Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
CELF1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CELF1 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. 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. 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. Belongs to the CELF/BRUNOL family. 4 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Cell development/differentiation; RNA binding protein; RNA processing
Cellular Component: membrane; cytoplasm; nucleolus; nucleus; ribonucleoprotein complex
Molecular Function: mRNA binding; protein binding; translation initiation factor binding; RNA binding; translation repressor activity, nucleic acid binding; BRE binding; nucleotide binding
Biological Process: mRNA splice site selection; embryonic development; regulation of RNA splicing; negative regulation of translation; positive regulation of multicellular organism growth; mRNA processing; spermatid development; RNA interference; germ cell development
Reference #:  Q92879 (UniProtKB)
Alt. Names/Synonyms: 50 kDa nuclear polyadenylated RNA-binding protein; bruno-like 2; Bruno-like protein 2; BRUNOL2; CELF-1; CELF1; CUG RNA-binding protein; CUG triplet repeat RNA-binding protein 1; CUG triplet repeat, RNA binding protein 1; CUG triplet repeat, RNA-binding protein 1; CUG-BP; CUG-BP- and ETR-3-like factor 1; CUG-BP1; CUGBP; CUGBP Elav-like family member 1; CUGBP, Elav-like family member 1; CUGBP1; Deadenylation factor CUG-BP; EDEN-BP; EDEN-BP homolog; embryo deadenylation element binding protein; Embryo deadenylation element-binding protein homolog; hNab50; NAB50; NAPOR; nuclear polyadenylated RNA-binding protein, 50-kD; RNA-binding protein BRUNOL-2
Gene Symbols: CELF1
Molecular weight: 52,063 Da
Basal Isoelectric point: 8.7  Predict pI for various phosphorylation states
Select Structure to View Below

CELF1

Protein Structure Not Found.


STRING  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
translation, altered: S28‑p, S302‑p
molecular association, regulation: S28‑p, S302‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 - gap
0 6 - gap
0 2 T4-p ____MNGtLDHPDQP
0 1 K17 QPDLDAIKMFVGQVP
3 3 S28-p GQVPRTWsEKDLREL
0 1 K30 VPRTWsEKDLRELFE
1 1 S52-p INVLRDRsQNPPQSk
0 13 K59-ub sQNPPQSkGCCFVTF
0 7 K70-ub FVTFYTRkAALEAQN
0 1 K118 FIGMISKKCTENDIR
0 1 K166 AMAQTAIKAMHQAQt
1 0 T173-p KAMHQAQtMEGCssP
1 0 S178-p AQtMEGCssPMVVKF
1 2 S179-p QtMEGCssPMVVKFA
1 0 S241-p LLQQTASsGNLNTLS
1 0 S300-p VLTSSGSsPsSSSSN
3 0 S302-p TSSGSsPsSSSSNSV
0 11 K436-ub SAKVFIDkQTNLSKC
  CELF1 iso4  
S18-p EMMVDHCsLNSsPVS
S22-p DHCsLNSsPVSKKMN
T31-p VSKKMNGtLDHPDQP
K44 QPDLDAIKMFVGQVP
S55 GQVPRTWSEKDLREL
K57 VPRTWSEKDLRELFE
S79 INVLRDRSQNPPQSK
K86 SQNPPQSKGCCFVTF
K97 FVTFYTRKAALEAQN
K144 FIGMISKKCTENDIR
K192 AMAQTAIKAMHQAQT
T199 KAMHQAQTMEGCSSP
S204 AQTMEGCSSPMVVKF
S205 QTMEGCSSPMVVKFA
S267 LLQQTASSGNLNTLS
S326 VLTSSGSSPSSSSSN
S328 TSSGSSPSSSSSNSV
K462 SAKVFIDKQTNLSKC
  mouse

► Hide Isoforms
 
- gap
- gap
T4 ____MNGTLDHPDQP
K17 QPDLDAIKMFVGQVP
S28-p GQVPRTWsEkDLREL
K30-ub VPRTWsEkDLRELFE
S52-p INILRDRsQNPPQSK
K59 sQNPPQSKGCCFVTF
K70-ub FVTFYTRkAALEAQN
K118-ub FIGMISKkCTENDIR
K166-ub TMAQTAIkAMHQAQT
T173 kAMHQAQTMEGCSSP
S178 AQTMEGCSSPMVVKF
S179 QTMEGCSSPMVVKFA
S241 LLQQTASSGNLNTLS
S300 VLTSSGSSPsSSSSN
S302-p TSSGSSPsSSSSNSV
K436-ub SAKVFIDkQTNLSKC
  CELF1 iso4  
S18-p EMMVDHCsLNSsPVS
S22-p DHCsLNSsPVSKKMN
T31 VSKKMNGTLDHPDQP
K44-ub QPDLDAIkMFVGQVP
S55 GQVPRTWSEKDLREL
K57 VPRTWSEKDLRELFE
S79 INILRDRSQNPPQSK
K86 SQNPPQSKGCCFVTF
K97 FVTFYTRKAALEAQN
K145 FIGMISKKCTENDIR
K193 TMAQTAIKAMHQAQT
T200 KAMHQAQTMEGCSSP
S205 AQTMEGCSSPMVVKF
S206 QTMEGCSSPMVVKFA
S268 LLQQTASSGNLNTLS
S327 VLTSSGSSPSSSSSN
S329 TSSGSSPSSSSSNSV
K463 SAKVFIDKQTNLSKC
  rat

 
- gap
- gap
T4 ____MNGTLDHPDQP
K17 QPDLDAIKMFVGQVP
S28 GQVPRTWSEKDLREL
K30 VPRTWSEKDLRELFE
S52 INILRDRSQNPPQSK
K59 SQNPPQSKGCCFVTF
K70 FVTFYTRKAALEAQN
K118 FIGMISKKCTENDIR
K166 TMAQTAIKAMHQAQT
T173 KAMHQAQTMEGCSSP
S178 AQTMEGCSSPMVVKF
S179 QTMEGCSSPMVVKFA
S241 LLQQTANSGNLNTLS
S301 LTSSAGSSPSSSSSN
S303 SSAGSSPSSSSSNSV
K437 SAKVFIDKQTNLSKC
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.