CELF1_MOUSE
ID CELF1_MOUSE Reviewed; 486 AA.
AC P28659; A2AFW9; A2AFX0; A2AFX1; A2AFX2; Q3U0N2; Q3UP93; Q3UY22; Q8R532;
AC Q99PE1; Q9CXE5; Q9EPJ8; Q9JI37;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=CUGBP Elav-like family member 1;
DE Short=CELF-1;
DE AltName: Full=50 kDa nuclear polyadenylated RNA-binding protein;
DE AltName: Full=Brain protein F41;
DE AltName: Full=Bruno-like protein 2;
DE AltName: Full=CUG triplet repeat RNA-binding protein 1;
DE Short=CUG-BP1;
DE AltName: Full=CUG-BP- and ETR-3-like factor 1;
DE AltName: Full=Deadenylation factor CUG-BP;
DE AltName: Full=Deadenylation factor EDEN-BP;
DE AltName: Full=Embryo deadenylation element-binding protein homolog;
DE Short=EDEN-BP homolog;
DE AltName: Full=RNA-binding protein BRUNOL-2;
GN Name=Celf1; Synonyms=Brunol2, Cugbp, Cugbp1;
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] (ISOFORM 1).
RC STRAIN=SWR/J; TISSUE=Ovary;
RX PubMed=11707455; DOI=10.1074/jbc.m109362200;
RA Paillard L., Legagneux V., Maniey D., Osborne H.B.;
RT "c-Jun ARE targets mRNA deadenylation by an EDEN-BP (embryo deadenylation
RT element-binding protein)-dependent pathway.";
RL J. Biol. Chem. 277:3232-3235(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=11686919; DOI=10.1093/oxfordjournals.jbchem.a003022;
RA Takahashi N., Sasagawa N., Usuki F., Kino Y., Kawahara H., Sorimachi H.,
RA Maeda T., Suzuki K., Ishiura S.;
RT "Coexpression of the CUG-binding protein reduces DM protein kinase
RT expression in COS cells.";
RL J. Biochem. 130:581-587(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J;
RC TISSUE=Embryonic liver, Fetal spleen, Olfactory bulb, 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 [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 STRAIN=Czech II; TISSUE=Mammary gland;
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 [MRNA] OF 52-486 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Fetus;
RX PubMed=10893231; DOI=10.1074/jbc.m003083200;
RA Good P.J., Chen Q., Warner S.J., Herring D.C.;
RT "A family of human RNA-binding proteins related to the Drosophila Bruno
RT translational regulator.";
RL J. Biol. Chem. 275:28583-28592(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 96-420 (ISOFORM 3).
RA Suzuki H., Inoue K.;
RT "Bruno-like RNA-binding protein.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 127-445 (ISOFORM 1).
RA Kato K.;
RL Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases.
RN [9]
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 [10]
RP FUNCTION, PHOSPHORYLATION, INDUCTION, AND RNA-BINDING.
RX PubMed=15082764; DOI=10.1128/mcb.24.9.3682-3691.2004;
RA Baldwin B.R., Timchenko N.A., Zahnow C.A.;
RT "Epidermal growth factor receptor stimulation activates the RNA binding
RT protein CUG-BP1 and increases expression of C/EBPbeta-LIP in mammary
RT epithelial cells.";
RL Mol. Cell. Biol. 24:3682-3691(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 FUNCTION, IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CALR;
RP CALR3; HSPA5 AND HSP90B1, IDENTIFICATION BY MASS SPECTROMETRY,
RP PHOSPHORYLATION AT SER-302, MUTAGENESIS OF SER-302, ASSOCIATION WITH
RP POLYSOMES, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16931514; DOI=10.1074/jbc.m605701200;
RA Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H.,
RA Hershey J.W., Timchenko N.A.;
RT "Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-
RT binding protein beta in old liver.";
RL J. Biol. Chem. 281:32806-32819(2006).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=17130239; DOI=10.1128/mcb.01009-06;
RA Kress C., Gautier-Courteille C., Osborne H.B., Babinet C., Paillard L.;
RT "Inactivation of CUG-BP1/CELF1 causes growth, viability, and
RT spermatogenesis defects in mice.";
RL Mol. Cell. Biol. 27:1146-1157(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 (ISOFORM 4), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, 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 cardiac isoforms of TNNT2
CC during heart remodeling at the juvenile to adult transition (By
CC similarity). Acts as both an activator and repressor of a pair of
CC coregulated exons: promotes inclusion of the smooth muscle (SM) exon
CC but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs (By
CC similarity). Activates SM exon 5 inclusion by antagonizing the
CC repressive effect of PTB (By similarity). Promotes exclusion of exon 11
CC of the INSR pre-mRNA (By similarity). Inhibits, together with HNRNPH1,
CC insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast (By
CC similarity). Increases translation and controls the choice of
CC translation initiation codon of CEBPB mRNA (By similarity). Increases
CC mRNA translation of CEBPB in aging liver. Increases translation of
CC CDKN1A mRNA by antagonizing the repressive effect of CALR3 (By
CC similarity). Mediates rapid cytoplasmic mRNA deadenylation (By
CC similarity). Recruits the deadenylase PARN to the poly(A) tail of EDEN-
CC containing mRNAs to promote their deadenylation (By similarity).
CC Required for completion of spermatogenesis. Binds to (CUG)n triplet
CC repeats in the 3'-UTR of transcripts such as DMPK and to Bruno response
CC elements (BREs) (By similarity). Binds to muscle-specific splicing
CC enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2
CC pre-mRNA (By similarity). Binds to AU-rich sequences (AREs or EDEN-
CC like) localized in the 3'-UTR of JUN and FOS mRNAs. Binds to the IR RNA
CC (By similarity). Binds to the 5'-region of CDKN1A and CEBPB mRNAs (By
CC similarity). Binds with the 5'-region of CEBPB mRNA in aging liver. May
CC be a specific regulator of miRNA biogenesis. Binds to primary microRNA
CC pri-MIR140 and, with CELF2, negatively regulates the processing to
CC mature miRNA (By similarity). {ECO:0000250|UniProtKB:Q92879,
CC ECO:0000269|PubMed:15082764, ECO:0000269|PubMed:16931514,
CC ECO:0000269|PubMed:17130239}.
CC -!- SUBUNIT: Associates with polysomes (By similarity). Interacts with
CC HNRNPH1; the interaction in RNA-dependent. Interacts with PARN (By
CC similarity). Component of an EIF2 complex at least composed of
CC CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5.
CC {ECO:0000250, ECO:0000269|PubMed:16931514}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=RNA-binding activity is
CC detected in both nuclear and cytoplasmic compartments. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1; Synonyms=LYLQ;
CC IsoId=P28659-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28659-2; Sequence=VSP_005786;
CC Name=3; Synonyms=A;
CC IsoId=P28659-3; Sequence=VSP_005786, VSP_005787;
CC Name=4;
CC IsoId=P28659-4; Sequence=VSP_026789;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, uterus, diaphragm,
CC lung, spleen, testis, mammary gland, adipose, eye and brain (at protein
CC level). Strongly expressed in aging liver (at protein level). Expressed
CC in lung, stomach, heart to very low levels (at protein level).
CC Expressed in germ cells of the seminiferous tubules except in the
CC central region that contains the elongated spermatids and spermatozoa
CC (at protein level). Expressed in Leydig cells of the interstitial
CC tissue (at protein level). Expressed in the heart, skeletal muscle,
CC testis (from spermatogonia to round spermatids), spleen, lung,
CC neocortex, cerebellar cortex, hippocampus and other areas, abundant in
CC the putamen, and poorly expressed in the thalamus and in the brain
CC stem. {ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:11686919,
CC ECO:0000269|PubMed:15830352, ECO:0000269|PubMed:16931514,
CC ECO:0000269|PubMed:17130239}.
CC -!- DEVELOPMENTAL STAGE: Expressed in heart, muscle, brain, liver, thigh,
CC stomach and lung at 14 dpc (at protein level). Expressed from the two-
CC cell to blastocyst stages. Expressed in tail region, somites, cephalic
CC structures and limb buds at 10.5 dpc. {ECO:0000269|PubMed:11158314,
CC ECO:0000269|PubMed:15830352, ECO:0000269|PubMed:17130239}.
CC -!- INDUCTION: Its RNA-binding activity on CEBPB mRNA increases in response
CC to EGF. {ECO:0000269|PubMed:15082764}.
CC -!- DOMAIN: RRM1 and RRM2 domains preferentially target UGU(U/G)-rich mRNA
CC elements. {ECO:0000250}.
CC -!- PTM: Phosphorylated. Phosphorylated by CDK4 on Ser-302. Its
CC phosphorylation status increases in aging liver and is important for
CC the formation of the EIF2 complex and activation of CEBPB mRNA
CC translation. Hyperphosphorylated in the EIF2 complex. EGFR signaling
CC regulates its phosphorylation status in epithelial cells.
CC {ECO:0000269|PubMed:15082764, ECO:0000269|PubMed:16931514}.
CC -!- SIMILARITY: Belongs to the CELF/BRUNOL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA43691.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ007987; CAC20707.1; -; mRNA.
DR EMBL; AF267535; AAF78957.1; -; mRNA.
DR EMBL; AK135030; BAE22391.1; -; mRNA.
DR EMBL; AK143698; BAE25504.1; -; mRNA.
DR EMBL; AK014492; BAB29392.1; -; mRNA.
DR EMBL; AK156725; BAE33820.1; -; mRNA.
DR EMBL; AL672241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021393; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF314172; AAK00297.1; -; mRNA.
DR EMBL; AB050499; BAB87831.1; -; mRNA.
DR EMBL; X61451; CAA43691.1; ALT_FRAME; mRNA.
DR CCDS; CCDS16420.1; -. [P28659-4]
DR CCDS; CCDS16421.1; -. [P28659-1]
DR PIR; S16865; S16865.
DR RefSeq; NP_001231820.1; NM_001244891.1. [P28659-1]
DR RefSeq; NP_001231832.1; NM_001244903.1. [P28659-1]
DR RefSeq; NP_059064.2; NM_017368.3. [P28659-4]
DR RefSeq; NP_941955.1; NM_198683.2. [P28659-1]
DR RefSeq; XP_006498727.1; XM_006498664.1.
DR RefSeq; XP_006498728.1; XM_006498665.3.
DR RefSeq; XP_006498732.1; XM_006498669.1. [P28659-4]
DR AlphaFoldDB; P28659; -.
DR BMRB; P28659; -.
DR SMR; P28659; -.
DR BioGRID; 198980; 20.
DR STRING; 10090.ENSMUSP00000070438; -.
DR iPTMnet; P28659; -.
DR PhosphoSitePlus; P28659; -.
DR EPD; P28659; -.
DR jPOST; P28659; -.
DR MaxQB; P28659; -.
DR PaxDb; P28659; -.
DR PeptideAtlas; P28659; -.
DR PRIDE; P28659; -.
DR ProteomicsDB; 281572; -. [P28659-1]
DR ProteomicsDB; 281573; -. [P28659-2]
DR ProteomicsDB; 281574; -. [P28659-3]
DR ProteomicsDB; 281575; -. [P28659-4]
DR Antibodypedia; 4239; 395 antibodies from 34 providers.
DR DNASU; 13046; -.
DR Ensembl; ENSMUST00000005643; ENSMUSP00000005643; ENSMUSG00000005506. [P28659-4]
DR Ensembl; ENSMUST00000068747; ENSMUSP00000070438; ENSMUSG00000005506. [P28659-1]
DR Ensembl; ENSMUST00000111448; ENSMUSP00000107075; ENSMUSG00000005506. [P28659-3]
DR Ensembl; ENSMUST00000111449; ENSMUSP00000107076; ENSMUSG00000005506. [P28659-1]
DR Ensembl; ENSMUST00000111451; ENSMUSP00000107078; ENSMUSG00000005506. [P28659-1]
DR Ensembl; ENSMUST00000111452; ENSMUSP00000107079; ENSMUSG00000005506. [P28659-4]
DR Ensembl; ENSMUST00000111455; ENSMUSP00000107082; ENSMUSG00000005506. [P28659-4]
DR Ensembl; ENSMUST00000177642; ENSMUSP00000136109; ENSMUSG00000005506. [P28659-1]
DR GeneID; 13046; -.
DR KEGG; mmu:13046; -.
DR UCSC; uc008ktx.2; mouse. [P28659-1]
DR UCSC; uc008kua.2; mouse. [P28659-4]
DR CTD; 10658; -.
DR MGI; MGI:1342295; Celf1.
DR VEuPathDB; HostDB:ENSMUSG00000005506; -.
DR eggNOG; KOG0144; Eukaryota.
DR GeneTree; ENSGT00940000158970; -.
DR HOGENOM; CLU_015367_0_2_1; -.
DR InParanoid; P28659; -.
DR OMA; QWHKPRK; -.
DR OrthoDB; 1209165at2759; -.
DR PhylomeDB; P28659; -.
DR TreeFam; TF314924; -.
DR BioGRID-ORCS; 13046; 7 hits in 72 CRISPR screens.
DR ChiTaRS; Celf1; mouse.
DR PRO; PR:P28659; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P28659; protein.
DR Bgee; ENSMUSG00000005506; Expressed in lens of camera-type eye and 83 other tissues.
DR ExpressionAtlas; P28659; baseline and differential.
DR Genevisible; P28659; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISO:MGI.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:ARUK-UCL.
DR GO; GO:0097356; C:perinucleolar compartment; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0042835; F:BRE binding; ISS:UniProtKB.
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; IDA:MGI.
DR GO; GO:0036002; F:pre-mRNA binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0031369; F:translation initiation factor binding; IDA:MGI.
DR GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR GO; GO:0061157; P:mRNA destabilization; ISO:MGI.
DR GO; GO:0006376; P:mRNA splice site selection; IDA:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
DR GO; GO:0016441; P:post-transcriptional gene silencing; ISO:MGI.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; ISO:MGI.
DR GO; GO:0043484; P:regulation of RNA splicing; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
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; 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 SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Cytoplasm; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation.
FT CHAIN 1..486
FT /note="CUGBP Elav-like family member 1"
FT /id="PRO_0000081539"
FT DOMAIN 16..99
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 108..188
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 401..479
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 277..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q92879"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92879"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92879"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16931514"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92879"
FT VAR_SEQ 1
FT /note="M -> MAAFKLDFLPEMMVDHCSLNSSPVSKKM (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_026789"
FT VAR_SEQ 231..234
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.7"
FT /id="VSP_005786"
FT VAR_SEQ 297
FT /note="S -> SA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.7"
FT /id="VSP_005787"
FT MUTAGEN 302
FT /note="S->G: Reduces CDK4-mediated phosphorylation."
FT /evidence="ECO:0000269|PubMed:16931514"
FT CONFLICT 192
FT /note="K -> E (in Ref. 7; BAB87831)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="L -> P (in Ref. 2; AAF78957)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="P -> T (in Ref. 2; AAF78957)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="G -> R (in Ref. 2; AAF78957)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="G -> A (in Ref. 2; AAF78957)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="N -> Y (in Ref. 3; BAE33820)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="Q -> R (in Ref. 3; BAE25504)"
FT /evidence="ECO:0000305"
FT MOD_RES P28659-4:18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 486 AA; 52107 MW; ABB22D331A62B584 CRC64;
MNGTLDHPDQ PDLDAIKMFV GQVPRTWSEK DLRELFEQYG AVYEINILRD RSQNPPQSKG
CCFVTFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE KNNAVEDRKL FIGMISKKCT
ENDIRVMFSS FGQIEECRIL RGPDGLSRGC AFVTFTTRTM AQTAIKAMHQ AQTMEGCSSP
MVVKFADTQK DKEQKRMAQQ LQQQMQQISA ASVWGNLAGL NTLGPQYLAL YLQLLQQTAS
SGNLNTLSSL HPMGGLNAMQ LQNLAALAAA ASAAQNTPSG TNALTTSSSP LSVLTSSGSS
PSSSSSNSVN PIASLGALQT LAGATAGLNV GSLAGMAALN GGLGSSGLSN GTGSTMEALT
QAYSGIQQYA AAALPTLYNQ NLLTQQSIGA AGSQKEGPEG ANLFIYHLPQ EFGDQDLLQM
FMPFGNVVSA KVFIDKQTNL SKCFGFVSYD NPVSAQAAIQ SMNGFQIGMK RLKVQLKRSK
NDSKPY
