O95319 (CELF2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	508 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 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 process	mRNA processing
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
Molecular function	Repressor
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA 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_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Traceable author statement PubMed 9887331. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 508	508	CUGBP Elav-like family member 2		PRO_0000295189
Regions
	Domain	40 – 123	84	RRM 1
	Domain	132 – 212	81	RRM 2
	Domain	423 – 501	79	RRM 3
	Region	1 – 283	283	Necessary for RNA-binding, TNNT2 exon 5 and NMDA R1 exon 21 inclusion
	Region	357 – 508	152	Necessary for RNA-binding, TNNT2 exon 5 and NMDA R1 exon 21 inclusion
	Compositional bias	284 – 397	114	Ala-rich
Natural variations
	Alternative sequence	1 – 24	24	Missing in isoform 2 and isoform 5.		VSP_026796
	Alternative sequence	1 – 18	18	MRCPK…ELLLS → MMVEGRLLVPDRI in isoform 3 and isoform 4.		VSP_026797
	Alternative sequence	358	1	A → AVAQMLS in isoform 2 and isoform 4.		VSP_026798
	Alternative sequence	358	1	A → AGTINTPRSKRLLLPKDNN in isoform 3.		VSP_026799
	Alternative sequence	359	1	G → GTINS in isoform 5.		VSP_026800
	Natural variant	438	1	D → H. Ref.1 Ref.3 Corresponds to variant rs1050942 [ dbSNP | Ensembl ].		VAR_052202

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (NAPOR-3) [UniParc]. Last modified May 1, 1999. Version 1. Checksum: C65F337D462717F2	FASTA	508	54,285
	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
	Isoform 2 (NAPOR-1) [UniParc]. Checksum: 3A17B1F5F31AC5BD	FASTA	490	52,268
	10 20 30 40 50 60 MNGALDHSDQ PDPDAIKMFV GQIPRSWSEK ELKELFEPYG AVYQINVLRD RSQNPPQSKG 70 80 90 100 110 120 CCFVTFYTRK AALEAQNALH NIKTLPGMHH PIQMKPADSE KSNAVEDRKL FIGMVSKKCN 130 140 150 160 170 180 ENDIRVMFSP FGQIEECRIL RGPDGLSRGC AFVTFSTRAM AQNAIKAMHQ SQTMEGCSSP 190 200 210 220 230 240 IVVKFADTQK DKEQRRLQQQ LAQQMQQLNT ATWGNLTGLG GLTPQYLALL QQATSSSNLG 250 260 270 280 290 300 AFSGIQQMAG MNALQLQNLA TLAAAAAAAQ TSATSTNANP LSTTSSALGA LTSPVAASTP 310 320 330 340 350 360 NSTAGAAMNS LTSLGTLQGL AGATVGLNNI NALAVAQMLS GMAALNGGLG ATGLTNGTAG 370 380 390 400 410 420 TMDALTQAYS GIQQYAAAAL PTLYSQSLLQ QQSAAGSQKE GPEGANLFIY HLPQEFGDQD 430 440 450 460 470 480 ILQMFMPFGN VISAKVFIDK QTNLSKCFGF VSYDNPVSAQ AAIQAMNGFQ IGMKRLKVQL 490 KRSKNDSKPY
	Isoform 3 [UniParc]. Checksum: DD6E4F77FE6B4073	FASTA	521	55,754
	10 20 30 40 50 60 MMVEGRLLVP DRINGTANKM NGALDHSDQP DPDAIKMFVG QIPRSWSEKE LKELFEPYGA 70 80 90 100 110 120 VYQINVLRDR SQNPPQSKGC CFVTFYTRKA ALEAQNALHN IKTLPGMHHP IQMKPADSEK 130 140 150 160 170 180 SNAVEDRKLF IGMVSKKCNE NDIRVMFSPF GQIEECRILR GPDGLSRGCA FVTFSTRAMA 190 200 210 220 230 240 QNAIKAMHQS QTMEGCSSPI VVKFADTQKD KEQRRLQQQL AQQMQQLNTA TWGNLTGLGG 250 260 270 280 290 300 LTPQYLALLQ QATSSSNLGA FSGIQQMAGM NALQLQNLAT LAAAAAAAQT SATSTNANPL 310 320 330 340 350 360 STTSSALGAL TSPVAASTPN STAGAAMNSL TSLGTLQGLA GATVGLNNIN ALAGTINTPR 370 380 390 400 410 420 SKRLLLPKDN NGMAALNGGL GATGLTNGTA GTMDALTQAY SGIQQYAAAA LPTLYSQSLL 430 440 450 460 470 480 QQQSAAGSQK EGPEGANLFI YHLPQEFGDQ DILQMFMPFG NVISAKVFID KQTNLSKCFG 490 500 510 520 FVSYDNPVSA QAAIQAMNGF QIGMKRLKVQ LKRSKNDSKP Y
	Isoform 4 (NAPOR-2) [UniParc]. Checksum: 4A0DB5E2372193ED	FASTA	509	54,365
	10 20 30 40 50 60 MMVEGRLLVP DRINGTANKM NGALDHSDQP DPDAIKMFVG QIPRSWSEKE LKELFEPYGA 70 80 90 100 110 120 VYQINVLRDR SQNPPQSKGC CFVTFYTRKA ALEAQNALHN IKTLPGMHHP IQMKPADSEK 130 140 150 160 170 180 SNAVEDRKLF IGMVSKKCNE NDIRVMFSPF GQIEECRILR GPDGLSRGCA FVTFSTRAMA 190 200 210 220 230 240 QNAIKAMHQS QTMEGCSSPI VVKFADTQKD KEQRRLQQQL AQQMQQLNTA TWGNLTGLGG 250 260 270 280 290 300 LTPQYLALLQ QATSSSNLGA FSGIQQMAGM NALQLQNLAT LAAAAAAAQT SATSTNANPL 310 320 330 340 350 360 STTSSALGAL TSPVAASTPN STAGAAMNSL TSLGTLQGLA GATVGLNNIN ALAVAQMLSG 370 380 390 400 410 420 MAALNGGLGA TGLTNGTAGT MDALTQAYSG IQQYAAAALP TLYSQSLLQQ QSAAGSQKEG 430 440 450 460 470 480 PEGANLFIYH LPQEFGDQDI LQMFMPFGNV ISAKVFIDKQ TNLSKCFGFV SYDNPVSAQA 490 500 AIQAMNGFQI GMKRLKVQLK RSKNDSKPY
	Isoform 5 [UniParc]. Checksum: CBB835681201C245	FASTA	488	52,054
	10 20 30 40 50 60 MNGALDHSDQ PDPDAIKMFV GQIPRSWSEK ELKELFEPYG AVYQINVLRD RSQNPPQSKG 70 80 90 100 110 120 CCFVTFYTRK AALEAQNALH NIKTLPGMHH PIQMKPADSE KSNAVEDRKL FIGMVSKKCN 130 140 150 160 170 180 ENDIRVMFSP FGQIEECRIL RGPDGLSRGC AFVTFSTRAM AQNAIKAMHQ SQTMEGCSSP 190 200 210 220 230 240 IVVKFADTQK DKEQRRLQQQ LAQQMQQLNT ATWGNLTGLG GLTPQYLALL QQATSSSNLG 250 260 270 280 290 300 AFSGIQQMAG MNALQLQNLA TLAAAAAAAQ TSATSTNANP LSTTSSALGA LTSPVAASTP 310 320 330 340 350 360 NSTAGAAMNS LTSLGTLQGL AGATVGLNNI NALAGTINSM AALNGGLGAT GLTNGTAGTM 370 380 390 400 410 420 DALTQAYSGI QQYAAAALPT LYSQSLLQQQ SAAGSQKEGP EGANLFIYHL PQEFGDQDIL 430 440 450 460 470 480 QMFMPFGNVI SAKVFIDKQT NLSKCFGFVS YDNPVSAQAA IQAMNGFQIG MKRLKVQLKR SKNDSKPY

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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 , AF295063, AF295064, AF295065, AF295066, AF295067 Genomic DNA. Translation: AAK72223.1. AF295068 , AF295063, AF295064, AF295065, AF295066, AF295067, AF314199 Genomic DNA. Translation: AAK72224.1. AF295068 , 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.
IPI	IPI00410277. IPI00607544. IPI00845479. IPI00845480. IPI00853320.
RefSeq	NP_001020247.1. NM_001025076.2. NP_001020248.1. NM_001025077.2. NP_001077060.1. NM_001083591.1. NP_006552.3. NM_006561.3.
UniGene	Hs.309288.
3D structure databases
HSSP	HSSP built from PDB template 2CPZ based on UniProtKB Q92879.
ProteinModelPortal	O95319.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95319. 4 interactions.
MINT	MINT-2868664.
STRING	9606.ENSP00000389951.
PTM databases
PhosphoSite	O95319.
2D gel databases
UCD-2DPAGE	O95319.
Proteomic databases
PaxDb	O95319.
PRIDE	O95319.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000315874; ENSP00000315328; ENSG00000048740. ENST00000354440; ENSP00000346426; ENSG00000048740. ENST00000379261; ENSP00000368563; ENSG00000048740. ENST00000399850; ENSP00000382743; ENSG00000048740. ENST00000416382; ENSP00000406451; ENSG00000048740. ENST00000417956; ENSP00000404834; ENSG00000048740. ENST00000427450; ENSP00000388530; ENSG00000048740.
GeneID	10659.
KEGG	hsa:10659.
UCSC	uc001iki.4. human. uc001ikk.2. human. uc001iko.4. human. uc001ikp.4. human. uc010qbj.1. human.
Organism-specific databases
CTD	10659.
GeneCards	GC10P011049.
HGNC	HGNC:2550. CELF2.
HPA	CAB016395. HPA035813.
MIM	602538. gene.
neXtProt	NX_O95319.
PharmGKB	PA27046.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG251494.
HOVERGEN	HBG107646.
KO	K13207.
Gene expression databases
ArrayExpress	O95319.
Bgee	O95319.
CleanEx	HS_CUGBP2.
Genevestigator	O95319.
Family and domain databases
Gene3D	3.30.70.330. 3 hits.
InterPro	IPR002343. Hud_Sxl_RNA. IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. [Graphical view]
Pfam	PF00076. RRM_1. 3 hits. [Graphical view]
PRINTS	PR00961. HUDSXLRNA.
SMART	SM00360. RRM. 3 hits. [Graphical view]
PROSITE	PS50102. RRM. 3 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CELF2. human.
GenomeRNAi	10659.
NextBio	40529.
SOURCE	Search...

Entry information

Entry name

CELF2_HUMAN

Accession

Primary (citable) accession number: O95319
Secondary accession number(s): B7ZAN9 , 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:	May 1, 2013
This is version 98 of the entry and version 1 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.