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Q92879 (CELF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Protein existenceEvidence 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.23

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 processmRNA processing
mRNA splicing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   Molecular functionActivator
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA 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 processing

Traceable author statement Ref.1. Source: ProtInc

mRNA splice site selection

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of translation

Non-traceable author statement Ref.2. Source: GOC

positive regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

regulation of RNA splicing

Inferred from direct assay Ref.17. Source: UniProtKB

spermatid development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

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_functionBRE binding

Inferred from direct assay Ref.2. Source: UniProtKB

RNA binding

Inferred from direct assay Ref.17. Source: UniProtKB

mRNA binding

Inferred from direct assay Ref.15. Source: BHF-UCL

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.17. Source: UniProtKB

translation repressor activity, nucleic acid binding

Non-traceable author statement Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 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.
Isoform 6 (identifier: Q92879-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 486486CUGBP Elav-like family member 1
PRO_0000081538

Regions

Domain16 – 9984RRM 1
Domain108 – 18881RRM 2
Domain401 – 47979RRM 3
Compositional bias287 – 30822Ser-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.20
Modified residue3021Phosphoserine By similarity

Natural variations

Alternative sequence1 – 1717Missing in isoform 5.
VSP_045043
Alternative sequence11M → MAAFKLDFLPEMMVDHCSLN SSPVSKKM in isoform 4.
VSP_026787
Alternative sequence1041Missing in isoform 4, isoform 5 and isoform 6.
VSP_026788
Alternative sequence231 – 2344Missing in isoform 2 and isoform 3.
VSP_005784
Alternative sequence2971S → SA in isoform 3.
VSP_005785

Experimental info

Mutagenesis631F → 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
Mutagenesis3311G → 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
Mutagenesis4721L → 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

......................................................... 486
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (LYLQ) [UniParc].

Last modified October 18, 2001. Version 2.
Checksum: C4C13D772273A01D

FASTA48652,063
        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 

« Hide

Isoform 2 [UniParc].

Checksum: AC0863DB01A22163
Show »

FASTA48251,546
Isoform 3 (A) [UniParc].

Checksum: 0C8D6B707E157FD1
Show »

FASTA48351,617
Isoform 4 [UniParc].

Checksum: 2A099A7F4E0F5358
Show »

FASTA51255,001
Isoform 5 [UniParc].

Checksum: 7CD2C6BFBE344830
Show »

FASTA46850,130
Isoform 6 [UniParc].

Checksum: 37B0006E19EC012A
Show »

FASTA48551,992

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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].
[22]"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.
[23]"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, DOMAINS RRM.
+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.
CCDSCCDS31482.1. [Q92879-1]
CCDS53622.1. [Q92879-6]
CCDS53623.1. [Q92879-4]
CCDS7938.1. [Q92879-2]
CCDS7939.1. [Q92879-3]
RefSeqNP_001020767.1. NM_001025596.2. [Q92879-1]
NP_001166110.1. NM_001172639.1. [Q92879-4]
NP_001166111.1. NM_001172640.1. [Q92879-6]
NP_006551.1. NM_006560.3. [Q92879-2]
NP_941989.1. NM_198700.2. [Q92879-3]
UniGeneHs.595333.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CPZNMR-A383-484[»]
2DHSNMR-A1-187[»]
2RQ4NMR-A383-484[»]
2RQCNMR-A383-484[»]
3NMRX-ray1.85A14-187[»]
3NNAX-ray1.90A14-187[»]
3NNCX-ray2.20A14-187[»]
3NNHX-ray2.75A/B/C/D14-100[»]
ProteinModelPortalQ92879.
SMRQ92879. Positions 1-187, 355-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115901. 15 interactions.
IntActQ92879. 9 interactions.
MINTMINT-1382906.
STRING9606.ENSP00000351409.

PTM databases

PhosphoSiteQ92879.

Polymorphism databases

DMDM17374605.

Proteomic databases

MaxQBQ92879.
PaxDbQ92879.
PRIDEQ92879.

Protocols and materials databases

DNASU10658.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310513; ENSP00000308386; ENSG00000149187. [Q92879-2]
ENST00000358597; ENSP00000351409; ENSG00000149187. [Q92879-1]
ENST00000361904; ENSP00000354639; ENSG00000149187. [Q92879-3]
ENST00000395290; ENSP00000378705; ENSG00000149187. [Q92879-6]
ENST00000395292; ENSP00000378706; ENSG00000149187. [Q92879-3]
ENST00000532048; ENSP00000435926; ENSG00000149187. [Q92879-4]
GeneID10658.
KEGGhsa:10658.
UCSCuc001nfk.2. human. [Q92879-4]
uc001nfl.3. human. [Q92879-1]
uc001nfm.3. human. [Q92879-3]
uc001nfn.3. human. [Q92879-2]

Organism-specific databases

CTD10658.
GeneCardsGC11M048801.
HGNCHGNC:2549. CELF1.
HPACAB016114.
HPA044597.
MIM601074. gene.
neXtProtNX_Q92879.
PharmGKBPA27045.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251494.
HOGENOMHOG000004754.
HOVERGENHBG107646.
InParanoidQ92879.
KOK13207.
OrthoDBEOG7DVDBR.
PhylomeDBQ92879.
TreeFamTF314924.

Gene expression databases

ArrayExpressQ92879.
BgeeQ92879.
CleanExHS_CUGBP1.
GenevestigatorQ92879.

Family and domain databases

Gene3D3.30.70.330. 3 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTSM00360. RRM. 3 hits.
[Graphical view]
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCELF1. human.
EvolutionaryTraceQ92879.
GeneWikiCUGBP1.
GenomeRNAi10658.
NextBio40521.
PROQ92879.
SOURCESearch...

Entry information

Entry nameCELF1_HUMAN
AccessionPrimary (citable) accession number: Q92879
Secondary accession number(s): B4E2U5 expand/collapse secondary AC list , D3DQS0, F8W940, Q4LE52, Q9NP83, Q9NR06
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 18, 2001
Last modified: July 9, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM