,STAT3,STAT6 phosphorylation
p-Y-STATs translocate to nucleus
Expression of STAT3-upregulated cytosolic proteins
Translocation of STAT1 dimer to nucleus
Binding of STAT1 to p-IFNGR1
Phosphorylation of STAT1 by JAK kinases
Release of STAT1 dimer from active receptor unit
PIAS1 binds p-STAT1 dimer
p-Y701-STAT1 and p-Y705-STAT3 dissociate from IL27:IL27 receptor
JAK1/JAK2 bound to IL12RB2:IL6ST receptor phosphorylates STAT1 and STAT4
STAT3 and STAT1 are phosphorylated by JAKs after IL27:IL27R interaction
STAT1, STAT3 bind p-Y611-IL27RA from Interleukin-27:Interleukin-27 receptor complex
p-STAT1:p-STAT4 translocates to the nucleus
p-Y701-STAT1:p-Y705-STAT3 translocates to the nucleus
JAK1/JAK2/TYK2 bound to IL6ST:IL6ST phosphorylate STAT1
STAT1 associates with IL6ST:IL6ST
p-STAT1 dissociates from IL6ST:IL6ST
p-STAT1 and p-STAT4 dissociate from IL12RB2:IL6ST receptor
STAT1 and STAT4 associate with IL12RB2:IL6ST receptor
JAK1,JAK2 bound to IL27RA:IL12RB2 receptor phosphorylate STAT1,STAT3
STAT1,STAT3 associate with IL27RA:IL12RB2 receptor
p-STAT1, p-STAT3 dissociate from IL27RA:IL12RB2 receptor
p-Y701-STAT1, p-Y705-STAT3, p-Y649-STAT5 dissociates from IL9:p-Y407-IL9R:JAK1:IL2RG:p-904,939-JAK3:p-Y705-STAT3
IL9:p-Y407-IL9R:JAK1:IL2RG:p-904,939-JAK3 binds STAT1, STAT3, STAT5A or STAT5B
p-Y701-STAT1 binds p-Y705-STAT3
p-Y701-STAT1:p-Y705-STAT3 translocates from the cytosol to the nucleus
p-Y701-STAT1 dimer translocates from the cytosol to the nucleus
IL9:p-Y116-IL9R:JAK1:IL2RG:p-904,939-JAK3:STAT3 phosphorylates STAT1, STAT3 or STAT5
IFNL1:p-Y343,Y517-IFNLR1:p-JAK1:IL10RB:p-TYK2:STAT1 phosphorylates STAT1, STAT2, STAT3, STAT4 and STAT5
p-STAT1, p-Y-STAT2, p-STAT3, p-STAT4, p-STAT5 dissociates from IFNL1:p-Y343,Y517-IFNLR1:p-JAK1:IL10RB:p-TYK2:p-STAT1,p-STAT2,p-STAT3,p-STAT4,p-STAT5
IL26:IL10RB:p-TYK2:IL20RA:p-JAK1 binds STAT1, STAT3
IL24:p-IL20RA:p-JAK1:IL20RB binds STAT1,STAT3
IL24:IL20RA:p-JAK1:IL20RB:STAT1,STAT3 phosphorylates STAT1 or STAT3
p-STAT1 dimer translocates from the cytosol to the nucleoplasm
p-STAT1 and p-STAT3 dissociates from IL26:IL10RB:p-TYK2:IL20RA:p-JAK1
IL26:IL10RB:p-TYK2:IL20RA:p-JAK1:STAT1,STAT3 phosphorylates STAT1,STAT3
IFNL1:p-Y434,Y517-IFNLR1:p-JAK1:IL10RB:p-TYK2 binds STAT1, STAT2, STAT3, STAT4, STAT5
p-STAT1,p-STAT3 dissociate from IL24:IL20RA:p-Y1022,Y1023-JAK1:IL20RB:p-STAT1, p-STAT3
IL21 receptor STAT phosphorylation
IL21 receptor STAT binding
STAT1 binds HEY1 gene promoter
Phosphorylation of STAT1 at Ser727
Formation of p-STAT1 homodimer
Translocation of ISGF3 complex to nucleus
Release of p-STAT2:p-STAT1 dimer
Interaction of IRF9 with p-STAT2:p-STAT1
Translocation of p-STAT1:p-STAT1 dimer to nucleus
Phosphorylation of STATs downstream of KIT mutants
Recruitment of STATs by KIT mutants
Dimerization of STATs downstream of KIT mutants
Disassociation and translocation of STATs to the nucleus downstream of KIT mutants
STAT binds to p-11Y PDGFRA extracellular domain dimers
STAT binds to the mutant PDGFRA receptor
p-STAT1 dimer binds KPNA1
p-STAT1dimer:KPNA1 binds KPNB1
SARS-CoV-2 N protein binds STAT1, STAT2
TYK2-dependent STAT1 and STAT3 phosphorylation
Phosphorylation of STAT1 on tyrosine-701 is enhanced by p-S172-IKBKE
p-Y701-STAT1 binds the NLRP3 gene
Dephosphorylation of STAT1 by SHP2
Dephosphorylation of p-STAT1 dimer by nuclear isoform of TCPTP
Falcon deep research report on STAT1
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STAT1 is the canonical JAK-STAT pathway transcription factor activated downstream of IFN receptors; phosphorylation on Tyr701 drives dimerization, nuclear translocation, and transcription of IFN-stimulated genes.
"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."
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STAT1 contains canonical STAT-family domains (N-terminal, coiled-coil, DNA-binding, linker, SH2, transactivation), with SH2 mediating receptor docking and dimerization via phosphotyrosine interactions.
"Recent authoritative reviews summarize canonical STAT-family domain organization present in STAT1: **N-terminal domain, coiled-coil domain, DNA-binding domain, linker, SH2 domain, and a C-terminal transactivation domain (TAD)**; these domains support receptor docking (via SH2), dimerization (via phosphotyrosine–SH2 interactions), DNA binding, and transcriptional activation."
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Tyr701 phosphorylation between SH2 and TAD enables STAT1 dimerization and nuclear translocation; Ser727 phosphorylation in the C-terminus modulates transcriptional activity.
"**Tyrosine phosphorylation**: IFN-receptor-associated JAKs phosphorylate STAT1 on a key tyrosine residue (**Tyr701**, located between SH2 and TAD), altering dimerization properties and enabling nuclear translocation and transcriptional activity."
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STAT1 homodimers form GAF and bind GAS DNA elements (predominantly IFN-gamma response); STAT1-STAT2-IRF9 forms ISGF3 and binds ISRE elements (type I/III IFN response).
"* **STAT1 homodimers** (historically **GAF**, gamma-interferon activation factor) bind **GAS** (gamma-activated sequence) DNA elements.
* **STAT1–STAT2 heterodimers** plus **IRF9** form **ISGF3**, which binds **ISRE**
(interferon-stimulated response element) DNA elements."
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STAT1's primary biochemical function is sequence-specific transcriptional regulation as part of IFN-activated transcription factor complexes (GAF and ISGF3) controlling ISG expression.
"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)."
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STAT1 is latent and cytoplasmic at baseline; upon tyrosine phosphorylation it dimerizes and translocates to the nucleus to bind GAS/ISRE DNA elements and regulate transcription.
"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."
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Nuclear import depends on importin alpha/KPNA1; the RSV NS1 protein can block STAT1 nuclear translocation by interfering with KPNA1 binding even when phosphorylation is intact, suppressing ISRE/GAS-driven antiviral gene induction.
"A 2024 mechanistic virology study illustrates that nuclear entry is a critical control point: respiratory syncytial virus (RSV) **NS1** can bind STAT1 and **reduce STAT1 nuclear translocation** (and reduce interaction with nuclear transport adaptor **KPNA1**) even when IFNα-induced STAT1 phosphorylation is enhanced, thereby suppressing ISRE/GAS promoter activity and antiviral gene induction."
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Cross-cell-type analyses identify 975 ISGs across 11 cell types with a core set of 166 robustly induced by type I IFNs; STAT1 homodimers predominate after IFN-gamma, STAT1-STAT2 heterodimers after type I/III IFN.
"A 2024 JBC review synthesizes a cross-cell-type analysis that identified **975 ISGs across 11 cell types**, including a **core set of 166 ISGs** robustly induced by type I IFNs. This review also emphasizes that tyrosine-phosphorylated STAT1 can form homodimers or STAT1–STAT2 heterodimers, and that the relative abundance depends on IFN type (more persistent STAT1 homodimers after IFNγ; STAT1–STAT2 heterodimers predominate after type I/III IFNs)."
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Time-resolved ChIP/RNA-seq shows GAS-driven genes respond early while ISRE-driven genes predominate later, with ISRE+GAS composite promoters serving as switch-like regulatory elements integrating IFNalpha and IFNgamma programs.
"The study reported **108 IFNα-specific** and **75 IFNγ-specific** integrated genes, and found that **GAS genes tend to be early responders** while **ISRE genes predominate later**, with **ISRE+GAS composite sites** acting as switch-like regulatory elements enabling mechanistic overlap between IFNα and IFNγ programs."
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STAT1 GOF is the most common STAT1 defect (>100 variants in >400 patients) and is associated with chronic mucocutaneous candidiasis in over 60% of patients; AR complete STAT1 deficiency abolishes type I/II/III IFN and IL-27 signaling and causes severe early-life infections.
"A 2024 clinical-genetics review reports that **STAT1 GOF is the most common STAT1 defect**, with **>100 different variants** described in **>400 patients**, and **chronic mucocutaneous candidiasis (CMC)** occurring in **>60%** of individuals with STAT1 GOF."