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 24-JAN-2024, entry version 204. DE RecName: Full=Interferon regulatory factor 2; DE Short=IRF-2; 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 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 [10] 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 [11] 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 [12] 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 [13] RP 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 [14] 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 [15] 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 [16] 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 [17] 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 [18] 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). CC -!- FUNCTION: Specifically binds to the upstream regulatory region of type CC I IFN and IFN-inducible MHC class I genes (the interferon consensus CC sequence (ICS)) and represses those genes. Also acts as an activator CC for several genes including H4 and IL7. Constitutively binds to the CC ISRE promoter to activate IL7. Involved in cell cycle regulation CC through binding the site II (HiNF-M) promoter region of H4 and CC activating transcription during cell growth. Antagonizes IRF1 CC transcriptional activation. {ECO:0000269|PubMed:12738767, CC ECO:0000269|PubMed:15226432, ECO:0000269|PubMed:18514056, CC ECO:0000269|PubMed:9540062}. CC -!- SUBUNIT: Interacts with BRD7, IRF2BP1 and IRF2BP2. Interacts with CC CREBBP in growing cells; the interaction acetylates IRF2 and regulates CC IRF2-dependent H4 promoter activity. {ECO:0000269|PubMed:11025449, CC ECO:0000269|PubMed:12738767, ECO:0000269|PubMed:12799427}. CC -!- INTERACTION: CC P14316; O95352: ATG7; NbExp=2; IntAct=EBI-2866589, EBI-987834; CC P14316; P85037: FOXK1; NbExp=3; IntAct=EBI-2866589, EBI-2509974; CC P14316; Q01167: FOXK2; NbExp=4; IntAct=EBI-2866589, EBI-2509991; CC P14316; P16298: PPP3CB; NbExp=2; IntAct=EBI-2866589, EBI-1759540; CC -!- SUBCELLULAR LOCATION: Nucleus. 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. 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 -!- MISCELLANEOUS: [Isoform 2]: Unable to bind to IRF2BP1 and IRF2BP2 CC corepressors and cannot mediate repression. {ECO:0000305}. 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_002199.3. [P14316-1] DR AlphaFoldDB; P14316; -. DR BMRB; P14316; -. DR SMR; P14316; -. DR BioGRID; 109868; 99. DR ELM; P14316; -. DR IntAct; P14316; 82. DR MINT; P14316; -. DR STRING; 9606.ENSP00000377218; -. DR GlyGen; P14316; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P14316; -. DR PhosphoSitePlus; P14316; -. DR BioMuta; IRF2; -. DR DMDM; 20141499; -. DR EPD; P14316; -. DR jPOST; P14316; -. DR MassIVE; P14316; -. DR MaxQB; P14316; -. DR PaxDb; 9606-ENSP00000377218; -. DR PeptideAtlas; P14316; -. DR ProteomicsDB; 53043; -. [P14316-1] DR ProteomicsDB; 53044; -. [P14316-2] DR Pumba; P14316; -. DR Antibodypedia; 17374; 614 antibodies from 45 providers. DR DNASU; 3660; -. DR Ensembl; ENST00000393593.8; ENSP00000377218.3; ENSG00000168310.12. [P14316-1] DR Ensembl; ENST00000504340.2; ENSP00000512878.1; ENSG00000168310.12. [P14316-1] DR Ensembl; ENST00000510814.6; ENSP00000424552.2; ENSG00000168310.12. [P14316-1] DR Ensembl; ENST00000696840.1; ENSP00000512918.1; ENSG00000168310.12. [P14316-1] DR Ensembl; ENST00000696841.1; ENSP00000512954.1; ENSG00000168310.12. [P14316-1] DR Ensembl; ENST00000696843.1; ENSP00000512920.1; ENSG00000168310.12. [P14316-1] DR Ensembl; ENST00000696845.1; ENSP00000512922.1; ENSG00000168310.12. [P14316-1] DR Ensembl; ENST00000696846.1; ENSP00000512923.1; ENSG00000168310.12. [P14316-1] DR Ensembl; ENST00000696848.1; ENSP00000512924.1; ENSG00000168310.12. [P14316-2] DR Ensembl; ENST00000696849.1; ENSP00000512925.1; ENSG00000168310.12. [P14316-1] DR Ensembl; ENST00000696851.1; ENSP00000512927.1; ENSG00000168310.12. [P14316-1] DR Ensembl; ENST00000696853.1; ENSP00000512929.1; ENSG00000168310.12. [P14316-2] 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 AGR; HGNC:6117; -. DR CTD; 3660; -. DR DisGeNET; 3660; -. DR GeneCards; IRF2; -. DR HGNC; HGNC:6117; IRF2. DR HPA; ENSG00000168310; Low tissue specificity. DR MIM; 147576; gene. DR neXtProt; NX_P14316; -. DR OpenTargets; ENSG00000168310; -. DR PharmGKB; PA29916; -. DR VEuPathDB; HostDB:ENSG00000168310; -. DR eggNOG; ENOG502QW7C; Eukaryota. DR GeneTree; ENSGT00940000159063; -. DR HOGENOM; CLU_056386_0_0_1; -. DR InParanoid; P14316; -. DR OMA; SSWPPFA; -. DR OrthoDB; 3740806at2759; -. DR PhylomeDB; P14316; -. DR TreeFam; TF328512; -. DR PathwayCommons; 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 BioGRID-ORCS; 3660; 43 hits in 1196 CRISPR screens. DR ChiTaRS; IRF2; human. DR GeneWiki; IRF2; -. DR GenomeRNAi; 3660; -. DR Pharos; P14316; Tbio. DR PRO; PR:P14316; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P14316; Protein. DR Bgee; ENSG00000168310; Expressed in monocyte and 163 other cell types or tissues. DR ExpressionAtlas; P14316; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005925; C:focal adhesion; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. 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; IMP:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. 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: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: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; IBA:GO_Central. DR CDD; cd00103; IRF; 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 Genevisible; P14316; HS. PE 1: Evidence at protein level; KW Acetylation; Activator; Alternative splicing; DNA-binding; Isopeptide bond; KW Nucleus; Phosphoprotein; 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 117..139 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 297..328 FT /note="Polar residues" 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 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 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 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 //