CELF1_HUMAN
ID CELF1_HUMAN Reviewed; 486 AA.
AC Q92879; B4E2U5; D3DQS0; F8W940; Q4LE52; Q9NP83; Q9NR06;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 204.
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=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=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, NAB50;
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 [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RP RNA-BINDING.
RX PubMed=8948631; DOI=10.1093/nar/24.22.4407;
RA Timchenko L.T., Miller J.W., Timchenko N.A., DeVore D.R., Datar K.V.,
RA Lin L., Roberts R., Caskey C.T., Swanson M.S.;
RT "Identification of a (CUG)n triplet repeat RNA-binding protein and its
RT expression in myotonic dystrophy.";
RL Nucleic Acids Res. 24:4407-4414(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, AND TISSUE
RP SPECIFICITY.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Skeletal muscle;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND RNA-BINDING.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Trachea;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
RA Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R.,
RA Okazaki N., Koga H., Nagase T., Ohara O.;
RT "Preparation of a set of expression-ready clones of mammalian long cDNAs
RT encoding large proteins by the ORF trap cloning method.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [10]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=10536163; DOI=10.1093/nar/27.22.4517;
RA Timchenko N.A., Welm A.L., Lu X., Timchenko L.T.;
RT "CUG repeat binding protein (CUGBP1) interacts with the 5' region of
RT C/EBPbeta mRNA and regulates translation of C/EBPbeta isoforms.";
RL Nucleic Acids Res. 27:4517-4525(1999).
RN [11]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=11124939; DOI=10.1074/jbc.m005960200;
RA Timchenko N.A., Cai Z.J., Welm A.L., Reddy S., Ashizawa T., Timchenko L.T.;
RT "RNA CUG repeats sequester CUGBP1 and alter protein levels and activity of
RT CUGBP1.";
RL J. Biol. Chem. 276:7820-7826(2001).
RN [12]
RP FUNCTION, RNA-BINDING, 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 [13]
RP FUNCTION, MUTAGENESIS OF PHE-63; GLY-331 AND LEU-472, AND RNA-BINDING.
RX PubMed=12799066; DOI=10.1016/s0248-4900(03)00010-8;
RA Paillard L., Legagneux V., Beverley Osborne H.;
RT "A functional deadenylation assay identifies human CUG-BP as a
RT deadenylation factor.";
RL Biol. Cell 95:107-113(2003).
RN [14]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=12649496; DOI=10.1261/rna.2191903;
RA Gromak N., Matlin A.J., Cooper T.A., Smith C.W.;
RT "Antagonistic regulation of alpha-actinin alternative splicing by CELF
RT proteins and polypyrimidine tract binding protein.";
RL RNA 9:443-456(2003).
RN [15]
RP FUNCTION, PHOSPHORYLATION, AND RNA-BINDING.
RX PubMed=14726956; DOI=10.1038/sj.emboj.7600052;
RA Iakova P., Wang G.-L., Timchenko L., Michalak M., Pereira-Smith O.M.,
RA Smith J.R., Timchenko N.A.;
RT "Competition of CUGBP1 and calreticulin for the regulation of p21
RT translation determines cell fate.";
RL EMBO J. 23:406-417(2004).
RN [16]
RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA Hillman R.T., Green R.E., Brenner S.E.;
RT "An unappreciated role for RNA surveillance.";
RL Genome Biol. 5:R8.1-R8.16(2004).
RN [17]
RP FUNCTION, INTERACTION WITH HNRNPH1, RNA-BINDING, AND INDUCTION.
RX PubMed=16946708; DOI=10.1038/sj.emboj.7601296;
RA Paul S., Dansithong W., Kim D., Rossi J., Webster N.J., Comai L., Reddy S.;
RT "Interaction of muscleblind, CUG-BP1 and hnRNP H proteins in DM1-associated
RT aberrant IR splicing.";
RL EMBO J. 25:4271-4283(2006).
RN [18]
RP TISSUE SPECIFICITY.
RX PubMed=16862542; DOI=10.1002/jnr.20980;
RA Leroy O., Dhaenens C.-M., Schraen-Maschke S., Belarbi K., Delacourte A.,
RA Andreadis A., Sablonniere B., Buee L., Sergeant N., Caillet-Boudin M.-L.;
RT "ETR-3 represses Tau exons 2/3 inclusion, a splicing event abnormally
RT enhanced in myotonic dystrophy type I.";
RL J. Neurosci. Res. 84:852-859(2006).
RN [19]
RP FUNCTION, INTERACTION WITH PARN, AND RNA-BINDING.
RX PubMed=16601207; DOI=10.1261/rna.59606;
RA Moraes K.C., Wilusz C.J., Wilusz J.;
RT "CUG-BP binds to RNA substrates and recruits PARN deadenylase.";
RL RNA 12:1084-1091(2006).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4 AND SER-179, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [23]
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 [24]
RP FUNCTION, AND MIRNA-BINDING.
RX PubMed=28431233; DOI=10.1016/j.molcel.2017.03.014;
RA Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L., Eichner N.,
RA Lehmann G., Schall K., Urlaub H., Meister G.;
RT "A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis.";
RL Mol. Cell 66:270-284(2017).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109, AND IDENTIFICATION BY MASS
RP 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 [26]
RP STRUCTURE BY NMR OF 383-484.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RNA-binding domain 3 in CUG triplet repeat RNA-
RT binding protein 1.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [27]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 14-187 IN COMPLEX WITH MRNA, AND
RP DOMAINS RRM.
RX PubMed=20947024; DOI=10.1016/j.str.2010.06.018;
RA Teplova M., Song J., Gaw H.Y., Teplov A., Patel D.J.;
RT "Structural insights into RNA recognition by the alternate-splicing
RT regulator CUG-binding protein 1.";
RL Structure 18:1364-1377(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. Specifically activates
CC exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling
CC at the juvenile to adult transition. Acts as both an activator and
CC repressor of a pair of coregulated exons: promotes inclusion of the
CC smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in
CC actinin pre-mRNAs. Activates SM exon 5 inclusion by antagonizing the
CC repressive effect of PTB. Promotes exclusion of exon 11 of the INSR
CC pre-mRNA. Inhibits, together with HNRNPH1, insulin receptor (IR) pre-
CC mRNA exon 11 inclusion in myoblast. Increases translation and controls
CC the choice of translation initiation codon of CEBPB mRNA. Increases
CC mRNA translation of CEBPB in aging liver (By similarity). Increases
CC translation of CDKN1A mRNA by antagonizing the repressive effect of
CC CALR3. Mediates rapid cytoplasmic mRNA deadenylation. Recruits the
CC deadenylase PARN to the poly(A) tail of EDEN-containing mRNAs to
CC promote their deadenylation. Required for completion of spermatogenesis
CC (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of
CC transcripts such as DMPK and to Bruno response elements (BREs). Binds
CC to muscle-specific splicing enhancer (MSE) intronic sites flanking the
CC alternative exon 5 of TNNT2 pre-mRNA. Binds to AU-rich sequences (AREs
CC or EDEN-like) localized in the 3'-UTR of JUN and FOS mRNAs. Binds to
CC the IR RNA. Binds to the 5'-region of CDKN1A and CEBPB mRNAs. Binds
CC with the 5'-region of CEBPB mRNA in aging liver. May be a specific
CC regulator of miRNA biogenesis. Binds to primary microRNA pri-MIR140
CC and, with CELF2, negatively regulates the processing to mature miRNA
CC (PubMed:28431233). {ECO:0000250, ECO:0000269|PubMed:10536163,
CC ECO:0000269|PubMed:11124939, ECO:0000269|PubMed:11158314,
CC ECO:0000269|PubMed:12649496, ECO:0000269|PubMed:12799066,
CC ECO:0000269|PubMed:14726956, ECO:0000269|PubMed:16601207,
CC ECO:0000269|PubMed:16946708, ECO:0000269|PubMed:28431233}.
CC -!- SUBUNIT: Component of an EIF2 complex at least composed of
CC CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5.
CC Associates with polysomes (By similarity). Interacts with HNRNPH1; the
CC interaction in RNA-dependent. Interacts with PARN. {ECO:0000250,
CC ECO:0000269|PubMed:16601207, ECO:0000269|PubMed:16946708,
CC ECO:0000269|PubMed:20947024}.
CC -!- INTERACTION:
CC Q92879-3; Q13148: TARDBP; NbExp=3; IntAct=EBI-21370617, EBI-372899;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8948631}. Cytoplasm
CC {ECO:0000269|PubMed:8948631}. Note=RNA-binding activity is detected in
CC both nuclear and cytoplasmic compartments.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=LYLQ;
CC IsoId=Q92879-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92879-2; Sequence=VSP_005784;
CC Name=3; Synonyms=A;
CC IsoId=Q92879-3; Sequence=VSP_005784, VSP_005785;
CC Name=4;
CC IsoId=Q92879-4; Sequence=VSP_026787, VSP_026788;
CC Name=5;
CC IsoId=Q92879-5; Sequence=VSP_045043, VSP_026788;
CC Name=6;
CC IsoId=Q92879-6; Sequence=VSP_026788;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10893231,
CC ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:16862542}.
CC -!- INDUCTION: Up-regulated in myotonic dystrophy pathophysiology (DM).
CC {ECO:0000269|PubMed:16946708}.
CC -!- DOMAIN: RRM1 and RRM2 domains preferentially target UGU(U/G)-rich mRNA
CC elements. {ECO:0000269|PubMed:20947024}.
CC -!- PTM: Phosphorylated. Its phosphorylation status increases in senescent
CC cells. {ECO:0000269|PubMed:14726956}.
CC -!- MISCELLANEOUS: [Isoform 1]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay.
CC -!- SIMILARITY: Belongs to the CELF/BRUNOL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE06101.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U63289; AAC50895.1; -; mRNA.
DR EMBL; AF248648; AAF86230.1; -; mRNA.
DR EMBL; AF267533; AAF78955.1; -; mRNA.
DR EMBL; AF267534; AAF78956.1; -; mRNA.
DR EMBL; AJ007988; CAC20566.1; -; mRNA.
DR EMBL; AK304430; BAG65257.1; -; mRNA.
DR EMBL; AB210019; BAE06101.1; ALT_INIT; mRNA.
DR EMBL; AC090559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW67909.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW67912.1; -; Genomic_DNA.
DR EMBL; BC031079; AAH31079.1; -; mRNA.
DR CCDS; CCDS31482.1; -. [Q92879-1]
DR CCDS; CCDS53622.1; -. [Q92879-6]
DR CCDS; CCDS53623.1; -. [Q92879-4]
DR CCDS; CCDS7938.1; -. [Q92879-2]
DR CCDS; CCDS7939.1; -. [Q92879-3]
DR RefSeq; NP_001020767.1; NM_001025596.2. [Q92879-1]
DR RefSeq; NP_001166110.1; NM_001172639.1. [Q92879-4]
DR RefSeq; NP_001166111.1; NM_001172640.1. [Q92879-6]
DR RefSeq; NP_006551.1; NM_006560.3. [Q92879-2]
DR RefSeq; NP_941989.1; NM_198700.2. [Q92879-3]
DR RefSeq; XP_011518161.1; XM_011519859.1. [Q92879-3]
DR RefSeq; XP_016872613.1; XM_017017124.1.
DR RefSeq; XP_016872614.1; XM_017017125.1.
DR RefSeq; XP_016872615.1; XM_017017126.1.
DR RefSeq; XP_016872616.1; XM_017017127.1.
DR RefSeq; XP_016872617.1; XM_017017128.1.
DR RefSeq; XP_016872618.1; XM_017017129.1.
DR RefSeq; XP_016872619.1; XM_017017130.1.
DR RefSeq; XP_016872620.1; XM_017017131.1.
DR RefSeq; XP_016872621.1; XM_017017132.1.
DR RefSeq; XP_016872622.1; XM_017017133.1.
DR RefSeq; XP_016872623.1; XM_017017134.1.
DR RefSeq; XP_016872624.1; XM_017017135.1.
DR PDB; 2CPZ; NMR; -; A=383-484.
DR PDB; 2DHS; NMR; -; A=1-187.
DR PDB; 2RQ4; NMR; -; A=383-484.
DR PDB; 2RQC; NMR; -; A=383-484.
DR PDB; 3NMR; X-ray; 1.85 A; A=14-187.
DR PDB; 3NNA; X-ray; 1.90 A; A=14-187.
DR PDB; 3NNC; X-ray; 2.20 A; A=14-187.
DR PDB; 3NNH; X-ray; 2.75 A; A/B/C/D=14-100.
DR PDBsum; 2CPZ; -.
DR PDBsum; 2DHS; -.
DR PDBsum; 2RQ4; -.
DR PDBsum; 2RQC; -.
DR PDBsum; 3NMR; -.
DR PDBsum; 3NNA; -.
DR PDBsum; 3NNC; -.
DR PDBsum; 3NNH; -.
DR AlphaFoldDB; Q92879; -.
DR SMR; Q92879; -.
DR BioGRID; 115901; 271.
DR IntAct; Q92879; 37.
DR MINT; Q92879; -.
DR STRING; 9606.ENSP00000435926; -.
DR GlyGen; Q92879; 7 sites, 1 O-linked glycan (7 sites).
DR iPTMnet; Q92879; -.
DR MetOSite; Q92879; -.
DR PhosphoSitePlus; Q92879; -.
DR SwissPalm; Q92879; -.
DR BioMuta; CELF1; -.
DR DMDM; 17374605; -.
DR EPD; Q92879; -.
DR jPOST; Q92879; -.
DR MassIVE; Q92879; -.
DR MaxQB; Q92879; -.
DR PaxDb; Q92879; -.
DR PeptideAtlas; Q92879; -.
DR PRIDE; Q92879; -.
DR ProteomicsDB; 30255; -.
DR ProteomicsDB; 75565; -. [Q92879-1]
DR ProteomicsDB; 75566; -. [Q92879-2]
DR ProteomicsDB; 75567; -. [Q92879-3]
DR ProteomicsDB; 75568; -. [Q92879-4]
DR Antibodypedia; 4239; 395 antibodies from 34 providers.
DR DNASU; 10658; -.
DR Ensembl; ENST00000310513.10; ENSP00000308386.5; ENSG00000149187.19. [Q92879-2]
DR Ensembl; ENST00000358597.7; ENSP00000351409.3; ENSG00000149187.19. [Q92879-1]
DR Ensembl; ENST00000361904.7; ENSP00000354639.3; ENSG00000149187.19. [Q92879-3]
DR Ensembl; ENST00000395290.6; ENSP00000378705.2; ENSG00000149187.19. [Q92879-6]
DR Ensembl; ENST00000395292.6; ENSP00000378706.2; ENSG00000149187.19. [Q92879-3]
DR Ensembl; ENST00000532048.5; ENSP00000435926.1; ENSG00000149187.19. [Q92879-4]
DR GeneID; 10658; -.
DR KEGG; hsa:10658; -.
DR UCSC; uc001nfk.3; human. [Q92879-1]
DR CTD; 10658; -.
DR DisGeNET; 10658; -.
DR GeneCards; CELF1; -.
DR HGNC; HGNC:2549; CELF1.
DR HPA; ENSG00000149187; Low tissue specificity.
DR MIM; 601074; gene.
DR neXtProt; NX_Q92879; -.
DR NIAGADS; ENSG00000149187; -.
DR OpenTargets; ENSG00000149187; -.
DR PharmGKB; PA27045; -.
DR VEuPathDB; HostDB:ENSG00000149187; -.
DR eggNOG; KOG0144; Eukaryota.
DR GeneTree; ENSGT00940000158970; -.
DR HOGENOM; CLU_015367_0_2_1; -.
DR InParanoid; Q92879; -.
DR PhylomeDB; Q92879; -.
DR TreeFam; TF314924; -.
DR PathwayCommons; Q92879; -.
DR SignaLink; Q92879; -.
DR SIGNOR; Q92879; -.
DR BioGRID-ORCS; 10658; 39 hits in 1092 CRISPR screens.
DR ChiTaRS; CELF1; human.
DR EvolutionaryTrace; Q92879; -.
DR GeneWiki; CUGBP1; -.
DR GenomeRNAi; 10658; -.
DR Pharos; Q92879; Tbio.
DR PRO; PR:Q92879; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q92879; protein.
DR Bgee; ENSG00000149187; Expressed in secondary oocyte and 214 other tissues.
DR ExpressionAtlas; Q92879; baseline and differential.
DR Genevisible; Q92879; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:ARUK-UCL.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0097356; C:perinucleolar compartment; IDA:ARUK-UCL.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0042835; F:BRE binding; IDA:UniProtKB.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:ARUK-UCL.
DR GO; GO:0003729; F:mRNA binding; IDA:BHF-UCL.
DR GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; NAS:UniProtKB.
DR GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; NAS:UniProtKB.
DR GO; GO:0007281; P:germ cell development; NAS:UniProtKB.
DR GO; GO:0061157; P:mRNA destabilization; ISS:ARUK-UCL.
DR GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
DR GO; GO:0006376; P:mRNA splice site selection; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:ARUK-UCL.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0010942; P:positive regulation of cell death; IMP:ARUK-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0016441; P:post-transcriptional gene silencing; IDA:ARUK-UCL.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; NAS:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:ARUK-UCL.
DR GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
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 IDEAL; IID00490; -.
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 3D-structure; Acetylation; Activator; Alternative splicing; Cytoplasm;
KW Isopeptide bond; 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_0000081538"
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:0007744|PubMed:19413330"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P28659"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045043"
FT VAR_SEQ 1
FT /note="M -> MAAFKLDFLPEMMVDHCSLNSSPVSKKM (in isoform 4)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_026787"
FT VAR_SEQ 104
FT /note="Missing (in isoform 4, isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.6"
FT /id="VSP_026788"
FT VAR_SEQ 231..234
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11686919,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8948631"
FT /id="VSP_005784"
FT VAR_SEQ 297
FT /note="S -> SA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11686919,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_005785"
FT MUTAGEN 63
FT /note="F->L: Does not reduce RNA-binding; when associated
FT with D-331 and F-472. Abolishes ARE/EDEN-dependent
FT deadenylation; when associated with D-331 and F-472."
FT /evidence="ECO:0000269|PubMed:12799066"
FT MUTAGEN 331
FT /note="G->D: Does not reduce RNA-binding; when associated
FT with L-63 and F-472. Abolishes ARE/EDEN-dependent
FT deadenylation; when associated with D-331 and F-472."
FT /evidence="ECO:0000269|PubMed:12799066"
FT MUTAGEN 472
FT /note="L->F: Does not reduce RNA-binding; when associated
FT with L-63 and D-331. Abolishes ARE/EDEN-dependent
FT deadenylation; when associated with D-331 and F-472."
FT /evidence="ECO:0000269|PubMed:12799066"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:3NMR"
FT HELIX 29..37
FT /evidence="ECO:0007829|PDB:3NMR"
FT STRAND 42..50
FT /evidence="ECO:0007829|PDB:3NMR"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:3NMR"
FT STRAND 57..68
FT /evidence="ECO:0007829|PDB:3NMR"
FT HELIX 69..79
FT /evidence="ECO:0007829|PDB:3NMR"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:3NMR"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:3NMR"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3NMR"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:3NMR"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:3NMR"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:3NMR"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:3NMR"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:3NMR"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:2DHS"
FT STRAND 147..157
FT /evidence="ECO:0007829|PDB:3NMR"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:3NMR"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:2DHS"
FT TURN 174..177
FT /evidence="ECO:0007829|PDB:2DHS"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:3NMR"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:2RQ4"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:2RQ4"
FT TURN 399..401
FT /evidence="ECO:0007829|PDB:2RQC"
FT STRAND 403..407
FT /evidence="ECO:0007829|PDB:2CPZ"
FT HELIX 414..421
FT /evidence="ECO:0007829|PDB:2CPZ"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:2CPZ"
FT STRAND 428..434
FT /evidence="ECO:0007829|PDB:2CPZ"
FT STRAND 436..438
FT /evidence="ECO:0007829|PDB:2CPZ"
FT STRAND 440..448
FT /evidence="ECO:0007829|PDB:2CPZ"
FT HELIX 452..462
FT /evidence="ECO:0007829|PDB:2CPZ"
FT STRAND 473..475
FT /evidence="ECO:0007829|PDB:2CPZ"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:2RQ4"
SQ SEQUENCE 486 AA; 52063 MW; C4C13D772273A01D CRC64;
MNGTLDHPDQ PDLDAIKMFV GQVPRTWSEK DLRELFEQYG AVYEINVLRD RSQNPPQSKG
CCFVTFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE KNNAVEDRKL FIGMISKKCT
ENDIRVMFSS FGQIEECRIL RGPDGLSRGC AFVTFTTRAM 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
