ILF2_HUMAN
ID ILF2_HUMAN Reviewed; 390 AA.
AC Q12905; A6NDB0; B2R8G7; Q5SR10; Q5SR11; Q7L7R3; Q9BWD4; Q9P1N0;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Interleukin enhancer-binding factor 2;
DE AltName: Full=Nuclear factor of activated T-cells 45 kDa;
GN Name=ILF2; Synonyms=NF45; ORFNames=PRO3063;
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 [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 62-75; 82-102
RP AND 330-343, AND SUBCELLULAR LOCATION.
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 TISSUE=Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-390.
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Zhou W.,
RA Bi J., Zhang Y., Liu M., He F.;
RT "Functional prediction of the coding sequences of 32 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH G22P1;
RP PRKDC AND XRCC5.
RX PubMed=9442054; DOI=10.1074/jbc.273.4.2136;
RA Ting N.S.Y., Kao P.N., Chan D.W., Lintott L.G., Lees-Miller S.P.;
RT "DNA-dependent protein kinase interacts with antigen receptor response
RT element binding proteins NF90 and NF45.";
RL J. Biol. Chem. 273:2136-2145(1998).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=11790298; DOI=10.1016/s0960-9822(01)00650-9;
RA Andersen J.S., Lyon C.E., Fox A.H., Leung A.K.L., Lam Y.W., Steen H.,
RA Mann M., Lamond A.I.;
RT "Directed proteomic analysis of the human nucleolus.";
RL Curr. Biol. 12:1-11(2002).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271;
RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
RA Greco A., Hochstrasser D.F., Diaz J.-J.;
RT "Functional proteomic analysis of human nucleolus.";
RL Mol. Biol. Cell 13:4100-4109(2002).
RN [11]
RP FUNCTION, AND INTERACTION WITH ILF3.
RX PubMed=11739746; DOI=10.1128/mcb.22.1.343-356.2002;
RA Reichman T.W., Muniz L.C., Mathews M.B.;
RT "The RNA binding protein nuclear factor 90 functions as both a positive and
RT negative regulator of gene expression in mammalian cells.";
RL Mol. Cell. Biol. 22:343-356(2002).
RN [12]
RP IDENTIFICATION IN A COMPLEX WITH ILF3; YLPM1; KHDRBS1; RBMX; NCOA5 AND
RP PPP1CA.
RX PubMed=17890166; DOI=10.1016/j.bbapap.2007.07.015;
RA Ulke-Lemee A., Trinkle-Mulcahy L., Chaulk S., Bernstein N.K., Morrice N.,
RA Glover M., Lamond A.I., Moorhead G.B.G.;
RT "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside
RT kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-G.";
RL Biochim. Biophys. Acta 1774:1339-1350(2007).
RN [13]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17289661; DOI=10.1074/mcp.m600346-mcp200;
RA Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R.,
RA Johnsen A.H., Christiansen J., Nielsen F.C.;
RT "Molecular composition of IMP1 ribonucleoprotein granules.";
RL Mol. Cell. Proteomics 6:798-811(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-388, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [15]
RP FUNCTION, AND INTERACTION WITH ILF3.
RX PubMed=18458058; DOI=10.1128/mcb.00120-08;
RA Guan D., Altan-Bonnet N., Parrott A.M., Arrigo C.J., Li Q.,
RA Khaleduzzaman M., Li H., Lee C.G., Pe'ery T., Mathews M.B.;
RT "Nuclear factor 45 (NF45) is a regulatory subunit of complexes with
RT NF90/110 involved in mitotic control.";
RL Mol. Cell. Biol. 28:4629-4641(2008).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21123651; DOI=10.1101/gad.1965010;
RA Harashima A., Guettouche T., Barber G.N.;
RT "Phosphorylation of the NFAR proteins by the dsRNA-dependent protein kinase
RT PKR constitutes a novel mechanism of translational regulation and cellular
RT defense.";
RL Genes Dev. 24:2640-2653(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-68, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP IDENTIFICATION BY 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 [20]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-16 AND ARG-24, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
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).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [22]
RP FUNCTION (MICROBIAL INFECTION).
RX PubMed=26891316; DOI=10.3390/v8020047;
RA Li Y., Belshan M.;
RT "NF45 and NF90 Bind HIV-1 RNA and Modulate HIV Gene Expression.";
RL Viruses 8:0-0(2016).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-186 AND LYS-364, 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 [24]
RP FUNCTION, INTERACTION WITH JAPANESE ENCEPHALITIS VIRUS NS3 (MICROBIAL
RP INFECTION), AND SUBCELLULAR LOCATION.
RX PubMed=31212927; DOI=10.3390/v11060559;
RA Cui X., Qian P., Rao T., Wei Y., Zhao F., Zhang H., Chen H., Li X.;
RT "Cellular Interleukin Enhancer-Binding Factor 2, ILF2, Inhibits Japanese
RT Encephalitis Virus Replication In Vitro.";
RL Viruses 11:0-0(2019).
RN [25]
RP FUNCTION, INTERACTION WITH ENTEROVIRUS 71 PROTEIN 2B (MICROBIAL INFECTION),
RP AND SUBCELLULAR LOCATION.
RX PubMed=31878072; DOI=10.3390/v12010022;
RA Jin J., Wang W., Ai S., Liu W., Song Y., Luo Z., Zhang Q., Wu K., Liu Y.,
RA Wu J.;
RT "Enterovirus 71 Represses Interleukin Enhancer-Binding Factor 2 Production
RT and Nucleus Translocation to Antagonize ILF2 Antiviral Effects.";
RL Viruses 12:0-0(2019).
RN [26]
RP FUNCTION.
RX PubMed=32433969; DOI=10.1016/j.celrep.2020.107660;
RA Nourreddine S., Lavoie G., Paradis J., Ben El Kadhi K., Meant A.,
RA Aubert L., Grondin B., Gendron P., Chabot B., Bouvier M., Carreno S.,
RA Roux P.P.;
RT "NF45 and NF90 Regulate Mitotic Gene Expression by Competing with Staufen-
RT Mediated mRNA Decay.";
RL Cell Rep. 31:107660-107660(2020).
RN [27]
RP UBIQUITINATION AT LYS-45, MUTAGENESIS OF LYS-45, AND INTERACTION WITH CRBN.
RX PubMed=33009960; DOI=10.1007/s10930-020-09918-9;
RA Lian Q., Gao Y., Li Q., He X., Jiang X., Pu Z., Xu G.;
RT "Cereblon Promotes the Ubiquitination and Proteasomal Degradation of
RT Interleukin Enhancer-Binding Factor 2.";
RL Protein J. 39:411-421(2020).
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:18458058, PubMed:31212927). Essential for the
CC efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the
CC nucleus. Together with ILF3, forms an RNA-binding complex that is
CC required for mitotic progression and cytokinesis by regulating the
CC expression of a cluster of mitotic genes. Mechanistically, competes
CC with STAU1/STAU2-mediated mRNA decay (PubMed:32433969). Also plays a
CC role in the inhibition of various viruses including Japanese
CC encephalitis virus or enterovirus 71. {ECO:0000269|PubMed:10574923,
CC ECO:0000269|PubMed:11739746, ECO:0000269|PubMed:18458058,
CC ECO:0000269|PubMed:21123651, ECO:0000269|PubMed:31212927,
CC ECO:0000269|PubMed:32433969, ECO:0000269|PubMed:9442054}.
CC -!- FUNCTION: (Microbial infection) Plays a positive role in HIV-1 virus
CC production by binding to and thereby stabilizing HIV-1 RNA, together
CC with ILF3. {ECO:0000269|PubMed:26891316}.
CC -!- SUBUNIT: Forms heterodimers with ILF3 (PubMed:18458058). ILF2-ILF3
CC heterodimers may also bind to PRKDC/XRCC7: this may stabilize the
CC interaction of PRKDC/XRCC7 and the heterodimeric complex of G22P1/KU70
CC and XRCC5/KU80. Forms a complex with ILF3, YLPM1, KHDRBS1, RBMX, NCOA5
CC and PPP1CA. Identified in a IGF2BP1-dependent mRNP granule complex
CC containing untranslated mRNAs. Interacts with IGF2BP1. Interacts with
CC CRBN; this interaction promotes ubiquitination and subsequent
CC degradation of ILF2 (PubMed:33009960). {ECO:0000269|PubMed:10574923,
CC ECO:0000269|PubMed:11739746, ECO:0000269|PubMed:17289661,
CC ECO:0000269|PubMed:17890166, ECO:0000269|PubMed:18458058,
CC ECO:0000269|PubMed:33009960, ECO:0000269|PubMed:9442054}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Japanese encephalitis
CC virus protein NS3. {ECO:0000269|PubMed:31212927}.
CC -!- SUBUNIT: (Microbial infection) Interacts with enterovirus 71 protein
CC 2B; this interaction relocalizes ILF2 from the nucleus to the
CC cytoplasm. {ECO:0000269|PubMed:31878072}.
CC -!- INTERACTION:
CC Q12905; Q0VD86: INCA1; NbExp=3; IntAct=EBI-357925, EBI-6509505;
CC Q12905; P46940: IQGAP1; NbExp=3; IntAct=EBI-357925, EBI-297509;
CC Q12905; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-357925, EBI-16439278;
CC Q12905; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-357925, EBI-79165;
CC Q12905; Q08752: PPID; NbExp=4; IntAct=EBI-357925, EBI-716596;
CC Q12905; P14373: TRIM27; NbExp=3; IntAct=EBI-357925, EBI-719493;
CC Q12905; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-357925, EBI-12030590;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm
CC {ECO:0000269|PubMed:31212927, ECO:0000269|PubMed:31878072}. Nucleus
CC {ECO:0000269|PubMed:31878072}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs.
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:0000269|PubMed:33009960}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA20993.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF29591.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA.; Evidence={ECO:0000305};
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DR EMBL; U10323; AAA20993.1; ALT_FRAME; mRNA.
DR EMBL; AY099265; AAM45141.1; -; Genomic_DNA.
DR EMBL; AK313364; BAG36164.1; -; mRNA.
DR EMBL; AL592150; CAI18796.1; -; Genomic_DNA.
DR EMBL; AL713889; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53286.1; -; Genomic_DNA.
DR EMBL; BC000382; AAH00382.1; -; mRNA.
DR EMBL; AF113702; AAF29591.1; ALT_SEQ; mRNA.
DR CCDS; CCDS1050.1; -.
DR PIR; A54857; A54857.
DR RefSeq; NP_001254738.1; NM_001267809.1.
DR RefSeq; NP_004506.2; NM_004515.3.
DR AlphaFoldDB; Q12905; -.
DR SMR; Q12905; -.
DR BioGRID; 109821; 467.
DR CORUM; Q12905; -.
DR IntAct; Q12905; 169.
DR MINT; Q12905; -.
DR STRING; 9606.ENSP00000355011; -.
DR ChEMBL; CHEMBL4295811; -.
DR GlyGen; Q12905; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12905; -.
DR PhosphoSitePlus; Q12905; -.
DR SwissPalm; Q12905; -.
DR BioMuta; ILF2; -.
DR DMDM; 62510764; -.
DR SWISS-2DPAGE; Q12905; -.
DR CPTAC; CPTAC-223; -.
DR CPTAC; CPTAC-224; -.
DR EPD; Q12905; -.
DR jPOST; Q12905; -.
DR MassIVE; Q12905; -.
DR MaxQB; Q12905; -.
DR PaxDb; Q12905; -.
DR PeptideAtlas; Q12905; -.
DR PRIDE; Q12905; -.
DR ProteomicsDB; 59013; -.
DR Antibodypedia; 1451; 425 antibodies from 39 providers.
DR DNASU; 3608; -.
DR Ensembl; ENST00000361891.9; ENSP00000355011.4; ENSG00000143621.17.
DR GeneID; 3608; -.
DR KEGG; hsa:3608; -.
DR MANE-Select; ENST00000361891.9; ENSP00000355011.4; NM_004515.4; NP_004506.2.
DR UCSC; uc001fcr.5; human.
DR CTD; 3608; -.
DR DisGeNET; 3608; -.
DR GeneCards; ILF2; -.
DR HGNC; HGNC:6037; ILF2.
DR HPA; ENSG00000143621; Low tissue specificity.
DR MIM; 603181; gene.
DR neXtProt; NX_Q12905; -.
DR OpenTargets; ENSG00000143621; -.
DR PharmGKB; PA29852; -.
DR VEuPathDB; HostDB:ENSG00000143621; -.
DR eggNOG; KOG3793; Eukaryota.
DR GeneTree; ENSGT00940000154879; -.
DR InParanoid; Q12905; -.
DR OMA; MEGDASY; -.
DR OrthoDB; 1145212at2759; -.
DR PhylomeDB; Q12905; -.
DR TreeFam; TF320194; -.
DR PathwayCommons; Q12905; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q12905; -.
DR SIGNOR; Q12905; -.
DR BioGRID-ORCS; 3608; 627 hits in 1085 CRISPR screens.
DR ChiTaRS; ILF2; human.
DR GeneWiki; ILF2; -.
DR GenomeRNAi; 3608; -.
DR Pharos; Q12905; Tbio.
DR PRO; PR:Q12905; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q12905; protein.
DR Bgee; ENSG00000143621; Expressed in ganglionic eminence and 206 other tissues.
DR ExpressionAtlas; Q12905; baseline and differential.
DR Genevisible; Q12905; HS.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR DisProt; DP01564; -.
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 Activator; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..390
FT /note="Interleukin enhancer-binding factor 2"
FT /id="PRO_0000126063"
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:0000250|UniProtKB:Q9CXY6"
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:0007744|PubMed:23186163"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 388
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT CROSSLNK 45
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:33009960"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 364
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 45
FT /note="K->R: Completely abolishes the effect of CRBN on
FT ILF2."
FT /evidence="ECO:0000269|PubMed:33009960"
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
