CELF2_MOUSE
ID CELF2_MOUSE Reviewed; 508 AA.
AC Q9Z0H4; A2AS10; A2AS11; A2AS15; Q3TNX4; Q3TTI4; Q3TUB8; Q3U668; Q3U7J8;
AC Q3U9F2; Q3UVH4; Q9R0B2; Q9Z187;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=CUGBP Elav-like family member 2;
DE Short=CELF-2;
DE AltName: Full=Bruno-like protein 3;
DE AltName: Full=CUG triplet repeat RNA-binding protein 2;
DE Short=CUG-BP2;
DE AltName: Full=CUG-BP- and ETR-3-like factor 2;
DE AltName: Full=ELAV-type RNA-binding protein 3;
DE Short=ETR-3;
DE Short=mETR-3;
DE AltName: Full=Neuroblastoma apoptosis-related RNA-binding protein;
DE Short=mNapor;
DE AltName: Full=RNA-binding protein BRUNOL-3;
GN Name=Celf2; Synonyms=Cugbp2, Napor;
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 [MRNA] (ISOFORMS 1 AND 7), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10524244; DOI=10.1016/s0378-1119(99)00312-1;
RA Choi D.-K., Ito T., Tsukahara F., Hirai M., Sakaki Y.;
RT "Developmentally-regulated expression of mNapor encoding an apoptosis-
RT induced ELAV-type RNA binding protein.";
RL Gene 237:135-142(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), RNA-BINDING, AND ALTERNATIVE
RP SPLICING.
RC STRAIN=C57BL/6 X CBA; TISSUE=Heart;
RX PubMed=9887331; DOI=10.1093/hmg/8.1.53;
RA Lu X., Timchenko N.A., Timchenko L.T.;
RT "Cardiac elav-type RNA-binding protein (ETR-3) binds to RNA CUG repeats
RT expanded in myotonic dystrophy.";
RL Hum. Mol. Genet. 8:53-60(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4; 5 AND 6),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-508 (ISOFORM 8), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-508 (ISOFORM 11).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Brain, Lung, Testis, and Urinary bladder;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 PROTEIN SEQUENCE OF 58-73 AND 95-107, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [7]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=11158314; DOI=10.1128/mcb.21.4.1285-1296.2001;
RA Ladd A.N., Charlet-B N., Cooper T.A.;
RT "The CELF family of RNA binding proteins is implicated in cell-specific and
RT developmentally regulated alternative splicing.";
RL Mol. Cell. Biol. 21:1285-1296(2001).
RN [8]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=12022233; DOI=10.1017/s1355838202027036;
RA Zhang W., Liu H., Han K., Grabowski P.J.;
RT "Region-specific alternative splicing in the nervous system: implications
RT for regulation by the RNA-binding protein NAPOR.";
RL RNA 8:671-685(2002).
RN [9]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND RNA-BINDING.
RX PubMed=12535526; DOI=10.1016/s1097-2765(03)00012-1;
RA Mukhopadhyay D., Houchen C.W., Kennedy S., Dieckgraefe B.K., Anant S.;
RT "Coupled mRNA stabilization and translational silencing of cyclooxygenase-2
RT by a novel RNA binding protein, CUGBP2.";
RL Mol. Cell 11:113-126(2003).
RN [10]
RP FUNCTION, RNA-BINDING, INDUCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15358864; DOI=10.1073/pnas.0406066101;
RA Murmu N., Jung J., Mukhopadhyay D., Houchen C.W., Riehl T.E., Stenson W.F.,
RA Morrison A.R., Arumugam T., Dieckgraefe B.K., Anant S.;
RT "Dynamic antagonism between RNA-binding protein CUGBP2 and cyclooxygenase-
RT 2-mediated prostaglandin E2 in radiation damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13873-13878(2004).
RN [11]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15830352; DOI=10.1002/dvdy.20382;
RA Ladd A.N., Stenberg M.G., Swanson M.S., Cooper T.A.;
RT "Dynamic balance between activation and repression regulates pre-mRNA
RT alternative splicing during heart development.";
RL Dev. Dyn. 233:783-793(2005).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, 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).
CC -!- FUNCTION: RNA-binding protein implicated in the regulation of several
CC post-transcriptional events. Involved in pre-mRNA alternative splicing,
CC mRNA translation and stability. Mediates exon inclusion and/or
CC exclusion in pre-mRNA that are subject to tissue-specific and
CC developmentally regulated alternative splicing (By similarity).
CC Specifically activates exon 5 inclusion of TNNT2 in embryonic, but not
CC adult, skeletal muscle (By similarity). Activates TNNT2 exon 5
CC inclusion by antagonizing the repressive effect of PTB (By similarity).
CC Acts as both an activator and repressor of a pair of coregulated exons:
CC promotes inclusion of the smooth muscle (SM) exon but exclusion of the
CC non-muscle (NM) exon in actinin pre-mRNAs (By similarity). Promotes
CC inclusion of exonS 21 and exclusion of exon 5 of the NMDA receptor R1
CC pre-mRNA (By similarity). Involved in the apoB RNA editing activity (By
CC similarity). Increases COX2 mRNA stability and inhibits COX2 mRNA
CC translation in epithelial cells after radiation injury. Modulates the
CC cellular apoptosis program by regulating COX2-mediated prostaglandin E2
CC (PGE2) expression. Binds to (CUG)n triplet repeats in the 3'-UTR of
CC transcripts such as DMPK (By similarity). Binds to the muscle-specific
CC splicing enhancer (MSE) intronic sites flanking the TNNT2 alternative
CC exon 5 (By similarity). Binds preferentially to UG-rich sequences, in
CC particular UG repeat and UGUU motifs (By similarity). Binds to apoB
CC mRNA, specifically to AU-rich sequences located immediatly upstream of
CC the edited cytidine (By similarity). Binds AU-rich sequences in the 3'-
CC UTR of COX2 mRNA. Binds to an intronic RNA element responsible for the
CC silencing of exon 21 splicing. Binds to (CUG)n repeats. May be a
CC specific regulator of miRNA biogenesis. Binds to primary microRNA pri-
CC MIR140 and, with CELF1, negatively regulates the processing to mature
CC miRNA (By similarity). {ECO:0000250|UniProtKB:O95319,
CC ECO:0000269|PubMed:12022233, ECO:0000269|PubMed:12535526,
CC ECO:0000269|PubMed:15358864}.
CC -!- SUBUNIT: Interacts with A1CF. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15830352}. Cytoplasm
CC {ECO:0000269|PubMed:15830352}. Note=Colocalizes with APOBEC1 and A1CF
CC (By similarity). RNA-binding activity is detected in both nuclear and
CC cytoplasmic compartments (By similarity). Accumulates in the cytoplasm
CC after ionizing radiation. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1; Synonyms=Napor-3;
CC IsoId=Q9Z0H4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z0H4-2; Sequence=VSP_026803;
CC Name=3;
CC IsoId=Q9Z0H4-3; Sequence=VSP_026801, VSP_026806;
CC Name=4;
CC IsoId=Q9Z0H4-4; Sequence=VSP_026802, VSP_026805;
CC Name=5;
CC IsoId=Q9Z0H4-5; Sequence=VSP_026802, VSP_026806;
CC Name=6;
CC IsoId=Q9Z0H4-6; Sequence=VSP_026803, VSP_026806;
CC Name=7; Synonyms=Napor-1;
CC IsoId=Q9Z0H4-7; Sequence=VSP_026802;
CC Name=8;
CC IsoId=Q9Z0H4-8; Sequence=VSP_026806;
CC Name=9;
CC IsoId=Q9Z0H4-9; Sequence=VSP_026804;
CC Name=11;
CC IsoId=Q9Z0H4-11; Sequence=VSP_026806, VSP_026808;
CC -!- TISSUE SPECIFICITY: Expressed in tongue, spleen and brain (at protein
CC level). Expressed in liver, thigh, stomach, lung and heart to very low
CC levels (at protein level). Expressed in heart, brain, lung and muscle.
CC {ECO:0000269|PubMed:10524244, ECO:0000269|PubMed:11158314,
CC ECO:0000269|PubMed:15358864, ECO:0000269|PubMed:15830352}.
CC -!- DEVELOPMENTAL STAGE: Expressed in heart, muscle, brain, liver, thigh,
CC stomach and lung at 14 dpc (at protein level). Expressed in embryo at
CC 7, 11 and 17 dpc. Expressed in the developing central nervous system
CC from 12 to 16 dpc. {ECO:0000269|PubMed:11158314,
CC ECO:0000269|PubMed:15830352}.
CC -!- INDUCTION: Up-regulated following ionizing radiation in the crypt
CC epithelial cells of the intestin. Down-regulated by bacterial
CC lipopolysaccharides (LPS). Down-regulated by prostaglandin E2 following
CC ionizing radiation. {ECO:0000269|PubMed:12535526,
CC ECO:0000269|PubMed:15358864}.
CC -!- MISCELLANEOUS: [Isoform 9]: Gene prediction based on similarity to rat
CC ortholog. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CELF/BRUNOL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE31371.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- SEQUENCE CAUTION: [Isoform 7]:
CC Sequence=CAA77110.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF090696; AAD13763.1; -; mRNA.
DR EMBL; AF090697; AAD13764.1; -; mRNA.
DR EMBL; Y18298; CAA77110.1; ALT_FRAME; mRNA.
DR EMBL; AK137292; BAE23295.1; -; mRNA.
DR EMBL; AK151818; BAE30715.1; -; mRNA.
DR EMBL; AK152628; BAE31371.1; ALT_INIT; mRNA.
DR EMBL; AK153267; BAE31857.1; -; mRNA.
DR EMBL; AK160861; BAE36053.1; -; mRNA.
DR EMBL; AK161349; BAE36341.1; -; mRNA.
DR EMBL; AK164914; BAE37963.1; -; mRNA.
DR EMBL; AL845492; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929240; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026856; AAH26856.1; -; mRNA.
DR CCDS; CCDS50491.1; -. [Q9Z0H4-7]
DR CCDS; CCDS50492.1; -. [Q9Z0H4-4]
DR CCDS; CCDS50494.1; -. [Q9Z0H4-9]
DR CCDS; CCDS59633.1; -. [Q9Z0H4-2]
DR CCDS; CCDS84468.1; -. [Q9Z0H4-5]
DR RefSeq; NP_001103698.1; NM_001110228.1. [Q9Z0H4-9]
DR RefSeq; NP_001103699.1; NM_001110229.1. [Q9Z0H4-6]
DR RefSeq; NP_001103700.1; NM_001110230.1. [Q9Z0H4-2]
DR RefSeq; NP_001103701.1; NM_001110231.1. [Q9Z0H4-4]
DR RefSeq; NP_001103702.1; NM_001110232.1. [Q9Z0H4-7]
DR RefSeq; NP_001153764.1; NM_001160292.1.
DR RefSeq; NP_001153765.1; NM_001160293.1. [Q9Z0H4-9]
DR RefSeq; NP_001297376.1; NM_001310447.1.
DR RefSeq; NP_001334023.1; NM_001347094.1. [Q9Z0H4-5]
DR RefSeq; NP_034290.2; NM_010160.2.
DR RefSeq; XP_006497400.1; XM_006497337.3. [Q9Z0H4-9]
DR RefSeq; XP_017170933.1; XM_017315444.1.
DR RefSeq; XP_017170953.1; XM_017315464.1.
DR AlphaFoldDB; Q9Z0H4; -.
DR SMR; Q9Z0H4; -.
DR BioGRID; 199537; 1.
DR STRING; 10090.ENSMUSP00000110584; -.
DR iPTMnet; Q9Z0H4; -.
DR PhosphoSitePlus; Q9Z0H4; -.
DR SwissPalm; Q9Z0H4; -.
DR EPD; Q9Z0H4; -.
DR MaxQB; Q9Z0H4; -.
DR PaxDb; Q9Z0H4; -.
DR PeptideAtlas; Q9Z0H4; -.
DR PRIDE; Q9Z0H4; -.
DR ProteomicsDB; 281169; -. [Q9Z0H4-1]
DR ProteomicsDB; 281170; -. [Q9Z0H4-2]
DR ProteomicsDB; 281171; -. [Q9Z0H4-3]
DR ProteomicsDB; 281172; -. [Q9Z0H4-4]
DR ProteomicsDB; 281173; -. [Q9Z0H4-5]
DR ProteomicsDB; 281174; -. [Q9Z0H4-6]
DR ProteomicsDB; 281175; -. [Q9Z0H4-7]
DR ProteomicsDB; 281176; -. [Q9Z0H4-8]
DR ProteomicsDB; 281177; -. [Q9Z0H4-9]
DR ProteomicsDB; 281178; -. [Q9Z0H4-11]
DR Antibodypedia; 5602; 242 antibodies from 27 providers.
DR DNASU; 14007; -.
DR Ensembl; ENSMUST00000002176; ENSMUSP00000002176; ENSMUSG00000002107. [Q9Z0H4-7]
DR Ensembl; ENSMUST00000100429; ENSMUSP00000097996; ENSMUSG00000002107. [Q9Z0H4-7]
DR Ensembl; ENSMUST00000114924; ENSMUSP00000110574; ENSMUSG00000002107. [Q9Z0H4-9]
DR Ensembl; ENSMUST00000114927; ENSMUSP00000110577; ENSMUSG00000002107. [Q9Z0H4-5]
DR Ensembl; ENSMUST00000114934; ENSMUSP00000110584; ENSMUSG00000002107. [Q9Z0H4-9]
DR Ensembl; ENSMUST00000142941; ENSMUSP00000120459; ENSMUSG00000002107. [Q9Z0H4-4]
DR Ensembl; ENSMUST00000150624; ENSMUSP00000138297; ENSMUSG00000002107. [Q9Z0H4-5]
DR Ensembl; ENSMUST00000182706; ENSMUSP00000138764; ENSMUSG00000002107. [Q9Z0H4-2]
DR Ensembl; ENSMUST00000182851; ENSMUSP00000138363; ENSMUSG00000002107. [Q9Z0H4-1]
DR GeneID; 14007; -.
DR KEGG; mmu:14007; -.
DR UCSC; uc008ign.2; mouse. [Q9Z0H4-3]
DR UCSC; uc008igp.2; mouse. [Q9Z0H4-4]
DR UCSC; uc008igq.3; mouse. [Q9Z0H4-11]
DR UCSC; uc008igr.3; mouse. [Q9Z0H4-9]
DR UCSC; uc008igs.3; mouse. [Q9Z0H4-2]
DR UCSC; uc008igt.3; mouse. [Q9Z0H4-6]
DR UCSC; uc008igv.3; mouse. [Q9Z0H4-1]
DR CTD; 10659; -.
DR MGI; MGI:1338822; Celf2.
DR VEuPathDB; HostDB:ENSMUSG00000002107; -.
DR eggNOG; KOG0144; Eukaryota.
DR GeneTree; ENSGT00940000155461; -.
DR HOGENOM; CLU_015367_0_2_1; -.
DR InParanoid; Q9Z0H4; -.
DR OMA; PMGNGMN; -.
DR OrthoDB; 1209165at2759; -.
DR PhylomeDB; Q9Z0H4; -.
DR TreeFam; TF314924; -.
DR BioGRID-ORCS; 14007; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Celf2; mouse.
DR PRO; PR:Q9Z0H4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9Z0H4; protein.
DR Bgee; ENSMUSG00000002107; Expressed in rostral migratory stream and 258 other tissues.
DR ExpressionAtlas; Q9Z0H4; baseline and differential.
DR Genevisible; Q9Z0H4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0090543; C:Flemming body; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0106222; F:lncRNA binding; IPI:MGI.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; ISO:MGI.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0036002; F:pre-mRNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISO:MGI.
DR GO; GO:0006376; P:mRNA splice site selection; IDA:MGI.
DR GO; GO:0016441; P:post-transcriptional gene silencing; ISO:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd12631; RRM1_CELF1_2_Bruno; 1.
DR CDD; cd12634; RRM2_CELF1_2; 1.
DR CDD; cd12638; RRM3_CELF1_2; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR034196; CELF1/2_RRM1.
DR InterPro; IPR034198; CELF1/2_RRM2.
DR InterPro; IPR034199; CELF1/2_RRM3.
DR InterPro; IPR002343; Hud_Sxl_RNA.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 3.
DR PRINTS; PR00961; HUDSXLRNA.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Direct protein sequencing;
KW mRNA processing; Nucleus; Reference proteome; Repeat; Repressor;
KW RNA-binding.
FT CHAIN 1..508
FT /note="CUGBP Elav-like family member 2"
FT /id="PRO_0000295190"
FT DOMAIN 40..123
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 132..212
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 423..501
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..283
FT /note="Necessary for RNA-binding, TNNT2 exon 5 and NMDA R1
FT exon 21 inclusion"
FT /evidence="ECO:0000250"
FT REGION 357..508
FT /note="Necessary for RNA-binding, TNNT2 exon 5 and NMDA R1
FT exon 21 inclusion"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..274
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026801"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform 4, isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:10524244,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9887331"
FT /id="VSP_026802"
FT VAR_SEQ 1..17
FT /note="MRCPKSAVTMRNEELLL -> MVSLISDLDSLRGWKALRETATELSGSPP
FT (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026803"
FT VAR_SEQ 1
FT /note="M -> MFERTSELAFVETISVESM (in isoform 9)"
FT /evidence="ECO:0000305"
FT /id="VSP_026804"
FT VAR_SEQ 358
FT /note="A -> AVAQMLS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026805"
FT VAR_SEQ 359
FT /note="G -> GTINS (in isoform 3, isoform 5, isoform 6,
FT isoform 8 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026806"
FT VAR_SEQ 419..466
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026808"
FT CONFLICT 218
FT /note="Q -> K (in Ref. 2; CAA77110)"
FT /evidence="ECO:0000305"
FT CONFLICT 245
FT /note="G -> E (in Ref. 2; CAA77110)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="P -> T (in Ref. 3; BAE30715/BAE31857)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 54271 MW; C35CBEF598749A79 CRC64;
MRCPKSAVTM RNEELLLSNG TANKMNGALD HSDQPDPDAI KMFVGQIPRS WSEKELKELF
EPYGAVYQIN VLRDRSQNPP QSKGCCFVTF YTRKAALEAQ NALHNIKTLP GMHHPIQMKP
ADSEKSNAVE DRKLFIGMVS KKCNENDIRV MFSPFGQIEE CRILRGPDGL SRGCAFVTFS
TRAMAQNAIK AMHQSQTMEG CSSPIVVKFA DTQKDKEQRR LQQQLAQQMQ QLNTATWGNL
TGLGGLTPQY LALLQQATSS SNLGAFSGIQ QMAGMNALQL QNLATLAAAA AAAQTSATST
NANPLSSTSS ALGALTSPVA ASTPNSTAGA AMNSLTSLGT LQGLAGATVG LNNINALAGM
AALNGGLGAT GLTNGTAGTM DALTQAYSGI QQYAAAALPT LYSQSLLQQQ SAAGSQKEGP
EGANLFIYHL PQEFGDQDIL QMFMPFGNVI SAKVFIDKQT NLSKCFGFVS YDNPVSAQAA
IQAMNGFQIG MKRLKVQLKR SKNDSKPY
