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O95319

- CELF2_HUMAN

UniProt

O95319 - CELF2_HUMAN

Protein

CUGBP Elav-like family member 2

Gene

CELF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of TNNT2 in embryonic, but not adult, skeletal muscle. Activates TNNT2 exon 5 inclusion by antagonizing the repressive effect of PTB. Acts as both an activator and repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs. Promotes inclusion of exonS 21 and exclusion of exon 5 of the NMDA receptor R1 pre-mRNA. Involved in the apoB RNA editing activity. Increases COX2 mRNA stability and inhibits COX2 mRNA translation in epithelial cells after radiation injury By similarity. Modulates the cellular apoptosis program by regulating COX2-mediated prostaglandin E2 (PGE2) expression By similarity. Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK. Binds to the muscle-specific splicing enhancer (MSE) intronic sites flanking the TNNT2 alternative exon 5. Binds preferentially to UG-rich sequences, in particular UG repeat and UGUU motifs. Binds to apoB mRNA, specifically to AU-rich sequences located immediatly upstream of the edited cytidine. Binds AU-rich sequences in the 3'-UTR of COX2 mRNA By similarity. Binds to an intronic RNA element responsible for the silencing of exon 21 splicing By similarity. Binds to (CUG)n repeats By similarity.By similarity

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. RNA binding Source: ProtInc

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW
    2. regulation of heart contraction Source: ProtInc
    3. RNA processing Source: ProtInc

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CUGBP Elav-like family member 2
    Short name:
    CELF-2
    Alternative name(s):
    Bruno-like protein 3
    CUG triplet repeat RNA-binding protein 2
    Short name:
    CUG-BP2
    CUG-BP- and ETR-3-like factor 2
    ELAV-type RNA-binding protein 3
    Short name:
    ETR-3
    Neuroblastoma apoptosis-related RNA-binding protein
    Short name:
    hNAPOR
    RNA-binding protein BRUNOL-3
    Gene namesi
    Name:CELF2
    Synonyms:BRUNOL3, CUGBP2, ETR3, NAPOR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:2550. CELF2.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Accumulates in the cytoplasm after ionizing radiation By similarity. Colocalizes with APOBEC1 and A1CF. RNA-binding activity is detected in both nuclear and cytoplasmic compartments.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27046.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 508508CUGBP Elav-like family member 2PRO_0000295189Add
    BLAST

    Proteomic databases

    MaxQBiO95319.
    PaxDbiO95319.
    PRIDEiO95319.

    2D gel databases

    UCD-2DPAGEO95319.

    PTM databases

    PhosphoSiteiO95319.

    Expressioni

    Tissue specificityi

    Expressed in frontal cortex. Isoform 1 is expressed in brain and lung. Isoform 2 is expressed in heart, brain, placenta, lung, liver, kidney, skeletal muscle and pancreas. Isoform 4 is expressed in heart, lung, skeletal muscle, kidney and pancreas.5 Publications

    Developmental stagei

    Isoform 1 is expressed in fetal brain. Isoform 2 is expressed in fetal heart, brain, thymus, lung, liver, skeletal muscle, kidney and spleen. Isoform 4 is expressed in fetal heart, brain, thymus, lung and skeletal muscle.2 Publications

    Gene expression databases

    ArrayExpressiO95319.
    BgeeiO95319.
    CleanExiHS_CUGBP2.
    GenevestigatoriO95319.

    Organism-specific databases

    HPAiCAB016395.
    HPA035813.

    Interactioni

    Subunit structurei

    Interacts with A1CF.By similarity

    Protein-protein interaction databases

    BioGridi115902. 8 interactions.
    IntActiO95319. 5 interactions.
    MINTiMINT-2868664.
    STRINGi9606.ENSP00000389951.

    Structurei

    3D structure databases

    ProteinModelPortaliO95319.
    SMRiO95319. Positions 6-211, 388-506.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 12384RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini132 – 21281RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini423 – 50179RRM 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 283283Necessary for RNA-binding, TNNT2 exon 5 and NMDA R1 exon 21 inclusionAdd
    BLAST
    Regioni357 – 508152Necessary for RNA-binding, TNNT2 exon 5 and NMDA R1 exon 21 inclusionAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi284 – 397114Ala-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CELF/BRUNOL family.Curated
    Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG251494.
    HOVERGENiHBG107646.
    KOiK13207.
    OrthoDBiEOG7DVDBR.
    PhylomeDBiO95319.

    Family and domain databases

    Gene3Di3.30.70.330. 3 hits.
    InterProiIPR002343. Hud_Sxl_RNA.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 3 hits.
    [Graphical view]
    PRINTSiPR00961. HUDSXLRNA.
    SMARTiSM00360. RRM. 3 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 3 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95319-1) [UniParc]FASTAAdd to Basket

    Also known as: NAPOR-3

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MRCPKSAVTM RNEELLLSNG TANKMNGALD HSDQPDPDAI KMFVGQIPRS    50
    WSEKELKELF EPYGAVYQIN VLRDRSQNPP QSKGCCFVTF YTRKAALEAQ 100
    NALHNIKTLP GMHHPIQMKP ADSEKSNAVE DRKLFIGMVS KKCNENDIRV 150
    MFSPFGQIEE CRILRGPDGL SRGCAFVTFS TRAMAQNAIK AMHQSQTMEG 200
    CSSPIVVKFA DTQKDKEQRR LQQQLAQQMQ QLNTATWGNL TGLGGLTPQY 250
    LALLQQATSS SNLGAFSGIQ QMAGMNALQL QNLATLAAAA AAAQTSATST 300
    NANPLSTTSS ALGALTSPVA ASTPNSTAGA AMNSLTSLGT LQGLAGATVG 350
    LNNINALAGM AALNGGLGAT GLTNGTAGTM DALTQAYSGI QQYAAAALPT 400
    LYSQSLLQQQ SAAGSQKEGP EGANLFIYHL PQEFGDQDIL QMFMPFGNVI 450
    SAKVFIDKQT NLSKCFGFVS YDNPVSAQAA IQAMNGFQIG MKRLKVQLKR 500
    SKNDSKPY 508
    Length:508
    Mass (Da):54,285
    Last modified:May 1, 1999 - v1
    Checksum:iC65F337D462717F2
    GO
    Isoform 2 (identifier: O95319-2) [UniParc]FASTAAdd to Basket

    Also known as: NAPOR-1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-24: Missing.
         358-358: A → AVAQMLS

    Show »
    Length:490
    Mass (Da):52,268
    Checksum:i3A17B1F5F31AC5BD
    GO
    Isoform 3 (identifier: O95319-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-18: MRCPKSAVTMRNEELLLS → MMVEGRLLVPDRI
         358-358: A → AGTINTPRSKRLLLPKDNN

    Show »
    Length:521
    Mass (Da):55,754
    Checksum:iDD6E4F77FE6B4073
    GO
    Isoform 4 (identifier: O95319-4) [UniParc]FASTAAdd to Basket

    Also known as: NAPOR-2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-18: MRCPKSAVTMRNEELLLS → MMVEGRLLVPDRI
         358-358: A → AVAQMLS

    Show »
    Length:509
    Mass (Da):54,365
    Checksum:i4A0DB5E2372193ED
    GO
    Isoform 5 (identifier: O95319-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-24: Missing.
         359-359: G → GTINS

    Show »
    Length:488
    Mass (Da):52,054
    Checksum:iCBB835681201C245
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti438 – 4381D → H.2 Publications
    Corresponds to variant rs1050942 [ dbSNP | Ensembl ].
    VAR_052202

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2424Missing in isoform 2 and isoform 5. 4 PublicationsVSP_026796Add
    BLAST
    Alternative sequencei1 – 1818MRCPK…ELLLS → MMVEGRLLVPDRI in isoform 3 and isoform 4. 2 PublicationsVSP_026797Add
    BLAST
    Alternative sequencei358 – 3581A → AVAQMLS in isoform 2 and isoform 4. 3 PublicationsVSP_026798
    Alternative sequencei358 – 3581A → AGTINTPRSKRLLLPKDNN in isoform 3. 1 PublicationVSP_026799
    Alternative sequencei359 – 3591G → GTINS in isoform 5. 2 PublicationsVSP_026800

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF090694 mRNA. Translation: AAD13761.1.
    AF090693 mRNA. Translation: AAD13760.1.
    AF036956 mRNA. Translation: AAD02074.1.
    U69546 mRNA. Translation: AAB09040.1.
    AF295068
    , AF295063, AF295064, AF295065, AF295066, AF295067 Genomic DNA. Translation: AAK72223.1.
    AF295068
    , AF295063, AF295064, AF295065, AF295066, AF295067, AF314199 Genomic DNA. Translation: AAK72224.1.
    AF295068
    , AF295063, AF295064, AF295065, AF295066, AF295067 Genomic DNA. Translation: AAK92699.1.
    AF432906 mRNA. Translation: AAL27627.1.
    AK316354 mRNA. Translation: BAH14725.1.
    AL157704, AC026887, AL136320 Genomic DNA. Translation: CAH70230.1.
    AL136320, AC026887, AL157704 Genomic DNA. Translation: CAI20169.1.
    CH471072 Genomic DNA. Translation: EAW86346.1.
    BC036391 mRNA. Translation: AAH36391.1.
    CCDSiCCDS41488.1. [O95319-2]
    CCDS44354.1. [O95319-1]
    CCDS44356.1. [O95319-5]
    RefSeqiNP_001020247.1. NM_001025076.2. [O95319-2]
    NP_001020248.1. NM_001025077.2. [O95319-1]
    NP_001077060.1. NM_001083591.1. [O95319-5]
    NP_006552.3. NM_006561.3.
    UniGeneiHs.309288.

    Genome annotation databases

    EnsembliENST00000399850; ENSP00000382743; ENSG00000048740. [O95319-2]
    ENST00000416382; ENSP00000406451; ENSG00000048740. [O95319-1]
    ENST00000417956; ENSP00000404834; ENSG00000048740. [O95319-5]
    ENST00000608830; ENSP00000476999; ENSG00000048740. [O95319-5]
    GeneIDi10659.
    KEGGihsa:10659.
    UCSCiuc001iki.4. human. [O95319-1]
    uc001ikk.2. human. [O95319-3]
    uc001iko.4. human. [O95319-5]
    uc001ikp.4. human. [O95319-2]
    uc010qbj.1. human. [O95319-4]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF090694 mRNA. Translation: AAD13761.1 .
    AF090693 mRNA. Translation: AAD13760.1 .
    AF036956 mRNA. Translation: AAD02074.1 .
    U69546 mRNA. Translation: AAB09040.1 .
    AF295068
    , AF295063 , AF295064 , AF295065 , AF295066 , AF295067 Genomic DNA. Translation: AAK72223.1 .
    AF295068
    , AF295063 , AF295064 , AF295065 , AF295066 , AF295067 , AF314199 Genomic DNA. Translation: AAK72224.1 .
    AF295068
    , AF295063 , AF295064 , AF295065 , AF295066 , AF295067 Genomic DNA. Translation: AAK92699.1 .
    AF432906 mRNA. Translation: AAL27627.1 .
    AK316354 mRNA. Translation: BAH14725.1 .
    AL157704 , AC026887 , AL136320 Genomic DNA. Translation: CAH70230.1 .
    AL136320 , AC026887 , AL157704 Genomic DNA. Translation: CAI20169.1 .
    CH471072 Genomic DNA. Translation: EAW86346.1 .
    BC036391 mRNA. Translation: AAH36391.1 .
    CCDSi CCDS41488.1. [O95319-2 ]
    CCDS44354.1. [O95319-1 ]
    CCDS44356.1. [O95319-5 ]
    RefSeqi NP_001020247.1. NM_001025076.2. [O95319-2 ]
    NP_001020248.1. NM_001025077.2. [O95319-1 ]
    NP_001077060.1. NM_001083591.1. [O95319-5 ]
    NP_006552.3. NM_006561.3.
    UniGenei Hs.309288.

    3D structure databases

    ProteinModelPortali O95319.
    SMRi O95319. Positions 6-211, 388-506.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115902. 8 interactions.
    IntActi O95319. 5 interactions.
    MINTi MINT-2868664.
    STRINGi 9606.ENSP00000389951.

    PTM databases

    PhosphoSitei O95319.

    2D gel databases

    UCD-2DPAGE O95319.

    Proteomic databases

    MaxQBi O95319.
    PaxDbi O95319.
    PRIDEi O95319.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000399850 ; ENSP00000382743 ; ENSG00000048740 . [O95319-2 ]
    ENST00000416382 ; ENSP00000406451 ; ENSG00000048740 . [O95319-1 ]
    ENST00000417956 ; ENSP00000404834 ; ENSG00000048740 . [O95319-5 ]
    ENST00000608830 ; ENSP00000476999 ; ENSG00000048740 . [O95319-5 ]
    GeneIDi 10659.
    KEGGi hsa:10659.
    UCSCi uc001iki.4. human. [O95319-1 ]
    uc001ikk.2. human. [O95319-3 ]
    uc001iko.4. human. [O95319-5 ]
    uc001ikp.4. human. [O95319-2 ]
    uc010qbj.1. human. [O95319-4 ]

    Organism-specific databases

    CTDi 10659.
    GeneCardsi GC10P011049.
    HGNCi HGNC:2550. CELF2.
    HPAi CAB016395.
    HPA035813.
    MIMi 602538. gene.
    neXtProti NX_O95319.
    PharmGKBi PA27046.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG251494.
    HOVERGENi HBG107646.
    KOi K13207.
    OrthoDBi EOG7DVDBR.
    PhylomeDBi O95319.

    Miscellaneous databases

    ChiTaRSi CELF2. human.
    GeneWikii CUGBP2.
    GenomeRNAii 10659.
    NextBioi 40529.
    PROi O95319.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95319.
    Bgeei O95319.
    CleanExi HS_CUGBP2.
    Genevestigatori O95319.

    Family and domain databases

    Gene3Di 3.30.70.330. 3 hits.
    InterProi IPR002343. Hud_Sxl_RNA.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 3 hits.
    [Graphical view ]
    PRINTSi PR00961. HUDSXLRNA.
    SMARTi SM00360. RRM. 3 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Fluorescent differential display analysis of gene expression in apoptotic neuroblastoma cells."
      Choi D.-K., Ito T., Mitsui Y., Sakaki Y.
      Gene 223:21-31(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT HIS-438.
      Tissue: Brain.
    2. "Developmentally-regulated expression of mNapor encoding an apoptosis-induced ELAV-type RNA binding protein."
      Choi D.-K., Ito T., Tsukahara F., Hirai M., Sakaki Y.
      Gene 237:135-142(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Brain.
    3. "A family of human RNA-binding proteins related to the Drosophila Bruno translational regulator."
      Good P.J., Chen Q., Warner S.J., Herring D.C.
      J. Biol. Chem. 275:28583-28592(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, VARIANT HIS-438.
      Tissue: Heart.
    4. "Genomic organization and isoform-specific tissue expression of human NAPOR (CUGBP2) as a candidate gene for familial arrhythmogenic right ventricular dysplasia."
      Li D., Bachinski L.L., Roberts R.
      Genomics 74:396-401(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    5. "Mutation screening of the NAPOR gene: a candidate for adult-onset primary open angle glaucoma (GLC1E) on 10p14."
      Sarfarazi M., Rezaie T.
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
      Tissue: Synovium.
    7. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    10. "Identification of a (CUG)n triplet repeat RNA-binding protein and its expression in myotonic dystrophy."
      Timchenko L.T., Miller J.W., Timchenko N.A., DeVore D.R., Datar K.V., Lin L., Roberts R., Caskey C.T., Swanson M.S.
      Nucleic Acids Res. 24:4407-4414(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, RNA-BINDING.
    11. "Novel role for RNA-binding protein CUGBP2 in mammalian RNA editing. CUGBP2 modulates C to U editing of apolipoprotein B mRNA by interacting with apobec-1 and ACF, the apobec-1 complementation factor."
      Anant S., Henderson J.O., Mukhopadhyay D., Navaratnam N., Kennedy S., Min J., Davidson N.O.
      J. Biol. Chem. 276:47338-47351(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
    12. "The CELF family of RNA binding proteins is implicated in cell-specific and developmentally regulated alternative splicing."
      Ladd A.N., Charlet-B N., Cooper T.A.
      Mol. Cell. Biol. 21:1285-1296(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING, TISSUE SPECIFICITY.
    13. "Dynamic antagonism between ETR-3 and PTB regulates cell type-specific alternative splicing."
      Charlet-B N., Logan P., Singh G., Cooper T.A.
      Mol. Cell 9:649-658(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    14. "Antagonistic regulation of alpha-actinin alternative splicing by CELF proteins and polypyrimidine tract binding protein."
      Gromak N., Matlin A.J., Cooper T.A., Smith C.W.
      RNA 9:443-456(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    15. "ETR-3 and CELF4 protein domains required for RNA binding and splicing activity in vivo."
      Singh G., Charlet-B N., Han J., Cooper T.A.
      Nucleic Acids Res. 32:1232-1241(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING.
    16. "Identification of putative new splicing targets for ETR-3 using sequences identified by systematic evolution of ligands by exponential enrichment."
      Faustino N.A., Cooper T.A.
      Mol. Cell. Biol. 25:879-887(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    17. "Identification of CELF splicing activation and repression domains in vivo."
      Han J., Cooper T.A.
      Nucleic Acids Res. 33:2769-2780(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "ETR-3 represses Tau exons 2/3 inclusion, a splicing event abnormally enhanced in myotonic dystrophy type I."
      Leroy O., Dhaenens C.-M., Schraen-Maschke S., Belarbi K., Delacourte A., Andreadis A., Sablonniere B., Buee L., Sergeant N., Caillet-Boudin M.-L.
      J. Neurosci. Res. 84:852-859(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCELF2_HUMAN
    AccessioniPrimary (citable) accession number: O95319
    Secondary accession number(s): B7ZAN9
    , Q7KYU4, Q8N499, Q92950, Q96NW9, Q96RQ5, Q96RQ6, Q9UL67
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 10, 2007
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3