IRF2_HUMAN
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 03-AUG-2022, entry version 196.
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}.
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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; 98.
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; P14316; -.
DR PeptideAtlas; P14316; -.
DR PRIDE; P14316; -.
DR ProteomicsDB; 53043; -. [P14316-1]
DR ProteomicsDB; 53044; -. [P14316-2]
DR Antibodypedia; 17374; 542 antibodies from 45 providers.
DR DNASU; 3660; -.
DR Ensembl; ENST00000393593.8; ENSP00000377218.3; ENSG00000168310.11. [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 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; NAEGRPH; -.
DR OrthoDB; 734108at2759; -.
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; 40 hits in 1115 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 161 other tissues.
DR ExpressionAtlas; P14316; baseline and differential.
DR Genevisible; P14316; HS.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR CDD; cd00103; IRF; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR019817; Interferon_reg_fac_CS.
DR InterPro; IPR001346; Interferon_reg_fact_DNA-bd_dom.
DR InterPro; IPR017431; IRF1/IRF2.
DR InterPro; IPR031218; IRF2.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11949:SF22; PTHR11949:SF22; 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; SSF46785; 1.
DR PROSITE; PS00601; IRF_1; 1.
DR PROSITE; PS51507; IRF_2; 1.
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 IRF2-
FT mediation activation of ISRE and H4 promoters. Increased
FT inhibition of IRF1-mediated transcription. Additional small
FT loss of sumoylation; when associated with R-166. Great loss
FT of sumoylation; when associated with R-296. Abolishes
FT sumoylation. Greatly increased activation of ISRE and H4
FT promoters and further increased ability to inhibit IRF1-
FT mediated transcription; when associated with R-166 and R-
FT 293."
FT /evidence="ECO:0000269|PubMed:18514056"
FT MUTAGEN 166
FT /note="K->R: Little loss of sumoylation. Increases IRF2-
FT mediation activation of ISRE and H4 promoters. Increased
FT inhibition of IRF1-mediated transcription. Greater loss of
FT sumoylation; when associated with R-137. Further loss of
FT sumoylation; when associated with R-293. Abolishes
FT sumoylation. Greatly increased activation of ISRE and H4
FT promoters and further increased ability to inhibit IRF1-
FT mediated transcription; when associated with R-137 and R-
FT 293."
FT /evidence="ECO:0000269|PubMed:18514056"
FT MUTAGEN 293
FT /note="K->R: Some loss of sumoylation. Increases IRF2-
FT mediation activation of ISRE and H4 promoters. Increased
FT inhibition of IRF1-mediated transcription. Further small
FT loss of sumoylation; when associated with R-166. Great loss
FT of sumoylation; when associated with R-137. Abolishes
FT sumoylation. Greatly increased activation of ISRE and H4
FT promoters and further increased ability to inhibit IRF1-
FT mediated transcription; when associated with R-166 and R-
FT 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
