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P28659

- CELF1_MOUSE

UniProt

P28659 - CELF1_MOUSE

Protein

CUGBP Elav-like family member 1

Gene

Celf1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (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 By similarity. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition By similarity. 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 By similarity. Activates SM exon 5 inclusion by antagonizing the repressive effect of PTB By similarity. Promotes exclusion of exon 11 of the INSR pre-mRNA By similarity. Inhibits, together with HNRNPH1, insulin receptor (IR) pre-mRNA exon 11 inclusion in myoblast By similarity. Increases translation and controls the choice of translation initiation codon of CEBPB mRNA By similarity. Increases mRNA translation of CEBPB in aging liver. Increases translation of CDKN1A mRNA by antagonizing the repressive effect of CALR3 By similarity. Mediates rapid cytoplasmic mRNA deadenylation By similarity. Recruits the deadenylase PARN to the poly(A) tail of EDEN-containing mRNAs to promote their deadenylation By similarity. Required for completion of spermatogenesis. Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK and to Bruno response elements (BREs) By similarity. Binds to muscle-specific splicing enhancer (MSE) intronic sites flanking the alternative exon 5 of TNNT2 pre-mRNA By similarity. Binds to AU-rich sequences (AREs or EDEN-like) localized in the 3'-UTR of JUN and FOS mRNAs. Binds to the IR RNA By similarity. Binds to the 5'-region of CDKN1A and CEBPB mRNAs By similarity. Binds with the 5'-region of CEBPB mRNA in aging liver.By similarity3 Publications

    GO - Molecular functioni

    1. BRE binding Source: UniProtKB
    2. mRNA binding Source: Ensembl
    3. nucleotide binding Source: InterPro
    4. RNA binding Source: UniProtKB
    5. translation initiation factor binding Source: MGI

    GO - Biological processi

    1. mRNA splice site selection Source: MGI
    2. positive regulation of multicellular organism growth Source: MGI
    3. regulation of RNA splicing Source: UniProtKB
    4. spermatid development Source: MGI

    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
    Brain protein F41
    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
    Deadenylation factor EDEN-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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1342295. Celf1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi302 – 3021S → G: Reduces CDK4-mediated phosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 486486CUGBP Elav-like family member 1PRO_0000081539Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei302 – 3021Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated. Phosphorylated by CDK4 on Ser-302. Its phosphorylation status increases in aging liver and is important for the formation of the EIF2 complex and activation of CEBPB mRNA translation. Hyperphosphorylated in the EIF2 complex. EGFR signaling regulates its phosphorylation status in epithelial cells.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP28659.
    PaxDbiP28659.
    PRIDEiP28659.

    PTM databases

    PhosphoSiteiP28659.

    Expressioni

    Tissue specificityi

    Expressed in skeletal muscle, uterus, diaphragm, lung, spleen, testis, mammary gland, adipose, eye and brain (at protein level). Strongly expressed in aging liver (at protein level). Expressed in lung, stomach, heart to very low levels (at protein level). Expressed in germ cells of the seminiferous tubules except in the central region that contains the elongated spermatids and spermatozoa (at protein level). Expressed in Leydig cells of the interstitial tissue (at protein level). Expressed in the heart, skeletal muscle, testis (from spermatogonia to round spermatids), spleen, lung, neocortex, cerebellar cortex, hippocampus and other areas, abundant in the putamen, and poorly expressed in the thalamus and in the brain stem.5 Publications

    Developmental stagei

    Expressed in heart, muscle, brain, liver, thigh, stomach and lung at 14 dpc (at protein level). Expressed from the two-cell to blastocyst stages. Expressed in tail region, somites, cephalic structures and limb buds at 10.5 dpc.3 Publications

    Inductioni

    Its RNA-binding activity on CEBPB mRNA increases in response to EGF.1 Publication

    Gene expression databases

    BgeeiP28659.
    CleanExiMM_CUGBP1.
    GenevestigatoriP28659.

    Interactioni

    Subunit structurei

    Associates with polysomes By similarity. Interacts with HNRNPH1; the interaction in RNA-dependent. Interacts with PARN By similarity. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5.By similarity1 Publication

    Protein-protein interaction databases

    IntActiP28659. 1 interaction.
    MINTiMINT-4092581.

    Structurei

    3D structure databases

    ProteinModelPortaliP28659.
    SMRiP28659. Positions 1-187, 355-484.
    ModBaseiSearch...
    MobiDBiSearch...

    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.By similarity

    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.
    GeneTreeiENSGT00560000076837.
    HOVERGENiHBG107646.
    InParanoidiP28659.
    KOiK13207.
    OMAiPTLYNQS.
    OrthoDBiEOG7DVDBR.
    PhylomeDBiP28659.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: P28659-1) [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 AVYEINILRD    50
    RSQNPPQSKG CCFVTFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE 100
    KNNAVEDRKL FIGMISKKCT ENDIRVMFSS FGQIEECRIL RGPDGLSRGC 150
    AFVTFTTRTM 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
    Length:486
    Mass (Da):52,107
    Last modified:October 18, 2001 - v2
    Checksum:iABB22D331A62B584
    GO
    Isoform 2 (identifier: P28659-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:482
    Mass (Da):51,590
    Checksum:i5419764243BC0587
    GO
    Isoform 3 (identifier: P28659-3) [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):51,661
    Checksum:i88B57A65E75761F5
    GO
    Isoform 4 (identifier: P28659-4) [UniParc]FASTAAdd to Basket

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

    Note: Gene prediction based on similarity to human ortholog. No experimental confirmation available.

    Show »
    Length:513
    Mass (Da):55,116
    Checksum:iE9CF94A90B3556D6
    GO

    Sequence cautioni

    The sequence CAA43691.1 differs from that shown. Reason: Frameshift at position 367.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti192 – 1921K → E in BAB87831. 1 PublicationCurated
    Sequence conflicti291 – 2911L → P in AAF78957. (PubMed:11686919)Curated
    Sequence conflicti301 – 3011P → T in AAF78957. (PubMed:11686919)Curated
    Sequence conflicti335 – 3351G → R in AAF78957. (PubMed:11686919)Curated
    Sequence conflicti347 – 3471G → A in AAF78957. (PubMed:11686919)Curated
    Sequence conflicti402 – 4021N → Y in BAE33820. (PubMed:16141072)Curated
    Sequence conflicti466 – 4661Q → R in BAE25504. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MAAFKLDFLPEMMVDHCSLN SSPVSKKM in isoform 4. CuratedVSP_026789
    Alternative sequencei231 – 2344Missing in isoform 2 and isoform 3. 2 PublicationsVSP_005786
    Alternative sequencei297 – 2971S → SA in isoform 3. 2 PublicationsVSP_005787

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007987 mRNA. Translation: CAC20707.1.
    AF267535 mRNA. Translation: AAF78957.1.
    AK135030 mRNA. Translation: BAE22391.1.
    AK143698 mRNA. Translation: BAE25504.1.
    AK014492 mRNA. Translation: BAB29392.1.
    AK156725 mRNA. Translation: BAE33820.1.
    AL672241 Genomic DNA. Translation: CAM15320.1.
    AL672241 Genomic DNA. Translation: CAM15321.1.
    AL672241 Genomic DNA. Translation: CAM15322.1.
    AL672241 Genomic DNA. Translation: CAM15323.1.
    BC021393 mRNA. No translation available.
    AF314172 mRNA. Translation: AAK00297.1.
    AB050499 mRNA. Translation: BAB87831.1.
    X61451 mRNA. Translation: CAA43691.1. Frameshift.
    CCDSiCCDS16420.1. [P28659-4]
    CCDS16421.1. [P28659-1]
    PIRiS16865.
    RefSeqiNP_001231820.1. NM_001244891.1. [P28659-1]
    NP_001231832.1. NM_001244903.1. [P28659-1]
    NP_059064.2. NM_017368.3. [P28659-4]
    NP_941955.1. NM_198683.2. [P28659-1]
    XP_006498727.1. XM_006498664.1.
    XP_006498728.1. XM_006498665.1.
    XP_006498729.1. XM_006498666.1. [P28659-3]
    XP_006498732.1. XM_006498669.1. [P28659-4]
    UniGeneiMm.29495.
    Mm.490161.

    Genome annotation databases

    EnsembliENSMUST00000005643; ENSMUSP00000005643; ENSMUSG00000005506. [P28659-4]
    ENSMUST00000068726; ENSMUSP00000064323; ENSMUSG00000005506.
    ENSMUST00000068747; ENSMUSP00000070438; ENSMUSG00000005506. [P28659-1]
    ENSMUST00000111448; ENSMUSP00000107075; ENSMUSG00000005506. [P28659-3]
    ENSMUST00000111449; ENSMUSP00000107076; ENSMUSG00000005506. [P28659-1]
    ENSMUST00000111451; ENSMUSP00000107078; ENSMUSG00000005506. [P28659-1]
    ENSMUST00000111452; ENSMUSP00000107079; ENSMUSG00000005506. [P28659-4]
    ENSMUST00000111455; ENSMUSP00000107082; ENSMUSG00000005506. [P28659-4]
    ENSMUST00000177642; ENSMUSP00000136109; ENSMUSG00000005506. [P28659-1]
    GeneIDi13046.
    KEGGimmu:13046.
    UCSCiuc008ktx.2. mouse. [P28659-1]
    uc008kua.2. mouse. [P28659-4]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ007987 mRNA. Translation: CAC20707.1 .
    AF267535 mRNA. Translation: AAF78957.1 .
    AK135030 mRNA. Translation: BAE22391.1 .
    AK143698 mRNA. Translation: BAE25504.1 .
    AK014492 mRNA. Translation: BAB29392.1 .
    AK156725 mRNA. Translation: BAE33820.1 .
    AL672241 Genomic DNA. Translation: CAM15320.1 .
    AL672241 Genomic DNA. Translation: CAM15321.1 .
    AL672241 Genomic DNA. Translation: CAM15322.1 .
    AL672241 Genomic DNA. Translation: CAM15323.1 .
    BC021393 mRNA. No translation available.
    AF314172 mRNA. Translation: AAK00297.1 .
    AB050499 mRNA. Translation: BAB87831.1 .
    X61451 mRNA. Translation: CAA43691.1 . Frameshift.
    CCDSi CCDS16420.1. [P28659-4 ]
    CCDS16421.1. [P28659-1 ]
    PIRi S16865.
    RefSeqi NP_001231820.1. NM_001244891.1. [P28659-1 ]
    NP_001231832.1. NM_001244903.1. [P28659-1 ]
    NP_059064.2. NM_017368.3. [P28659-4 ]
    NP_941955.1. NM_198683.2. [P28659-1 ]
    XP_006498727.1. XM_006498664.1.
    XP_006498728.1. XM_006498665.1.
    XP_006498729.1. XM_006498666.1. [P28659-3 ]
    XP_006498732.1. XM_006498669.1. [P28659-4 ]
    UniGenei Mm.29495.
    Mm.490161.

    3D structure databases

    ProteinModelPortali P28659.
    SMRi P28659. Positions 1-187, 355-484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P28659. 1 interaction.
    MINTi MINT-4092581.

    PTM databases

    PhosphoSitei P28659.

    Proteomic databases

    MaxQBi P28659.
    PaxDbi P28659.
    PRIDEi P28659.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005643 ; ENSMUSP00000005643 ; ENSMUSG00000005506 . [P28659-4 ]
    ENSMUST00000068726 ; ENSMUSP00000064323 ; ENSMUSG00000005506 .
    ENSMUST00000068747 ; ENSMUSP00000070438 ; ENSMUSG00000005506 . [P28659-1 ]
    ENSMUST00000111448 ; ENSMUSP00000107075 ; ENSMUSG00000005506 . [P28659-3 ]
    ENSMUST00000111449 ; ENSMUSP00000107076 ; ENSMUSG00000005506 . [P28659-1 ]
    ENSMUST00000111451 ; ENSMUSP00000107078 ; ENSMUSG00000005506 . [P28659-1 ]
    ENSMUST00000111452 ; ENSMUSP00000107079 ; ENSMUSG00000005506 . [P28659-4 ]
    ENSMUST00000111455 ; ENSMUSP00000107082 ; ENSMUSG00000005506 . [P28659-4 ]
    ENSMUST00000177642 ; ENSMUSP00000136109 ; ENSMUSG00000005506 . [P28659-1 ]
    GeneIDi 13046.
    KEGGi mmu:13046.
    UCSCi uc008ktx.2. mouse. [P28659-1 ]
    uc008kua.2. mouse. [P28659-4 ]

    Organism-specific databases

    CTDi 10658.
    MGIi MGI:1342295. Celf1.

    Phylogenomic databases

    eggNOGi NOG251494.
    GeneTreei ENSGT00560000076837.
    HOVERGENi HBG107646.
    InParanoidi P28659.
    KOi K13207.
    OMAi PTLYNQS.
    OrthoDBi EOG7DVDBR.
    PhylomeDBi P28659.
    TreeFami TF314924.

    Miscellaneous databases

    ChiTaRSi CELF1. mouse.
    NextBioi 282946.
    PROi P28659.
    SOURCEi Search...

    Gene expression databases

    Bgeei P28659.
    CleanExi MM_CUGBP1.
    Genevestigatori P28659.

    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. "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).
      Strain: Swiss.
      Tissue: Ovary.
    2. "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] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Liver.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Strain: C57BL/6J.
      Tissue: Embryonic liver, Fetal spleen, Olfactory bulb and Spleen.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "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 1).
      Strain: Czech II.
      Tissue: Mammary gland.
    6. "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] OF 52-486 (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Fetus.
    7. "Bruno-like RNA-binding protein."
      Suzuki H., Inoue K.
      Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 96-420 (ISOFORM 3).
    8. Kato K.
      Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 127-445 (ISOFORM 1).
    9. "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: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    10. "Epidermal growth factor receptor stimulation activates the RNA binding protein CUG-BP1 and increases expression of C/EBPbeta-LIP in mammary epithelial cells."
      Baldwin B.R., Timchenko N.A., Zahnow C.A.
      Mol. Cell. Biol. 24:3682-3691(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, INDUCTION, RNA-BINDING.
    11. "Dynamic balance between activation and repression regulates pre-mRNA alternative splicing during heart development."
      Ladd A.N., Stenberg M.G., Swanson M.S., Cooper T.A.
      Dev. Dyn. 233:783-793(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    12. "Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-binding protein beta in old liver."
      Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H., Hershey J.W., Timchenko N.A.
      J. Biol. Chem. 281:32806-32819(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CALR; CALR3; HSPA5 AND HSP90B1, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-302, MUTAGENESIS OF SER-302, ASSOCIATION WITH POLYSOMES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    13. "Inactivation of CUG-BP1/CELF1 causes growth, viability, and spermatogenesis defects in mice."
      Kress C., Gautier-Courteille C., Osborne H.B., Babinet C., Paillard L.
      Mol. Cell. Biol. 27:1146-1157(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiCELF1_MOUSE
    AccessioniPrimary (citable) accession number: P28659
    Secondary accession number(s): A2AFW9
    , A2AFX0, A2AFX1, A2AFX2, Q3U0N2, Q3UP93, Q3UY22, Q8R532, Q99PE1, Q9CXE5, Q9EPJ8, Q9JI37
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: October 18, 2001
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3