CELF1
entrez
10658
canonical
uniprot
Q92879
canonical
ensembl
ENSG00000149187
resolver
ensp
ENSP00000308386
resolver
ensp
ENSP00000351409
resolver
ensp
ENSP00000354639
resolver
ensp
ENSP00000378705
resolver
ensp
ENSP00000378706
resolver
ensp
ENSP00000435926
resolver
ensp
ENSP00000436864
resolver
ensp
ENSP00000508525
resolver
ensp
ENSP00000541744
resolver
ensp
ENSP00000541745
resolver
ensp
ENSP00000541746
resolver
ensp
ENSP00000541747
resolver
ensp
ENSP00000541748
resolver
ensp
ENSP00000541749
resolver
ensp
ENSP00000541750
resolver
ensp
ENSP00000619407
resolver
ensp
ENSP00000619408
resolver
ensp
ENSP00000619409
resolver
ensp
ENSP00000619410
resolver
ensp
ENSP00000668541
resolver
ensp
ENSP00000668545
resolver
ensp
ENSP00000708249
resolver
ensp
ENSP00000708251
resolver
ensp
ENSP00000708252
resolver
enst
ENST00000531165
resolver
enst
ENST00000687097
resolver
enst
ENST00000871685
resolver
enst
ENST00000871686
resolver
enst
ENST00000871687
resolver
enst
ENST00000871688
resolver
enst
ENST00000871690
resolver
enst
ENST00000871691
resolver
enst
ENST00000949348
resolver
enst
ENST00000949349
resolver
enst
ENST00000949351
resolver
genesymbol
CELF1
resolver
genesymbol_syn
BRUNOL2
resolver
genesymbol_syn
CUGBP
resolver
genesymbol_syn
CUGBP1
resolver
genesymbol_syn
NAB50
resolver
hgnc
HGNC:2549
resolver
uniprot
B4E2U5
resolver
uniprot
D3DQS0
resolver
uniprot
F8W940
resolver
uniprot
G5EA30
resolver
uniprot
Q4LE52
resolver
uniprot
Q9NP83
resolver
uniprot
Q9NR06
resolver
uniprot_entry
CELF1_HUMAN
resolver
uniprot_entry
G5EA30_HUMAN
resolver
uniprot_sec
B4E2U5
resolver
uniprot_sec
D3DQS0
resolver
uniprot_sec
F8W940
resolver
uniprot_sec
Q4LE52
resolver
uniprot_sec
Q9NP83
resolver
uniprot_sec
Q9NR06
resolver
amino_acid_sequence
MNGTLDHPDQPDLDAIKMFVGQVPRTWSEKDLRELFEQYGAVYEINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNMKVLPGMHHPIQMKPADSEKNNAVEDRKLFIGMISKKCTENDIRVMFSSFGQIEECRILRGPDGLSRGCAFVTFTTRAMAQTAIKAMHQAQTMEGCSSPMVVKFADTQKDKEQKRMAQQLQQQMQQISAASVWGNLAGLNTLGPQYLALYLQLLQQTASSGNLNTLSSLHPMGGLNAMQLQNLAALAAAASAAQNTPSGTNALTTSSSPLSVLTSSGSSPSSSSSNSVNPIASLGALQTLAGATAGLNVGSLAGMAALNGGLGSSGLSNGTGSTMEALTQAYSGIQQYAAAALPTLYNQNLLTQQSIGAAGSQKEGPEGANLFIYHLPQEFGDQDLLQMFMPFGNVVSAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQSMNGFQIGMKRLKVQLKRSKNDSKPY
uniprot
proteins
function
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. Specifically activates exon 5 inclusion of cardiac isoforms of TNNT2 during heart remodeling at the juvenile to adult transition. Acts both as an activator and as a 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. May be a specific regulator of miRNA biogenesis. Binds to primary microRNA pri-MIR140 and, with CELF2, negatively regulates the processing to mature miRNA (PubMed:28431233). {ECO:0000250, ECO:0000269|PubMed:10536163, ECO:0000269|PubMed:11124939, ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:12649496, ECO:0000269|PubMed:12799066, ECO:0000269|PubMed:14726956, ECO:0000269|PubMed:16601207, ECO:0000269|PubMed:16946708, ECO:0000269|PubMed:28431233}.
uniprot
proteins
mass_dalton
52063
uniprot
proteins
mutagenesis
MUTAGEN 63; /note="F->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."; /evidence="ECO:0000269|PubMed:12799066"; MUTAGEN 331; /note="G->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."; /evidence="ECO:0000269|PubMed:12799066"; MUTAGEN 472; /note="L->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."; /evidence="ECO:0000269|PubMed:12799066
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Its phosphorylation status increases in senescent cells. {ECO:0000269|PubMed:14726956}.
uniprot
proteins
protein_family
CELF/BRUNOL family
uniprot
proteins
pubmed
10536163
uniprot
proteins
pubmed
10893231
uniprot
proteins
pubmed
11124939
uniprot
proteins
pubmed
11158314
uniprot
proteins
pubmed
11686919
uniprot
proteins
pubmed
11707455
uniprot
proteins
pubmed
12649496
uniprot
proteins
pubmed
12799066
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14726956
uniprot
proteins
pubmed
14759258
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
16601207
uniprot
proteins
pubmed
16862542
uniprot
proteins
pubmed
16946708
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20947024
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28431233
uniprot
proteins
pubmed
8948631
uniprot
proteins
sequence_length
486
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8948631}. Cytoplasm {ECO:0000269|PubMed:8948631}. Note=RNA-binding activity is detected in both nuclear and cytoplasmic compartments.
uniprot
proteins