ILF2_MOUSE
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 03-AUG-2022, entry version 150.
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 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; 65.
DR IntAct; Q9CXY6; 9.
DR MINT; Q9CXY6; -.
DR STRING; 10090.ENSMUSP00000001042; -.
DR iPTMnet; Q9CXY6; -.
DR PhosphoSitePlus; Q9CXY6; -.
DR EPD; Q9CXY6; -.
DR jPOST; Q9CXY6; -.
DR MaxQB; Q9CXY6; -.
DR PaxDb; Q9CXY6; -.
DR PRIDE; Q9CXY6; -.
DR ProteomicsDB; 269476; -.
DR Antibodypedia; 1451; 425 antibodies from 39 providers.
DR DNASU; 67781; -.
DR Ensembl; ENSMUST00000001042; ENSMUSP00000001042; ENSMUSG00000001016.
DR GeneID; 67781; -.
DR KEGG; mmu:67781; -.
DR UCSC; uc008qcj.1; mouse.
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; MEGDASY; -.
DR OrthoDB; 1145212at2759; -.
DR PhylomeDB; Q9CXY6; -.
DR TreeFam; TF320194; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 67781; 21 hits in 77 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 281 other tissues.
DR Genevisible; Q9CXY6; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 transcription, DNA-templated; ISS:UniProtKB.
DR DisProt; DP01563; -.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR006561; DZF_dom.
DR InterPro; IPR043519; NT_sf.
DR Pfam; PF07528; DZF; 1.
DR SMART; SM00572; DZF; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS51703; DZF; 1.
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
