CELF2_HUMAN
ID CELF2_HUMAN Reviewed; 508 AA.
AC O95319; B7ZAN9; Q7KYU4; Q8N499; Q92950; Q96NW9; Q96RQ5; Q96RQ6; Q9UL67;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 168.
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 AltName: Full=Neuroblastoma apoptosis-related RNA-binding protein;
DE Short=hNAPOR;
DE AltName: Full=RNA-binding protein BRUNOL-3;
GN Name=CELF2; Synonyms=BRUNOL3, CUGBP2, ETR3, NAPOR;
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 4), AND VARIANT HIS-438.
RC TISSUE=Brain;
RX PubMed=9858671; DOI=10.1016/s0378-1119(98)00364-3;
RA Choi D.-K., Ito T., Mitsui Y., Sakaki Y.;
RT "Fluorescent differential display analysis of gene expression in apoptotic
RT neuroblastoma cells.";
RL Gene 223:21-31(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND VARIANT
RP HIS-438.
RC TISSUE=Heart;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11414768; DOI=10.1006/geno.2001.6558;
RA Li D., Bachinski L.L., Roberts R.;
RT "Genomic organization and isoform-specific tissue expression of human NAPOR
RT (CUGBP2) as a candidate gene for familial arrhythmogenic right ventricular
RT dysplasia.";
RL Genomics 74:396-401(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RA Sarfarazi M., Rezaie T.;
RT "Mutation screening of the NAPOR gene: a candidate for adult-onset primary
RT open angle glaucoma (GLC1E) on 10p14.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Synovium;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
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=Brain;
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 SUBCELLULAR LOCATION, AND 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 [11]
RP FUNCTION, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=11577082; DOI=10.1074/jbc.m104911200;
RA Anant S., Henderson J.O., Mukhopadhyay D., Navaratnam N., Kennedy S.,
RA Min J., Davidson N.O.;
RT "Novel role for RNA-binding protein CUGBP2 in mammalian RNA editing. CUGBP2
RT modulates C to U editing of apolipoprotein B mRNA by interacting with
RT apobec-1 and ACF, the apobec-1 complementation factor.";
RL J. Biol. Chem. 276:47338-47351(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, AND RNA-BINDING.
RX PubMed=11931771; DOI=10.1016/s1097-2765(02)00479-3;
RA Charlet-B N., Logan P., Singh G., Cooper T.A.;
RT "Dynamic antagonism between ETR-3 and PTB regulates cell type-specific
RT alternative splicing.";
RL Mol. Cell 9:649-658(2002).
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, SUBCELLULAR LOCATION, AND RNA-BINDING.
RX PubMed=14973222; DOI=10.1093/nar/gkh275;
RA Singh G., Charlet-B N., Han J., Cooper T.A.;
RT "ETR-3 and CELF4 protein domains required for RNA binding and splicing
RT activity in vivo.";
RL Nucleic Acids Res. 32:1232-1241(2004).
RN [16]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=15657417; DOI=10.1128/mcb.25.3.879-887.2005;
RA Faustino N.A., Cooper T.A.;
RT "Identification of putative new splicing targets for ETR-3 using sequences
RT identified by systematic evolution of ligands by exponential enrichment.";
RL Mol. Cell. Biol. 25:879-887(2005).
RN [17]
RP FUNCTION.
RX PubMed=15894795; DOI=10.1093/nar/gki561;
RA Han J., Cooper T.A.;
RT "Identification of CELF splicing activation and repression domains in
RT vivo.";
RL Nucleic Acids Res. 33:2769-2780(2005).
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 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 [20]
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 [21]
RP INVOLVEMENT IN DEE97, VARIANTS DEE97 GLY-493 AND SER-507, CHARACTERIZATION
RP OF VARIANTS DEE97 GLY-493 AND SER-507, AND SUBCELLULAR LOCATION.
RX PubMed=33131106; DOI=10.1002/humu.24130;
RA Itai T., Hamanaka K., Sasaki K., Wagner M., Kotzaeridou U., Broesse I.,
RA Ries M., Kobayashi Y., Tohyama J., Kato M., Ong W.P., Chew H.B.,
RA Rethanavelu K., Ranza E., Blanc X., Uchiyama Y., Tsuchida N., Fujita A.,
RA Azuma Y., Koshimizu E., Mizuguchi T., Takata A., Miyake N., Takahashi H.,
RA Miyagi E., Tsurusaki Y., Doi H., Taguri M., Antonarakis S.E., Nakashima M.,
RA Saitsu H., Miyatake S., Matsumoto N.;
RT "De novo variants in CELF2 that disrupt the nuclear localization signal
RT cause developmental and epileptic encephalopathy.";
RL Hum. Mutat. 42:66-76(2021).
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 TNNT2 in embryonic, but not adult, skeletal muscle.
CC Activates TNNT2 exon 5 inclusion by antagonizing the repressive effect
CC of PTB. 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.
CC Promotes inclusion of exonS 21 and exclusion of exon 5 of the NMDA
CC receptor R1 pre-mRNA. Involved in the apoB RNA editing activity.
CC Increases COX2 mRNA stability and inhibits COX2 mRNA translation in
CC epithelial cells after radiation injury (By similarity). Modulates the
CC cellular apoptosis program by regulating COX2-mediated prostaglandin E2
CC (PGE2) expression (By similarity). Binds to (CUG)n triplet repeats in
CC the 3'-UTR of transcripts such as DMPK. Binds to the muscle-specific
CC splicing enhancer (MSE) intronic sites flanking the TNNT2 alternative
CC exon 5. Binds preferentially to UG-rich sequences, in particular UG
CC repeat and UGUU motifs. Binds to apoB mRNA, specifically to AU-rich
CC sequences located immediatly upstream of the edited cytidine. Binds AU-
CC rich sequences in the 3'-UTR of COX2 mRNA (By similarity). Binds to an
CC intronic RNA element responsible for the silencing of exon 21 splicing
CC (By similarity). Binds to (CUG)n repeats (By similarity). 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 (PubMed:28431233). {ECO:0000250|UniProtKB:Q9Z0H4,
CC ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:11577082,
CC ECO:0000269|PubMed:11931771, ECO:0000269|PubMed:12649496,
CC ECO:0000269|PubMed:14973222, ECO:0000269|PubMed:15657417,
CC ECO:0000269|PubMed:15894795, ECO:0000269|PubMed:28431233}.
CC -!- SUBUNIT: Interacts with A1CF. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33131106}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q7T2T1, ECO:0000250|UniProtKB:Q9Z0H4}.
CC Note=Accumulates in the cytoplasm after ionizing radiation (By
CC similarity). Colocalizes with APOBEC1 and A1CF. RNA-binding activity is
CC detected in both nuclear and cytoplasmic compartments. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=NAPOR-3;
CC IsoId=O95319-1; Sequence=Displayed;
CC Name=2; Synonyms=NAPOR-1;
CC IsoId=O95319-2; Sequence=VSP_026796, VSP_026798;
CC Name=3;
CC IsoId=O95319-3; Sequence=VSP_026797, VSP_026799;
CC Name=4; Synonyms=NAPOR-2;
CC IsoId=O95319-4; Sequence=VSP_026797, VSP_026798;
CC Name=5;
CC IsoId=O95319-5; Sequence=VSP_026796, VSP_026800;
CC -!- TISSUE SPECIFICITY: Expressed in frontal cortex. Isoform 1 is expressed
CC in brain and lung. Isoform 2 is expressed in heart, brain, placenta,
CC lung, liver, kidney, skeletal muscle and pancreas. Isoform 4 is
CC expressed in heart, lung, skeletal muscle, kidney and pancreas.
CC {ECO:0000269|PubMed:10524244, ECO:0000269|PubMed:10893231,
CC ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:11414768,
CC ECO:0000269|PubMed:16862542}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is expressed in fetal brain. Isoform 2
CC is expressed in fetal heart, brain, thymus, lung, liver, skeletal
CC muscle, kidney and spleen. Isoform 4 is expressed in fetal heart,
CC brain, thymus, lung and skeletal muscle. {ECO:0000269|PubMed:10524244,
CC ECO:0000269|PubMed:11414768}.
CC -!- DISEASE: Developmental and epileptic encephalopathy 97 (DEE97)
CC [MIM:619561]: A form of epileptic encephalopathy, a heterogeneous group
CC of early-onset epilepsies characterized by refractory seizures,
CC neurodevelopmental impairment, and poor prognosis. Development is
CC normal prior to seizure onset, after which cognitive and motor delays
CC become apparent. DEE97 is an autosomal dominant form.
CC {ECO:0000269|PubMed:33131106}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CELF/BRUNOL family. {ECO:0000305}.
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DR EMBL; AF090694; AAD13761.1; -; mRNA.
DR EMBL; AF090693; AAD13760.1; -; mRNA.
DR EMBL; AF036956; AAD02074.1; -; mRNA.
DR EMBL; U69546; AAB09040.1; -; mRNA.
DR EMBL; AF295068; AAK72223.1; -; Genomic_DNA.
DR EMBL; AF295063; AAK72223.1; JOINED; Genomic_DNA.
DR EMBL; AF295064; AAK72223.1; JOINED; Genomic_DNA.
DR EMBL; AF295065; AAK72223.1; JOINED; Genomic_DNA.
DR EMBL; AF295066; AAK72223.1; JOINED; Genomic_DNA.
DR EMBL; AF295067; AAK72223.1; JOINED; Genomic_DNA.
DR EMBL; AF295068; AAK72224.1; -; Genomic_DNA.
DR EMBL; AF295063; AAK72224.1; JOINED; Genomic_DNA.
DR EMBL; AF295064; AAK72224.1; JOINED; Genomic_DNA.
DR EMBL; AF295065; AAK72224.1; JOINED; Genomic_DNA.
DR EMBL; AF295066; AAK72224.1; JOINED; Genomic_DNA.
DR EMBL; AF295067; AAK72224.1; JOINED; Genomic_DNA.
DR EMBL; AF314199; AAK72224.1; JOINED; Genomic_DNA.
DR EMBL; AF295068; AAK92699.1; -; Genomic_DNA.
DR EMBL; AF295063; AAK92699.1; JOINED; Genomic_DNA.
DR EMBL; AF295064; AAK92699.1; JOINED; Genomic_DNA.
DR EMBL; AF295065; AAK92699.1; JOINED; Genomic_DNA.
DR EMBL; AF295066; AAK92699.1; JOINED; Genomic_DNA.
DR EMBL; AF295067; AAK92699.1; JOINED; Genomic_DNA.
DR EMBL; AF432906; AAL27627.1; -; mRNA.
DR EMBL; AK316354; BAH14725.1; -; mRNA.
DR EMBL; AC026887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157704; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86346.1; -; Genomic_DNA.
DR EMBL; BC036391; AAH36391.1; -; mRNA.
DR CCDS; CCDS41488.1; -. [O95319-2]
DR CCDS; CCDS44354.1; -. [O95319-1]
DR CCDS; CCDS44356.1; -. [O95319-5]
DR RefSeq; NP_001020247.1; NM_001025076.2. [O95319-2]
DR RefSeq; NP_001020248.1; NM_001025077.2. [O95319-1]
DR RefSeq; NP_001077060.1; NM_001083591.1. [O95319-5]
DR RefSeq; NP_001313246.1; NM_001326317.1.
DR RefSeq; NP_001313247.1; NM_001326318.1. [O95319-2]
DR RefSeq; NP_001313248.1; NM_001326319.1.
DR RefSeq; NP_001313249.1; NM_001326320.1. [O95319-2]
DR RefSeq; NP_001313250.1; NM_001326321.1.
DR RefSeq; NP_001313253.1; NM_001326324.1. [O95319-2]
DR RefSeq; NP_001313257.1; NM_001326328.1. [O95319-2]
DR RefSeq; NP_001313258.1; NM_001326329.1.
DR RefSeq; NP_001313259.1; NM_001326330.1. [O95319-2]
DR RefSeq; NP_001313261.1; NM_001326332.1. [O95319-1]
DR RefSeq; NP_001313262.1; NM_001326333.1.
DR RefSeq; NP_001313263.1; NM_001326334.1. [O95319-2]
DR RefSeq; NP_001313265.1; NM_001326336.1.
DR RefSeq; NP_001313268.1; NM_001326339.1.
DR RefSeq; NP_001313269.1; NM_001326340.1.
DR RefSeq; NP_001313271.1; NM_001326342.1.
DR RefSeq; NP_001313272.1; NM_001326343.1.
DR RefSeq; NP_001313273.1; NM_001326344.1.
DR RefSeq; NP_001313274.1; NM_001326345.1. [O95319-2]
DR RefSeq; NP_001313277.1; NM_001326348.1.
DR RefSeq; NP_001313278.1; NM_001326349.1. [O95319-2]
DR RefSeq; NP_006552.3; NM_006561.3.
DR RefSeq; XP_011517596.1; XM_011519294.2.
DR RefSeq; XP_011517599.1; XM_011519297.1.
DR RefSeq; XP_016871042.1; XM_017015553.1.
DR RefSeq; XP_016871043.1; XM_017015554.1.
DR PDB; 2MY7; NMR; -; A=416-508.
DR PDB; 2MY8; NMR; -; A=416-508.
DR PDB; 4LJM; X-ray; 3.00 A; A/B=416-508.
DR PDB; 4LMZ; X-ray; 2.78 A; A=36-211.
DR PDB; 4TLQ; X-ray; 2.50 A; A/B=416-508.
DR PDB; 5M8I; NMR; -; A=416-508.
DR PDBsum; 2MY7; -.
DR PDBsum; 2MY8; -.
DR PDBsum; 4LJM; -.
DR PDBsum; 4LMZ; -.
DR PDBsum; 4TLQ; -.
DR PDBsum; 5M8I; -.
DR AlphaFoldDB; O95319; -.
DR BMRB; O95319; -.
DR SMR; O95319; -.
DR BioGRID; 115902; 43.
DR IntAct; O95319; 8.
DR MINT; O95319; -.
DR GlyGen; O95319; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; O95319; -.
DR MetOSite; O95319; -.
DR PhosphoSitePlus; O95319; -.
DR BioMuta; CELF2; -.
DR UCD-2DPAGE; O95319; -.
DR EPD; O95319; -.
DR jPOST; O95319; -.
DR MassIVE; O95319; -.
DR MaxQB; O95319; -.
DR PaxDb; O95319; -.
DR PeptideAtlas; O95319; -.
DR PRIDE; O95319; -.
DR ProteomicsDB; 50802; -. [O95319-1]
DR ProteomicsDB; 50803; -. [O95319-2]
DR ProteomicsDB; 50804; -. [O95319-3]
DR ProteomicsDB; 50805; -. [O95319-4]
DR ProteomicsDB; 50806; -. [O95319-5]
DR Antibodypedia; 5602; 242 antibodies from 27 providers.
DR DNASU; 10659; -.
DR Ensembl; ENST00000399850.7; ENSP00000382743.3; ENSG00000048740.19. [O95319-2]
DR Ensembl; ENST00000416382.6; ENSP00000406451.2; ENSG00000048740.19. [O95319-1]
DR Ensembl; ENST00000417956.6; ENSP00000404834.3; ENSG00000048740.19. [O95319-2]
DR Ensembl; ENST00000608830.5; ENSP00000476999.1; ENSG00000048740.19. [O95319-5]
DR Ensembl; ENST00000631460.1; ENSP00000488582.1; ENSG00000048740.19. [O95319-1]
DR Ensembl; ENST00000632728.1; ENSP00000487802.1; ENSG00000048740.19. [O95319-2]
DR Ensembl; ENST00000638035.1; ENSP00000490401.1; ENSG00000048740.19. [O95319-2]
DR GeneID; 10659; -.
DR KEGG; hsa:10659; -.
DR UCSC; uc031vxc.2; human. [O95319-1]
DR CTD; 10659; -.
DR DisGeNET; 10659; -.
DR GeneCards; CELF2; -.
DR HGNC; HGNC:2550; CELF2.
DR HPA; ENSG00000048740; Tissue enhanced (bone).
DR MIM; 602538; gene.
DR MIM; 619561; phenotype.
DR neXtProt; NX_O95319; -.
DR OpenTargets; ENSG00000048740; -.
DR Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
DR PharmGKB; PA27046; -.
DR VEuPathDB; HostDB:ENSG00000048740; -.
DR eggNOG; KOG0144; Eukaryota.
DR GeneTree; ENSGT00940000155461; -.
DR HOGENOM; CLU_015367_0_2_1; -.
DR InParanoid; O95319; -.
DR OMA; PMGNGMN; -.
DR OrthoDB; 1209165at2759; -.
DR PhylomeDB; O95319; -.
DR PathwayCommons; O95319; -.
DR SignaLink; O95319; -.
DR SIGNOR; O95319; -.
DR BioGRID-ORCS; 10659; 10 hits in 1078 CRISPR screens.
DR ChiTaRS; CELF2; human.
DR GeneWiki; CUGBP2; -.
DR GenomeRNAi; 10659; -.
DR Pharos; O95319; Tbio.
DR PRO; PR:O95319; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O95319; protein.
DR Bgee; ENSG00000048740; Expressed in CA1 field of hippocampus and 213 other tissues.
DR ExpressionAtlas; O95319; baseline and differential.
DR Genevisible; O95319; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0090543; C:Flemming body; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006376; P:mRNA splice site selection; IDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0008016; P:regulation of heart contraction; TAS:ProtInc.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
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 3D-structure; Alternative splicing; Cytoplasm; Disease variant; Epilepsy;
KW Intellectual disability; mRNA processing; Nucleus; Reference proteome;
KW Repeat; Repressor; RNA-binding.
FT CHAIN 1..508
FT /note="CUGBP Elav-like family member 2"
FT /id="PRO_0000295189"
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 REGION 357..508
FT /note="Necessary for RNA-binding, TNNT2 exon 5 and NMDA R1
FT exon 21 inclusion"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10524244,
FT ECO:0000303|PubMed:10893231, ECO:0000303|PubMed:14702039,
FT ECO:0000303|Ref.5"
FT /id="VSP_026796"
FT VAR_SEQ 1..18
FT /note="MRCPKSAVTMRNEELLLS -> MMVEGRLLVPDRI (in isoform 3
FT and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9858671"
FT /id="VSP_026797"
FT VAR_SEQ 358
FT /note="A -> AVAQMLS (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10524244,
FT ECO:0000303|PubMed:10893231, ECO:0000303|PubMed:9858671"
FT /id="VSP_026798"
FT VAR_SEQ 358
FT /note="A -> AGTINTPRSKRLLLPKDNN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026799"
FT VAR_SEQ 359
FT /note="G -> GTINS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.5"
FT /id="VSP_026800"
FT VARIANT 438
FT /note="D -> H (in dbSNP:rs1050942)"
FT /evidence="ECO:0000269|PubMed:10893231,
FT ECO:0000269|PubMed:9858671"
FT /id="VAR_052202"
FT VARIANT 493
FT /note="R -> G (in DEE97; unknown pathological significance;
FT mislocalized to the cytoplasm)"
FT /evidence="ECO:0000269|PubMed:33131106"
FT /id="VAR_086490"
FT VARIANT 507
FT /note="P -> S (in DEE97; mislocalized to the cytoplasm)"
FT /evidence="ECO:0000269|PubMed:33131106"
FT /id="VAR_086491"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:4LMZ"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:4LMZ"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:4LMZ"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:4LMZ"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:4LMZ"
FT STRAND 81..92
FT /evidence="ECO:0007829|PDB:4LMZ"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:4LMZ"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:4LMZ"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:4LMZ"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:4LMZ"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:4LMZ"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:4LMZ"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:4LMZ"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:4LMZ"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:4LMZ"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:4LMZ"
FT STRAND 171..182
FT /evidence="ECO:0007829|PDB:4LMZ"
FT HELIX 183..192
FT /evidence="ECO:0007829|PDB:4LMZ"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:4LMZ"
FT STRAND 424..429
FT /evidence="ECO:0007829|PDB:4TLQ"
FT HELIX 436..443
FT /evidence="ECO:0007829|PDB:4TLQ"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:4TLQ"
FT STRAND 449..456
FT /evidence="ECO:0007829|PDB:4TLQ"
FT TURN 458..460
FT /evidence="ECO:0007829|PDB:4TLQ"
FT STRAND 463..473
FT /evidence="ECO:0007829|PDB:4TLQ"
FT HELIX 474..484
FT /evidence="ECO:0007829|PDB:4TLQ"
FT STRAND 495..498
FT /evidence="ECO:0007829|PDB:4TLQ"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:5M8I"
SQ SEQUENCE 508 AA; 54285 MW; C65F337D462717F2 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
NANPLSTTSS ALGALTSPVA ASTPNSTAGA AMNSLTSLGT LQGLAGATVG LNNINALAGM
AALNGGLGAT GLTNGTAGTM DALTQAYSGI QQYAAAALPT LYSQSLLQQQ SAAGSQKEGP
EGANLFIYHL PQEFGDQDIL QMFMPFGNVI SAKVFIDKQT NLSKCFGFVS YDNPVSAQAA
IQAMNGFQIG MKRLKVQLKR SKNDSKPY
