ID IRF2_HUMAN Reviewed; 349 AA. AC P14316; D6RCK5; H0Y8S3; Q6IAS7; Q96B99; DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot. DT 11-FEB-2002, sequence version 2. DT 04-NOV-2026, entry version 215. DE RecName: Full=Interferon regulatory factor 2 {ECO:0000303|PubMed:2813069}; DE Short=IRF-2 {ECO:0000303|PubMed:2813069}; GN Name=IRF2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=T-cell; RX PubMed=2813069; DOI=10.1093/nar/17.20.8372; RA Itoh S., Harada H., Fujita T., Mimura T., Taniguchi T.; RT "Sequence of a cDNA coding for human IRF-2."; RL Nucleic Acids Res. 17:8372-8372(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8106512; DOI=10.1016/s0021-9258(17)37685-8; RA Cha Y., Deisseroth A.B.; RT "Human interferon regulatory factor 2 gene. Intron-exon organization and RT functional analysis of 5'-flanking region."; RL J. Biol. Chem. 269:5279-5287(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Trachea; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Skin; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [9] RP FUNCTION. RX PubMed=7687740; DOI=10.1128/mcb.13.8.4531-4538.1993; RA Tanaka N., Kawakami T., Taniguchi T.; RT "Recognition DNA sequences of interferon regulatory factor 1 (IRF-1) and RT IRF-2, regulators of cell growth and the interferon system."; RL Mol. Cell. Biol. 13:4531-4538(1993). RN [10] RP INDUCTION. RX PubMed=7507207; DOI=10.1128/mcb.14.2.1500-1509.1994; RA Harada H., Takahashi E., Itoh S., Harada K., Hori T.A., Taniguchi T.; RT "Structure and regulation of the human interferon regulatory factor 1 (IRF- RT 1) and IRF-2 genes: implications for a gene network in the interferon RT system."; RL Mol. Cell. Biol. 14:1500-1509(1994). RN [11] RP DNA-BINDING, AND FUNCTION AS AN ACTIVATOR. RX PubMed=9540062; DOI=10.1023/a:1006888731301; RA Aziz F., van Wijnen A.J., Vaughan P.S., Wu S., Shakoori A.R., Lian J.B., RA Soprano K.J., Stein J.L., Stein G.S.; RT "The integrated activities of IRF-2 (HiNF-M), CDP/cut (HiNF-D) and H4TF-2 RT (HiNF-P) regulate transcription of a cell cycle controlled human histone H4 RT gene: mechanistic differences between distinct H4 genes."; RL Mol. Biol. Rep. 25:1-12(1998). RN [12] RP INTERACTION WITH BRD7. RX PubMed=11025449; RX DOI=10.1002/1097-4652(200011)185:2<269::aid-jcp12>3.0.co;2-l; RA Staal A., Enserink J.M., Stein J.L., Stein G.S., van Wijnen A.J.; RT "Molecular characterization of celtix-1, a bromodomain protein interacting RT with the transcription factor interferon regulatory factor 2."; RL J. Cell. Physiol. 185:269-279(2000). RN [13] RP ALTERNATIVE SPLICING. RX PubMed=11058120; DOI=10.1093/nar/28.21.4219; RA Koenig Merediz S.A., Schmidt M., Hoppe G.J., Alfken J., Meraro D., RA Levi B.Z., Neubauer A., Wittig B.; RT "Cloning of an interferon regulatory factor 2 isoform with different RT regulatory ability."; RL Nucleic Acids Res. 28:4219-4224(2000). RN [14] RP ACETYLATION AT LYS-75 AND LYS-78, INTERACTION WITH CREBBP, FUNCTION, RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF LYS-75 AND LYS-78. RX PubMed=12738767; DOI=10.1074/jbc.m213037200; RA Masumi A., Yamakawa Y., Fukazawa H., Ozato K., Komuro K.; RT "Interferon regulatory factor-2 regulates cell growth through its RT acetylation."; RL J. Biol. Chem. 278:25401-25407(2003). RN [15] RP FUNCTION, ALTERNATIVE SPLICING, AND INTERACTION WITH IRF2BP1 AND IRF2BP2. RX PubMed=12799427; DOI=10.1093/nar/gkg431; RA Childs K.S., Goodbourn S.; RT "Identification of novel co-repressor molecules for interferon regulatory RT factor-2."; RL Nucleic Acids Res. 31:3016-3026(2003). RN [16] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=15226432; DOI=10.1128/mcb.24.14.6298-6310.2004; RA Oshima S., Nakamura T., Namiki S., Okada E., Tsuchiya K., Okamoto R., RA Yamazaki M., Yokota T., Aida M., Yamaguchi Y., Kanai T., Handa H., RA Watanabe M.; RT "Interferon regulatory factor 1 (IRF-1) and IRF-2 distinctively up-regulate RT gene expression and production of interleukin-7 in human intestinal RT epithelial cells."; RL Mol. Cell. Biol. 24:6298-6310(2004). RN [17] RP SUMOYLATION AT LYS-137; LYS-166 AND LYS-293, FUNCTION, AND MUTAGENESIS OF RP LYS-137; LYS-166 AND LYS-293. RX PubMed=18514056; DOI=10.1016/j.bbrc.2008.05.103; RA Han K.-J., Jiang L., Shu H.-B.; RT "Regulation of IRF2 transcriptional activity by its sumoylation."; RL Biochem. Biophys. Res. Commun. 372:772-778(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-137, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-137 AND LYS-260, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [21] RP FUNCTION, AND INTERACTION WITH TASOR2. RX PubMed=39013473; DOI=10.1016/j.molcel.2024.06.020; RA Danac J.M.C., Matthews R.E., Gungi A., Qin C., Parsons H., Antrobus R., RA Timms R.T., Tchasovnikarova I.A.; RT "Competition between two HUSH complexes orchestrates the immune response to RT retroelement invasion."; RL Mol. Cell 84:2870-2881(2024). RN [22] RP INTERACTION WITH TASOR2. RX PubMed=39489739; DOI=10.1038/s41467-024-53761-w; RA Jensvold Z.D., Flood J.R., Christenson A.E., Lewis P.W.; RT "Interplay between two paralogous human silencing hub (HuSH) complexes in RT regulating LINE-1 element silencing."; RL Nat. Commun. 15:9492-9492(2024). CC -!- FUNCTION: DNA-binding transcription factor that specifically binds to CC the upstream regulatory region of type I interferon (IFN) and IFN- CC inducible genes and regulates their expression (PubMed:39013473, CC PubMed:7687740). Mainly acts as a transcription repressor, repressing CC expression (PubMed:39013473). Also acts as an activator for several CC genes including H4 and IL7 (PubMed:15226432, PubMed:9540062). CC Constitutively binds to the ISRE promoter to activate IL7 CC (PubMed:15226432). Involved in cell cycle regulation through binding CC the site II (HiNF-M) promoter region of H4 and activating transcription CC during cell growth (PubMed:9540062). Antagonizes IRF1 transcriptional CC activation (By similarity). {ECO:0000250|UniProtKB:P23906, CC ECO:0000269|PubMed:15226432, ECO:0000269|PubMed:39013473, CC ECO:0000269|PubMed:7687740, ECO:0000269|PubMed:9540062}. CC -!- FUNCTION: [Isoform 2]: Unable to bind to IRF2BP1 and IRF2BP2 CC corepressors and cannot mediate repression. CC {ECO:0000269|PubMed:12799427}. CC -!- SUBUNIT: Interacts with BRD7, IRF2BP1 and IRF2BP2 (PubMed:11025449, CC PubMed:12799427). Interacts with CREBBP in growing cells; the CC interaction acetylates IRF2 and regulates IRF2-dependent H4 promoter CC activity (PubMed:12738767). Interacts with TASOR2; promoting CC recruitment of the HUSH2 complex to interferon-stimulated genes and CC transcription silencing (PubMed:39013473, PubMed:39489739). CC {ECO:0000269|PubMed:11025449, ECO:0000269|PubMed:12738767, CC ECO:0000269|PubMed:12799427, ECO:0000269|PubMed:39013473, CC ECO:0000269|PubMed:39489739}. CC -!- INTERACTION: CC P14316; O95352: ATG7; NbExp=2; IntAct=EBI-2866589, EBI-987834; CC P14316; P85037: FOXK1; NbExp=4; IntAct=EBI-2866589, EBI-2509974; CC P14316; Q01167: FOXK2; NbExp=5; IntAct=EBI-2866589, EBI-2509991; CC P14316; P16298: PPP3CB; NbExp=2; IntAct=EBI-2866589, EBI-1759540; CC P14316; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-2866589, EBI-745958; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P23906}. CC Chromosome {ECO:0000250|UniProtKB:P23906}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P14316-1; Sequence=Displayed; CC Name=2; Synonyms=IRF-2s, IRF-2[S]; CC IsoId=P14316-2; Sequence=VSP_043965; CC -!- TISSUE SPECIFICITY: Expressed throughout the epithelium of the colon. CC Also expressed in lamina propria. {ECO:0000269|PubMed:15226432}. CC -!- INDUCTION: By viruses and IFN. {ECO:0000269|PubMed:7507207}. CC -!- PTM: Acetylated by CBP/ p300 during cell-growth. Acetylation on Lys-75 CC is required for stimulation of H4 promoter activity. CC {ECO:0000269|PubMed:12738767}. CC -!- PTM: The major sites of sumoylation are Lys-137 and Lys-293. CC Sumoylation with SUMO1 increases its transcriptional repressor activity CC on IRF1 and diminishes its ability to activate ISRE and H4 promoter. CC {ECO:0000269|PubMed:18514056}. CC -!- SIMILARITY: Belongs to the IRF family. {ECO:0000255|PROSITE- CC ProRule:PRU00840}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X15949; CAA34073.1; -; mRNA. DR EMBL; BT007264; AAP35928.1; -; mRNA. DR EMBL; AK312953; BAG35793.1; -; mRNA. DR EMBL; CR457077; CAG33358.1; -; mRNA. DR EMBL; AC099343; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471056; EAX04677.1; -; Genomic_DNA. DR EMBL; CH471056; EAX04678.1; -; Genomic_DNA. DR EMBL; CH471056; EAX04680.1; -; Genomic_DNA. DR EMBL; BC015803; AAH15803.1; -; mRNA. DR CCDS; CCDS3835.1; -. [P14316-1] DR PIR; A53340; A53340. DR RefSeq; NP_002190.2; NM_002199.4. [P14316-1] DR PDB; 8YTG; X-ray; 1.45 A; B=331-338. DR BMRB; P14316; -. DR SMR; P14316; -. DR BioGRID; 109868; 107. DR ELM; P14316; -. DR IntAct; P14316; 92. DR STRING; 9606.ENSP00000377218; -. DR NDEx; IQUERY-CP-IRF2; 5 NDEx IQuery Curated Pathways. DR GlyGen; P14316; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P14316; -. DR PhosphoSitePlus; P14316; -. DR BioMuta; IRF2; -. DR DMDM; 20141499; -. DR PaxDb; 9606-ENSP00000377218; -. DR PeptideAtlas; P14316; -. DR ProteomicsDB; 53043; -. [P14316-1] DR ProteomicsDB; 53044; -. [P14316-2] DR Pumba; P14316; -. DR jPOST; P14316; -. DR MassIVE; P14316; -. DR DNASU; 3660; -. DR Ensembl; ENST00000393593.8; ENSP00000377218.3; ENSG00000168310.13. [P14316-1] DR Ensembl; ENST00000504340.2; ENSP00000512878.1; ENSG00000168310.13. [P14316-1] DR Ensembl; ENST00000510814.6; ENSP00000424552.2; ENSG00000168310.13. [P14316-1] DR Ensembl; ENST00000696840.1; ENSP00000512918.1; ENSG00000168310.13. [P14316-1] DR Ensembl; ENST00000696841.1; ENSP00000512954.1; ENSG00000168310.13. [P14316-1] DR Ensembl; ENST00000696843.1; ENSP00000512920.1; ENSG00000168310.13. [P14316-1] DR Ensembl; ENST00000696845.1; ENSP00000512922.1; ENSG00000168310.13. [P14316-1] DR Ensembl; ENST00000696846.1; ENSP00000512923.1; ENSG00000168310.13. [P14316-1] DR Ensembl; ENST00000696848.1; ENSP00000512924.1; ENSG00000168310.13. [P14316-2] DR Ensembl; ENST00000696849.1; ENSP00000512925.1; ENSG00000168310.13. [P14316-1] DR Ensembl; ENST00000696851.1; ENSP00000512927.1; ENSG00000168310.13. [P14316-1] DR Ensembl; ENST00000696853.1; ENSP00000512929.1; ENSG00000168310.13. [P14316-2] DR Ensembl; ENST00000883919.1; ENSP00000553978.1; ENSG00000168310.13. [P14316-1] DR Ensembl; ENST00000883920.1; ENSP00000553979.1; ENSG00000168310.13. [P14316-1] DR Ensembl; ENST00000956295.1; ENSP00000626354.1; ENSG00000168310.13. [P14316-1] DR Ensembl; ENST00000956296.1; ENSP00000626355.1; ENSG00000168310.13. [P14316-1] DR GeneID; 3660; -. DR KEGG; hsa:3660; -. DR MANE-Select; ENST00000393593.8; ENSP00000377218.3; NM_002199.4; NP_002190.2. DR UCSC; uc003iwf.5; human. [P14316-1] DR CTD; 3660; -. DR DisGeNET; 3660; -. DR VEuPathDB; HostDB:ENSG00000168310; -. DR GeneCards; IRF2; -. DR HGNC; HGNC:6117; IRF2. DR AGR; HGNC:6117; -. DR HPA; ENSG00000168310; Low tissue specificity. DR MalaCards; IRF2; -. DR MIM; 147576; gene. DR OpenTargets; ENSG00000168310; -. DR ClinPGx; PA29916; -. DR eggNOG; ENOG502QW7C; Eukaryota. DR GeneTree; ENSGT00940000159063; -. DR HOGENOM; CLU_056386_0_0_1; -. DR InParanoid; P14316; -. DR OMA; ADPFKGH; -. DR OrthoDB; 6538197at2759; -. DR PhylomeDB; P14316; -. DR Reactome; R-HSA-5620971; Pyroptosis. DR Reactome; R-HSA-877300; Interferon gamma signaling. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; P14316; -. DR SIGNOR; P14316; -. DR ChiTaRS; IRF2; human. DR Agora; ENSG00000168310; -. DR GeneWiki; IRF2; -. DR GenomeRNAi; 3660; -. DR PRO; PR:P14316; -. DR Bgee; ENSG00000168310; Expressed in monocyte and 163 other cell types or tissues. DR ExpressionAtlas; P14316; baseline and differential. DR CDD; cd00103; IRF; 1. DR FunFam; 1.10.10.10:FF:000065; Interferon regulatory factor; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR019817; Interferon_reg_fac_CS. DR InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom. DR InterPro; IPR017431; IRF1/IRF2. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR11949; INTERFERON REGULATORY FACTOR; 1. DR PANTHER; PTHR11949:SF22; INTERFERON REGULATORY FACTOR 2; 1. DR Pfam; PF00605; IRF; 1. DR PIRSF; PIRSF038196; IFN_RF1/2; 1. DR PRINTS; PR00267; INTFRNREGFCT. DR SMART; SM00348; IRF; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00601; IRF_1; 1. DR PROSITE; PS51507; IRF_2; 1. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0000785; C:chromatin; IDA:UniProt. DR GO; GO:0005694; C:chromosome; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:UniProt. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:NTNU_SB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0008283; P:cell population proliferation; TAS:ProtInc. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:0002376; P:immune system process; IBA:GO_Central. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:ProtInc. DR GO; GO:0032480; P:negative regulation of type I interferon production; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IDA:MGI. DR Proteomes; UP000005640; Chromosome 4. DR PathwayCommons; P14316; -. DR Pharos; P14316; Tbio. DR Antibodypedia; 17374; 605 antibodies from 48 providers. DR RNAct; P14316; protein. DR BioGRID-ORCS; 3660; 43 hits in 1196 CRISPR screens. DR AlphaFoldDB; P14316; -. DR FunCoup; P14316; 1788. DR PAN-GO; P14316; 5 GO annotations based on evolutionary models. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; Chromosome; KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; KW Proteomics identification; Reference proteome; Repressor; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..349 FT /note="Interferon regulatory factor 2" FT /id="PRO_0000154549" FT DNA_BIND 5..113 FT /note="IRF tryptophan pentad repeat" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00840" FT REGION 117..148 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 228..251 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 297..349 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 125..140 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 228..239 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 314..324 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 75 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:12738767" FT MOD_RES 78 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:12738767" FT MOD_RES 225 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT CROSSLNK 137 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000269|PubMed:18514056" FT CROSSLNK 137 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 166 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:18514056" FT CROSSLNK 260 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 293 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:18514056" FT VAR_SEQ 177..178 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_043965" FT MUTAGEN 75 FT /note="K->R: Diminished acetylation by both CREBBP/p300 and FT PCAF. Greatly reduced enhancement of H4 promoter activity." FT /evidence="ECO:0000269|PubMed:12738767" FT MUTAGEN 78 FT /note="K->R: Greatly diminished acetylation by PCAF. Lesser FT loss of acetylation by CREBBP/p300. Loss of DNA binding and FT no enhancement of H4 promoter activity." FT /evidence="ECO:0000269|PubMed:12738767" FT MUTAGEN 137 FT /note="K->R: Some loss of sumoylation. Increases FT IRF2-mediation activation of ISRE and H4 promoters. FT Increased inhibition of IRF1-mediated transcription. FT Additional small loss of sumoylation; when associated with FT R-166. Great loss of sumoylation; when associated with FT R-296. Abolishes sumoylation. Greatly increased activation FT of ISRE and H4 promoters and further increased ability to FT inhibit IRF1-mediated transcription; when associated with FT R-166 and R-293." FT /evidence="ECO:0000269|PubMed:18514056" FT MUTAGEN 166 FT /note="K->R: Little loss of sumoylation. Increases FT IRF2-mediation activation of ISRE and H4 promoters. FT Increased inhibition of IRF1-mediated transcription. FT Greater loss of sumoylation; when associated with R-137. FT Further loss of sumoylation; when associated with R-293. FT Abolishes sumoylation. Greatly increased activation of ISRE FT and H4 promoters and further increased ability to inhibit FT IRF1-mediated transcription; when associated with R-137 and FT R-293." FT /evidence="ECO:0000269|PubMed:18514056" FT MUTAGEN 293 FT /note="K->R: Some loss of sumoylation. Increases FT IRF2-mediation activation of ISRE and H4 promoters. FT Increased inhibition of IRF1-mediated transcription. FT Further small loss of sumoylation; when associated with FT R-166. Great loss of sumoylation; when associated with FT R-137. Abolishes sumoylation. Greatly increased activation FT of ISRE and H4 promoters and further increased ability to FT inhibit IRF1-mediated transcription; when associated with FT R-166 and R-293." FT /evidence="ECO:0000269|PubMed:18514056" FT CONFLICT 58 FT /note="W -> R (in Ref. 1; CAA34073)" FT /evidence="ECO:0000305" SQ SEQUENCE 349 AA; 39354 MW; 6298341652466560 CRC64; MPVERMRMRP WLEEQINSNT IPGLKWLNKE KKIFQIPWMH AARHGWDVEK DAPLFRNWAI HTGKHQPGVD KPDPKTWKAN FRCAMNSLPD IEEVKDKSIK KGNNAFRVYR MLPLSERPSK KGKKPKTEKE DKVKHIKQEP VESSLGLSNG VSDLSPEYAV LTSTIKNEVD STVNIIVVGQ SHLDSNIENQ EIVTNPPDIC QVVEVTTESD EQPVSMSELY PLQISPVSSY AESETTDSVP SDEESAEGRP HWRKRNIEGK QYLSNMGTRG SYLLPGMASF VTSNKPDLQV TIKEESNPVP YNSSWPPFQD LPLSSSMTPA SSSSRPDRET RASVIKKTSD ITQARVKSC //