ID   ILF2_MOUSE              Reviewed;         390 AA.
AC   Q9CXY6; Q3U083; Q5RKG0; Q8CCY9; Q99KS3;
DT   12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 158.
DE   RecName: Full=Interleukin enhancer-binding factor 2;
DE   AltName: Full=Nuclear factor of activated T-cells 45 kDa;
GN   Name=Ilf2; Synonyms=Nf45;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7519613; DOI=10.1016/s0021-9258(17)32048-3;
RA   Kao P.N., Chen L., Brock G., Ng J., Kenny J., Smith A.J., Corthesy B.;
RT   "Cloning and expression of cyclosporin A- and FK506-sensitive nuclear
RT   factor of activated T-cells: NF45 and NF90.";
RL   J. Biol. Chem. 269:20691-20699(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Head, Medulla oblongata, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Czech II; TISSUE=Mammary tumor;
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   [4]
RP   FUNCTION, AND INTERACTION WITH ILF3.
RX   PubMed=10574923; DOI=10.1074/jbc.274.49.34598;
RA   Satoh M., Shaheen V.M., Kao P.N., Okano T., Shaw M., Yoshida H.,
RA   Richards H.B., Reeves W.H.;
RT   "Autoantibodies define a family of proteins with conserved double-stranded
RT   RNA-binding domains as well as DNA binding activity.";
RL   J. Biol. Chem. 274:34598-34604(1999).
RN   [5]
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=11804788; DOI=10.1016/s0925-4773(01)00612-8;
RA   Lopez-Fernandez L.A., Parraga M., del Mazo J.;
RT   "Ilf2 is regulated during meiosis and associated to transcriptionally
RT   active chromatin.";
RL   Mech. Dev. 111:153-157(2002).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-16 AND ARG-24, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: Chromatin-interacting protein that forms a stable heterodimer
CC       with interleukin enhancer-binding factor 3/ILF3 and plays a role in
CC       several biological processes including transcription, innate immunity
CC       or cell growth (PubMed:10574923). Essential for the efficient
CC       reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus.
CC       Together with ILF3, forms an RNA-binding complex that is required for
CC       mitotic progression and cytokinesis by regulating the expression of a
CC       cluster of mitotic genes. Mechanistically, competes with STAU1/STAU2-
CC       mediated mRNA decay. Also plays a role in the inhibition of various
CC       viruses including Japanese encephalitis virus or enterovirus 71 (By
CC       similarity) (PubMed:10574923). {ECO:0000250|UniProtKB:Q12905,
CC       ECO:0000269|PubMed:10574923}.
CC   -!- SUBUNIT: Forms heterodimers with ILF3. ILF2-ILF3 heterodimers may also
CC       bind to PRKDC/XRCC7: this may stabilize the interaction of PRKDC/XRCC7
CC       and the heterodimeric complex of G22P1/KU70 and XRCC5/KU80. Forms a
CC       complex with ILF3, YLPM1, KHDRBS1, RBMX, NCOA5 and PPP1CA. Identified
CC       in a IGF2BP1-dependent mRNP granule complex containing untranslated
CC       mRNAs. Interacts with IGF2BP1. Interacts with CRBN; this interaction
CC       promotes ubiquitination and subsequent degradation of ILF2.
CC       {ECO:0000250|UniProtKB:Q12905}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000250|UniProtKB:Q12905}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q12905}. Nucleus {ECO:0000250|UniProtKB:Q12905}.
CC       Note=Localized in cytoplasmic mRNP granules containing untranslated
CC       mRNAs. {ECO:0000250|UniProtKB:Q12905}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, kidney and ovary; highly
CC       expressed in testis, particularly within pachytene cells.
CC       {ECO:0000269|PubMed:11804788}.
CC   -!- DEVELOPMENTAL STAGE: Expression in testis begins with developmental
CC       differentiation of pachytene spermatocytes.
CC       {ECO:0000269|PubMed:11804788}.
CC   -!- PTM: Ubiquitinated at Lys-45 by CRBN with polyubiquitin chains by the
CC       CUL4-RING E3 ligase (CRL4-CRBN) and then degraded by the proteasome.
CC       {ECO:0000250|UniProtKB:Q12905}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27594.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AF458249; AAL59388.1; -; Genomic_DNA.
DR   EMBL; AK013858; BAB29021.1; -; mRNA.
DR   EMBL; AK031892; BAC27594.1; ALT_SEQ; mRNA.
DR   EMBL; AK078003; BAC37097.1; -; mRNA.
DR   EMBL; AK157129; BAE33972.1; -; mRNA.
DR   EMBL; BC004033; AAH04033.1; -; mRNA.
DR   EMBL; BC024718; AAH24718.1; -; mRNA.
DR   CCDS; CCDS17530.1; -.
DR   RefSeq; NP_080650.1; NM_026374.3.
DR   PDB; 4AT7; X-ray; 1.90 A; A=29-390.
DR   PDB; 4AT8; X-ray; 2.69 A; A/C=29-390.
DR   PDB; 4AT9; X-ray; 2.80 A; A=29-390.
DR   PDB; 4ATB; X-ray; 3.10 A; A/C=29-390.
DR   PDBsum; 4AT7; -.
DR   PDBsum; 4AT8; -.
DR   PDBsum; 4AT9; -.
DR   PDBsum; 4ATB; -.
DR   AlphaFoldDB; Q9CXY6; -.
DR   SMR; Q9CXY6; -.
DR   BioGRID; 212438; 66.
DR   IntAct; Q9CXY6; 9.
DR   MINT; Q9CXY6; -.
DR   STRING; 10090.ENSMUSP00000001042; -.
DR   GlyGen; Q9CXY6; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9CXY6; -.
DR   PhosphoSitePlus; Q9CXY6; -.
DR   SwissPalm; Q9CXY6; -.
DR   EPD; Q9CXY6; -.
DR   jPOST; Q9CXY6; -.
DR   MaxQB; Q9CXY6; -.
DR   PaxDb; 10090-ENSMUSP00000001042; -.
DR   ProteomicsDB; 269476; -.
DR   Pumba; Q9CXY6; -.
DR   Antibodypedia; 1451; 474 antibodies from 39 providers.
DR   DNASU; 67781; -.
DR   Ensembl; ENSMUST00000001042.10; ENSMUSP00000001042.9; ENSMUSG00000001016.13.
DR   GeneID; 67781; -.
DR   KEGG; mmu:67781; -.
DR   UCSC; uc008qcj.1; mouse.
DR   AGR; MGI:1915031; -.
DR   CTD; 3608; -.
DR   MGI; MGI:1915031; Ilf2.
DR   VEuPathDB; HostDB:ENSMUSG00000001016; -.
DR   eggNOG; KOG3793; Eukaryota.
DR   GeneTree; ENSGT00940000154879; -.
DR   HOGENOM; CLU_064863_1_0_1; -.
DR   InParanoid; Q9CXY6; -.
DR   OMA; YLAIEMS; -.
DR   OrthoDB; 5388448at2759; -.
DR   PhylomeDB; Q9CXY6; -.
DR   TreeFam; TF320194; -.
DR   Reactome; R-MMU-6798695; Neutrophil degranulation.
DR   Reactome; R-MMU-9833482; PKR-mediated signaling.
DR   BioGRID-ORCS; 67781; 23 hits in 82 CRISPR screens.
DR   ChiTaRS; Ilf2; mouse.
DR   PRO; PR:Q9CXY6; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9CXY6; Protein.
DR   Bgee; ENSMUSG00000001016; Expressed in ventricular zone and 284 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; IDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   DisProt; DP01563; -.
DR   Gene3D; 1.10.1410.40; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   InterPro; IPR006561; DZF_dom.
DR   InterPro; IPR049402; DZF_dom_C.
DR   InterPro; IPR049401; DZF_dom_N.
DR   InterPro; IPR043519; NT_sf.
DR   PANTHER; PTHR46447; INTERLEUKIN ENHANCER-BINDING FACTOR; 1.
DR   PANTHER; PTHR46447:SF1; INTERLEUKIN ENHANCER-BINDING FACTOR 2; 1.
DR   Pfam; PF20965; DZF_C; 1.
DR   Pfam; PF07528; DZF_N; 1.
DR   SMART; SM00572; DZF; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   PROSITE; PS51703; DZF; 1.
DR   Genevisible; Q9CXY6; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Cytoplasm; DNA-binding; Isopeptide bond;
KW   Methylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..390
FT                   /note="Interleukin enhancer-binding factor 2"
FT                   /id="PRO_0000126064"
FT   DOMAIN          24..371
FT                   /note="DZF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01040"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..390
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         16
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         16
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         24
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         52
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12905"
FT   MOD_RES         68
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12905"
FT   MOD_RES         388
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12905"
FT   CROSSLNK        45
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q12905"
FT   CROSSLNK        186
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q12905"
FT   CROSSLNK        364
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q12905"
FT   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   HELIX           51..64
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   HELIX           68..90
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   TURN            94..98
FT                   /evidence="ECO:0007829|PDB:4AT8"
FT   STRAND          99..105
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   HELIX           106..110
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   STRAND          119..128
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   HELIX           132..149
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   STRAND          151..153
FT                   /evidence="ECO:0007829|PDB:4AT9"
FT   STRAND          156..160
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   STRAND          163..167
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   STRAND          172..179
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   HELIX           181..185
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   TURN            189..191
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   HELIX           195..214
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   HELIX           218..233
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   HELIX           235..237
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   HELIX           242..254
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   STRAND          256..260
FT                   /evidence="ECO:0007829|PDB:4ATB"
FT   HELIX           264..276
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   TURN            277..280
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   STRAND          292..294
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   HELIX           298..301
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   HELIX           304..322
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   HELIX           326..329
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   STRAND          332..334
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   HELIX           337..340
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   STRAND          344..346
FT                   /evidence="ECO:0007829|PDB:4AT7"
FT   STRAND          349..351
FT                   /evidence="ECO:0007829|PDB:4AT7"
SQ   SEQUENCE   390 AA;  43062 MW;  75BAD022DCD4EE01 CRC64;
     MRGDRGRGRG GRFGSRGGPG GGFRPFVPHI PFDFYLCEMA FPRVKPAPDE TSFSEALLKR
     NQDLAPNSAE QASILSLVTK INNVIDNLIV APGTFEVQIE EVRQVGSYKK GTMTTGHNVA
     DLVVILKILP TLEAVAALGN KVVESLRAQD PSEVLTMLTN ETGFEISSSD ATVKILITTV
     PPNLRKLDPE LHLDIKVLQS ALAAIRHARW FEENASQSTV KVLIRLLKDL RIRFPGFEPL
     TPWILDLLGH YAVMNNPTRQ PLALNVAYRR CLQILAAGLF LPGSVGITDP CESGNFRVHT
     VMTLEQQDMV CYTAQTLVRI LSHGGFRKIL GQEGDASYLA SEISTWDGVI VTPSEKAYEK
     PPEKKEGEEE EENTEEPPQG EEEESMETQE
//