Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
Combined Automated Annotation using Multiple IEA Methods
Interferons as gene activators. Indications for repeated gene duplication during the evolution of a cluster of interferon-activatable genes on murine chromosome 1.
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The Ifi204 gene lies within a cluster of interferon-activatable genes on murine chromosome 1 that arose by repeated gene duplication. The 202 and 204 gene products share conserved 200-amino acid segments and similar regulatory regions with interferon-responsive enhancers.
"sequences of three genes from the cluster (the 201, 202, and 204 genes) are very similar in a segment extending from at least 550 nucleotides upstream of the 3' end of the transcription initiation region to beyond the first exon intron border (96% similarity between the 202 and 204 genes and 89% similarity between the 201 and 204 genes)"
The interferon-inducible nucleolar p204 protein binds the ribosomal RNA-specific UBF1 transcription factor and inhibits ribosomal RNA transcription.
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p204 is primarily nucleolar and inhibits rRNA transcription by binding UBF1. Interferon treatment induces p204 and retards cell proliferation via inhibition of rRNA transcription.
"p204, a member of the interferon-inducible p200 family of murine proteins, is primarily nucleolar...This induction resulted in retardation of cell proliferation and inhibition of rRNA transcription in vivo...A direct interaction between p204 and UBF1 was revealed in vitro in pull-down assays, and in vivo by co-immunoprecipitation from cell extracts"
The MyoD-inducible p204 protein overcomes the inhibition of myoblast differentiation by Id proteins.
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p204 is required for C2C12 myoblast differentiation. It binds Id1, Id2, and Id3, overcomes their inhibition of MyoD/E47-dependent transcription, and promotes their ubiquitination and degradation. p204 is phosphorylated and translocated from nucleus to cytoplasm during myoblast fusion.
"p204 is required for the differentiation of C2C12 myoblasts...it enables the differentiation, at least in part, by overcoming the inhibition of the activities of the MyoD and E47 proteins by the Id proteins: Id1, Id2, and Id3...p204 bound to the Id proteins in vitro and in vivo"
The mouse interferon-inducible gene Ifi204 product interacts with the Tpr protein, a component of the nuclear pore complex.
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p204 interacts with the Tpr protein (nucleoporin) in yeast two-hybrid and coimmunoprecipitation experiments. Tpr mediates p204 translocation from cytoplasm to nucleus following IFN treatment. p204 localizes to nucleolus and nuclear inclusion bodies.
"We have used yeast two-hybrid screening to isolate cDNA-encoding proteins interacting with the protein encoded by the interferon (IFN)-inducible gene Ifi204...in vivo interaction was demonstrated by coimmunoprecipitation experiments...it appears to mediate p204 translocation from the cytoplasmic to the nuclear compartment following IFN treatment"
A member of the Pyrin family, IFI16, is a novel BRCA1-associated protein involved in the p53-mediated apoptosis pathway.
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Human IFI16 interacts with BRCA1 via its Pyrin domain and participates in p53-mediated apoptosis. IFI16 localizes to nucleoplasm and nucleoli. This paper is about human IFI16, and ISO annotations to mouse Ifi204 are based on orthology transfer.
"IFI16 contains the Pyrin/PAAD/DAPIN domain, commonly found in cell death-associated proteins. BRCA1 (aa 502-802) interacted with the IFI16 Pyrin domain (aa 1-130). We found that IFI16 was localized in the nucleoplasm and nucleoli"
The interferon-inducible p204 protein acts as a transcriptional coactivator of Cbfa1 and enhances osteoblast differentiation.
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p204 acts as a transcriptional coactivator of Cbfa1/Runx2 during osteoblast differentiation. It is expressed in embryonic osteoblasts and hypertrophic chondrocytes. Both HIN domains bind Runx2. Overexpression enhances BMP-2-induced osteoblast differentiation with elevated alkaline phosphatase and osteocalcin.
"p204 is expressed in embryonic osteoblasts and hypertrophic chondrocytes in the growth plate as well as in the calvaria osteoblasts of neonatal mice... Overexpression of p204 enhances the BMP-2-induced osteoblast differentiation in vitro, as revealed by elevated alkaline phosphatase activity and osteocalcin production. p204 acts as a cofactor of Cbfa1"
The interferon-inducible gene, Ifi204, is transcriptionally activated in response to M-CSF, and its expression favors macrophage differentiation in myeloid progenitor cells.
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Ifi204 is activated by M-CSF and promotes macrophage differentiation. Enforced expression decreases proliferation and favors macrophage differentiation of FD-Fms cells.
"Ifi204 was transcriptionally activated in response to M-CSF...enforced expression of Ifi204 strongly decreased IL-3- and M-CSF-dependent proliferation and conversely, favored macrophage differentiation of FD-Fms cells in response to M-CSF"
p204 is required for the differentiation of P19 murine embryonal carcinoma cells to beating cardiac myocytes: its expression is activated by the cardiac Gata4, Nkx2.5, and Tbx5 proteins.
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p204 is required for cardiac myocyte differentiation. Expression is synergistically activated by cardiac transcription factors Gata4, Nkx2.5, and Tbx5. Contains a nuclear export signal required for cytoplasmic translocation during differentiation.
"p204 was also required for the differentiation of cultured P19 murine embryonal carcinoma stem cells to beating cardiac myocytes...p204 expression was synergistically transactivated by the cardiac Gata4, Nkx2.5, and Tbx5 transcription factors...p204 contains a nuclear export signal and was partially translocated to the cytoplasm during the differentiation"
An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome.
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This paper primarily identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome. AIM2 binds dsDNA via its HIN domain and recruits ASC. The paper is not primarily about Ifi204/p204. ISO annotations to Ifi204 from this reference are based on orthology transfer from human IFI16.
"AIM2 showed specificity for double-stranded DNA. It also recruited the inflammasome adaptor ASC and localized to ASC 'speckles'...AIM2 was sufficient for inflammasome activation"
Developmental profiling of spiral ganglion neurons reveals insights into auditory circuit assembly.
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Transcriptomic profiling study of spiral ganglion neurons. Ifi204 is one of many genes with altered expression during auditory development. The study does not functionally characterize Ifi204 in inner ear development.
"We catalogued gene expression in mouse SG neurons from embryonic day 12, when SG neurons first extend projections, up until postnatal day 15, after the onset of hearing...exhibit a dramatic increase in immune gene expression"
The mammalian PYHIN gene family - phylogeny, evolution and expression.
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The mouse PYHIN family has 14 members (vs 4 in human), all arising by lineage-specific duplication on chromosome 1. Only AIM2 has clear orthology across species. The other mouse genes, including Ifi204, arose by duplication and rearrangement within the mouse lineage.
"Placental mammals show variable family expansions, from one gene in cow to four in human and 14 in mouse...The other 13 mouse genes have arisen by duplication and rearrangement within the lineage"
Impact of lactobacilli on orally acquired listeriosis.
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Ifi204 is one of many interferon-stimulated genes whose expression is affected by lactobacilli treatment during Listeria infection. The paper does not functionally characterize Ifi204 in bacterial response.
"A whole genome intestinal transcriptomic analysis revealed that each Lactobacillus changes expression of a specific subset of genes during infection, with IFN-stimulated genes (ISGs) being the most affected by both lactobacilli"
cGAS and Ifi204 cooperate to produce type I IFNs in response to Francisella infection.
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cGAS and Ifi204 are both required for the STING-dependent type I IFN response to Francisella novicida in murine macrophages. CRISPR knockouts of cGAS, Ifi204, and Sting in RAW264.7 cells demonstrate cooperation between cGAS and Ifi204 in dsDNA sensing.
"the cytosolic DNA sensors, cyclic GMP-AMP synthase (cGAS) and Ifi204, are both required for the STING-dependent type I IFN response to F. novicida infection in both primary and immortalized murine macrophages"
The Central Role of IFI204 in IFN-β Release and Autophagy Activation during Mycobacterium bovis Infection.
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IFI204 is acetylated upon M. bovis infection, translocates from nucleus to cytoplasm, and recruits STING to activate TBK1-IRF3 signaling and IFN-beta production. Knockdown blocks IFN-beta production and autophagy marker LC3 expression.
"Knockdown of the IFI204 in immortalized and primary murine macrophages blocked IFN-beta production and autophagy marker LC3 expression"
DNA Sensor IFI204 Contributes to Host Defense Against Staphylococcus aureus Infection in Mice.
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IFI204-deficient mice show increased susceptibility to S. aureus pulmonary infection with decreased inflammatory cytokines, impaired STING-IRF3 and NF-kB pathways, and defective extracellular trap formation in macrophages and neutrophils.
"IFI204 deficiency results in decreased survival, increased bacterial loads, severe organs damage, and decreased recruitment of neutrophils and macrophages"
Structural mechanism of DNA recognition by the p204 HIN domain.
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Crystal structures of p204 HINa, HINb, and HINab:dsDNA complex reveal non-sequence-specific dsDNA binding via alpha-2 helices and linker region. Both HINa and HINb are required for dsDNA recognition. HINa dimerization interface is involved in DNA binding.
"p204 HINab binds dsDNA mainly through alpha2 helix of HINa and HINb, and the linker between them...Both HINa and HINb are vital for HINab recognition of dsDNA, as confirmed by fluorescence polarization assays"
Falcon deep research report on mouse Ifi204 function