P28659 (CELF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Celf1
Synonyms:	Brunol2, Cugbp, Cugbp1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA splice site selection Inferred from direct assay Ref.9. Source: MGI positive regulation of multicellular organism growth Inferred from mutant phenotype Ref.13. Source: MGI regulation of RNA splicing Inferred from sequence or structural similarity. Source: UniProtKB spermatid development Inferred from mutant phenotype Ref.13. Source: MGI
Cellular_component	cytoplasm Inferred from direct assay Ref.13PubMed 19075228. Source: MGI nucleus Inferred from direct assay Ref.11Ref.13PubMed 19075228. Source: MGI
Molecular_function	BRE binding Inferred from sequence or structural similarity. Source: UniProtKB mRNA binding Inferred from electronic annotation. Source: Compara nucleotide binding Inferred from electronic annotation. Source: InterPro translation initiation factor binding Inferred from direct assay Ref.12. Source: MGI
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 486	486	CUGBP Elav-like family member 1		PRO_0000081539
Regions
	Domain	16 – 99	84	RRM 1
	Domain	108 – 188	81	RRM 2
	Domain	401 – 479	79	RRM 3
	Compositional bias	287 – 308	22	Ser-rich
Amino acid modifications
	Modified residue	302	1	Phosphoserine Ref.12
Natural variations
	Alternative sequence	1	1	M → MAAFKLDFLPEMMVDHCSLN SSPVSKKM in isoform 4.		VSP_026789
	Alternative sequence	231 – 234	4	Missing in isoform 2 and isoform 3.		VSP_005786
	Alternative sequence	297	1	S → SA in isoform 3.		VSP_005787
Experimental info
	Mutagenesis	302	1	S → G: Reduces CDK4-mediated phosphorylation. Ref.12
	Sequence conflict	192	1	K → E in BAB87831. Ref.7
	Sequence conflict	291	1	L → P in AAF78957. Ref.2
	Sequence conflict	301	1	P → T in AAF78957. Ref.2
	Sequence conflict	335	1	G → R in AAF78957. Ref.2
	Sequence conflict	347	1	G → A in AAF78957. Ref.2
	Sequence conflict	402	1	N → Y in BAE33820. Ref.3
	Sequence conflict	466	1	Q → R in BAE25504. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (LYLQ) [UniParc]. Last modified October 18, 2001. Version 2. Checksum: ABB22D331A62B584	FASTA	486	52,107
	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
	Isoform 2 [UniParc]. Checksum: 5419764243BC0587	FASTA	482	51,590
	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 LQQTASSGNL 250 260 270 280 290 300 NTLSSLHPMG GLNAMQLQNL AALAAAASAA QNTPSGTNAL TTSSSPLSVL TSSGSSPSSS 310 320 330 340 350 360 SSNSVNPIAS LGALQTLAGA TAGLNVGSLA GMAALNGGLG SSGLSNGTGS TMEALTQAYS 370 380 390 400 410 420 GIQQYAAAAL PTLYNQNLLT QQSIGAAGSQ KEGPEGANLF IYHLPQEFGD QDLLQMFMPF 430 440 450 460 470 480 GNVVSAKVFI DKQTNLSKCF GFVSYDNPVS AQAAIQSMNG FQIGMKRLKV QLKRSKNDSK PY
	Isoform 3 (A) [UniParc]. Checksum: 88B57A65E75761F5	FASTA	483	51,661
	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 LQQTASSGNL 250 260 270 280 290 300 NTLSSLHPMG GLNAMQLQNL AALAAAASAA QNTPSGTNAL TTSSSPLSVL TSSAGSSPSS 310 320 330 340 350 360 SSSNSVNPIA SLGALQTLAG ATAGLNVGSL AGMAALNGGL GSSGLSNGTG STMEALTQAY 370 380 390 400 410 420 SGIQQYAAAA LPTLYNQNLL TQQSIGAAGS QKEGPEGANL FIYHLPQEFG DQDLLQMFMP 430 440 450 460 470 480 FGNVVSAKVF IDKQTNLSKC FGFVSYDNPV SAQAAIQSMN GFQIGMKRLK VQLKRSKNDS KPY
	Isoform 4 [UniParc]. Checksum: E9CF94A90B3556D6	FASTA	513	55,116
	10 20 30 40 50 60 MAAFKLDFLP EMMVDHCSLN SSPVSKKMNG TLDHPDQPDL DAIKMFVGQV PRTWSEKDLR 70 80 90 100 110 120 ELFEQYGAVY EINILRDRSQ NPPQSKGCCF VTFYTRKAAL EAQNALHNMK VLPGMHHPIQ 130 140 150 160 170 180 MKPADSEKNN AVEDRKLFIG MISKKCTEND IRVMFSSFGQ IEECRILRGP DGLSRGCAFV 190 200 210 220 230 240 TFTTRTMAQT AIKAMHQAQT MEGCSSPMVV KFADTQKDKE QKRMAQQLQQ QMQQISAASV 250 260 270 280 290 300 WGNLAGLNTL GPQYLALYLQ LLQQTASSGN LNTLSSLHPM GGLNAMQLQN LAALAAAASA 310 320 330 340 350 360 AQNTPSGTNA LTTSSSPLSV LTSSGSSPSS SSSNSVNPIA SLGALQTLAG ATAGLNVGSL 370 380 390 400 410 420 AGMAALNGGL GSSGLSNGTG STMEALTQAY SGIQQYAAAA LPTLYNQNLL TQQSIGAAGS 430 440 450 460 470 480 QKEGPEGANL FIYHLPQEFG DQDLLQMFMP FGNVVSAKVF IDKQTNLSKC FGFVSYDNPV 490 500 510 SAQAAIQSMN GFQIGMKRLK VQLKRSKNDS KPY

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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.
IPI	IPI00123205. IPI00229237. IPI00229238. IPI00395213.
PIR	S16865.
RefSeq	NP_001231820.1. NM_001244891.1. NP_001231832.1. NM_001244903.1. NP_059064.2. NM_017368.3. NP_941955.1. NM_198683.2.
UniGene	Mm.29495. Mm.490161.
3D structure databases
ProteinModelPortal	P28659.
SMR	P28659. Positions 1-187, 355-484.
ModBase	Search...
PTM databases
PhosphoSite	P28659.
Proteomic databases
PaxDb	P28659.
PRIDE	P28659.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000005643; ENSMUSP00000005643; ENSMUSG00000005506. ENSMUST00000068726; ENSMUSP00000064323; ENSMUSG00000005506. ENSMUST00000068747; ENSMUSP00000070438; ENSMUSG00000005506. ENSMUST00000111448; ENSMUSP00000107075; ENSMUSG00000005506. ENSMUST00000111449; ENSMUSP00000107076; ENSMUSG00000005506. ENSMUST00000111451; ENSMUSP00000107078; ENSMUSG00000005506. ENSMUST00000111452; ENSMUSP00000107079; ENSMUSG00000005506. ENSMUST00000111455; ENSMUSP00000107082; ENSMUSG00000005506. ENSMUST00000177642; ENSMUSP00000136109; ENSMUSG00000005506.
GeneID	13046.
KEGG	mmu:13046.
UCSC	uc008ktx.1. mouse.
Organism-specific databases
CTD	10658.
MGI	MGI:1342295. Celf1.
Phylogenomic databases
eggNOG	NOG251494.
GeneTree	ENSGT00560000076837.
HOVERGEN	HBG107646.
InParanoid	P28659.
KO	K13207.
OMA	PTLYNQS.
Gene expression databases
Bgee	P28659.
CleanEx	MM_CUGBP1.
Genevestigator	P28659.
GermOnline	ENSMUSG00000005506. Mus musculus.
Family and domain databases
Gene3D	3.30.70.330. 3 hits.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. [Graphical view]
Pfam	PF00076. RRM_1. 3 hits. [Graphical view]
SMART	SM00360. RRM. 3 hits. [Graphical view]
PROSITE	PS50102. RRM. 3 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CELF1. mouse.
NextBio	282946.
SOURCE	Search...

Entry information

Entry name

CELF1_MOUSE

Accession

Primary (citable) accession number: P28659
Secondary accession number(s): A2AFW9 , 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:	May 1, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program