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 27-MAR-2024, entry version 177. 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 both as an activator and as a 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 immediately upstream of the edited cytidine. Binds CC AU-rich sequences in the 3'-UTR of COX2 mRNA (By similarity). Binds to CC an intronic RNA element responsible for the silencing of exon 21 CC splicing (By similarity). Binds to (CUG)n repeats (By similarity). May CC be a specific regulator of miRNA biogenesis. Binds to primary microRNA CC pri-MIR140 and, with CELF1, negatively regulates the processing to CC mature 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 47. DR IntAct; O95319; 8. DR MINT; O95319; -. DR STRING; 9606.ENSP00000488422; -. DR GlyCosmos; O95319; 3 sites, 2 glycans. DR GlyGen; O95319; 3 sites, 2 O-linked glycans (3 sites). DR iPTMnet; O95319; -. DR MetOSite; O95319; -. DR PhosphoSitePlus; O95319; -. DR BioMuta; CELF2; -. DR EPD; O95319; -. DR jPOST; O95319; -. DR MassIVE; O95319; -. DR MaxQB; O95319; -. DR PeptideAtlas; 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 Pumba; O95319; -. DR Antibodypedia; 5602; 273 antibodies from 28 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 AGR; HGNC:2550; -. DR DisGeNET; 10659; -. DR GeneCards; CELF2; -. DR HGNC; HGNC:2550; CELF2. DR HPA; ENSG00000048740; Tissue enhanced (bone). DR MalaCards; CELF2; -. 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; PWKQYFS; -. DR OrthoDB; 406581at2759; -. DR PhylomeDB; O95319; -. DR PathwayCommons; O95319; -. DR SignaLink; O95319; -. DR SIGNOR; O95319; -. DR BioGRID-ORCS; 10659; 11 hits in 1154 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 215 other cell types or tissues. DR ExpressionAtlas; O95319; baseline and differential. 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:0036002; F:pre-mRNA binding; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006376; P:mRNA splice site recognition; 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 PANTHER; PTHR24012:SF699; CUGBP ELAV-LIKE FAMILY MEMBER 2; 1. DR PANTHER; PTHR24012; RNA BINDING PROTEIN; 1. DR Pfam; PF00076; RRM_1; 3. DR PRINTS; PR00961; HUDSXLRNA. DR SMART; SM00360; RRM; 3. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50102; RRM; 3. DR UCD-2DPAGE; O95319; -. DR Genevisible; O95319; HS. 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; uncertain 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 //