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O95319

- CELF2_HUMAN

UniProt

O95319 - CELF2_HUMAN

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Protein

CUGBP Elav-like family member 2

Gene

CELF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA binding Source: ProtInc

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
  2. regulation of heart contraction Source: ProtInc
  3. RNA processing Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
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 namesi
Name:CELF2
Synonyms:BRUNOL3, CUGBP2, ETR3, NAPOR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:2550. CELF2.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27046.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508CUGBP Elav-like family member 2PRO_0000295189Add
BLAST

Proteomic databases

MaxQBiO95319.
PaxDbiO95319.
PRIDEiO95319.

2D gel databases

UCD-2DPAGEO95319.

PTM databases

PhosphoSiteiO95319.

Expressioni

Tissue specificityi

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.5 Publications

Developmental stagei

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.2 Publications

Gene expression databases

BgeeiO95319.
CleanExiHS_CUGBP2.
ExpressionAtlasiO95319. baseline and differential.
GenevestigatoriO95319.

Organism-specific databases

HPAiCAB016395.
HPA035813.

Interactioni

Subunit structurei

Interacts with A1CF.By similarity

Protein-protein interaction databases

BioGridi115902. 8 interactions.
IntActiO95319. 5 interactions.
MINTiMINT-2868664.
STRINGi9606.ENSP00000389951.

Structurei

Secondary structure

1
508
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 454Combined sources
Helixi53 – 608Combined sources
Helixi61 – 633Combined sources
Beta strandi66 – 749Combined sources
Beta strandi76 – 794Combined sources
Beta strandi81 – 9212Combined sources
Helixi93 – 10311Combined sources
Turni104 – 1063Combined sources
Beta strandi117 – 1204Combined sources
Helixi122 – 1243Combined sources
Helixi129 – 1313Combined sources
Beta strandi133 – 1386Combined sources
Helixi145 – 1528Combined sources
Helixi153 – 1553Combined sources
Beta strandi158 – 1658Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi171 – 18212Combined sources
Helixi183 – 19210Combined sources
Beta strandi206 – 2094Combined sources
Beta strandi424 – 4296Combined sources
Helixi436 – 4438Combined sources
Helixi444 – 4463Combined sources
Beta strandi449 – 4568Combined sources
Turni458 – 4603Combined sources
Beta strandi463 – 47311Combined sources
Helixi474 – 48411Combined sources
Beta strandi495 – 4984Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4LJMX-ray3.00A/B416-508[»]
4LMZX-ray2.78A36-211[»]
ProteinModelPortaliO95319.
SMRiO95319. Positions 6-211, 388-499.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini40 – 12384RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini132 – 21281RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini423 – 50179RRM 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 283283Necessary for RNA-binding, TNNT2 exon 5 and NMDA R1 exon 21 inclusionAdd
BLAST
Regioni357 – 508152Necessary for RNA-binding, TNNT2 exon 5 and NMDA R1 exon 21 inclusionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi284 – 397114Ala-richAdd
BLAST

Sequence similaritiesi

Belongs to the CELF/BRUNOL family.Curated
Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG251494.
GeneTreeiENSGT00560000076837.
HOVERGENiHBG107646.
InParanoidiO95319.
KOiK13207.
OrthoDBiEOG7DVDBR.
PhylomeDBiO95319.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR002343. Hud_Sxl_RNA.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 3 hits.
[Graphical view]
PRINTSiPR00961. HUDSXLRNA.
SMARTiSM00360. RRM. 3 hits.
[Graphical view]
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95319-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MRCPKSAVTM RNEELLLSNG TANKMNGALD HSDQPDPDAI KMFVGQIPRS
60 70 80 90 100
WSEKELKELF EPYGAVYQIN VLRDRSQNPP QSKGCCFVTF YTRKAALEAQ
110 120 130 140 150
NALHNIKTLP GMHHPIQMKP ADSEKSNAVE DRKLFIGMVS KKCNENDIRV
160 170 180 190 200
MFSPFGQIEE CRILRGPDGL SRGCAFVTFS TRAMAQNAIK AMHQSQTMEG
210 220 230 240 250
CSSPIVVKFA DTQKDKEQRR LQQQLAQQMQ QLNTATWGNL TGLGGLTPQY
260 270 280 290 300
LALLQQATSS SNLGAFSGIQ QMAGMNALQL QNLATLAAAA AAAQTSATST
310 320 330 340 350
NANPLSTTSS ALGALTSPVA ASTPNSTAGA AMNSLTSLGT LQGLAGATVG
360 370 380 390 400
LNNINALAGM AALNGGLGAT GLTNGTAGTM DALTQAYSGI QQYAAAALPT
410 420 430 440 450
LYSQSLLQQQ SAAGSQKEGP EGANLFIYHL PQEFGDQDIL QMFMPFGNVI
460 470 480 490 500
SAKVFIDKQT NLSKCFGFVS YDNPVSAQAA IQAMNGFQIG MKRLKVQLKR

SKNDSKPY
Length:508
Mass (Da):54,285
Last modified:May 1, 1999 - v1
Checksum:iC65F337D462717F2
GO
Isoform 2 (identifier: O95319-2) [UniParc]FASTAAdd to Basket

Also known as: NAPOR-1

The sequence of this isoform differs from the canonical sequence as follows:
     1-24: Missing.
     358-358: A → AVAQMLS

Show »
Length:490
Mass (Da):52,268
Checksum:i3A17B1F5F31AC5BD
GO
Isoform 3 (identifier: O95319-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MRCPKSAVTMRNEELLLS → MMVEGRLLVPDRI
     358-358: A → AGTINTPRSKRLLLPKDNN

Show »
Length:521
Mass (Da):55,754
Checksum:iDD6E4F77FE6B4073
GO
Isoform 4 (identifier: O95319-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:509
Mass (Da):54,365
Checksum:i4A0DB5E2372193ED
GO
Isoform 5 (identifier: O95319-5) [UniParc]FASTAAdd to Basket

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

Show »
Length:488
Mass (Da):52,054
Checksum:iCBB835681201C245
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti438 – 4381D → H.2 Publications
Corresponds to variant rs1050942 [ dbSNP | Ensembl ].
VAR_052202

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2424Missing in isoform 2 and isoform 5. 4 PublicationsVSP_026796Add
BLAST
Alternative sequencei1 – 1818MRCPK…ELLLS → MMVEGRLLVPDRI in isoform 3 and isoform 4. 2 PublicationsVSP_026797Add
BLAST
Alternative sequencei358 – 3581A → AVAQMLS in isoform 2 and isoform 4. 3 PublicationsVSP_026798
Alternative sequencei358 – 3581A → AGTINTPRSKRLLLPKDNN in isoform 3. 1 PublicationVSP_026799
Alternative sequencei359 – 3591G → GTINS in isoform 5. 2 PublicationsVSP_026800

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41488.1. [O95319-2]
CCDS44354.1. [O95319-1]
CCDS44356.1. [O95319-5]
RefSeqiNP_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.
UniGeneiHs.309288.

Genome annotation databases

EnsembliENST00000399850; ENSP00000382743; ENSG00000048740. [O95319-2]
ENST00000416382; ENSP00000406451; ENSG00000048740. [O95319-1]
ENST00000417956; ENSP00000404834; ENSG00000048740. [O95319-2]
ENST00000608830; ENSP00000476999; ENSG00000048740. [O95319-5]
GeneIDi10659.
KEGGihsa:10659.
UCSCiuc001iki.4. human. [O95319-1]
uc001ikk.2. human. [O95319-3]
uc001iko.4. human. [O95319-5]
uc001ikp.4. human. [O95319-2]
uc010qbj.1. human. [O95319-4]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS41488.1. [O95319-2 ]
CCDS44354.1. [O95319-1 ]
CCDS44356.1. [O95319-5 ]
RefSeqi NP_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.
UniGenei Hs.309288.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4LJM X-ray 3.00 A/B 416-508 [» ]
4LMZ X-ray 2.78 A 36-211 [» ]
ProteinModelPortali O95319.
SMRi O95319. Positions 6-211, 388-499.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115902. 8 interactions.
IntActi O95319. 5 interactions.
MINTi MINT-2868664.
STRINGi 9606.ENSP00000389951.

PTM databases

PhosphoSitei O95319.

2D gel databases

UCD-2DPAGE O95319.

Proteomic databases

MaxQBi O95319.
PaxDbi O95319.
PRIDEi O95319.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000399850 ; ENSP00000382743 ; ENSG00000048740 . [O95319-2 ]
ENST00000416382 ; ENSP00000406451 ; ENSG00000048740 . [O95319-1 ]
ENST00000417956 ; ENSP00000404834 ; ENSG00000048740 . [O95319-2 ]
ENST00000608830 ; ENSP00000476999 ; ENSG00000048740 . [O95319-5 ]
GeneIDi 10659.
KEGGi hsa:10659.
UCSCi uc001iki.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

CTDi 10659.
GeneCardsi GC10P011049.
HGNCi HGNC:2550. CELF2.
HPAi CAB016395.
HPA035813.
MIMi 602538. gene.
neXtProti NX_O95319.
PharmGKBi PA27046.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG251494.
GeneTreei ENSGT00560000076837.
HOVERGENi HBG107646.
InParanoidi O95319.
KOi K13207.
OrthoDBi EOG7DVDBR.
PhylomeDBi O95319.

Miscellaneous databases

ChiTaRSi CELF2. human.
GeneWikii CUGBP2.
GenomeRNAii 10659.
NextBioi 40529.
PROi O95319.
SOURCEi Search...

Gene expression databases

Bgeei O95319.
CleanExi HS_CUGBP2.
ExpressionAtlasi O95319. baseline and differential.
Genevestigatori O95319.

Family and domain databases

Gene3Di 3.30.70.330. 3 hits.
InterProi IPR002343. Hud_Sxl_RNA.
IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00076. RRM_1. 3 hits.
[Graphical view ]
PRINTSi PR00961. HUDSXLRNA.
SMARTi SM00360. RRM. 3 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCELF2_HUMAN
AccessioniPrimary (citable) accession number: O95319
Secondary accession number(s): B7ZAN9
, Q7KYU4, Q8N499, Q92950, Q96NW9, Q96RQ5, Q96RQ6, Q9UL67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 10, 2007
Last sequence update: May 1, 1999
Last modified: November 26, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3