{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O14862","secondaryAccessions":["A8K7M7","Q5T3V9","Q96FG9"],"uniProtkbId":"AIM2_HUMAN","entryAudit":{"firstPublicDate":"1999-07-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1998-01-01","entryVersion":180,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9242382"}],"value":"Interferon-inducible protein AIM2"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9242382"}],"value":"Absent in melanoma 2"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9242382"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:357"}],"value":"AIM2"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q91VJ1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17726700"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158675"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158676"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158679"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20566831"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23530044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26197926"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26583071"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29440442"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33980849"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37364111"}],"value":"Sensor component of the AIM2 inflammasome, which mediates inflammasome activation in response to the presence of double-stranded DNA (dsDNA) in the cytosol, leading to subsequent pyroptosis (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831, PubMed:23530044, PubMed:26197926, PubMed:26583071, PubMed:29440442, PubMed:33980849, PubMed:37364111). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831, PubMed:26197926, PubMed:29440442, PubMed:33980849). Acts as a recognition receptor (PRR): specifically recognizes and binds dsDNA in the cytosol, and mediates the formation of the inflammasome polymeric complex composed of AIM2, CASP1 and PYCARD/ASC (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831, PubMed:26197926, PubMed:29440442, PubMed:33980849). Recruitment of pro-caspase-1 (proCASP1) to the AIM2 inflammasome promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), promoting cytokine secretion (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831). In some cells, CASP1 activation mediates cleavage and activation of GSDMD, triggering pyroptosis without promoting cytokine secretion (PubMed:19158675, PubMed:19158676). Detects cytosolic dsDNA of viral and bacterial origin in a non-sequence-specific manner (PubMed:17726700, PubMed:19158675, PubMed:19158676, PubMed:19158679, PubMed:20566831, PubMed:26197926, PubMed:26583071, PubMed:29440442, PubMed:33980849). Involved in the DNA damage response caused by acute ionizing radiation by mediating pyroptosis of intestinal epithelial cells and bone marrow cells in response to double-strand DNA breaks (By similarity). Mechanistically, AIM2 senses DNA damage in the nucleus to mediate inflammasome assembly and inflammatory cell death (By similarity). Also acts as a regulator of neurodevelopment via its role in the DNA damage response: acts by promoting neural cell death in response to DNA damage in the developing brain, thereby purging genetically compromised cells of the central nervous system (By similarity). Pyroptosis mediated by the AIM2 inflammasome in response to DNA damage is dependent on GSDMD without involving IL1B and IL18 cytokine secretion (By similarity). Also acts as a mediator of pyroptosis, necroptosis and apoptosis (PANoptosis), an integral part of host defense against pathogens, in response to bacterial infection (By similarity). Can also trigger PYCARD/ASC-dependent, caspase-1-independent cell death that involves caspase-8 (CASP8) (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q91VJ1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16432157"}],"value":"Also acts as a tumor suppressor independently of its role in inflammatory response (PubMed:16432157). Able to suppress overt cell proliferation in enterocytes: restricts stem cell proliferation in the intestinal mucosa in an inflammasome-independent manner, contributing to a decrease in the likelihood of colorectal cancer development (By similarity). AIM2 suppresses cell proliferation by inhibiting phosphorylation of AKT1 at 'Ser-473', preventing AKT1 activation and AKT-mTOR signaling pathway (By similarity). Inhibits AKT1 phosphorylation both by inhibiting the activity of PRKDC/DNA-PK kinase and promoting dephosphorylation by PP2A phosphatase (By similarity). Also acts as a key regulator of regulatory T-cells (Treg) homeostasis by promoting their stability: acts by preventing AKT1 activation (By similarity). Its role in Treg homeostasis is important to restain autoimmune diseases (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q91VJ1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16432157"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158675"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158676"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22483801"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26197926"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27498865"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29440442"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30104205"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33980849"}],"value":"Inactive in absence of double-stranded DNA (dsDNA) (PubMed:22483801, PubMed:26197926). Homooligomerizes upon binding to dsDNA, dsDNA serving as an oligomerization platform (PubMed:26197926, PubMed:33980849). AIM2 requires large dsDNA to generate a structural template that couples dsDNA ligand-binding and homooligomerization (PubMed:26197926). Homooligomerization is followed by recruitment of PYCARD/ASC to initiate speck formation (nucleation) (PubMed:22483801, PubMed:26197926, PubMed:29440442, PubMed:33980849). AIM2 and PYCARD/ASC homooligomer filaments assemble bidirectionally and the recognition between AIM2 and PYCARD/ASC oligomers occurs in a head-to-tail manner (PubMed:33980849). Clustered PYCARD/ASC nucleates the formation of CASP1 filaments through the interaction of their respective CARD domains, acting as a platform for CASP1 polymerization and activation (PubMed:19158675, PubMed:19158676). Active CASP1 then specifically processes protein precursors, such as gasdermin-D (GSDMD), IL1B and IL18, leading to the release of mature cytokines in the extracellular milieu or pyroptosis, depending on cell type (PubMed:16432157, PubMed:19158675, PubMed:19158676). AIM2 can be activated in response to events that cause genomic DNA (HIV protease inhibitor nelfinavir) or mitochondrial DNA release in the cytoplasm (such as Perfluoroalkyl substance pollutants or cholesterol overload) (By similarity). Activation of the AIM2 inflammasome is inhibited by isoform IFI16-beta of IFI16, which prevents the interaction between AIM2 and PYCARD/ASC (PubMed:30104205). Activation of the AIM2 inflammasome is inhibited by TRIM11, which promotes autophagy-dependent degradation of AIM2 (PubMed:27498865)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q91VJ1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15582594"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158675"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158676"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158679"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22046441"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22483801"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22801494"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22869553"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23530044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24406744"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24531343"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26197926"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26583071"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27498865"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29440442"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30104205"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33980849"}],"value":"Self-associates; forms homooligomers in response to cytosolic double-stranded DNA (dsDNA) and the dsDNA seems to serve as oligomerization platform (PubMed:15582594, PubMed:19158676, PubMed:24406744, PubMed:26197926, PubMed:26583071, PubMed:29440442, PubMed:33980849). Component of AIM2 inflammasome, which consists of a signal sensor component (AIM2), an adapter (PYCARD/ASC), which recruits an effector pro-inflammatory caspase (CASP1) (PubMed:22483801, PubMed:22869553, PubMed:33980849). Interacts (via pyrin domain) with PYCARD/ASC (via pyrin domain); interaction is direct (PubMed:19158675, PubMed:19158679, PubMed:23530044, PubMed:29440442, PubMed:33980849). Component of the AIM2 PANoptosome complex, a multiprotein complex that drives inflammatory cell death (PANoptosis) (By similarity). Interacts with PYDC5; disrupts assembly of the AIM2 inflammasome complex (PubMed:24531343). Interacts with EIF2AK2/PKR (PubMed:22801494). Interacts with MAPRE1 (PubMed:22869553). Interacts with IFI16 (PubMed:22046441). Interacts with isoform IFI16-beta of IFI16; preventing the interaction between AIM2 and PYCARD/ASC (PubMed:30104205). Interacts with RACK1; promoting association with PP2A phosphatase and dephosphorylation of AKT1 (By similarity). Interacts with TRIM11; promoting AIM2 recruitment to autophagosomes and autophagy-dependent degradation (PubMed:27498865)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"37364111"}],"value":"(Microbial infection) Interacts with human herpesvirus 8 protein SOX/ORF37; this interaction inhibits AIM2 polymerization and subsequent inflammasome activation"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"O14862","intActId":"EBI-6253193"},"interactantTwo":{"uniProtKBAccession":"O14862","geneName":"AIM2","intActId":"EBI-6253193"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O14862","intActId":"EBI-6253193"},"interactantTwo":{"uniProtKBAccession":"Q9ULZ3","geneName":"PYCARD","intActId":"EBI-751215"},"numberOfExperiments":13,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q91VJ1"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158675"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158676"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158679"}],"value":"Activated inflammasomes can aggregate in the cytosol as speck-like particles (PubMed:19158675, PubMed:19158676, PubMed:19158679). Activated inflammasomes can also aggregate in the nucleus in response to DNA damage: AIM2 is recruited to double-strand DNA breaks and mediates activation of the AIM2 inflammasome (By similarity)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158675"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158676"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158679"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24531343"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8454910"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158676"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158679"}],"value":"Inflammasome","id":"SL-0488"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15582594"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9242382"}],"value":"Expressed in spleen, small intestine, peripheral blood leukocytes, and testis"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15582594"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158679"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9242382"}],"value":"By IFNG/IFN-gamma and IFNB1/IFN-beta"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158675"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158676"}],"value":"The pyrin domain mediates homotypic interaction with PYCARD/ASC (PubMed:19158675, PubMed:19158676)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22483801"}],"value":"The HIN-200 domain mediates dsDNA binding via electrostatic interactions"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27498865"}],"value":"Degraded via selective autophagy following interaction with TRIM11"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17726700"}],"value":"Defects in AIM2 may be a cause of microsatellite unstable colon cancers"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the HIN-200 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22483801"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26197926"}],"value":"According to a report, AIM2 is autoinhibited in absence of double-stranded DNA (dsDNA) due to an interaction between the pyrin and HIN-200 domains that induce a closed conformation (PubMed:22483801). However, it was later shown that AIM2 is not autoinhibited and that dsDNA acts as a molecular ruler to promote its homooligomerization (PubMed:26197926)"}],"commentType":"CAUTION"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Frameshift","sequence":"AAH10940.1","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"Interferon-inducible protein AIM2","featureId":"PRO_0000153726"},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"Pyrin","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00061"}]},{"type":"Domain","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"HIN-200","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00106"}]},{"type":"Natural variant","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"in dbSNP:rs2276405","featureCrossReferences":[{"database":"dbSNP","id":"rs2276405"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17726700"}],"featureId":"VAR_022022","alternativeSequence":{"originalSequence":"E","alternativeSequences":["K"]}},{"type":"Natural variant","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"in dbSNP:rs778047649","featureCrossReferences":[{"database":"dbSNP","id":"rs778047649"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17726700"}],"featureId":"VAR_043379","alternativeSequence":{"originalSequence":"C","alternativeSequences":["Y"]}},{"type":"Mutagenesis","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"Impaired double-stranded DNA (dsDNA)-binding, preventing homooligomerization.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26197926"}],"alternativeSequence":{"originalSequence":"LL","alternativeSequences":["AA"]}},{"type":"Mutagenesis","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"Impaired homooligomerization.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33980849"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"Fails to activate interleukin-1 beta production.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158679"}],"alternativeSequence":{"originalSequence":"L","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"In Mut2; abolished interaction with PYCARD/ASC. Abolished ability to bind double-stranded DNA (dsDNA).","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23530044"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26197926"}],"alternativeSequence":{"originalSequence":"DEELD","alternativeSequences":["AAALA"]}},{"type":"Mutagenesis","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Impaired ability to nucleate with PYCARD/ASC.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33980849"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["K"]}},{"type":"Mutagenesis","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Impaired homooligomerization.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33980849"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["K"]}},{"type":"Mutagenesis","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"In Mut1; abolished interaction with PYCARD/ASC.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23530044"}],"alternativeSequence":{"originalSequence":"FF","alternativeSequences":["AA"]}},{"type":"Mutagenesis","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Abolished ability to homooligomerize.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24406744"}],"alternativeSequence":{"originalSequence":"F","alternativeSequences":["G"]}},{"type":"Mutagenesis","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Strongly impaired ability to homooligomerize.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24406744"}],"alternativeSequence":{"originalSequence":"F","alternativeSequences":["L"]}},{"type":"Mutagenesis","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Impaired ability to homooligomerize.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24406744"}],"alternativeSequence":{"originalSequence":"F","alternativeSequences":["W","Y"]}},{"type":"Mutagenesis","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"Impaired homooligomerization.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33980849"}],"alternativeSequence":{"originalSequence":"A","alternativeSequences":["R","D"]}},{"type":"Mutagenesis","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"Impaired homooligomerization.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33980849"}],"alternativeSequence":{"originalSequence":"I","alternativeSequences":["D"]}},{"type":"Mutagenesis","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"Impaired double-stranded DNA (dsDNA)-binding, preventing homooligomerization.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26197926"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"Impaired ability to form AIM2 inflammasome filaments in response to double-stranded DNA (dsDNA).","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33980849"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["L"]}},{"type":"Mutagenesis","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"Impaired ability to nucleate with PYCARD/ASC.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33980849"}],"alternativeSequence":{"originalSequence":"M","alternativeSequences":["D"]}},{"type":"Mutagenesis","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"Strongly reduced ability to homooligomerize upon double-stranded DNA (dsDNA)-binding.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26197926"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"Impairs DNA binding; when associated with A-160; A-K162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22483801"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22483801"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204. Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204; A-244; A-251; A-309; A-311; A-355 and A-337.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"22483801"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"Impairs DNA binding.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19158679"}],"alternativeSequence":{"originalSequence":"F","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"Strongly reduced ability to homooligomerize upon double-stranded DNA (dsDNA)-binding.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26197926"}],"alternativeSequence":{"originalSequence":"F","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"Impaired double-stranded DNA (dsDNA)-binding, preventing homooligomerization.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26197926"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"Impairs DNA binding; when associated with A-160; A-162; A-163; A-198; A-204. 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