Full text data of ILF2
ILF2
(NF45)
[Confidence: low (only semi-automatic identification from reviews)]
Interleukin enhancer-binding factor 2 (Nuclear factor of activated T-cells 45 kDa)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Interleukin enhancer-binding factor 2 (Nuclear factor of activated T-cells 45 kDa)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q12905
ID ILF2_HUMAN Reviewed; 390 AA.
AC Q12905; A6NDB0; B2R8G7; Q5SR10; Q5SR11; Q7L7R3; Q9BWD4; Q9P1N0;
read moreDT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 22-JAN-2014, entry version 113.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 62-75;
RP 82-102 AND 330-343, AND SUBCELLULAR LOCATION.
RX PubMed=7519613;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Zhou W., Bi J., Zhang Y., Liu M., He F.;
RT "Functional prediction of the coding sequences of 32 new genes deduced
RT by 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
RP G22P1; 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-
RT stranded 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], AND MASS SPECTROMETRY.
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
RT positive and negative regulator of gene expression in mammalian
RT 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.,
RA Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.;
RT "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative
RT nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-
RT G.";
RL Biochim. Biophys. Acta 1774:1339-1350(2007).
RN [13]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1,
RP AND 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 MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 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
RT kinase PKR constitutes a novel mechanism of translational regulation
RT and cellular defense.";
RL Genes Dev. 24:2640-2653(2010).
RN [16]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Appears to function predominantly as a heterodimeric
CC complex with ILF3. This complex may regulate transcription of the
CC IL2 gene during T-cell activation. It can also promote the
CC formation of stable DNA-dependent protein kinase holoenzyme
CC complexes on DNA. Essential for the efficient reshuttling of ILF3
CC (isoform 1 and isoform 2) into the nucleus.
CC -!- SUBUNIT: Forms heterodimers with ILF3. ILF2-ILF3 heterodimers may
CC also bind to PRKDC/XRCC7: this may stabilize the interaction of
CC PRKDC/XRCC7 and the heterodimeric complex of G22P1/KU70 and
CC 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.
CC -!- INTERACTION:
CC Q08752:PPID; NbExp=4; IntAct=EBI-357925, EBI-716596;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Nucleus.
CC Note=Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs.
CC -!- SIMILARITY: Contains 1 DZF domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA20993.1; Type=Frameshift; Positions=376;
CC Sequence=AAF29591.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA;
CC Sequence=CAI13611.1; Type=Erroneous gene model prediction;
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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; AL713889; CAI13610.1; -; Genomic_DNA.
DR EMBL; AL713889; CAI13611.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL713889; CAI13612.1; -; Genomic_DNA.
DR EMBL; AL592150; CAI13612.1; JOINED; Genomic_DNA.
DR EMBL; AL592150; CAI18796.1; -; Genomic_DNA.
DR EMBL; AL713889; CAI18796.1; JOINED; Genomic_DNA.
DR EMBL; CH471121; EAW53286.1; -; Genomic_DNA.
DR EMBL; BC000382; AAH00382.1; -; mRNA.
DR EMBL; AF113702; AAF29591.1; ALT_SEQ; mRNA.
DR PIR; A54857; A54857.
DR RefSeq; NP_001254738.1; NM_001267809.1.
DR RefSeq; NP_004506.2; NM_004515.3.
DR UniGene; Hs.75117; -.
DR ProteinModelPortal; Q12905; -.
DR SMR; Q12905; 29-361.
DR IntAct; Q12905; 55.
DR MINT; MINT-4999942; -.
DR STRING; 9606.ENSP00000355011; -.
DR PhosphoSite; Q12905; -.
DR DMDM; 62510764; -.
DR SWISS-2DPAGE; Q12905; -.
DR PaxDb; Q12905; -.
DR PRIDE; Q12905; -.
DR DNASU; 3608; -.
DR Ensembl; ENST00000361891; ENSP00000355011; ENSG00000143621.
DR GeneID; 3608; -.
DR KEGG; hsa:3608; -.
DR UCSC; uc001fcr.4; human.
DR CTD; 3608; -.
DR GeneCards; GC01M153634; -.
DR HGNC; HGNC:6037; ILF2.
DR HPA; HPA007484; -.
DR MIM; 603181; gene.
DR neXtProt; NX_Q12905; -.
DR PharmGKB; PA29852; -.
DR eggNOG; NOG247512; -.
DR HOVERGEN; HBG052120; -.
DR InParanoid; Q12905; -.
DR KO; K13089; -.
DR OMA; FEENAHH; -.
DR OrthoDB; EOG75XGM4; -.
DR ChiTaRS; ILF2; human.
DR GeneWiki; ILF2; -.
DR GenomeRNAi; 3608; -.
DR NextBio; 14105; -.
DR PRO; PR:Q12905; -.
DR ArrayExpress; Q12905; -.
DR Bgee; Q12905; -.
DR CleanEx; HS_ILF2; -.
DR Genevestigator; Q12905; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IDA:UniProtKB.
DR InterPro; IPR006116; 2-5-oligoadenylate_synth_N.
DR InterPro; IPR006561; DZF.
DR Pfam; PF07528; DZF; 1.
DR SMART; SM00572; DZF; 1.
PE 1: Evidence at protein level;
KW Activator; Complete proteome; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1 390 Interleukin enhancer-binding factor 2.
FT /FTId=PRO_0000126063.
FT DOMAIN 104 338 DZF.
FT COMPBIAS 366 372 Poly-Glu.
FT COMPBIAS 381 384 Poly-Glu.
FT MOD_RES 388 388 Phosphothreonine.
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
//
ID ILF2_HUMAN Reviewed; 390 AA.
AC Q12905; A6NDB0; B2R8G7; Q5SR10; Q5SR11; Q7L7R3; Q9BWD4; Q9P1N0;
read moreDT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 2.
DT 22-JAN-2014, entry version 113.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], PROTEIN SEQUENCE OF 62-75;
RP 82-102 AND 330-343, AND SUBCELLULAR LOCATION.
RX PubMed=7519613;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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.,
RA Zhou W., Bi J., Zhang Y., Liu M., He F.;
RT "Functional prediction of the coding sequences of 32 new genes deduced
RT by 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
RP G22P1; 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-
RT stranded 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], AND MASS SPECTROMETRY.
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
RT positive and negative regulator of gene expression in mammalian
RT 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.,
RA Morrice N., Glover M., Lamond A.I., Moorhead G.B.G.;
RT "The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative
RT nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-
RT G.";
RL Biochim. Biophys. Acta 1774:1339-1350(2007).
RN [13]
RP IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1,
RP AND 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 MASS
RP SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA Lerenthal Y., Shiloh Y., 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 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
RT kinase PKR constitutes a novel mechanism of translational regulation
RT and cellular defense.";
RL Genes Dev. 24:2640-2653(2010).
RN [16]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Appears to function predominantly as a heterodimeric
CC complex with ILF3. This complex may regulate transcription of the
CC IL2 gene during T-cell activation. It can also promote the
CC formation of stable DNA-dependent protein kinase holoenzyme
CC complexes on DNA. Essential for the efficient reshuttling of ILF3
CC (isoform 1 and isoform 2) into the nucleus.
CC -!- SUBUNIT: Forms heterodimers with ILF3. ILF2-ILF3 heterodimers may
CC also bind to PRKDC/XRCC7: this may stabilize the interaction of
CC PRKDC/XRCC7 and the heterodimeric complex of G22P1/KU70 and
CC 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.
CC -!- INTERACTION:
CC Q08752:PPID; NbExp=4; IntAct=EBI-357925, EBI-716596;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Cytoplasm. Nucleus.
CC Note=Localized in cytoplasmic mRNP granules containing
CC untranslated mRNAs.
CC -!- SIMILARITY: Contains 1 DZF domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA20993.1; Type=Frameshift; Positions=376;
CC Sequence=AAF29591.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA;
CC Sequence=CAI13611.1; Type=Erroneous gene model prediction;
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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; AL713889; CAI13610.1; -; Genomic_DNA.
DR EMBL; AL713889; CAI13611.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL713889; CAI13612.1; -; Genomic_DNA.
DR EMBL; AL592150; CAI13612.1; JOINED; Genomic_DNA.
DR EMBL; AL592150; CAI18796.1; -; Genomic_DNA.
DR EMBL; AL713889; CAI18796.1; JOINED; Genomic_DNA.
DR EMBL; CH471121; EAW53286.1; -; Genomic_DNA.
DR EMBL; BC000382; AAH00382.1; -; mRNA.
DR EMBL; AF113702; AAF29591.1; ALT_SEQ; mRNA.
DR PIR; A54857; A54857.
DR RefSeq; NP_001254738.1; NM_001267809.1.
DR RefSeq; NP_004506.2; NM_004515.3.
DR UniGene; Hs.75117; -.
DR ProteinModelPortal; Q12905; -.
DR SMR; Q12905; 29-361.
DR IntAct; Q12905; 55.
DR MINT; MINT-4999942; -.
DR STRING; 9606.ENSP00000355011; -.
DR PhosphoSite; Q12905; -.
DR DMDM; 62510764; -.
DR SWISS-2DPAGE; Q12905; -.
DR PaxDb; Q12905; -.
DR PRIDE; Q12905; -.
DR DNASU; 3608; -.
DR Ensembl; ENST00000361891; ENSP00000355011; ENSG00000143621.
DR GeneID; 3608; -.
DR KEGG; hsa:3608; -.
DR UCSC; uc001fcr.4; human.
DR CTD; 3608; -.
DR GeneCards; GC01M153634; -.
DR HGNC; HGNC:6037; ILF2.
DR HPA; HPA007484; -.
DR MIM; 603181; gene.
DR neXtProt; NX_Q12905; -.
DR PharmGKB; PA29852; -.
DR eggNOG; NOG247512; -.
DR HOVERGEN; HBG052120; -.
DR InParanoid; Q12905; -.
DR KO; K13089; -.
DR OMA; FEENAHH; -.
DR OrthoDB; EOG75XGM4; -.
DR ChiTaRS; ILF2; human.
DR GeneWiki; ILF2; -.
DR GenomeRNAi; 3608; -.
DR NextBio; 14105; -.
DR PRO; PR:Q12905; -.
DR ArrayExpress; Q12905; -.
DR Bgee; Q12905; -.
DR CleanEx; HS_ILF2; -.
DR Genevestigator; Q12905; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:UniProtKB.
DR GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-dependent; IDA:UniProtKB.
DR InterPro; IPR006116; 2-5-oligoadenylate_synth_N.
DR InterPro; IPR006561; DZF.
DR Pfam; PF07528; DZF; 1.
DR SMART; SM00572; DZF; 1.
PE 1: Evidence at protein level;
KW Activator; Complete proteome; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1 390 Interleukin enhancer-binding factor 2.
FT /FTId=PRO_0000126063.
FT DOMAIN 104 338 DZF.
FT COMPBIAS 366 372 Poly-Glu.
FT COMPBIAS 381 384 Poly-Glu.
FT MOD_RES 388 388 Phosphothreonine.
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
//
MIM
603181
*RECORD*
*FIELD* NO
603181
*FIELD* TI
*603181 INTERLEUKIN ENHANCER-BINDING FACTOR 2; ILF2
;;NUCLEAR FACTOR OF ACTIVATED T CELLS, 45-KD; NF45
read more*FIELD* TX
CLONING
Nuclear factor of activated T cells (NFAT; see 600490) is a
transcription factor required for T-cell expression of interleukin-2
(IL2; 147680). NFAT binds to a sequence known as the antigen receptor
response element-2 (ARRE2) in the IL2 enhancer. Purified NFAT contains
45- and 90-kD subunits. Kao et al. (1994) cloned cDNAs encoding NF45 and
NF90 (603182). The NF45 gene encodes a 405-amino acid polypeptide with
distant similarity to DNA topoisomerase II (126430) and a prokaryotic
RNA polymerase that melts DNA to initiate transcription. Northern and
Western blot analysis revealed that NF45 and NF90 were expressed in
several cell types, including both unstimulated and stimulated Jurkat T
cells.
GENE FUNCTION
Kao et al. (1994) showed that NF45 and NF90 proteins formed an NFAT
DNA-binding activity that was enhanced by T-cell stimulation and
inhibited by cyclosporin A and FK506.
*FIELD* RF
1. Kao, P. N.; Chen, L.; Brock, G.; Ng, J.; Kenny, J.; Smith, A. J.;
Corthesy, B.: Cloning and expression of cyclosporin A- and FK506-sensitive
nuclear factor of activated T-cells: NF45 and NF90. J. Biol. Chem. 269:
20691-20699, 1994.
*FIELD* CD
Jennifer P. Macke: 10/22/1998
*FIELD* ED
mgross: 02/19/2009
alopez: 10/22/1998
*RECORD*
*FIELD* NO
603181
*FIELD* TI
*603181 INTERLEUKIN ENHANCER-BINDING FACTOR 2; ILF2
;;NUCLEAR FACTOR OF ACTIVATED T CELLS, 45-KD; NF45
read more*FIELD* TX
CLONING
Nuclear factor of activated T cells (NFAT; see 600490) is a
transcription factor required for T-cell expression of interleukin-2
(IL2; 147680). NFAT binds to a sequence known as the antigen receptor
response element-2 (ARRE2) in the IL2 enhancer. Purified NFAT contains
45- and 90-kD subunits. Kao et al. (1994) cloned cDNAs encoding NF45 and
NF90 (603182). The NF45 gene encodes a 405-amino acid polypeptide with
distant similarity to DNA topoisomerase II (126430) and a prokaryotic
RNA polymerase that melts DNA to initiate transcription. Northern and
Western blot analysis revealed that NF45 and NF90 were expressed in
several cell types, including both unstimulated and stimulated Jurkat T
cells.
GENE FUNCTION
Kao et al. (1994) showed that NF45 and NF90 proteins formed an NFAT
DNA-binding activity that was enhanced by T-cell stimulation and
inhibited by cyclosporin A and FK506.
*FIELD* RF
1. Kao, P. N.; Chen, L.; Brock, G.; Ng, J.; Kenny, J.; Smith, A. J.;
Corthesy, B.: Cloning and expression of cyclosporin A- and FK506-sensitive
nuclear factor of activated T-cells: NF45 and NF90. J. Biol. Chem. 269:
20691-20699, 1994.
*FIELD* CD
Jennifer P. Macke: 10/22/1998
*FIELD* ED
mgross: 02/19/2009
alopez: 10/22/1998