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CUGBP Elav-like family member 1 (CELF-1) (50 kDa nuclear polyadenylated RNA-binding protein) (Bruno-like protein 2) (CUG triplet repeat RNA-binding protein 1) (CUG-BP1) (CUG-BP- and ETR-3-like factor 1) (Deadenylation factor CUG-BP) (Embryo deadenylation element-binding protein homolog) (EDEN-BP homolog) (RNA-binding protein BRUNOL-2)

 CELF1_HUMAN             Reviewed;         486 AA.
Q92879; B4E2U5; D3DQS0; F8W940; Q4LE52; Q9NP83; Q9NR06;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
18-OCT-2001, sequence version 2.
25-OCT-2017, entry version 174.
RecName: Full=CUGBP Elav-like family member 1;
Short=CELF-1;
AltName: Full=50 kDa nuclear polyadenylated RNA-binding protein;
AltName: Full=Bruno-like protein 2;
AltName: Full=CUG triplet repeat RNA-binding protein 1;
Short=CUG-BP1;
AltName: Full=CUG-BP- and ETR-3-like factor 1;
AltName: Full=Deadenylation factor CUG-BP;
AltName: Full=Embryo deadenylation element-binding protein homolog;
Short=EDEN-BP homolog;
AltName: Full=RNA-binding protein BRUNOL-2;
Name=CELF1; Synonyms=BRUNOL2, CUGBP, CUGBP1, NAB50;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
RNA-BINDING.
PubMed=8948631; DOI=10.1093/nar/24.22.4407;
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.;
"Identification of a (CUG)n triplet repeat RNA-binding protein and its
expression in myotonic dystrophy.";
Nucleic Acids Res. 24:4407-4414(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), RNA-BINDING, AND TISSUE
SPECIFICITY.
PubMed=10893231; DOI=10.1074/jbc.M003083200;
Good P.J., Chen Q., Warner S.J., Herring D.C.;
"A family of human RNA-binding proteins related to the Drosophila
Bruno translational regulator.";
J. Biol. Chem. 275:28583-28592(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain, and Skeletal muscle;
PubMed=11686919; DOI=10.1093/oxfordjournals.jbchem.a003022;
Takahashi N., Sasagawa N., Usuki F., Kino Y., Kawahara H.,
Sorimachi H., Maeda T., Suzuki K., Ishiura S.;
"Coexpression of the CUG-binding protein reduces DM protein kinase
expression in COS cells.";
J. Biochem. 130:581-587(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND RNA-BINDING.
PubMed=11707455; DOI=10.1074/jbc.M109362200;
Paillard L., Legagneux V., Maniey D., Osborne H.B.;
"c-Jun ARE targets mRNA deadenylation by an EDEN-BP (embryo
deadenylation element-binding protein)-dependent pathway.";
J. Biol. Chem. 277:3232-3235(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Brain;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
FUNCTION, AND RNA-BINDING.
PubMed=10536163; DOI=10.1093/nar/27.22.4517;
Timchenko N.A., Welm A.L., Lu X., Timchenko L.T.;
"CUG repeat binding protein (CUGBP1) interacts with the 5' region of
C/EBPbeta mRNA and regulates translation of C/EBPbeta isoforms.";
Nucleic Acids Res. 27:4517-4525(1999).
[11]
FUNCTION, AND RNA-BINDING.
PubMed=11124939; DOI=10.1074/jbc.M005960200;
Timchenko N.A., Cai Z.J., Welm A.L., Reddy S., Ashizawa T.,
Timchenko L.T.;
"RNA CUG repeats sequester CUGBP1 and alter protein levels and
activity of CUGBP1.";
J. Biol. Chem. 276:7820-7826(2001).
[12]
FUNCTION, RNA-BINDING, AND TISSUE SPECIFICITY.
PubMed=11158314; DOI=10.1128/MCB.21.4.1285-1296.2001;
Ladd A.N., Charlet-B N., Cooper T.A.;
"The CELF family of RNA binding proteins is implicated in cell-
specific and developmentally regulated alternative splicing.";
Mol. Cell. Biol. 21:1285-1296(2001).
[13]
FUNCTION, MUTAGENESIS OF PHE-63; GLY-331 AND LEU-472, AND RNA-BINDING.
PubMed=12799066; DOI=10.1016/S0248-4900(03)00010-8;
Paillard L., Legagneux V., Beverley Osborne H.;
"A functional deadenylation assay identifies human CUG-BP as a
deadenylation factor.";
Biol. Cell 95:107-113(2003).
[14]
FUNCTION, AND RNA-BINDING.
PubMed=12649496; DOI=10.1261/rna.2191903;
Gromak N., Matlin A.J., Cooper T.A., Smith C.W.;
"Antagonistic regulation of alpha-actinin alternative splicing by CELF
proteins and polypyrimidine tract binding protein.";
RNA 9:443-456(2003).
[15]
FUNCTION, PHOSPHORYLATION, AND RNA-BINDING.
PubMed=14726956; DOI=10.1038/sj.emboj.7600052;
Iakova P., Wang G.-L., Timchenko L., Michalak M., Pereira-Smith O.M.,
Smith J.R., Timchenko N.A.;
"Competition of CUGBP1 and calreticulin for the regulation of p21
translation determines cell fate.";
EMBO J. 23:406-417(2004).
[16]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:R8.1-R8.16(2004).
[17]
FUNCTION, INTERACTION WITH HNRNPH1, RNA-BINDING, AND INDUCTION.
PubMed=16946708; DOI=10.1038/sj.emboj.7601296;
Paul S., Dansithong W., Kim D., Rossi J., Webster N.J., Comai L.,
Reddy S.;
"Interaction of muscleblind, CUG-BP1 and hnRNP H proteins in DM1-
associated aberrant IR splicing.";
EMBO J. 25:4271-4283(2006).
[18]
TISSUE SPECIFICITY.
PubMed=16862542; DOI=10.1002/jnr.20980;
Leroy O., Dhaenens C.-M., Schraen-Maschke S., Belarbi K.,
Delacourte A., Andreadis A., Sablonniere B., Buee L., Sergeant N.,
Caillet-Boudin M.-L.;
"ETR-3 represses Tau exons 2/3 inclusion, a splicing event abnormally
enhanced in myotonic dystrophy type I.";
J. Neurosci. Res. 84:852-859(2006).
[19]
FUNCTION, INTERACTION WITH PARN, AND RNA-BINDING.
PubMed=16601207; DOI=10.1261/rna.59606;
Moraes K.C., Wilusz C.J., Wilusz J.;
"CUG-BP binds to RNA substrates and recruits PARN deadenylase.";
RNA 12:1084-1091(2006).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-4 AND SER-179, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[25]
FUNCTION, AND MIRNA-BINDING.
PubMed=28431233; DOI=10.1016/j.molcel.2017.03.014;
Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L.,
Eichner N., Lehmann G., Schall K., Urlaub H., Meister G.;
"A Compendium of RNA-Binding Proteins that Regulate MicroRNA
Biogenesis.";
Mol. Cell 66:270-284(2017).
[26]
STRUCTURE BY NMR OF 383-484.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RNA-binding domain 3 in CUG triplet repeat RNA-
binding protein 1.";
Submitted (NOV-2005) to the PDB data bank.
[27]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 14-187 IN COMPLEX WITH MRNA,
AND DOMAINS RRM.
PubMed=20947024; DOI=10.1016/j.str.2010.06.018;
Teplova M., Song J., Gaw H.Y., Teplov A., Patel D.J.;
"Structural insights into RNA recognition by the alternate-splicing
regulator CUG-binding protein 1.";
Structure 18:1364-1377(2010).
-!- 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 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. 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}.
-!- SUBUNIT: 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.
{ECO:0000250, ECO:0000269|PubMed:16601207,
ECO:0000269|PubMed:16946708, ECO:0000269|PubMed:20947024}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8948631}.
Cytoplasm {ECO:0000269|PubMed:8948631}. Note=RNA-binding activity
is detected in both nuclear and cytoplasmic compartments.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=LYLQ;
IsoId=Q92879-1; Sequence=Displayed;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=2;
IsoId=Q92879-2; Sequence=VSP_005784;
Name=3; Synonyms=A;
IsoId=Q92879-3; Sequence=VSP_005784, VSP_005785;
Name=4;
IsoId=Q92879-4; Sequence=VSP_026787, VSP_026788;
Name=5;
IsoId=Q92879-5; Sequence=VSP_045043, VSP_026788;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q92879-6; Sequence=VSP_026788;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10893231,
ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:16862542}.
-!- INDUCTION: Up-regulated in myotonic dystrophy pathophysiology
(DM). {ECO:0000269|PubMed:16946708}.
-!- DOMAIN: RRM1 and RRM2 domains preferentially target UGU(U/G)-rich
mRNA elements. {ECO:0000269|PubMed:20947024}.
-!- PTM: Phosphorylated. Its phosphorylation status increases in
senescent cells. {ECO:0000269|PubMed:14726956}.
-!- SIMILARITY: Belongs to the CELF/BRUNOL family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAE06101.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U63289; AAC50895.1; -; mRNA.
EMBL; AF248648; AAF86230.1; -; mRNA.
EMBL; AF267533; AAF78955.1; -; mRNA.
EMBL; AF267534; AAF78956.1; -; mRNA.
EMBL; AJ007988; CAC20566.1; -; mRNA.
EMBL; AK304430; BAG65257.1; -; mRNA.
EMBL; AB210019; BAE06101.1; ALT_INIT; mRNA.
EMBL; AC090559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW67909.1; -; Genomic_DNA.
EMBL; CH471064; EAW67912.1; -; Genomic_DNA.
EMBL; BC031079; AAH31079.1; -; mRNA.
CCDS; CCDS31482.1; -. [Q92879-1]
CCDS; CCDS53622.1; -. [Q92879-6]
CCDS; CCDS53623.1; -. [Q92879-4]
CCDS; CCDS7938.1; -. [Q92879-2]
CCDS; CCDS7939.1; -. [Q92879-3]
RefSeq; NP_001020767.1; NM_001025596.2. [Q92879-1]
RefSeq; NP_001166110.1; NM_001172639.1. [Q92879-4]
RefSeq; NP_001166111.1; NM_001172640.1. [Q92879-6]
RefSeq; NP_006551.1; NM_006560.3. [Q92879-2]
RefSeq; NP_941989.1; NM_198700.2. [Q92879-3]
RefSeq; XP_011518161.1; XM_011519859.1. [Q92879-3]
RefSeq; XP_016872613.1; XM_017017124.1. [Q92879-1]
RefSeq; XP_016872614.1; XM_017017125.1. [Q92879-1]
RefSeq; XP_016872615.1; XM_017017126.1. [Q92879-1]
RefSeq; XP_016872616.1; XM_017017127.1. [Q92879-1]
RefSeq; XP_016872617.1; XM_017017128.1. [Q92879-1]
RefSeq; XP_016872618.1; XM_017017129.1. [Q92879-1]
RefSeq; XP_016872619.1; XM_017017130.1. [Q92879-1]
RefSeq; XP_016872620.1; XM_017017131.1. [Q92879-1]
RefSeq; XP_016872621.1; XM_017017132.1. [Q92879-1]
RefSeq; XP_016872622.1; XM_017017133.1. [Q92879-3]
RefSeq; XP_016872623.1; XM_017017134.1. [Q92879-3]
RefSeq; XP_016872624.1; XM_017017135.1. [Q92879-2]
UniGene; Hs.595333; -.
PDB; 2CPZ; NMR; -; A=383-484.
PDB; 2DHS; NMR; -; A=1-187.
PDB; 2RQ4; NMR; -; A=383-484.
PDB; 2RQC; NMR; -; A=383-484.
PDB; 3NMR; X-ray; 1.85 A; A=14-187.
PDB; 3NNA; X-ray; 1.90 A; A=14-187.
PDB; 3NNC; X-ray; 2.20 A; A=14-187.
PDB; 3NNH; X-ray; 2.75 A; A/B/C/D=14-100.
PDBsum; 2CPZ; -.
PDBsum; 2DHS; -.
PDBsum; 2RQ4; -.
PDBsum; 2RQC; -.
PDBsum; 3NMR; -.
PDBsum; 3NNA; -.
PDBsum; 3NNC; -.
PDBsum; 3NNH; -.
ProteinModelPortal; Q92879; -.
SMR; Q92879; -.
BioGrid; 115901; 23.
IntAct; Q92879; 19.
MINT; MINT-1382906; -.
STRING; 9606.ENSP00000435926; -.
iPTMnet; Q92879; -.
PhosphoSitePlus; Q92879; -.
BioMuta; CELF1; -.
DMDM; 17374605; -.
EPD; Q92879; -.
MaxQB; Q92879; -.
PaxDb; Q92879; -.
PeptideAtlas; Q92879; -.
PRIDE; Q92879; -.
DNASU; 10658; -.
Ensembl; ENST00000310513; ENSP00000308386; ENSG00000149187. [Q92879-2]
Ensembl; ENST00000358597; ENSP00000351409; ENSG00000149187. [Q92879-1]
Ensembl; ENST00000361904; ENSP00000354639; ENSG00000149187. [Q92879-3]
Ensembl; ENST00000395290; ENSP00000378705; ENSG00000149187. [Q92879-6]
Ensembl; ENST00000395292; ENSP00000378706; ENSG00000149187. [Q92879-3]
Ensembl; ENST00000532048; ENSP00000435926; ENSG00000149187. [Q92879-4]
GeneID; 10658; -.
KEGG; hsa:10658; -.
UCSC; uc001nfk.3; human. [Q92879-1]
CTD; 10658; -.
DisGeNET; 10658; -.
EuPathDB; HostDB:ENSG00000149187.17; -.
GeneCards; CELF1; -.
HGNC; HGNC:2549; CELF1.
HPA; CAB016114; -.
HPA; HPA044597; -.
MIM; 601074; gene.
neXtProt; NX_Q92879; -.
OpenTargets; ENSG00000149187; -.
PharmGKB; PA27045; -.
eggNOG; KOG0146; Eukaryota.
eggNOG; ENOG410XNTW; LUCA.
GeneTree; ENSGT00560000076837; -.
HOGENOM; HOG000004754; -.
HOVERGEN; HBG107646; -.
InParanoid; Q92879; -.
KO; K13207; -.
PhylomeDB; Q92879; -.
TreeFam; TF314924; -.
ChiTaRS; CELF1; human.
EvolutionaryTrace; Q92879; -.
GeneWiki; CUGBP1; -.
GenomeRNAi; 10658; -.
PRO; PR:Q92879; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149187; -.
CleanEx; HS_CUGBP1; -.
ExpressionAtlas; Q92879; baseline and differential.
Genevisible; Q92879; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; NAS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0042835; F:BRE binding; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:BHF-UCL.
GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000900; F:translation repressor activity, nucleic acid binding; NAS:UniProtKB.
GO; GO:0009790; P:embryo development; NAS:UniProtKB.
GO; GO:0007281; P:germ cell development; NAS:UniProtKB.
GO; GO:0006397; P:mRNA processing; TAS:ProtInc.
GO; GO:0006376; P:mRNA splice site selection; IDA:UniProtKB.
GO; GO:0043484; P:regulation of RNA splicing; IDA:UniProtKB.
GO; GO:0016246; P:RNA interference; NAS:UniProtKB.
CDD; cd12631; RRM1_CELF1_2_Bruno; 1.
CDD; cd12634; RRM2_CELF1_2; 1.
CDD; cd12638; RRM3_CELF1_2; 1.
InterPro; IPR034196; CELF1/2_RRM1.
InterPro; IPR034198; CELF1/2_RRM2.
InterPro; IPR034199; CELF1/2_RRM3.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
Pfam; PF00076; RRM_1; 3.
SMART; SM00360; RRM; 3.
SUPFAM; SSF54928; SSF54928; 3.
PROSITE; PS50102; RRM; 3.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Complete proteome; Cytoplasm; Isopeptide bond; mRNA processing;
mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
RNA-binding; Ubl conjugation.
CHAIN 1 486 CUGBP Elav-like family member 1.
/FTId=PRO_0000081538.
DOMAIN 16 99 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 108 188 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 401 479 RRM 3. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
COMPBIAS 287 308 Ser-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 4 4 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 179 179 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000250|UniProtKB:P28659}.
CROSSLNK 109 109 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 17 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045043.
VAR_SEQ 1 1 M -> MAAFKLDFLPEMMVDHCSLNSSPVSKKM (in
isoform 4). {ECO:0000303|Ref.6}.
/FTId=VSP_026787.
VAR_SEQ 104 104 Missing (in isoform 4, isoform 5 and
isoform 6). {ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.6}.
/FTId=VSP_026788.
VAR_SEQ 231 234 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:11686919,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8948631}.
/FTId=VSP_005784.
VAR_SEQ 297 297 S -> SA (in isoform 3).
{ECO:0000303|PubMed:11686919,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_005785.
MUTAGEN 63 63 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. {ECO:0000269|PubMed:12799066}.
MUTAGEN 331 331 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.
{ECO:0000269|PubMed:12799066}.
MUTAGEN 472 472 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.
{ECO:0000269|PubMed:12799066}.
STRAND 16 22 {ECO:0000244|PDB:3NMR}.
HELIX 29 37 {ECO:0000244|PDB:3NMR}.
STRAND 42 50 {ECO:0000244|PDB:3NMR}.
STRAND 52 55 {ECO:0000244|PDB:3NMR}.
STRAND 57 68 {ECO:0000244|PDB:3NMR}.
HELIX 69 79 {ECO:0000244|PDB:3NMR}.
TURN 80 82 {ECO:0000244|PDB:3NMR}.
STRAND 93 96 {ECO:0000244|PDB:3NMR}.
HELIX 98 100 {ECO:0000244|PDB:3NMR}.
HELIX 105 107 {ECO:0000244|PDB:3NMR}.
STRAND 108 114 {ECO:0000244|PDB:3NMR}.
HELIX 121 128 {ECO:0000244|PDB:3NMR}.
HELIX 129 131 {ECO:0000244|PDB:3NMR}.
STRAND 134 141 {ECO:0000244|PDB:3NMR}.
TURN 143 145 {ECO:0000244|PDB:2DHS}.
STRAND 147 157 {ECO:0000244|PDB:3NMR}.
HELIX 158 168 {ECO:0000244|PDB:3NMR}.
TURN 169 171 {ECO:0000244|PDB:2DHS}.
TURN 174 177 {ECO:0000244|PDB:2DHS}.
STRAND 182 185 {ECO:0000244|PDB:3NMR}.
HELIX 385 388 {ECO:0000244|PDB:2RQ4}.
STRAND 389 391 {ECO:0000244|PDB:2RQ4}.
TURN 399 401 {ECO:0000244|PDB:2RQC}.
STRAND 403 407 {ECO:0000244|PDB:2CPZ}.
HELIX 414 421 {ECO:0000244|PDB:2CPZ}.
HELIX 422 424 {ECO:0000244|PDB:2CPZ}.
STRAND 428 434 {ECO:0000244|PDB:2CPZ}.
STRAND 436 438 {ECO:0000244|PDB:2CPZ}.
STRAND 440 448 {ECO:0000244|PDB:2CPZ}.
HELIX 452 462 {ECO:0000244|PDB:2CPZ}.
STRAND 473 475 {ECO:0000244|PDB:2CPZ}.
STRAND 482 484 {ECO:0000244|PDB:2RQ4}.
SEQUENCE 486 AA; 52063 MW; C4C13D772273A01D CRC64;
MNGTLDHPDQ PDLDAIKMFV GQVPRTWSEK DLRELFEQYG AVYEINVLRD RSQNPPQSKG
CCFVTFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE KNNAVEDRKL FIGMISKKCT
ENDIRVMFSS FGQIEECRIL RGPDGLSRGC AFVTFTTRAM AQTAIKAMHQ AQTMEGCSSP
MVVKFADTQK DKEQKRMAQQ LQQQMQQISA ASVWGNLAGL NTLGPQYLAL YLQLLQQTAS
SGNLNTLSSL HPMGGLNAMQ LQNLAALAAA ASAAQNTPSG TNALTTSSSP LSVLTSSGSS
PSSSSSNSVN PIASLGALQT LAGATAGLNV GSLAGMAALN GGLGSSGLSN GTGSTMEALT
QAYSGIQQYA AAALPTLYNQ NLLTQQSIGA AGSQKEGPEG ANLFIYHLPQ EFGDQDLLQM
FMPFGNVVSA KVFIDKQTNL SKCFGFVSYD NPVSAQAAIQ SMNGFQIGMK RLKVQLKRSK
NDSKPY


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