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Q92879

- CELF1_HUMAN

UniProt

Q92879 - CELF1_HUMAN

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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

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. RNA binding Source: UniProtKB
  6. 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
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
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-KW
  2. membrane Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

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

BgeeiQ92879.
CleanExiHS_CUGBP1.
ExpressionAtlasiQ92879. baseline and differential.
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 – 227Combined sources
Helixi29 – 379Combined sources
Beta strandi42 – 509Combined sources
Beta strandi52 – 554Combined sources
Beta strandi57 – 6812Combined sources
Helixi69 – 7911Combined sources
Turni80 – 823Combined sources
Beta strandi93 – 964Combined sources
Helixi98 – 1003Combined sources
Helixi105 – 1073Combined sources
Beta strandi108 – 1147Combined sources
Helixi121 – 1288Combined sources
Helixi129 – 1313Combined sources
Beta strandi134 – 1418Combined sources
Turni143 – 1453Combined sources
Beta strandi147 – 15711Combined sources
Helixi158 – 16811Combined sources
Turni169 – 1713Combined sources
Turni174 – 1774Combined sources
Beta strandi182 – 1854Combined sources
Helixi385 – 3884Combined sources
Beta strandi389 – 3913Combined sources
Turni399 – 4013Combined sources
Beta strandi403 – 4075Combined sources
Helixi414 – 4218Combined sources
Helixi422 – 4243Combined sources
Beta strandi428 – 4347Combined sources
Beta strandi436 – 4383Combined sources
Beta strandi440 – 4489Combined sources
Helixi452 – 46211Combined sources
Beta strandi473 – 4753Combined sources
Beta strandi482 – 4843Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00560000076837.
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

        10         20         30         40         50
MNGTLDHPDQ PDLDAIKMFV GQVPRTWSEK DLRELFEQYG AVYEINVLRD
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
AFVTFTTRAM 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

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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 GC11M049904.
HGNCi HGNC:2549. CELF1.
HPAi CAB016114.
HPA044597.
MIMi 601074. gene.
neXtProti NX_Q92879.
PharmGKBi PA27045.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG251494.
GeneTreei ENSGT00560000076837.
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

Bgeei Q92879.
CleanExi HS_CUGBP1.
ExpressionAtlasi Q92879. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 146 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