CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001577
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 CUGBP Elav-like family member 2 
Protein Synonyms/Alias
 CELF-2; Bruno-like protein 3; CUG triplet repeat RNA-binding protein 2; CUG-BP2; CUG-BP- and ETR-3-like factor 2; ELAV-type RNA-binding protein 3; ETR-3; Neuroblastoma apoptosis-related RNA-binding protein; hNAPOR; RNA-binding protein BRUNOL-3 
Gene Name
 CELF2 
Gene Synonyms/Alias
 BRUNOL3; CUGBP2; ETR3; NAPOR 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
185AMAQNAIKAMHQSQTubiquitination[1]
Reference
 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724
Functional Description
 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 TNNT2 in embryonic, but not adult, skeletal muscle. Activates TNNT2 exon 5 inclusion by antagonizing the repressive effect of PTB. 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. Promotes inclusion of exonS 21 and exclusion of exon 5 of the NMDA receptor R1 pre- mRNA. Involved in the apoB RNA editing activity. Increases COX2 mRNA stability and inhibits COX2 mRNA translation in epithelial cells after radiation injury (By similarity). Modulates the cellular apoptosis program by regulating COX2-mediated prostaglandin E2 (PGE2) expression (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK. Binds to the muscle-specific splicing enhancer (MSE) intronic sites flanking the TNNT2 alternative exon 5. Binds preferentially to UG-rich sequences, in particular UG repeat and UGUU motifs. Binds to apoB mRNA, specifically to AU-rich sequences located immediatly upstream of the edited cytidine. Binds AU-rich sequences in the 3'-UTR of COX2 mRNA (By similarity). Binds to an intronic RNA element responsible for the silencing of exon 21 splicing (By similarity). Binds to (CUG)n repeats (By similarity). 
Sequence Annotation
 DOMAIN 40 123 RRM 1.
 DOMAIN 132 212 RRM 2.
 DOMAIN 423 501 RRM 3.
 REGION 1 283 Necessary for RNA-binding, TNNT2 exon 5
 REGION 357 508 Necessary for RNA-binding, TNNT2 exon 5  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; mRNA processing; Nucleus; Polymorphism; Reference proteome; Repeat; Repressor; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 508 AA 
Protein Sequence
MMVEGRLLVP DRINGTANKM NGALDHSDQP DPDAIKMFVG QIPRSWSEKE LKELFEPYGA 60
VYQINVLRDR SQNPPQSKGC CFVTFYTRKA ALEAQNALHN IKTLPGMHHP IQMKPADSEK 120
SNAVEDRKLF IGMVSKKCNE NDIRVMFSPF GQIEECRILR GPDGLSRGCA FVTFSTRAMA 180
QNAIKAMHQS QTMEGCSSPI VVKFADTQKD KEQRRLQQQL AQQMQQLNTA TWGNLTGLGG 240
LTPQYLALLQ QATSSSNLGA FSGIQQMAGM NALQLQNLAT LAAAAAAAQT SATSTNANPL 300
STTSSALGAL TSPVAASTPN STAGAAMNSL TSLGTLQGLA GATVGLNNIN ALAVAQMLSG 360
MAALNGGLGA TGLTNGTAGT MDALTQAYSG IQQYAAAALP TLYSQSLLQQ QSAAGSQKEG 420
PEGANLFIYH LPQEFGDQDI LQMFMPFGNV ISAKVFIDKQ TNLSKCFGFV SYDNPVSAQA 480
AIQAMNGFQI GMKRLKVQLK RSKNDSKPY 509 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0003723; F:RNA binding; TAS:ProtInc.
 GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
 GO:0008016; P:regulation of heart contraction; TAS:ProtInc.
 GO:0006396; P:RNA processing; TAS:ProtInc. 
Interpro
 IPR002343; Hud_Sxl_RNA.
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom. 
Pfam
 PF00076; RRM_1 
SMART
 SM00360; RRM 
PROSITE
 PS50102; RRM 
PRINTS
 PR00961; HUDSXLRNA.