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P28659 (CELF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Celf1
Synonyms:Brunol2, Cugbp, Cugbp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.12 Ref.13

Subunit structure

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. Ref.12

Subcellular location

Nucleus. Cytoplasm. Note: RNA-binding activity is detected in both nuclear and cytoplasmic compartments By similarity. Ref.11 Ref.12 Ref.13

Tissue specificity

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. Ref.2 Ref.9 Ref.11 Ref.12 Ref.13

Developmental stage

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. Ref.9 Ref.11 Ref.13

Induction

Its RNA-binding activity on CEBPB mRNA increases in response to EGF. Ref.10

Domain

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

Post-translational modification

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. Ref.10 Ref.12

Sequence similarities

Belongs to the CELF/BRUNOL family.

Contains 3 RRM (RNA recognition motif) domains.

Sequence caution

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

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: P28659-1)

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.
Isoform 2 (identifier: P28659-2)

The sequence of this isoform differs from the canonical sequence as follows:
     231-234: Missing.
Isoform 3 (identifier: P28659-3)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     231-234: Missing.
     297-297: S → SA
Isoform 4 (identifier: P28659-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486CUGBP Elav-like family member 1
PRO_0000081539

Regions

Domain16 – 9984RRM 1
Domain108 – 18881RRM 2
Domain401 – 47979RRM 3
Compositional bias287 – 30822Ser-rich

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue3021Phosphoserine Ref.12

Natural variations

Alternative sequence11M → MAAFKLDFLPEMMVDHCSLN SSPVSKKM in isoform 4.
VSP_026789
Alternative sequence231 – 2344Missing in isoform 2 and isoform 3.
VSP_005786
Alternative sequence2971S → SA in isoform 3.
VSP_005787

Experimental info

Mutagenesis3021S → G: Reduces CDK4-mediated phosphorylation. Ref.12
Sequence conflict1921K → E in BAB87831. Ref.7
Sequence conflict2911L → P in AAF78957. Ref.2
Sequence conflict3011P → T in AAF78957. Ref.2
Sequence conflict3351G → R in AAF78957. Ref.2
Sequence conflict3471G → A in AAF78957. Ref.2
Sequence conflict4021N → Y in BAE33820. Ref.3
Sequence conflict4661Q → R in BAE25504. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (LYLQ) [UniParc].

Last modified October 18, 2001. Version 2.
Checksum: ABB22D331A62B584

FASTA48652,107
        10         20         30         40         50         60 
MNGTLDHPDQ PDLDAIKMFV GQVPRTWSEK DLRELFEQYG AVYEINILRD RSQNPPQSKG 

        70         80         90        100        110        120 
CCFVTFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE KNNAVEDRKL FIGMISKKCT 

       130        140        150        160        170        180 
ENDIRVMFSS FGQIEECRIL RGPDGLSRGC AFVTFTTRTM AQTAIKAMHQ AQTMEGCSSP 

       190        200        210        220        230        240 
MVVKFADTQK DKEQKRMAQQ LQQQMQQISA ASVWGNLAGL NTLGPQYLAL YLQLLQQTAS 

       250        260        270        280        290        300 
SGNLNTLSSL HPMGGLNAMQ LQNLAALAAA ASAAQNTPSG TNALTTSSSP LSVLTSSGSS 

       310        320        330        340        350        360 
PSSSSSNSVN PIASLGALQT LAGATAGLNV GSLAGMAALN GGLGSSGLSN GTGSTMEALT 

       370        380        390        400        410        420 
QAYSGIQQYA AAALPTLYNQ NLLTQQSIGA AGSQKEGPEG ANLFIYHLPQ EFGDQDLLQM 

       430        440        450        460        470        480 
FMPFGNVVSA KVFIDKQTNL SKCFGFVSYD NPVSAQAAIQ SMNGFQIGMK RLKVQLKRSK 


NDSKPY 

« Hide

Isoform 2 [UniParc].

Checksum: 5419764243BC0587
Show »

FASTA48251,590
Isoform 3 (A) [UniParc].

Checksum: 88B57A65E75761F5
Show »

FASTA48351,661
Isoform 4 [UniParc].

Checksum: E9CF94A90B3556D6
Show »

FASTA51355,116

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS16420.1. [P28659-4]
CCDS16421.1. [P28659-1]
PIRS16865.
RefSeqNP_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]
UniGeneMm.29495.
Mm.490161.

3D structure databases

ProteinModelPortalP28659.
SMRP28659. Positions 1-187, 355-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP28659. 1 interaction.
MINTMINT-4092581.

PTM databases

PhosphoSiteP28659.

Proteomic databases

MaxQBP28659.
PaxDbP28659.
PRIDEP28659.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005643; 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]
GeneID13046.
KEGGmmu:13046.
UCSCuc008ktx.2. mouse. [P28659-1]
uc008kua.2. mouse. [P28659-4]

Organism-specific databases

CTD10658.
MGIMGI:1342295. Celf1.

Phylogenomic databases

eggNOGNOG251494.
GeneTreeENSGT00560000076837.
HOVERGENHBG107646.
InParanoidP28659.
KOK13207.
OMAPTLYNQS.
OrthoDBEOG7DVDBR.
PhylomeDBP28659.
TreeFamTF314924.

Gene expression databases

BgeeP28659.
CleanExMM_CUGBP1.
GenevestigatorP28659.

Family and domain databases

Gene3D3.30.70.330. 3 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTSM00360. RRM. 3 hits.
[Graphical view]
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCELF1. mouse.
NextBio282946.
PROP28659.
SOURCESearch...

Entry information

Entry nameCELF1_MOUSE
AccessionPrimary (citable) accession number: P28659
Secondary accession number(s): A2AFW9 expand/collapse secondary AC list , A2AFX0, A2AFX1, A2AFX2, Q3U0N2, Q3UP93, Q3UY22, Q8R532, Q99PE1, Q9CXE5, Q9EPJ8, Q9JI37
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 18, 2001
Last modified: July 9, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot