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P28659

- CELF1_MOUSE

UniProt

P28659 - CELF1_MOUSE

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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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 3021Phosphoserine1 Publication

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

        10         20         30         40         50
MNGTLDHPDQ PDLDAIKMFV GQVPRTWSEK DLRELFEQYG AVYEINILRD
60 70 80 90 100
RSQNPPQSKG CCFVTFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE
110 120 130 140 150
KNNAVEDRKL FIGMISKKCT ENDIRVMFSS FGQIEECRIL RGPDGLSRGC
160 170 180 190 200
AFVTFTTRTM AQTAIKAMHQ AQTMEGCSSP MVVKFADTQK DKEQKRMAQQ
210 220 230 240 250
LQQQMQQISA ASVWGNLAGL NTLGPQYLAL YLQLLQQTAS SGNLNTLSSL
260 270 280 290 300
HPMGGLNAMQ LQNLAALAAA ASAAQNTPSG TNALTTSSSP LSVLTSSGSS
310 320 330 340 350
PSSSSSNSVN PIASLGALQT LAGATAGLNV GSLAGMAALN GGLGSSGLSN
360 370 380 390 400
GTGSTMEALT QAYSGIQQYA AAALPTLYNQ NLLTQQSIGA AGSQKEGPEG
410 420 430 440 450
ANLFIYHLPQ EFGDQDLLQM FMPFGNVVSA KVFIDKQTNL SKCFGFVSYD
460 470 480
NPVSAQAAIQ SMNGFQIGMK RLKVQLKRSK NDSKPY
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

« Hide 'large scale' publications
  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 29, 2014
This is version 132 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