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O95319 (CELF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 2

Short name=CELF-2
Alternative name(s):
Bruno-like protein 3
CUG triplet repeat RNA-binding protein 2
Short name=CUG-BP2
CUG-BP- and ETR-3-like factor 2
ELAV-type RNA-binding protein 3
Short name=ETR-3
Neuroblastoma apoptosis-related RNA-binding protein
Short name=hNAPOR
RNA-binding protein BRUNOL-3
Gene names
Name:CELF2
Synonyms:BRUNOL3, CUGBP2, ETR3, NAPOR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length508 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 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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

Subunit structure

Interacts with A1CF By similarity.

Subcellular location

Nucleus. Cytoplasm. Note: Accumulates in the cytoplasm after ionizing radiation By similarity. Colocalizes with APOBEC1 and A1CF. RNA-binding activity is detected in both nuclear and cytoplasmic compartments. Ref.10 Ref.11 Ref.15

Tissue specificity

Expressed in frontal cortex. Isoform 1 is expressed in brain and lung. Isoform 2 is expressed in heart, brain, placenta, lung, liver, kidney, skeletal muscle and pancreas. Isoform 4 is expressed in heart, lung, skeletal muscle, kidney and pancreas. Ref.2 Ref.3 Ref.4 Ref.12 Ref.18

Developmental stage

Isoform 1 is expressed in fetal brain. Isoform 2 is expressed in fetal heart, brain, thymus, lung, liver, skeletal muscle, kidney and spleen. Isoform 4 is expressed in fetal heart, brain, thymus, lung and skeletal muscle. Ref.2 Ref.4

Sequence similarities

Belongs to the CELF/BRUNOL family.

Contains 3 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandRNA-binding
   Molecular functionRepressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA processing

Traceable author statement PubMed 9887331. Source: ProtInc

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of heart contraction

Traceable author statement PubMed 9887331. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Traceable author statement PubMed 9887331. Source: ProtInc

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95319-1)

Also known as: NAPOR-3;

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.
Isoform 2 (identifier: O95319-2)

Also known as: NAPOR-1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
     358-358: A → AVAQMLS
Isoform 3 (identifier: O95319-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MRCPKSAVTMRNEELLLS → MMVEGRLLVPDRI
     358-358: A → AGTINTPRSKRLLLPKDNN
Isoform 4 (identifier: O95319-4)

Also known as: NAPOR-2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MRCPKSAVTMRNEELLLS → MMVEGRLLVPDRI
     358-358: A → AVAQMLS
Isoform 5 (identifier: O95319-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
     359-359: G → GTINS

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 508508CUGBP Elav-like family member 2
PRO_0000295189

Regions

Domain40 – 12384RRM 1
Domain132 – 21281RRM 2
Domain423 – 50179RRM 3
Region1 – 283283Necessary for RNA-binding, TNNT2 exon 5 and NMDA R1 exon 21 inclusion
Region357 – 508152Necessary for RNA-binding, TNNT2 exon 5 and NMDA R1 exon 21 inclusion
Compositional bias284 – 397114Ala-rich

Natural variations

Alternative sequence1 – 2424Missing in isoform 2 and isoform 5.
VSP_026796
Alternative sequence1 – 1818MRCPK…ELLLS → MMVEGRLLVPDRI in isoform 3 and isoform 4.
VSP_026797
Alternative sequence3581A → AVAQMLS in isoform 2 and isoform 4.
VSP_026798
Alternative sequence3581A → AGTINTPRSKRLLLPKDNN in isoform 3.
VSP_026799
Alternative sequence3591G → GTINS in isoform 5.
VSP_026800
Natural variant4381D → H. Ref.1 Ref.3
Corresponds to variant rs1050942 [ dbSNP | Ensembl ].
VAR_052202

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (NAPOR-3) [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: C65F337D462717F2

FASTA50854,285
        10         20         30         40         50         60 
MRCPKSAVTM RNEELLLSNG TANKMNGALD HSDQPDPDAI KMFVGQIPRS WSEKELKELF 

        70         80         90        100        110        120 
EPYGAVYQIN VLRDRSQNPP QSKGCCFVTF YTRKAALEAQ NALHNIKTLP GMHHPIQMKP 

       130        140        150        160        170        180 
ADSEKSNAVE DRKLFIGMVS KKCNENDIRV MFSPFGQIEE CRILRGPDGL SRGCAFVTFS 

       190        200        210        220        230        240 
TRAMAQNAIK AMHQSQTMEG CSSPIVVKFA DTQKDKEQRR LQQQLAQQMQ QLNTATWGNL 

       250        260        270        280        290        300 
TGLGGLTPQY LALLQQATSS SNLGAFSGIQ QMAGMNALQL QNLATLAAAA AAAQTSATST 

       310        320        330        340        350        360 
NANPLSTTSS ALGALTSPVA ASTPNSTAGA AMNSLTSLGT LQGLAGATVG LNNINALAGM 

       370        380        390        400        410        420 
AALNGGLGAT GLTNGTAGTM DALTQAYSGI QQYAAAALPT LYSQSLLQQQ SAAGSQKEGP 

       430        440        450        460        470        480 
EGANLFIYHL PQEFGDQDIL QMFMPFGNVI SAKVFIDKQT NLSKCFGFVS YDNPVSAQAA 

       490        500 
IQAMNGFQIG MKRLKVQLKR SKNDSKPY 

« Hide

Isoform 2 (NAPOR-1) [UniParc].

Checksum: 3A17B1F5F31AC5BD
Show »

FASTA49052,268
Isoform 3 [UniParc].

Checksum: DD6E4F77FE6B4073
Show »

FASTA52155,754
Isoform 4 (NAPOR-2) [UniParc].

Checksum: 4A0DB5E2372193ED
Show »

FASTA50954,365
Isoform 5 [UniParc].

Checksum: CBB835681201C245
Show »

FASTA48852,054

References

« Hide 'large scale' references
[1]"Fluorescent differential display analysis of gene expression in apoptotic neuroblastoma cells."
Choi D.-K., Ito T., Mitsui Y., Sakaki Y.
Gene 223:21-31(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT HIS-438.
Tissue: Brain.
[2]"Developmentally-regulated expression of mNapor encoding an apoptosis-induced ELAV-type RNA binding protein."
Choi D.-K., Ito T., Tsukahara F., Hirai M., Sakaki Y.
Gene 237:135-142(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Brain.
[3]"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 2), TISSUE SPECIFICITY, VARIANT HIS-438.
Tissue: Heart.
[4]"Genomic organization and isoform-specific tissue expression of human NAPOR (CUGBP2) as a candidate gene for familial arrhythmogenic right ventricular dysplasia."
Li D., Bachinski L.L., Roberts R.
Genomics 74:396-401(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
[5]"Mutation screening of the NAPOR gene: a candidate for adult-onset primary open angle glaucoma (GLC1E) on 10p14."
Sarfarazi M., Rezaie T.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
[6]"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: Synovium.
[7]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [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: Brain.
[10]"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: SUBCELLULAR LOCATION, RNA-BINDING.
[11]"Novel role for RNA-binding protein CUGBP2 in mammalian RNA editing. CUGBP2 modulates C to U editing of apolipoprotein B mRNA by interacting with apobec-1 and ACF, the apobec-1 complementation factor."
Anant S., Henderson J.O., Mukhopadhyay D., Navaratnam N., Kennedy S., Min J., Davidson N.O.
J. Biol. Chem. 276:47338-47351(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION.
[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]"Dynamic antagonism between ETR-3 and PTB regulates cell type-specific alternative splicing."
Charlet-B N., Logan P., Singh G., Cooper T.A.
Mol. Cell 9:649-658(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, 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]"ETR-3 and CELF4 protein domains required for RNA binding and splicing activity in vivo."
Singh G., Charlet-B N., Han J., Cooper T.A.
Nucleic Acids Res. 32:1232-1241(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING.
[16]"Identification of putative new splicing targets for ETR-3 using sequences identified by systematic evolution of ligands by exponential enrichment."
Faustino N.A., Cooper T.A.
Mol. Cell. Biol. 25:879-887(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, RNA-BINDING.
[17]"Identification of CELF splicing activation and repression domains in vivo."
Han J., Cooper T.A.
Nucleic Acids Res. 33:2769-2780(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[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]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF090694 mRNA. Translation: AAD13761.1.
AF090693 mRNA. Translation: AAD13760.1.
AF036956 mRNA. Translation: AAD02074.1.
U69546 mRNA. Translation: AAB09040.1.
AF295068 expand/collapse EMBL AC list , AF295063, AF295064, AF295065, AF295066, AF295067 Genomic DNA. Translation: AAK72223.1.
AF295068 expand/collapse EMBL AC list , AF295063, AF295064, AF295065, AF295066, AF295067, AF314199 Genomic DNA. Translation: AAK72224.1.
AF295068 expand/collapse EMBL AC list , AF295063, AF295064, AF295065, AF295066, AF295067 Genomic DNA. Translation: AAK92699.1.
AF432906 mRNA. Translation: AAL27627.1.
AK316354 mRNA. Translation: BAH14725.1.
AL157704, AC026887, AL136320 Genomic DNA. Translation: CAH70230.1.
AL136320, AC026887, AL157704 Genomic DNA. Translation: CAI20169.1.
CH471072 Genomic DNA. Translation: EAW86346.1.
BC036391 mRNA. Translation: AAH36391.1.
CCDSCCDS41488.1. [O95319-2]
CCDS44354.1. [O95319-1]
CCDS44356.1. [O95319-5]
RefSeqNP_001020247.1. NM_001025076.2. [O95319-2]
NP_001020248.1. NM_001025077.2. [O95319-1]
NP_001077060.1. NM_001083591.1. [O95319-5]
NP_006552.3. NM_006561.3.
UniGeneHs.309288.

3D structure databases

ProteinModelPortalO95319.
SMRO95319. Positions 6-211, 388-506.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115902. 8 interactions.
IntActO95319. 5 interactions.
MINTMINT-2868664.
STRING9606.ENSP00000389951.

PTM databases

PhosphoSiteO95319.

2D gel databases

UCD-2DPAGEO95319.

Proteomic databases

MaxQBO95319.
PaxDbO95319.
PRIDEO95319.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315874; ENSP00000315328; ENSG00000048740. [O95319-2]
ENST00000354440; ENSP00000346426; ENSG00000048740. [O95319-2]
ENST00000379261; ENSP00000368563; ENSG00000048740. [O95319-1]
ENST00000399850; ENSP00000382743; ENSG00000048740. [O95319-2]
ENST00000416382; ENSP00000406451; ENSG00000048740. [O95319-1]
ENST00000417956; ENSP00000404834; ENSG00000048740. [O95319-5]
ENST00000427450; ENSP00000388530; ENSG00000048740. [O95319-2]
ENST00000608830; ENSP00000476999; ENSG00000048740. [O95319-5]
GeneID10659.
KEGGhsa:10659.
UCSCuc001iki.4. human. [O95319-1]
uc001ikk.2. human. [O95319-3]
uc001iko.4. human. [O95319-5]
uc001ikp.4. human. [O95319-2]
uc010qbj.1. human. [O95319-4]

Organism-specific databases

CTD10659.
GeneCardsGC10P011049.
HGNCHGNC:2550. CELF2.
HPACAB016395.
HPA035813.
MIM602538. gene.
neXtProtNX_O95319.
PharmGKBPA27046.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251494.
HOVERGENHBG107646.
KOK13207.
OrthoDBEOG7DVDBR.
PhylomeDBO95319.

Gene expression databases

ArrayExpressO95319.
BgeeO95319.
CleanExHS_CUGBP2.
GenevestigatorO95319.

Family and domain databases

Gene3D3.30.70.330. 3 hits.
InterProIPR002343. Hud_Sxl_RNA.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 3 hits.
[Graphical view]
PRINTSPR00961. HUDSXLRNA.
SMARTSM00360. RRM. 3 hits.
[Graphical view]
PROSITEPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCELF2. human.
GeneWikiCUGBP2.
GenomeRNAi10659.
NextBio40529.
PROO95319.
SOURCESearch...

Entry information

Entry nameCELF2_HUMAN
AccessionPrimary (citable) accession number: O95319
Secondary accession number(s): B7ZAN9 expand/collapse secondary AC list , Q7KYU4, Q8N499, Q92950, Q96NW9, Q96RQ5, Q96RQ6, Q9UL67
Entry history
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 108 of the entry and version 1 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM