Q92879 (CELF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	CELF1
Synonyms:	BRUNOL2, CUGBP, CUGBP1, NAB50

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	486 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.19
Subunit structure	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. Ref.17 Ref.19
Subcellular location	Nucleus. Cytoplasm. Note: RNA-binding activity is detected in both nuclear and cytoplasmic compartments. Ref.1
Tissue specificity	Ubiquitous. Ref.2 Ref.12 Ref.18
Induction	Up-regulated in myotonic dystrophy pathophysiology (DM). Ref.17
Domain	RRM1 and RRM2 domains preferentially target UGU(U/G)-rich mRNA elements. Ref.22
Post-translational modification	Phosphorylated. Its phosphorylation status increases in senescent cells. Ref.15
Sequence similarities	Belongs to the CELF/BRUNOL family. Contains 3 RRM (RNA recognition motif) domains.
Sequence caution	The sequence BAE06101.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	RNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA interference Non-traceable author statement Ref.2. Source: UniProtKB embryo development Non-traceable author statement Ref.2. Source: UniProtKB germ cell development Non-traceable author statement Ref.2. Source: UniProtKB mRNA splice site selection Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of multicellular organism growth Inferred from electronic annotation. Source: Compara regulation of RNA splicing Inferred from direct assay Ref.17. Source: UniProtKB spermatid development Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Non-traceable author statement Ref.2. Source: UniProtKB ribonucleoprotein complex Non-traceable author statement Ref.2. Source: UniProtKB
Molecular_function	BRE binding Inferred from direct assay Ref.2. Source: UniProtKB mRNA binding Inferred from direct assay Ref.15. Source: BHF-UCL nucleotide binding Inferred from electronic annotation. Source: InterPro translation repressor activity, nucleic acid binding Non-traceable author statement Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92879-1)

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.

Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

Isoform 2 (identifier: Q92879-2)

The sequence of this isoform differs from the canonical sequence as follows:
     231-234: Missing.

Isoform 3 (identifier: Q92879-3)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     231-234: Missing.
     297-297: S → SA

Isoform 4 (identifier: Q92879-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAAFKLDFLPEMMVDHCSLNSSPVSKKM
     104-104: Missing.

Isoform 5 (identifier: Q92879-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-17: Missing.
     104-104: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 486

486

CUGBP Elav-like family member 1

PRO_0000081538

Regions

Domain

16 – 99

84

RRM 1

Domain

108 – 188

81

RRM 2

Domain

401 – 479

79

RRM 3

Compositional bias

287 – 308

22

Ser-rich

Amino acid modifications

Modified residue

302

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 17

17

Missing in isoform 5.

VSP_045043

Alternative sequence

1

1

M → MAAFKLDFLPEMMVDHCSLN SSPVSKKM in isoform 4.

VSP_026787

Alternative sequence

104

1

Missing in isoform 4 and isoform 5.

VSP_026788

Alternative sequence

231 – 234

4

Missing in isoform 2 and isoform 3.

VSP_005784

Alternative sequence

297

1

S → SA in isoform 3.

VSP_005785

Experimental info

Mutagenesis

63

1

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. Ref.13

Mutagenesis

331

1

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. Ref.13

Mutagenesis

472

1

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. Ref.13

Secondary structure

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486

Helix Strand Turn

Details...

Beta strand

16 – 22

7

Helix

29 – 37

9

Beta strand

42 – 50

9

Beta strand

52 – 55

4

Beta strand

57 – 68

12

Helix

69 – 79

11

Turn

80 – 82

3

Beta strand

93 – 96

4

Helix

98 – 100

3

Helix

105 – 107

3

Beta strand

108 – 114

7

Helix

121 – 128

8

Helix

129 – 131

3

Beta strand

134 – 141

8

Turn

143 – 145

3

Beta strand

147 – 157

11

Helix

158 – 168

11

Turn

169 – 171

3

Turn

174 – 177

4

Beta strand

182 – 185

4

Helix

385 – 388

4

Beta strand

389 – 391

3

Turn

399 – 401

3

Beta strand

403 – 407

5

Helix

414 – 421

8

Helix

422 – 424

3

Beta strand

428 – 434

7

Beta strand

436 – 438

3

Beta strand

440 – 448

9

Helix

452 – 462

11

Beta strand

473 – 475

3

Beta strand

482 – 484

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (LYLQ) [UniParc]. Last modified October 18, 2001. Version 2. Checksum: C4C13D772273A01D	FASTA	486	52,063
	10 20 30 40 50 60 MNGTLDHPDQ PDLDAIKMFV GQVPRTWSEK DLRELFEQYG AVYEINVLRD RSQNPPQSKG 70 80 90 100 110 120 CCFVTFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE KNNAVEDRKL FIGMISKKCT 130 140 150 160 170 180 ENDIRVMFSS FGQIEECRIL RGPDGLSRGC AFVTFTTRAM AQTAIKAMHQ AQTMEGCSSP 190 200 210 220 230 240 MVVKFADTQK DKEQKRMAQQ LQQQMQQISA ASVWGNLAGL NTLGPQYLAL YLQLLQQTAS 250 260 270 280 290 300 SGNLNTLSSL HPMGGLNAMQ LQNLAALAAA ASAAQNTPSG TNALTTSSSP LSVLTSSGSS 310 320 330 340 350 360 PSSSSSNSVN PIASLGALQT LAGATAGLNV GSLAGMAALN GGLGSSGLSN GTGSTMEALT 370 380 390 400 410 420 QAYSGIQQYA AAALPTLYNQ NLLTQQSIGA AGSQKEGPEG ANLFIYHLPQ EFGDQDLLQM 430 440 450 460 470 480 FMPFGNVVSA KVFIDKQTNL SKCFGFVSYD NPVSAQAAIQ SMNGFQIGMK RLKVQLKRSK NDSKPY
	Isoform 2 [UniParc]. Checksum: AC0863DB01A22163	FASTA	482	51,546
	10 20 30 40 50 60 MNGTLDHPDQ PDLDAIKMFV GQVPRTWSEK DLRELFEQYG AVYEINVLRD RSQNPPQSKG 70 80 90 100 110 120 CCFVTFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE KNNAVEDRKL FIGMISKKCT 130 140 150 160 170 180 ENDIRVMFSS FGQIEECRIL RGPDGLSRGC AFVTFTTRAM AQTAIKAMHQ AQTMEGCSSP 190 200 210 220 230 240 MVVKFADTQK DKEQKRMAQQ LQQQMQQISA ASVWGNLAGL NTLGPQYLAL LQQTASSGNL 250 260 270 280 290 300 NTLSSLHPMG GLNAMQLQNL AALAAAASAA QNTPSGTNAL TTSSSPLSVL TSSGSSPSSS 310 320 330 340 350 360 SSNSVNPIAS LGALQTLAGA TAGLNVGSLA GMAALNGGLG SSGLSNGTGS TMEALTQAYS 370 380 390 400 410 420 GIQQYAAAAL PTLYNQNLLT QQSIGAAGSQ KEGPEGANLF IYHLPQEFGD QDLLQMFMPF 430 440 450 460 470 480 GNVVSAKVFI DKQTNLSKCF GFVSYDNPVS AQAAIQSMNG FQIGMKRLKV QLKRSKNDSK PY
	Isoform 3 (A) [UniParc]. Checksum: 0C8D6B707E157FD1	FASTA	483	51,617
	10 20 30 40 50 60 MNGTLDHPDQ PDLDAIKMFV GQVPRTWSEK DLRELFEQYG AVYEINVLRD RSQNPPQSKG 70 80 90 100 110 120 CCFVTFYTRK AALEAQNALH NMKVLPGMHH PIQMKPADSE KNNAVEDRKL FIGMISKKCT 130 140 150 160 170 180 ENDIRVMFSS FGQIEECRIL RGPDGLSRGC AFVTFTTRAM AQTAIKAMHQ AQTMEGCSSP 190 200 210 220 230 240 MVVKFADTQK DKEQKRMAQQ LQQQMQQISA ASVWGNLAGL NTLGPQYLAL LQQTASSGNL 250 260 270 280 290 300 NTLSSLHPMG GLNAMQLQNL AALAAAASAA QNTPSGTNAL TTSSSPLSVL TSSAGSSPSS 310 320 330 340 350 360 SSSNSVNPIA SLGALQTLAG ATAGLNVGSL AGMAALNGGL GSSGLSNGTG STMEALTQAY 370 380 390 400 410 420 SGIQQYAAAA LPTLYNQNLL TQQSIGAAGS QKEGPEGANL FIYHLPQEFG DQDLLQMFMP 430 440 450 460 470 480 FGNVVSAKVF IDKQTNLSKC FGFVSYDNPV SAQAAIQSMN GFQIGMKRLK VQLKRSKNDS KPY
	Isoform 4 [UniParc]. Checksum: 2A099A7F4E0F5358	FASTA	512	55,001
	10 20 30 40 50 60 MAAFKLDFLP EMMVDHCSLN SSPVSKKMNG TLDHPDQPDL DAIKMFVGQV PRTWSEKDLR 70 80 90 100 110 120 ELFEQYGAVY EINVLRDRSQ NPPQSKGCCF VTFYTRKAAL EAQNALHNMK VLPGMHHPIQ 130 140 150 160 170 180 MKPADSEKNN VEDRKLFIGM ISKKCTENDI RVMFSSFGQI EECRILRGPD GLSRGCAFVT 190 200 210 220 230 240 FTTRAMAQTA IKAMHQAQTM EGCSSPMVVK FADTQKDKEQ KRMAQQLQQQ MQQISAASVW 250 260 270 280 290 300 GNLAGLNTLG PQYLALYLQL LQQTASSGNL NTLSSLHPMG GLNAMQLQNL AALAAAASAA 310 320 330 340 350 360 QNTPSGTNAL TTSSSPLSVL TSSGSSPSSS SSNSVNPIAS LGALQTLAGA TAGLNVGSLA 370 380 390 400 410 420 GMAALNGGLG SSGLSNGTGS TMEALTQAYS GIQQYAAAAL PTLYNQNLLT QQSIGAAGSQ 430 440 450 460 470 480 KEGPEGANLF IYHLPQEFGD QDLLQMFMPF GNVVSAKVFI DKQTNLSKCF GFVSYDNPVS 490 500 510 AQAAIQSMNG FQIGMKRLKV QLKRSKNDSK PY
	Isoform 5 [UniParc]. Checksum: 7CD2C6BFBE344830	FASTA	468	50,130
	10 20 30 40 50 60 MFVGQVPRTW SEKDLRELFE QYGAVYEINV LRDRSQNPPQ SKGCCFVTFY TRKAALEAQN 70 80 90 100 110 120 ALHNMKVLPG MHHPIQMKPA DSEKNNVEDR KLFIGMISKK CTENDIRVMF SSFGQIEECR 130 140 150 160 170 180 ILRGPDGLSR GCAFVTFTTR AMAQTAIKAM HQAQTMEGCS SPMVVKFADT QKDKEQKRMA 190 200 210 220 230 240 QQLQQQMQQI SAASVWGNLA GLNTLGPQYL ALYLQLLQQT ASSGNLNTLS SLHPMGGLNA 250 260 270 280 290 300 MQLQNLAALA AAASAAQNTP SGTNALTTSS SPLSVLTSSG SSPSSSSSNS VNPIASLGAL 310 320 330 340 350 360 QTLAGATAGL NVGSLAGMAA LNGGLGSSGL SNGTGSTMEA LTQAYSGIQQ YAAAALPTLY 370 380 390 400 410 420 NQNLLTQQSI GAAGSQKEGP EGANLFIYHL PQEFGDQDLL QMFMPFGNVV SAKVFIDKQT 430 440 450 460 NLSKCFGFVS YDNPVSAQAA IQSMNGFQIG MKRLKVQLKR SKNDSKPY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." 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. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	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 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]	"An unappreciated role for RNA surveillance." Hillman R.T., Green R.E., Brenner S.E. Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract] 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"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.
[22]	"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, RRM DOMAINS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00034015.
IPI00218388.
IPI00218389.
IPI00853009.
IPI00956101.

RefSeq

NP_001020767.1. NM_001025596.2.
NP_001166110.1. NM_001172639.1.
NP_001166111.1. NM_001172640.1.
NP_006551.1. NM_006560.3.
NP_941989.1. NM_198700.2.

UniGene

Hs.595333.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q92879.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q92879. 4 interactions.

MINT

MINT-1382906.

STRING

9606.ENSP00000351409.

PTM databases

PhosphoSite

Q92879.

Polymorphism databases

DMDM

17374605.

Proteomic databases

PaxDb

Q92879.

PRIDE

Q92879.

Protocols and materials databases

DNASU

10658.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000310513; ENSP00000308386; ENSG00000149187.
ENST00000358597; ENSP00000351409; ENSG00000149187.
ENST00000361904; ENSP00000354639; ENSG00000149187.
ENST00000395292; ENSP00000378706; ENSG00000149187.
ENST00000532048; ENSP00000435926; ENSG00000149187.

GeneID

10658.

KEGG

hsa:10658.

UCSC

uc001nfk.2. human.
uc001nfl.3. human.
uc001nfm.3. human.
uc001nfn.3. human.

Organism-specific databases

CTD

10658.

GeneCards

GC11M047602.

HGNC

HGNC:2549. CELF1.

HPA

CAB016114.

MIM

601074. gene.

neXtProt

NX_Q92879.

PharmGKB

PA27045.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG251494.

HOGENOM

HOG000004754.

HOVERGEN

HBG107646.

InParanoid

Q92879.

KO

K13207.

OrthoDB

EOG4N8R4X.

PhylomeDB

Q92879.

Gene expression databases

ArrayExpress

Q92879.

Bgee

Q92879.

CleanEx

HS_CUGBP1.

Genevestigator

Q92879.

GermOnline

ENSG00000149187. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 3 hits.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00076. RRM_1. 3 hits.
[Graphical view]

SMART

SM00360. RRM. 3 hits.
[Graphical view]

PROSITE

PS50102. RRM. 3 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

CELF1. human.

EvolutionaryTrace

Q92879.

GenomeRNAi

10658.

NextBio

40521.

SOURCE

Search...

Entry information

Entry name

CELF1_HUMAN

Accession

Primary (citable) accession number: Q92879
Secondary accession number(s): B4E2U5 , D3DQS0, F8W940, Q4LE52, Q9NP83, Q9NR06

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	October 18, 2001
Last modified:	May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.