IFI16
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 2OQ0, 3B6Y, 3RLN, 3RLO, 3RNU, 4QGU
Identifiers
Aliases	IFI16, IFNGIP1, PYHIN2, interferon gamma inducible protein 16
External IDs	OMIM: 147586 MGI: 3695276 HomoloGene: 115929 GeneCards: IFI16
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1q23.1 Start 158,999,968 bp[1] End 159,055,155 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 H3 Start 173,393,849 bp[2] End 173,426,840 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in germinal epithelium pericardium palpebral conjunctiva Achilles tendon lymph node superficial temporal artery vena cava spleen human penis gums Top expressed in subcutaneous adipose tissue spleen thymus bone marrow white adipose tissue blood right lung body of femur triceps brachii muscle right lung lobe More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA-binding transcription repressor activity, RNA polymerase II-specific identical protein binding double-stranded DNA binding RNA polymerase II cis-regulatory region sequence-specific DNA binding DNA binding transcription factor binding protein binding RNA binding Cellular component nucleolus nucleoplasm nucleus membrane nuclear speck cytoplasm cytosol Biological process positive regulation of type I interferon production positive regulation of cytokine production intrinsic apoptotic signaling pathway by p53 class mediator cellular response to glucose starvation transcription, DNA-templated negative regulation of viral genome replication negative regulation of innate immune response monocyte differentiation cellular response to ionizing radiation negative regulation of DNA binding regulation of autophagy myeloid cell differentiation intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator apoptotic process hemopoiesis activation of cysteine-type endopeptidase activity autophagy negative regulation of cysteine-type endopeptidase activity negative regulation of transcription by RNA polymerase II positive regulation of interleukin-1 beta production regulation of transcription, DNA-templated regulation of gene expression, epigenetic cell population proliferation positive regulation of transcription by RNA polymerase II activation of innate immune response immune system process inflammatory response negative regulation of transcription, DNA-templated innate immune response defense response to virus cellular response to interferon-beta Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3428 623121 Ensembl ENSG00000163565 ENSMUSG00000073491 UniProt Q16666 n/a RefSeq (mRNA) NM_001206567 NM_005531 NM_001364867 NM_001376587 NM_001376588 NM_001376589 NM_001376591 NM_001376592 NM_001033384 NM_001177349 NM_001177350 NM_001368798 NM_001368799 RefSeq (protein) NP_001193496 NP_005522 NP_001351796 NP_001363516 NP_001363517 NP_001363518 NP_001363520 NP_001363521 n/a Location (UCSC) Chr 1: 159 – 159.06 Mb Chr 1: 173.39 – 173.43 Mb PubMed search [3] [4]
Wikidata
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Gamma-interferon-inducible protein Ifi-16 (Ifi-16) also known as interferon-inducible myeloid differentiation transcriptional activator is a protein that in humans is encoded by the IFI16 gene.^[5][6][7]

Function

This gene encodes a member of the HIN-200 (hematopoietic interferon-inducible nuclear antigens with 200 amino acid repeats) family of cytokines. The encoded protein contains domains involved in DNA binding, transcriptional regulation, and protein-protein interactions. The protein localizes to the nucleoplasm and nucleoli, and interacts with p53,^[8] retinoblastoma-1 and BRCA1.^[9] It modulates p53 function, and inhibits cell growth in the Ras/Raf signaling pathway.^[7] IFI16 has been shown to play a role in the sensing of intracellular DNA^[10] - a hallmark of virally infected cells - and has also been linked to the death of HIV-infected helper CD4 T cells by pyroptosis, a highly inflammatory form of programmed cell death.^[11][12] Recently, it has been shown how IFI16, once extracellularly released, can induce inflammation upon TLR4 binding, acting as a DAMP.^[13]