true1997-11-012024-01-24227IF16_HUMANA novel gene constitutively expressed in human lymphoid cells is inducible with interferon-gamma in myeloid cells.Trapani J.A.Browne K.A.Dawson M.J.Ramsay R.G.Eddy R.L.Show T.B.White P.C.Dupont B.doi:10.1007/bf002180441992Immunogenetics36369-376NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2)VARIANT HIS-103T-cellGenomic organization of IFI16, an interferon-inducible gene whose expression is associated with human myeloid cell differentiation: correlation of predicted protein domains with exon organization.Trapani J.A.Dawson M.J.Apostolidis V.A.Browne K.A.doi:10.1007/bf001778241994Immunogenetics40415-424NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2)VARIANT HIS-103Inhibition of AIM2 inflammasome activation by a novel transcript isoform of IFI16.Wang P.H.Ye Z.W.Deng J.J.Siu K.L.Gao W.W.Chaudhary V.Cheng Y.Fung S.Y.Yuen K.S.Ho T.H.Chan C.P.Zhang Y.Kok K.H.Yang W.Chan C.P.'Jin D.Y.doi:10.15252/embr.2018457372018EMBO Rep.19NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IFI16-BETA)FUNCTION (ISOFORM IFI16-BETA)SUBCELLULAR LOCATION (ISOFORM IFI16-BETA)INTERACTION WITH STING1 AND AIM2 (ISOFORM IFI16-BETA)TISSUE SPECIFICITY (ISOFORM IFI16-BETA)INDUCTION (ISOFORM IFI16-BETA)Jiang C.Zhang D.Peng Y.Zhang X.Han Z.Fu G.Chen Z.1999-11EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2)VARIANT HIS-103Bone marrowRole of IFI 16, a member of the interferon-inducible p200-protein family, in prostate epithelial cellular senescence.Xin H.Curry J.Johnstone R.W.Nickoloff B.J.Choubey D.doi:10.1038/sj.onc.12067542003Oncogene224831-4840NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2)FUNCTIONTISSUE SPECIFICITYINDUCTIONVARIANTS THR-179; SER-409 AND ASN-413Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T.Suzuki Y.Nishikawa T.Otsuki T.Sugiyama T.Irie R.Wakamatsu A.Hayashi K.Sato H.Nagai K.Kimura K.Makita H.Sekine M.Obayashi M.Nishi T.Shibahara T.Tanaka T.Ishii S.Yamamoto J.Saito K.Kawai Y.Isono Y.Nakamura Y.Nagahari K.Murakami K.Yasuda T.Iwayanagi T.Wagatsuma M.Shiratori A.Sudo H.Hosoiri T.Kaku Y.Kodaira H.Kondo H.Sugawara M.Takahashi M.Kanda K.Yokoi T.Furuya T.Kikkawa E.Omura Y.Abe K.Kamihara K.Katsuta N.Sato K.Tanikawa M.Yamazaki M.Ninomiya K.Ishibashi T.Yamashita H.Murakawa K.Fujimori K.Tanai H.Kimata M.Watanabe M.Hiraoka S.Chiba Y.Ishida S.Ono Y.Takiguchi S.Watanabe S.Yosida M.Hotuta T.Kusano J.Kanehori K.Takahashi-Fujii A.Hara H.Tanase T.-O.Nomura Y.Togiya S.Komai F.Hara R.Takeuchi K.Arita M.Imose N.Musashino K.Yuuki H.Oshima A.Sasaki N.Aotsuka S.Yoshikawa Y.Matsunawa H.Ichihara T.Shiohata N.Sano S.Moriya S.Momiyama H.Satoh N.Takami S.Terashima Y.Suzuki O.Nakagawa S.Senoh A.Mizoguchi H.Goto Y.Shimizu F.Wakebe H.Hishigaki H.Watanabe T.Sugiyama A.Takemoto M.Kawakami B.Yamazaki M.'Watanabe K.Kumagai A.Itakura S.Fukuzumi Y.Fujimori Y.Komiyama M.Tashiro H.Tanigami A.Fujiwara T.Ono T.Yamada K.Fujii Y.Ozaki K.Hirao M.Ohmori Y.Kawabata A.Hikiji T.Kobatake N.Inagaki H.Ikema Y.Okamoto S.Okitani R.Kawakami T.Noguchi S.Itoh T.Shigeta K.Senba T.Matsumura K.Nakajima Y.Mizuno T.Morinaga M.Sasaki M.Togashi T.Oyama M.Hata H.Watanabe M.'Komatsu T.Mizushima-Sugano J.Satoh T.Shirai Y.Takahashi Y.Nakagawa K.Okumura K.Nagase T.Nomura N.Kikuchi H.Masuho Y.Yamashita R.Nakai K.Yada T.Nakamura Y.'Ohara O.Isogai T.Sugano S.doi:10.1038/ng12852004Nat. Genet.3640-45NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4)VARIANTS THR-179; SER-409 AND ASN-413HippocampusThalamusTotoki Y.Toyoda A.Takeda T.Sakaki Y.Tanaka A.Yokoyama S.Ohara O.Nagase T.Kikuno R.F.2005-03EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)VARIANTS SER-409 AND ASN-413BrainThe DNA sequence and biological annotation of human chromosome 1.Gregory S.G.Barlow K.F.McLay K.E.Kaul R.Swarbreck D.Dunham A.Scott C.E.Howe K.L.Woodfine K.Spencer C.C.A.Jones M.C.Gillson C.Searle S.Zhou Y.Kokocinski F.McDonald L.Evans R.Phillips K.Atkinson A.Cooper R.Jones C.Hall R.E.Andrews T.D.Lloyd C.Ainscough R.Almeida J.P.Ambrose K.D.Anderson F.Andrew R.W.Ashwell R.I.S.Aubin K.Babbage A.K.Bagguley C.L.Bailey J.Beasley H.Bethel G.Bird C.P.Bray-Allen S.Brown J.Y.Brown A.J.Buckley D.Burton J.Bye J.Carder C.Chapman J.C.Clark S.Y.Clarke G.Clee C.Cobley V.Collier R.E.Corby N.Coville G.J.Davies J.Deadman R.Dunn M.Earthrowl M.Ellington A.G.Errington H.Frankish A.Frankland J.French L.Garner P.Garnett J.Gay L.Ghori M.R.J.Gibson R.Gilby L.M.Gillett W.Glithero R.J.Grafham D.V.Griffiths C.Griffiths-Jones S.Grocock R.Hammond S.Harrison E.S.I.Hart E.Haugen E.Heath P.D.Holmes S.Holt K.Howden P.J.Hunt A.R.Hunt S.E.Hunter G.Isherwood J.James R.Johnson C.Johnson D.Joy A.Kay M.Kershaw J.K.Kibukawa M.Kimberley A.M.King A.Knights A.J.Lad H.Laird G.Lawlor S.Leongamornlert D.A.Lloyd D.M.Loveland J.Lovell J.Lush M.J.Lyne R.Martin S.Mashreghi-Mohammadi M.Matthews L.Matthews N.S.W.McLaren S.Milne S.Mistry S.Moore M.J.F.Nickerson T.O'Dell C.N.Oliver K.Palmeiri A.Palmer S.A.Parker A.Patel D.Pearce A.V.Peck A.I.Pelan S.Phelps K.Phillimore B.J.Plumb R.Rajan J.Raymond C.Rouse G.Saenphimmachak C.Sehra H.K.Sheridan E.Shownkeen R.Sims S.Skuce C.D.Smith M.Steward C.Subramanian S.Sycamore N.Tracey A.Tromans A.Van Helmond Z.Wall M.Wallis J.M.White S.Whitehead S.L.Wilkinson J.E.Willey D.L.Williams H.Wilming L.Wray P.W.Wu Z.Coulson A.Vaudin M.Sulston J.E.Durbin R.M.Hubbard T.Wooster R.Dunham I.Carter N.P.McVean G.Ross M.T.Harrow J.Olson M.V.Beck S.Rogers J.Bentley D.R.doi:10.1038/nature047272006Nature441315-321NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project Teamdoi:10.1101/gr.25965042004Genome Res.142121-2127NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)VARIANTS THR-179; SER-409 AND ASN-413UterusIsotypic variants of the interferon-inducible transcriptional repressor IFI 16 arise through differential mRNA splicing.Johnstone R.W.Kershaw M.H.Trapani J.A.doi:10.1021/bi981069a1998Biochemistry3711924-11931ALTERNATIVE SPLICINGSUBUNITPHOSPHORYLATIONGLYCOSYLATIONIFI 16 gene encodes a nuclear protein whose expression is induced by interferons in human myeloid leukaemia cell lines.Dawson M.J.Trapani J.A.doi:10.1002/jcb.2405701061995J. Cell. Biochem.5739-51INDUCTIONSUBCELLULAR LOCATIONDNA-BINDINGThe closely linked genes encoding the myeloid nuclear differentiation antigen (MNDA) and IFI16 exhibit contrasting haemopoietic expression.Dawson M.J.Trapani J.A.Briggs R.C.Nicholl J.K.Sutherland G.R.Baker E.doi:10.1007/bf001884311995Immunogenetics4140-43TISSUE-SPECIFIC INDUCTIONThe IFN-inducible nucleoprotein IFI 16 is expressed in cells of the monocyte lineage, but is rapidly and markedly down-regulated in other myeloid precursor populations.Dawson M.J.Elwood N.J.Johnstone R.W.Trapani J.A.doi:10.1002/jlb.64.4.5461998J. Leukoc. Biol.64546-554TISSUE SPECIFIC INDUCTIONThe human interferon-inducible protein, IFI 16, is a repressor of transcription.Johnstone R.W.Kerry J.A.Trapani J.A.doi:10.1074/jbc.273.27.171721998J. Biol. Chem.27317172-17177FUNCTIONFunctional interaction between p53 and the interferon-inducible nucleoprotein IFI 16.Johnstone R.W.Wei W.Greenway A.Trapani J.A.doi:10.1038/sj.onc.12040052000Oncogene196033-6042FUNCTIONINTERACTION WITH TP53Proteomic characterization of the human centrosome by protein correlation profiling.Andersen J.S.Wilkinson C.J.Mayor T.Mortensen P.Nigg E.A.Mann M.doi:10.1038/nature021662003Nature426570-574IDENTIFICATION BY MASS SPECTROMETRYLymphoblastA member of the Pyrin family, IFI16, is a novel BRCA1-associated protein involved in the p53-mediated apoptosis pathway.Aglipay J.A.Lee S.W.Okada S.Fujiuchi N.Ohtsuka T.Kwak J.C.Wang Y.Johnstone R.W.Deng C.Qin J.Ouchi T.doi:10.1038/sj.onc.12070572003Oncogene228931-8938FUNCTIONINTERACTION WITH BRCA1A probability-based approach for high-throughput protein phosphorylation analysis and site localization.Beausoleil S.A.Villen J.Gerber S.A.Rush J.Gygi S.P.doi:10.1038/nbt12402006Nat. Biotechnol.241285-1292PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Cervix carcinomaA quantitative atlas of mitotic phosphorylation.Dephoure N.Zhou C.Villen J.Beausoleil S.A.Bakalarski C.E.Elledge S.J.Gygi S.P.doi:10.1073/pnas.08051391052008Proc. Natl. Acad. Sci. U.S.A.10510762-10767PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V.Lundgren D.H.Hwang S.-I.Rezaul K.Wu L.Eng J.K.Rodionov V.Han D.K.doi:10.1126/scisignal.20000072009Sci. Signal.2RA46PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Leukemic T-cellLysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C.Kumar C.Gnad F.Nielsen M.L.Rehman M.Walther T.C.Olsen J.V.Mann M.doi:10.1126/science.11753712009Science325834-840ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-214IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification.Blomster H.A.Imanishi S.Y.Siimes J.Kastu J.Morrice N.A.Eriksson J.E.Sistonen L.doi:10.1074/jbc.m110.1069552010J. Biol. Chem.28519324-19329SUMOYLATION AT LYS-561IFI16 is an innate immune sensor for intracellular DNA.Unterholzner L.Keating S.E.Baran M.Horan K.A.Jensen S.B.Sharma S.Sirois C.M.Jin T.Latz E.Xiao T.S.Fitzgerald K.A.Paludan S.R.Bowie A.G.doi:10.1038/ni.19322010Nat. Immunol.11997-1004FUNCTIONDNA-BINDINGINTERACTION WITH TMEM173INDUCTIONQuantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V.Vermeulen M.Santamaria A.Kumar C.Miller M.L.Jensen L.J.Gnad F.Cox J.Jensen T.S.Nigg E.A.Brunak S.Mann M.doi:10.1126/scisignal.20004752010Sci. Signal.3RA3PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-153 AND SER-575IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Initial characterization of the human central proteome.Burkard T.R.Planyavsky M.Kaupe I.Breitwieser F.P.Buerckstuemmer T.Bennett K.L.Superti-Furga G.Colinge J.doi:10.1186/1752-0509-5-172011BMC Syst. Biol.517IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]IFI16 acts as a nuclear pathogen sensor to induce the inflammasome in response to Kaposi Sarcoma-associated herpesvirus infection.Kerur N.Veettil M.V.Sharma-Walia N.Bottero V.Sadagopan S.Otageri P.Chandran B.doi:10.1016/j.chom.2011.04.0082011Cell Host Microbe9363-375FUNCTIONINTERACTION WITH PYCARD AND CASP1IFI16 induction by glucose restriction in human fibroblasts contributes to autophagy through activation of the ATM/AMPK/p53 pathway.Duan X.Ponomareva L.Veeranki S.Choubey D.doi:10.1371/journal.pone.00195322011PLoS ONE6E19532FUNCTIONINDUCTIONIFI16 protein mediates the anti-inflammatory actions of the type-I interferons through suppression of activation of caspase-1 by inflammasomes.Veeranki S.Duan X.Panchanathan R.Liu H.Choubey D.doi:10.1371/journal.pone.00270402011PLoS ONE6E27040FUNCTIONSUBCELLULAR LOCATIONINTERACTION WITH AIM2Preferential binding of IFI16 protein to cruciform structure and superhelical DNA.Brazda V.Coufal J.Liao J.C.Arrowsmith C.H.doi:10.1016/j.bbrc.2012.05.0652012Biochem. Biophys. Res. Commun.422716-720DNA-BINDINGThe intracellular DNA sensor IFI16 gene acts as restriction factor for human cytomegalovirus replication.Gariano G.R.Dell'Oste V.Bronzini M.Gatti D.Luganini A.De Andrea M.Gribaudo G.Gariglio M.Landolfo S.doi:10.1371/journal.ppat.10024982012PLoS Pathog.8E1002498FUNCTIONINTERACTION WITH SP1Nuclear IFI16 induction of IRF-3 signaling during herpesviral infection and degradation of IFI16 by the viral ICP0 protein.Orzalli M.H.DeLuca N.A.Knipe D.M.doi:10.1073/pnas.12113021092012Proc. Natl. Acad. Sci. U.S.A.109E3008-E3017FUNCTIONSUBCELLULAR LOCATIONPROTEASOMAL DEGRADATIONAcetylation modulates cellular distribution and DNA sensing ability of interferon-inducible protein IFI16.Li T.Diner B.A.Chen J.Cristea I.M.doi:10.1073/pnas.12034471092012Proc. Natl. Acad. Sci. U.S.A.10910558-10563SUBCELLULAR LOCATIONIDENTIFICATION BY MASS SPECTROMETRYPHOSPHORYLATION AT SER-95; SER-106; SER-153; SER-168; SER-174 AND SER-780ACETYLATION AT LYS-45; LYS-99; LYS-128; LYS-214; LYS-444; LYS-451; LYS-561; LYS-598 AND LYS-614MUTAGENESIS OF 96-ARG--LYS-100; LYS-99; LYS-128; 128-LYS--LYS-131; 134-LYS--LYS-136 AND 140-LYS--LYS-143Toward a comprehensive characterization of a human cancer cell phosphoproteome.Zhou H.Di Palma S.Preisinger C.Peng M.Polat A.N.Heck A.J.Mohammed S.doi:10.1021/pr300630k2013J. Proteome Res.12260-271PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Nuclear interferon-inducible protein 16 promotes silencing of herpesviral and transfected DNA.Orzalli M.H.Conwell S.E.Berrios C.DeCaprio J.A.Knipe D.M.doi:10.1073/pnas.13161941102013Proc. Natl. Acad. Sci. U.S.A.110E4492-E4501FUNCTIONSUBCELLULAR LOCATIONDifferential regulation of estrogen receptor alpha expression in breast cancer cells by metastasis-associated protein 1.Kang H.J.Lee M.H.Kang H.L.Kim S.H.Ahn J.R.Na H.Na T.Y.Kim Y.N.Seong J.K.Lee M.O.doi:10.1158/0008-5472.can-13-20202014Cancer Res.741484-1494FUNCTIONINTERACTION WITH MTA1SUBCELLULAR LOCATIONAn enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y.Song C.Cheng K.Dong M.Wang F.Huang J.Sun D.Wang L.Ye M.Zou H.doi:10.1016/j.jprot.2013.11.0142014J. Proteomics96253-262PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-153IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]LiverThe PYRIN domain-only protein POP3 inhibits ALR inflammasomes and regulates responses to infection with DNA viruses.Khare S.Ratsimandresy R.A.de Almeida L.Cuda C.M.Rellick S.L.Misharin A.V.Wallin M.C.Gangopadhyay A.Forte E.Gottwein E.Perlman H.Reed J.C.Greaves D.R.Dorfleutner A.Stehlik C.doi:10.1038/ni.28292014Nat. Immunol.15343-353SUBCELLULAR LOCATIONINTERACTION WITH PYDC5Uncovering global SUMOylation signaling networks in a site-specific manner.Hendriks I.A.D'Souza R.C.Yang B.Verlaan-de Vries M.Mann M.Vertegaal A.C.doi:10.1038/nsmb.28902014Nat. Struct. Mol. Biol.21927-936SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116 AND LYS-561IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.Impens F.Radoshevich L.Cossart P.Ribet D.doi:10.1073/pnas.14138251112014Proc. Natl. Acad. Sci. U.S.A.11112432-12437SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-561IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]SUMO-2 orchestrates chromatin modifiers in response to DNA damage.Hendriks I.A.Treffers L.W.Verlaan-de Vries M.Olsen J.V.Vertegaal A.C.doi:10.1016/j.celrep.2015.02.0332015Cell Rep.101778-1791SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-561 AND LYS-683IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.Hendriks I.A.Lyon D.Young C.Jensen L.J.Vertegaal A.C.Nielsen M.L.doi:10.1038/nsmb.33662017Nat. Struct. Mol. Biol.24325-336SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116; LYS-128; LYS-561 AND LYS-683IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]Interferon-inducible protein 16: insight into the interaction with tumor suppressor p53.Liao J.C.Lam R.Brazda V.Duan S.Ravichandran M.Ma J.Xiao T.Tempel W.Zuo X.Wang Y.X.Chirgadze N.Y.Arrowsmith C.H.doi:10.1016/j.str.2010.12.0152011Structure19418-429X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 192-393MUTAGENESIS OF TYR-218; GLU-222; TYR-267 AND GLU-272Structures of the HIN domain:DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor.Jin T.Perry A.Jiang J.Smith P.Curry J.A.Unterholzner L.Jiang Z.Horvath G.Rathinam V.A.Johnstone R.W.Hornung V.Latz E.Bowie A.G.Fitzgerald K.A.Xiao T.S.doi:10.1016/j.immuni.2012.02.0142012Immunity36561-571X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 571-766 IN COMPLEX WITH DOUBLE-STRANDED DNAMUTAGENESIS OF LYS-627; LYS-663; ARG-667; SER-670; LYS-674; LYS-732; LYS-734 AND LYS-759Crystal structure of the first HIN-200 domain of interferon-inducible protein 16.Northeast structural genomics consortium (NESG)2007-02PDBX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 192-393Crystal structure analysis of the second HIN domain of IFI16.Northeast structural genomics consortium (NESG)2007-11PDBX-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 571-766Sequence problems.Sequence problems.Different initiation.Different initiation.2.00A/B/C/D=192-3932.35A/B=571-7662.25A=571-7661.80A=571-7662.50A/B/C/D=571-7662.54A/B=192-3937491801 N-Linked glycan (1 site)1 site, 1 glycan2 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site)379 antibodies from 33 providershumanIFI16Low tissue specificitygeneEukaryotaSTING mediated induction of host immune responsesIRF3-mediated induction of type I IFN16 hits in 1166 CRISPR screenshumanTbioProteinExpressed in germinal epithelium of ovary and 218 other cell types or tissuesbaseline and differentialPyrinDeath Domain, FasNucleic acid-binding proteinsDAPINDEATH-like_dom_sfHIN-200HIN200/IF120xNA-bd_OB-foldGAMMA-INTERFERON-INDUCIBLE PROTEIN 16INTERFERON-INDUCIBLE PROTEIN AIM2 FAMILY MEMBERHINPYRINPYRINHIN-2000 domain-likeDAPINHIN_200HSGamma-interferon-inducible protein 16Ifi-16Interferon-inducible myeloid differentiation transcriptional activatorIFI16IFNGIP1Binds double-stranded DNA. Binds preferentially to supercoiled DNA and cruciform DNA structures. Seems to be involved in transcriptional regulation. May function as a transcriptional repressor. Could have a role in the regulation of hematopoietic differentiation through activation of unknown target genes. Controls cellular proliferation by modulating the functions of cell cycle regulatory factors including p53/TP53 and the retinoblastoma protein. May be involved in TP53-mediated transcriptional activation by enhancing TP53 sequence-specific DNA binding and modulating TP53 phosphorylation status. Seems to be involved in energy-level-dependent activation of the ATM/ AMPK/TP53 pathway coupled to regulation of autophagy. May be involved in regulation of TP53-mediated cell death also involving BRCA1. May be involved in the senescence of prostate epithelial cells. Involved in innate immune response by recognizing viral dsDNA in the cytosol and probably in the nucleus. After binding to viral DNA in the cytoplasm recruits TMEM173/STING and mediates the induction of IFN-beta. Has anti-inflammatory activity and inhibits the activation of the AIM2 inflammasome, probably via association with AIM2. Proposed to bind viral DNA in the nucleus, such as of Kaposi's sarcoma-associated herpesvirus, and to induce the formation of nuclear caspase-1-activating inflammasome formation via association with PYCARD. Inhibits replication of herpesviruses such as human cytomegalovirus (HCMV) probably by interfering with promoter recruitment of members of the Sp1 family of transcription factors. Necessary to activate the IRF3 signaling cascade during human herpes simplex virus 1 (HHV-1) infection and promotes the assembly of heterochromatin on herpesviral DNA and inhibition of viral immediate-early gene expression and replication. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer.Isoform that specifically inhibits the AIM2 inflammasome (PubMed:30104205). Binds double-stranded DNA (dsDNA) in the cytoplasm, impeding its detection by AIM2 (PubMed:30104205). Also prevents the interaction between AIM2 and PYCARD/ASC via its interaction with AIM2, thereby inhibiting assembly of the AIM2 inflammasome (PubMed:30104205). This isoform also weakly induce production of type I interferon-beta (IFNB1) via its interaction with STING1 (PubMed:30104205).Forms homooligomers; isoform 2 can self-associate or associate with isoform 1 or isoform 3. Interacts with TMEM173, AIM2, PYCARD and CASP1. Interacts with BRCA1, TP53, E2F1, RB1 and SP1. Interacts with MTA1. Interacts with PYDC5 (PubMed:24531343).Interacts with AIM2; preventing the interaction between AIM2 and PYCARD/ASC (PubMed:30104205). Interacts with STING1 (PubMed:30104205).Cellular distribution is dependent on the acetylation status of the multipartite nuclear localization signal (NLS); NLS acetylation promotes cytoplasmic localization. Localizes in the nucleus during human herpes simplex virus 1 (HHV-1) infection.Expressed in peripheral blood leukocytes, fibroblasts and lymphoid cells. Present in myeloid precursors (CD34+) and throughout monocyte development, but its expression is down-regulated in erythroid and polymorphonuclear precursor cells. Present in prostate, ovary and breast (at protein level).Widely expressed.Strongly induced by IFNG/IFN-gamma and, to a lesser extent, by alpha interferon. In HL-60 cells, maximum induction by IFNG/IFN-gamma occurs within 12 hours whereas, for IFN-alpha, only 10-fold induction was observed after 36 hours. Induced in vitro by dimethylsulfoxide, retinoic acid and 1,25 dihydroxyvitamin D3. Induced in monocytes by IFN-alpha and viral dsDNA. Induced by glucose restriction.By interferon-beta (IFNB1).The HIN-200 domains mediates dsDNA binding via electrostatic interactions.Ubiquitinated by human herpes simplex virus 1 (HHV-1) ICP0 protein; leading to degradation by the proteasome.Lysine acetylation in the multipartite nuclear localization signal (NLS) regulates the subcellular location. In vitro can be acetylated by p300/EP300 coupled to cytoplasmic localization.Phosphorylated on Ser and Thr.Isoform 3 seems to show a minor degree of complex carbohydrate addition.Major isoform.Belongs to the HIN-200 family.Intron retention.Probable cloning artifact.Extended N-terminus.Extended N-terminus.Gamma-interferon-inducible protein 16882561785Pyrin88HIN-200 1189389HIN-200 2562761Disordered91191Interaction with TP53 C-terminus192393Disordered390442Interaction with TP53 core domain571766Nuclear localization signal96100Nuclear localization signal128131Nuclear localization signal134136Nuclear localization signal140143Polar residues105120Basic and acidic residues123142Polar residues164Polar residues404Polar residues411N6-acetyllysine45Phosphoserine95N6-acetyllysine99Phosphoserine106N6-acetyllysine; alternatePhosphoserine153Phosphoserine168Phosphoserine174N6-acetyllysine214N6-acetyllysine444N6-acetyllysine451N6-acetyllysine; alternate561Phosphoserine575N6-acetyllysine598N6-acetyllysine614Phosphoserine780Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)683In isoform IFI16-beta.158In isoform 4.183In isoform 3.555In isoform 2.499In isoform IFI16-beta.470525H103T179E202S409N413S723S779Predominant cytoplasmic localization.Predominant cytoplasmic, reduces nuclear localization (mimics non-acetylated state).QMinor effect on nuclear localization (mimics acetylated state).RPredominant nuclear, some cytoplasmic localization.Predominant cytoplasmic, reduces nuclear localization (mimics non-acetylated state).QMinor effect on nuclear localization (mimics acetylated state).RMostly nuclear, minor cytoplasmic localization.Mostly nuclear, minor cytoplasmic localization.Abolishes TP53-mediated transcriptional activation; when associated with A-267.A218Abolishes TP53-mediated transcriptional activation; when associated with A-272.A222Abolishes TP53-mediated transcriptional activation; when associated with A-218.A267Abolishes TP53-mediated transcriptional activation; when associated with A-222.A272Impairs DNA binding; when associated with A-663; A-667; A-670; A-674; A-732; A-734 and A-759.A627Impairs DNA binding; when associated with A-627; A-667; A-670; A-674; A-732; A-734 and A-759.A663Impairs DNA binding; when associated with A-627; A-663; A-670; A-674; A-732; A-734 and A-759.A667Impairs DNA binding; when associated with A-627; A-663; A-667; A-674; A-732; A-734 and A-759.A670Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A-732; A-734 and A-759.A674Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-734 and A-759.A732Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-732 and A-759.A734Impairs DNA binding; when associated with A-627; A-663; A-667; A-670; A- 674; A-732 and A-734.A759G401S544RNNS737S205212216219225234239244247253254257259270273278281284286292298304307315327329338341348349351361372375379385388578585589592593596597605610615618620621624629634636638641644648652655657675679685699702709712718720724741744747749764false3false9false2false2false3false6ARBRCA1DHX58STING1IFI16TP532006-11-2838825630a7c04c680fd3f564defcd851bdc5f41IFI 16AMGKKYKNIVLLKGLEVINDYHFRMVKSLLSNDLKLNLKMREEYDKIQIADLMEEKFRGDAGLGKLIKIFEDIPTLEDLAETLKKEKLKVKGPALSRKRKKEVDATSPAPSTSSTVKTEGAEATPGAQKRKKSTKEKAGPKGSKVSEEQTQPPSPAGAGMSTAMGRSPSPKTSLSAPPNSSSTENPKTVAKCQVTPRRNVLQKRPVIVKVLSTTKPFEYETPEMEKKIMFHATVATQTQFFHVKVLNTSLKEKFNGKKIIIISDYLEYDSLLEVNEESTVSEAGPNQTFEVPNKIINRAKETLKIDILHKQASGNIVYGVFMLHKKTVNQKTTIYEIQDDRGKMDVVGTGQCHNIPCEEGDKLQLFCFRLRKKNQMSKLISEMHSFIQIKKKTNPRNNDPKSMKLPQEQRQLPYPSEASTTFPESHLRTPQMPPTTPSSSFFTKKSEDTISKMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHTPQMPPSTPSSSFLTTKSEDTISKMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHTPQMPPSTPSSSFLTTLKPRLKTEPEEVSIEDSAQSDLKEVMVLNATESFVYEPKEQKKMFHATVATENEVFRVKVFNIDLKEKFTPKKIIAIANYVCRNGFLEVYPFTLVADVNADRNMEIPKGLIRSASVTPKINQLCSQTKGSFVNGVFEVHKKNVRGEFTYYEIQDNTGKMEVVVHGRLTTINCEEGDKLKLTCFELAPKSGNTGELRSVIHSHIKVIKTRKNKKDILNPDSSMETSPDFFF2IFI 16BMGKKYKNIVLLKGLEVINDYHFRMVKSLLSNDLKLNLKMREEYDKIQIADLMEEKFRGDAGLGKLIKIFEDIPTLEDLAETLKKEKLKVKGPALSRKRKKEVDATSPAPSTSSTVKTEGAEATPGAQKRKKSTKEKAGPKGSKVSEEQTQPPSPAGAGMSTAMGRSPSPKTSLSAPPNSSSTENPKTVAKCQVTPRRNVLQKRPVIVKVLSTTKPFEYETPEMEKKIMFHATVATQTQFFHVKVLNTSLKEKFNGKKIIIISDYLEYDSLLEVNEESTVSEAGPNQTFEVPNKIINRAKETLKIDILHKQASGNIVYGVFMLHKKTVNQKTTIYEIQDDRGKMDVVGTGQCHNIPCEEGDKLQLFCFRLRKKNQMSKLISEMHSFIQIKKKTNPRNNDPKSMKLPQEQRQLPYPSEASTTFPESHLRTPQMPPTTPSSSFFTKKSEDTISKMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHTPQMPPSTPSSSFLTTLKPRLKTEPEEVSIEDSAQSDLKEVMVLNATESFVYEPKEQKKMFHATVATENEVFRVKVFNIDLKEKFTPKKIIAIANYVCRNGFLEVYPFTLVADVNADRNMEIPKGLIRSASVTPKINQLCSQTKGSFVNGVFEVHKKNVRGEFTYYEIQDNTGKMEVVVHGRLTTINCEEGDKLKLTCFELAPKSGNTGELRSVIHSHIKVIKTRKNKKDILNPDSSMETSPDFFF3IFI 16CMGKKYKNIVLLKGLEVINDYHFRMVKSLLSNDLKLNLKMREEYDKIQIADLMEEKFRGDAGLGKLIKIFEDIPTLEDLAETLKKEKLKVKGPALSRKRKKEVDATSPAPSTSSTVKTEGAEATPGAQKRKKSTKEKAGPKGSKVSEEQTQPPSPAGAGMSTAMGRSPSPKTSLSAPPNSSSTENPKTVAKCQVTPRRNVLQKRPVIVKVLSTTKPFEYETPEMEKKIMFHATVATQTQFFHVKVLNTSLKEKFNGKKIIIISDYLEYDSLLEVNEESTVSEAGPNQTFEVPNKIINRAKETLKIDILHKQASGNIVYGVFMLHKKTVNQKTTIYEIQDDRGKMDVVGTGQCHNIPCEEGDKLQLFCFRLRKKNQMSKLISEMHSFIQIKKKTNPRNNDPKSMKLPQEQRQLPYPSEASTTFPESHLRTPQMPPTTPSSSFFTKLKPRLKTEPEEVSIEDSAQSDLKEVMVLNATESFVYEPKEQKKMFHATVATENEVFRVKVFNIDLKEKFTPKKIIAIANYVCRNGFLEVYPFTLVADVNADRNMEIPKGLIRSASVTPKINQLCSQTKGSFVNGVFEVHKKNVRGEFTYYEIQDNTGKMEVVVHGRLTTINCEEGDKLKLTCFELAPKSGNTGELRSVIHSHIKVIKTRKNKKDILNPDSSMETSPDFFF4MGKKYKNIVLLKGLEVINDYHFRMVKSLLSNDLKLNLKMREEYDKIQIADLMEEKFRGDAGLGKLIKIFEDIPTLEDLAETLKKEKLKVKGPALSRKRKKEVDATSPAPSTSSTVKTEGAEATPGAQNPKTVAKCQVTPRRNVLQKRPVIVKVLSTTKPFEYETPEMEKKIMFHATVATQTQFFHVKVLNTSLKEKFNGKKIIIISDYLEYDSLLEVNEESTVSEAGPNQTFEVPNKIINRAKETLKIDILHKQASGNIVYGVFMLHKKTVNQKTTIYEIQDDRGKMDVVGTGQCHNIPCEEGDKLQLFCFRLRKKNQMSKLISEMHSFIQIKKKTNPRNNDPKSMKLPQEQRQLPYPSEASTTFPESHLRTPQMPPTTPSSSFFTKKSEDTISKMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHTPQMPPSTPSSSFLTTKSEDTISKMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHTPQMPPSTPSSSFLTTLKPRLKTEPEEVSIEDSAQSDLKEVMVLNATESFVYEPKEQKKMFHATVATENEVFRVKVFNIDLKEKFTPKKIIAIANYVCRNGFLEVYPFTLVADVNADRNMEIPKGLIRSASVTPKINQLCSQTKGSFVNGVFEVHKKNVRGEFTYYEIQDNTGKMEVVVHGRLTTINCEEGDKLKLTCFELAPKSGNTGELRSVIHSHIKVIKTRKNKKDILNPDSSMETSPDFFFIFI16-betaMSTAMGRSPSPKTSLSAPPNSSSTENPKTVAKCQVTPRRNVLQKRPVIVKVLSTTKPFEYETPEMEKKIMFHATVATQTQFFHVKVLNTSLKEKFNGKKIIIISDYLEYDSLLEVNEESTVSEAGPNQTFEVPNKIINRAKETLKIDILHKQASGNIVYGVFMLHKKTVNQKTTIYEIQDDRGKMDVVGTGQCHNIPCEEGDKLQLFCFRLRKKNQMSKLISEMHSFIQIKKKTNPRNNDPKSMKLPQEQRQLPYPSEASTTFPESHLRTPQMPPTTPSSSFFTKKSEDTISKMNDFMRMQILKEGSHFPGPFMTSIGPAESHPHTPQMPPSTPSSSFLTTLKPRLKTEPEEVSIEDSAQSDLKEVMVLNATESFVYEPKEQKKMFHATVATENEVFRVKVFNIDLKEKFTPKKIIAIANYVCRNGFLEVYPFTLVADVNADRNMEIPKGLIRSASVTPKINQLCSQTKGSFVNGVFEVHKKNVRGEFTYYEIQDNTGKMEVVVHGRLTTINCEEGDKLKLTCFELAPKSGNTGELRSVIHSHIKVIKTRKNKKDILNPDSSMETSPDFFFtruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetruetrue