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Q92879

- CELF1_HUMAN

UniProt

Q92879 - CELF1_HUMAN

Protein

CUGBP Elav-like family member 1

Gene

CELF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (18 Oct 2001)
      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 cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. 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. Activates SM exon 5 inclusion by antagonizing the repressive effect of PTB. Promotes exclusion of exon 11 of the INSR pre-mRNA. Inhibits, together with HNRNPH1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast. Increases translation and controls the choice of translation initiation codon of CEBPB mRNA. Increases mRNA translation of CEBPB in aging liver By similarity. Increases translation of CDKN1A mRNA by antagonizing the repressive effect of CALR3. Mediates rapid cytoplasmic mRNA deadenylation. Recruits the deadenylase PARN to the poly(A) tail of EDEN-containing mRNAs to promote their deadenylation. Required for completion of spermatogenesis By similarity. Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK and to Bruno response elements (BREs). Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA. Binds to AU-rich sequences (AREs or EDEN-like) localized in the 3'-UTR of JUN and FOS mRNAs. Binds to the IR RNA. Binds to the 5'-region of CDKN1A and CEBPB mRNAs. Binds with the 5'-region of CEBPB mRNA in aging liver.By similarity8 Publications

    GO - Molecular functioni

    1. BRE binding Source: UniProtKB
    2. mRNA binding Source: BHF-UCL
    3. nucleotide binding Source: InterPro
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. RNA binding Source: UniProtKB
    7. translation repressor activity, nucleic acid binding Source: UniProtKB

    GO - Biological processi

    1. embryo development Source: UniProtKB
    2. germ cell development Source: UniProtKB
    3. mRNA processing Source: ProtInc
    4. mRNA splice site selection Source: UniProtKB
    5. negative regulation of translation Source: GOC
    6. positive regulation of multicellular organism growth Source: Ensembl
    7. regulation of RNA splicing Source: UniProtKB
    8. RNA interference Source: UniProtKB
    9. spermatid development Source: Ensembl

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CUGBP Elav-like family member 1
    Short name:
    CELF-1
    Alternative name(s):
    50 kDa nuclear polyadenylated RNA-binding protein
    Bruno-like protein 2
    CUG triplet repeat RNA-binding protein 1
    Short name:
    CUG-BP1
    CUG-BP- and ETR-3-like factor 1
    Deadenylation factor CUG-BP
    Embryo deadenylation element-binding protein homolog
    Short name:
    EDEN-BP homolog
    RNA-binding protein BRUNOL-2
    Gene namesi
    Name:CELF1
    Synonyms:BRUNOL2, CUGBP, CUGBP1, NAB50
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:2549. CELF1.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: RNA-binding activity is detected in both nuclear and cytoplasmic compartments.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi63 – 631F → L: Does not reduce RNA-binding; when associated with D-331 and F-472. Abolishes ARE/EDEN-dependent deadenylation; when associated with D-331 and F-472. 1 Publication
    Mutagenesisi331 – 3311G → D: Does not reduce RNA-binding; when associated with L-63 and F-472. Abolishes ARE/EDEN-dependent deadenylation; when associated with D-331 and F-472. 1 Publication
    Mutagenesisi472 – 4721L → F: Does not reduce RNA-binding; when associated with L-63 and D-331. Abolishes ARE/EDEN-dependent deadenylation; when associated with D-331 and F-472. 1 Publication

    Organism-specific databases

    PharmGKBiPA27045.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486CUGBP Elav-like family member 1PRO_0000081538Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei302 – 3021PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated. Its phosphorylation status increases in senescent cells.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ92879.
    PaxDbiQ92879.
    PRIDEiQ92879.

    PTM databases

    PhosphoSiteiQ92879.

    Expressioni

    Tissue specificityi

    Ubiquitous.3 Publications

    Inductioni

    Up-regulated in myotonic dystrophy pathophysiology (DM).1 Publication

    Gene expression databases

    ArrayExpressiQ92879.
    BgeeiQ92879.
    CleanExiHS_CUGBP1.
    GenevestigatoriQ92879.

    Organism-specific databases

    HPAiCAB016114.
    HPA044597.

    Interactioni

    Subunit structurei

    Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Associates with polysomes By similarity. Interacts with HNRNPH1; the interaction in RNA-dependent. Interacts with PARN.By similarity3 Publications

    Protein-protein interaction databases

    BioGridi115901. 16 interactions.
    IntActiQ92879. 9 interactions.
    MINTiMINT-1382906.
    STRINGi9606.ENSP00000351409.

    Structurei

    Secondary structure

    1
    486
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi16 – 227
    Helixi29 – 379
    Beta strandi42 – 509
    Beta strandi52 – 554
    Beta strandi57 – 6812
    Helixi69 – 7911
    Turni80 – 823
    Beta strandi93 – 964
    Helixi98 – 1003
    Helixi105 – 1073
    Beta strandi108 – 1147
    Helixi121 – 1288
    Helixi129 – 1313
    Beta strandi134 – 1418
    Turni143 – 1453
    Beta strandi147 – 15711
    Helixi158 – 16811
    Turni169 – 1713
    Turni174 – 1774
    Beta strandi182 – 1854
    Helixi385 – 3884
    Beta strandi389 – 3913
    Turni399 – 4013
    Beta strandi403 – 4075
    Helixi414 – 4218
    Helixi422 – 4243
    Beta strandi428 – 4347
    Beta strandi436 – 4383
    Beta strandi440 – 4489
    Helixi452 – 46211
    Beta strandi473 – 4753
    Beta strandi482 – 4843

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CPZNMR-A383-484[»]
    2DHSNMR-A1-187[»]
    2RQ4NMR-A383-484[»]
    2RQCNMR-A383-484[»]
    3NMRX-ray1.85A14-187[»]
    3NNAX-ray1.90A14-187[»]
    3NNCX-ray2.20A14-187[»]
    3NNHX-ray2.75A/B/C/D14-100[»]
    ProteinModelPortaliQ92879.
    SMRiQ92879. Positions 1-187, 355-484.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92879.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 9984RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini108 – 18881RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini401 – 47979RRM 3PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi287 – 30822Ser-richAdd
    BLAST

    Domaini

    RRM1 and RRM2 domains preferentially target UGU(U/G)-rich mRNA elements.1 Publication

    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.
    HOGENOMiHOG000004754.
    HOVERGENiHBG107646.
    InParanoidiQ92879.
    KOiK13207.
    OrthoDBiEOG7DVDBR.
    PhylomeDBiQ92879.
    TreeFamiTF314924.

    Family and domain databases

    Gene3Di3.30.70.330. 3 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 3 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 3 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 3 hits.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92879-1) [UniParc]FASTAAdd to Basket

    Also known as: LYLQ

    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

    MNGTLDHPDQ PDLDAIKMFV GQVPRTWSEK DLRELFEQYG AVYEINVLRD    50
    RSQNPPQSKG CCFVTFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE 100
    KNNAVEDRKL FIGMISKKCT ENDIRVMFSS FGQIEECRIL RGPDGLSRGC 150
    AFVTFTTRAM AQTAIKAMHQ AQTMEGCSSP MVVKFADTQK DKEQKRMAQQ 200
    LQQQMQQISA ASVWGNLAGL NTLGPQYLAL YLQLLQQTAS SGNLNTLSSL 250
    HPMGGLNAMQ LQNLAALAAA ASAAQNTPSG TNALTTSSSP LSVLTSSGSS 300
    PSSSSSNSVN PIASLGALQT LAGATAGLNV GSLAGMAALN GGLGSSGLSN 350
    GTGSTMEALT QAYSGIQQYA AAALPTLYNQ NLLTQQSIGA AGSQKEGPEG 400
    ANLFIYHLPQ EFGDQDLLQM FMPFGNVVSA KVFIDKQTNL SKCFGFVSYD 450
    NPVSAQAAIQ SMNGFQIGMK RLKVQLKRSK NDSKPY 486

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Length:486
    Mass (Da):52,063
    Last modified:October 18, 2001 - v2
    Checksum:iC4C13D772273A01D
    GO
    Isoform 2 (identifier: Q92879-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         231-234: Missing.

    Show »
    Length:482
    Mass (Da):51,546
    Checksum:iAC0863DB01A22163
    GO
    Isoform 3 (identifier: Q92879-3) [UniParc]FASTAAdd to Basket

    Also known as: A

    The sequence of this isoform differs from the canonical sequence as follows:
         231-234: Missing.
         297-297: S → SA

    Show »
    Length:483
    Mass (Da):51,617
    Checksum:i0C8D6B707E157FD1
    GO
    Isoform 4 (identifier: Q92879-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MAAFKLDFLPEMMVDHCSLNSSPVSKKM
         104-104: Missing.

    Show »
    Length:512
    Mass (Da):55,001
    Checksum:i2A099A7F4E0F5358
    GO
    Isoform 5 (identifier: Q92879-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-17: Missing.
         104-104: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:468
    Mass (Da):50,130
    Checksum:i7CD2C6BFBE344830
    GO
    Isoform 6 (identifier: Q92879-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         104-104: Missing.

    Show »
    Length:485
    Mass (Da):51,992
    Checksum:i37B0006E19EC012A
    GO

    Sequence cautioni

    The sequence BAE06101.1 differs from that shown. Reason: Erroneous initiation.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1717Missing in isoform 5. 1 PublicationVSP_045043Add
    BLAST
    Alternative sequencei1 – 11M → MAAFKLDFLPEMMVDHCSLN SSPVSKKM in isoform 4. 1 PublicationVSP_026787
    Alternative sequencei104 – 1041Missing in isoform 4, isoform 5 and isoform 6. 2 PublicationsVSP_026788
    Alternative sequencei231 – 2344Missing in isoform 2 and isoform 3. 3 PublicationsVSP_005784
    Alternative sequencei297 – 2971S → SA in isoform 3. 2 PublicationsVSP_005785

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U63289 mRNA. Translation: AAC50895.1.
    AF248648 mRNA. Translation: AAF86230.1.
    AF267533 mRNA. Translation: AAF78955.1.
    AF267534 mRNA. Translation: AAF78956.1.
    AJ007988 mRNA. Translation: CAC20566.1.
    AK304430 mRNA. Translation: BAG65257.1.
    AB210019 mRNA. Translation: BAE06101.1. Different initiation.
    AC090559 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW67909.1.
    CH471064 Genomic DNA. Translation: EAW67912.1.
    BC031079 mRNA. Translation: AAH31079.1.
    CCDSiCCDS31482.1. [Q92879-1]
    CCDS53622.1. [Q92879-6]
    CCDS53623.1. [Q92879-4]
    CCDS7938.1. [Q92879-2]
    CCDS7939.1. [Q92879-3]
    RefSeqiNP_001020767.1. NM_001025596.2. [Q92879-1]
    NP_001166110.1. NM_001172639.1. [Q92879-4]
    NP_001166111.1. NM_001172640.1. [Q92879-6]
    NP_006551.1. NM_006560.3. [Q92879-2]
    NP_941989.1. NM_198700.2. [Q92879-3]
    UniGeneiHs.595333.

    Genome annotation databases

    EnsembliENST00000310513; ENSP00000308386; ENSG00000149187. [Q92879-2]
    ENST00000358597; ENSP00000351409; ENSG00000149187. [Q92879-1]
    ENST00000361904; ENSP00000354639; ENSG00000149187. [Q92879-3]
    ENST00000395290; ENSP00000378705; ENSG00000149187. [Q92879-6]
    ENST00000395292; ENSP00000378706; ENSG00000149187. [Q92879-3]
    ENST00000532048; ENSP00000435926; ENSG00000149187. [Q92879-4]
    GeneIDi10658.
    KEGGihsa:10658.
    UCSCiuc001nfk.2. human. [Q92879-4]
    uc001nfl.3. human. [Q92879-1]
    uc001nfm.3. human. [Q92879-3]
    uc001nfn.3. human. [Q92879-2]

    Polymorphism databases

    DMDMi17374605.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U63289 mRNA. Translation: AAC50895.1 .
    AF248648 mRNA. Translation: AAF86230.1 .
    AF267533 mRNA. Translation: AAF78955.1 .
    AF267534 mRNA. Translation: AAF78956.1 .
    AJ007988 mRNA. Translation: CAC20566.1 .
    AK304430 mRNA. Translation: BAG65257.1 .
    AB210019 mRNA. Translation: BAE06101.1 . Different initiation.
    AC090559 Genomic DNA. No translation available.
    CH471064 Genomic DNA. Translation: EAW67909.1 .
    CH471064 Genomic DNA. Translation: EAW67912.1 .
    BC031079 mRNA. Translation: AAH31079.1 .
    CCDSi CCDS31482.1. [Q92879-1 ]
    CCDS53622.1. [Q92879-6 ]
    CCDS53623.1. [Q92879-4 ]
    CCDS7938.1. [Q92879-2 ]
    CCDS7939.1. [Q92879-3 ]
    RefSeqi NP_001020767.1. NM_001025596.2. [Q92879-1 ]
    NP_001166110.1. NM_001172639.1. [Q92879-4 ]
    NP_001166111.1. NM_001172640.1. [Q92879-6 ]
    NP_006551.1. NM_006560.3. [Q92879-2 ]
    NP_941989.1. NM_198700.2. [Q92879-3 ]
    UniGenei Hs.595333.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CPZ NMR - A 383-484 [» ]
    2DHS NMR - A 1-187 [» ]
    2RQ4 NMR - A 383-484 [» ]
    2RQC NMR - A 383-484 [» ]
    3NMR X-ray 1.85 A 14-187 [» ]
    3NNA X-ray 1.90 A 14-187 [» ]
    3NNC X-ray 2.20 A 14-187 [» ]
    3NNH X-ray 2.75 A/B/C/D 14-100 [» ]
    ProteinModelPortali Q92879.
    SMRi Q92879. Positions 1-187, 355-484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115901. 16 interactions.
    IntActi Q92879. 9 interactions.
    MINTi MINT-1382906.
    STRINGi 9606.ENSP00000351409.

    PTM databases

    PhosphoSitei Q92879.

    Polymorphism databases

    DMDMi 17374605.

    Proteomic databases

    MaxQBi Q92879.
    PaxDbi Q92879.
    PRIDEi Q92879.

    Protocols and materials databases

    DNASUi 10658.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310513 ; ENSP00000308386 ; ENSG00000149187 . [Q92879-2 ]
    ENST00000358597 ; ENSP00000351409 ; ENSG00000149187 . [Q92879-1 ]
    ENST00000361904 ; ENSP00000354639 ; ENSG00000149187 . [Q92879-3 ]
    ENST00000395290 ; ENSP00000378705 ; ENSG00000149187 . [Q92879-6 ]
    ENST00000395292 ; ENSP00000378706 ; ENSG00000149187 . [Q92879-3 ]
    ENST00000532048 ; ENSP00000435926 ; ENSG00000149187 . [Q92879-4 ]
    GeneIDi 10658.
    KEGGi hsa:10658.
    UCSCi uc001nfk.2. human. [Q92879-4 ]
    uc001nfl.3. human. [Q92879-1 ]
    uc001nfm.3. human. [Q92879-3 ]
    uc001nfn.3. human. [Q92879-2 ]

    Organism-specific databases

    CTDi 10658.
    GeneCardsi GC11M048801.
    HGNCi HGNC:2549. CELF1.
    HPAi CAB016114.
    HPA044597.
    MIMi 601074. gene.
    neXtProti NX_Q92879.
    PharmGKBi PA27045.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG251494.
    HOGENOMi HOG000004754.
    HOVERGENi HBG107646.
    InParanoidi Q92879.
    KOi K13207.
    OrthoDBi EOG7DVDBR.
    PhylomeDBi Q92879.
    TreeFami TF314924.

    Miscellaneous databases

    ChiTaRSi CELF1. human.
    EvolutionaryTracei Q92879.
    GeneWikii CUGBP1.
    GenomeRNAii 10658.
    NextBioi 40521.
    PROi Q92879.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92879.
    Bgeei Q92879.
    CleanExi HS_CUGBP1.
    Genevestigatori Q92879.

    Family and domain databases

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

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, RNA-BINDING.
    2. "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 1), RNA-BINDING, TISSUE SPECIFICITY.
    3. "Coexpression of the CUG-binding protein reduces DM protein kinase expression in COS cells."
      Takahashi N., Sasagawa N., Usuki F., Kino Y., Kawahara H., Sorimachi H., Maeda T., Suzuki K., Ishiura S.
      J. Biochem. 130:581-587(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
      Tissue: Brain and Skeletal muscle.
    4. "c-Jun ARE targets mRNA deadenylation by an EDEN-BP (embryo deadenylation element-binding protein)-dependent pathway."
      Paillard L., Legagneux V., Maniey D., Osborne H.B.
      J. Biol. Chem. 277:3232-3235(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING.
    5. "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: Trachea.
    6. "Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
      Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Brain.
    7. 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: Testis.
    10. "CUG repeat binding protein (CUGBP1) interacts with the 5' region of C/EBPbeta mRNA and regulates translation of C/EBPbeta isoforms."
      Timchenko N.A., Welm A.L., Lu X., Timchenko L.T.
      Nucleic Acids Res. 27:4517-4525(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    11. "RNA CUG repeats sequester CUGBP1 and alter protein levels and activity of CUGBP1."
      Timchenko N.A., Cai Z.J., Welm A.L., Reddy S., Ashizawa T., Timchenko L.T.
      J. Biol. Chem. 276:7820-7826(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    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. "A functional deadenylation assay identifies human CUG-BP as a deadenylation factor."
      Paillard L., Legagneux V., Beverley Osborne H.
      Biol. Cell 95:107-113(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF PHE-63; GLY-331 AND LEU-472, 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. "Competition of CUGBP1 and calreticulin for the regulation of p21 translation determines cell fate."
      Iakova P., Wang G.-L., Timchenko L., Michalak M., Pereira-Smith O.M., Smith J.R., Timchenko N.A.
      EMBO J. 23:406-417(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, RNA-BINDING.
    16. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    17. "Interaction of muscleblind, CUG-BP1 and hnRNP H proteins in DM1-associated aberrant IR splicing."
      Paul S., Dansithong W., Kim D., Rossi J., Webster N.J., Comai L., Reddy S.
      EMBO J. 25:4271-4283(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HNRNPH1, RNA-BINDING, INDUCTION.
    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. "CUG-BP binds to RNA substrates and recruits PARN deadenylase."
      Moraes K.C., Wilusz C.J., Wilusz J.
      RNA 12:1084-1091(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PARN, RNA-BINDING.
    20. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Solution structure of RNA-binding domain 3 in CUG triplet repeat RNA-binding protein 1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 383-484.
    23. "Structural insights into RNA recognition by the alternate-splicing regulator CUG-binding protein 1."
      Teplova M., Song J., Gaw H.Y., Teplov A., Patel D.J.
      Structure 18:1364-1377(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 14-187 IN COMPLEX WITH MRNA, DOMAINS RRM.

    Entry informationi

    Entry nameiCELF1_HUMAN
    AccessioniPrimary (citable) accession number: Q92879
    Secondary accession number(s): B4E2U5
    , D3DQS0, F8W940, Q4LE52, Q9NP83, Q9NR06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: October 18, 2001
    Last modified: October 1, 2014
    This is version 144 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3