Protein:CELF2 |
Protein Summary |
 Gene summary |
| Gene name: CELF2 | ASpdb.0 ID: 10659 | Gene | Gene symbol | CELF2 | Gene ID | 10659 |
| Gene name | CUGBP Elav-like family member 2 |
| Synonyms | BRUNOL3|CELF-2|CUG-BP2|CUGBP2|DEE97|ETR-3|ETR3|NAPOR |
| Cytomap | 10p14 |
| Type of gene | protein-coding |
| Description | CUGBP Elav-like family member 2CUG triplet repeat RNA-binding protein 2CUG-BP- and ETR-3-like factor 2ELAV-type RNA-binding protein 3KDM2B/CELF2 fusionRNA-binding protein BRUNOL-3bruno-like protein 3neuroblastoma apoptosis-related RNA-binding prote |
| Modification date | 20240403 |
| UniProtAcc | O95319 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | CELF2 | GO:0005634 | nucleus | 11158314 |
| Gene | CELF2 | GO:0005654 | nucleoplasm | - |
| Gene | CELF2 | GO:0006376 | mRNA splice site recognition | 11158314 |
| Gene | CELF2 | GO:0036002 | pre-mRNA binding | 11158314 |
| Gene | CELF2 | GO:0043231 | intracellular membrane-bounded organelle | - |
| Gene | CELF2 | GO:0090543 | Flemming body | - |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| O95319-1 | O95319-1_4lmz_A.pdb | 4LMZ | X-ray | 2.78 | A | 36 | 211 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| O95319 | CELF2 | O95319-1 | O95319-2 | 508 | 490 | 1 | 24 | Deletion | none | none | 0 | 0 |
| O95319 | CELF2 | O95319-1 | O95319-2 | 508 | 490 | 358 | 358 | Substitution | A | AVAQMLS | 334 | 340 |
| O95319 | CELF2 | O95319-1 | O95319-3 | 508 | 521 | 1 | 18 | Substitution | MRCPKSAVTMRNEELLLS | MMVEGRLLVPDRI | 1 | 13 |
| O95319 | CELF2 | O95319-1 | O95319-3 | 508 | 521 | 358 | 358 | Substitution | A | AGTINTPRSKRLLLPKDNN | 353 | 371 |
| O95319 | CELF2 | O95319-1 | O95319-4 | 508 | 509 | 1 | 18 | Substitution | MRCPKSAVTMRNEELLLS | MMVEGRLLVPDRI | 1 | 13 |
| O95319 | CELF2 | O95319-1 | O95319-4 | 508 | 509 | 358 | 358 | Substitution | A | AVAQMLS | 353 | 359 |
| O95319 | CELF2 | O95319-1 | O95319-5 | 508 | 488 | 1 | 24 | Deletion | none | none | 0 | 0 |
| O95319 | CELF2 | O95319-1 | O95319-5 | 508 | 488 | 359 | 359 | Substitution | G | GTINS | 335 | 339 |
| Multiple sequence alignment of our canonical and alternatively spliced CELF2 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of CELF2 |
| UniProt-id | ENSG | ENST | ENSP |
| O95319-1 | ENSG00000048740.19 | ENST00000416382.6 | ENSP00000406451.2 |
| O95319-1 | ENSG00000048740.19 | ENST00000631460.1 | ENSP00000488582.1 |
| O95319-2 | ENSG00000048740.19 | ENST00000399850.7 | ENSP00000382743.3 |
| O95319-2 | ENSG00000048740.19 | ENST00000417956.6 | ENSP00000404834.3 |
| O95319-2 | ENSG00000048740.19 | ENST00000632728.1 | ENSP00000487802.1 |
| O95319-2 | ENSG00000048740.19 | ENST00000638035.1 | ENSP00000490401.1 |
| O95319-5 | ENSG00000048740.19 | ENST00000608830.5 | ENSP00000476999.1 |
| UniProt-id | NM ID | NP ID |
| O95319-1 | NM_001025077.2 | NP_001020248.1 |
| O95319-1 | NM_001326332.1 | NP_001313261.1 |
| O95319-2 | NM_001025076.2 | NP_001020247.1 |
| O95319-2 | NM_001326318.1 | NP_001313247.1 |
| O95319-2 | NM_001326320.1 | NP_001313249.1 |
| O95319-2 | NM_001326324.1 | NP_001313253.1 |
| O95319-2 | NM_001326328.1 | NP_001313257.1 |
| O95319-2 | NM_001326330.1 | NP_001313259.1 |
| O95319-2 | NM_001326334.1 | NP_001313263.1 |
| O95319-2 | NM_001326345.1 | NP_001313274.1 |
| O95319-2 | NM_001326349.1 | NP_001313278.1 |
| O95319-5 | NM_001083591.1 | NP_001077060.1 |
| Amino acid sequences of our canonical and alternatively spliced CELF2 |
| accession_id | Protein sequence |
| O95319-1 | MRCPKSAVTMRNEELLLSNGTANKMNGALDHSDQPDPDAIKMFVGQIPRSWSEKELKELFEPYGAVYQINVLRDRSQNPPQSKGCCFVTF YTRKAALEAQNALHNIKTLPGMHHPIQMKPADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFS TRAMAQNAIKAMHQSQTMEGCSSPIVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNLTGLGGLTPQYLALLQQATSSSNLGAFSGIQ QMAGMNALQLQNLATLAAAAAAAQTSATSTNANPLSTTSSALGALTSPVAASTPNSTAGAAMNSLTSLGTLQGLAGATVGLNNINALAGM AALNGGLGATGLTNGTAGTMDALTQAYSGIQQYAAAALPTLYSQSLLQQQSAAGSQKEGPEGANLFIYHLPQEFGDQDILQMFMPFGNVI |
| O95319-2 | MNGALDHSDQPDPDAIKMFVGQIPRSWSEKELKELFEPYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNIKTLPGMHH PIQMKPADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFSTRAMAQNAIKAMHQSQTMEGCSSP IVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNLTGLGGLTPQYLALLQQATSSSNLGAFSGIQQMAGMNALQLQNLATLAAAAAAAQ TSATSTNANPLSTTSSALGALTSPVAASTPNSTAGAAMNSLTSLGTLQGLAGATVGLNNINALAVAQMLSGMAALNGGLGATGLTNGTAG TMDALTQAYSGIQQYAAAALPTLYSQSLLQQQSAAGSQKEGPEGANLFIYHLPQEFGDQDILQMFMPFGNVISAKVFIDKQTNLSKCFGF |
| O95319-3 | MMVEGRLLVPDRINGTANKMNGALDHSDQPDPDAIKMFVGQIPRSWSEKELKELFEPYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKA ALEAQNALHNIKTLPGMHHPIQMKPADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFSTRAMA QNAIKAMHQSQTMEGCSSPIVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNLTGLGGLTPQYLALLQQATSSSNLGAFSGIQQMAGM NALQLQNLATLAAAAAAAQTSATSTNANPLSTTSSALGALTSPVAASTPNSTAGAAMNSLTSLGTLQGLAGATVGLNNINALAGTINTPR SKRLLLPKDNNGMAALNGGLGATGLTNGTAGTMDALTQAYSGIQQYAAAALPTLYSQSLLQQQSAAGSQKEGPEGANLFIYHLPQEFGDQ |
| O95319-4 | MMVEGRLLVPDRINGTANKMNGALDHSDQPDPDAIKMFVGQIPRSWSEKELKELFEPYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKA ALEAQNALHNIKTLPGMHHPIQMKPADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFSTRAMA QNAIKAMHQSQTMEGCSSPIVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNLTGLGGLTPQYLALLQQATSSSNLGAFSGIQQMAGM NALQLQNLATLAAAAAAAQTSATSTNANPLSTTSSALGALTSPVAASTPNSTAGAAMNSLTSLGTLQGLAGATVGLNNINALAVAQMLSG MAALNGGLGATGLTNGTAGTMDALTQAYSGIQQYAAAALPTLYSQSLLQQQSAAGSQKEGPEGANLFIYHLPQEFGDQDILQMFMPFGNV |
| O95319-5 | MNGALDHSDQPDPDAIKMFVGQIPRSWSEKELKELFEPYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNIKTLPGMHH PIQMKPADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFSTRAMAQNAIKAMHQSQTMEGCSSP IVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNLTGLGGLTPQYLALLQQATSSSNLGAFSGIQQMAGMNALQLQNLATLAAAAAAAQ TSATSTNANPLSTTSSALGALTSPVAASTPNSTAGAAMNSLTSLGTLQGLAGATVGLNNINALAGTINSMAALNGGLGATGLTNGTAGTM DALTQAYSGIQQYAAAALPTLYSQSLLQQQSAAGSQKEGPEGANLFIYHLPQEFGDQDILQMFMPFGNVISAKVFIDKQTNLSKCFGFVS |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| CELF2 (go to UniProt):O95319 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| O95319 | Region | 1 | 283 | Note=Necessary for RNA-binding%2C TNNT2 exon 5 and NMDA R1 exon 21 inclusion | Type=Deletion;Start=1;End=24 |
| O95319 | Region | 1 | 283 | Note=Necessary for RNA-binding%2C TNNT2 exon 5 and NMDA R1 exon 21 inclusion | Type=Substitution;Start=1;End=18 |
| O95319 | Region | 1 | 283 | Note=Necessary for RNA-binding%2C TNNT2 exon 5 and NMDA R1 exon 21 inclusion | Type=Substitution;Start=1;End=18 |
| O95319 | Region | 1 | 283 | Note=Necessary for RNA-binding%2C TNNT2 exon 5 and NMDA R1 exon 21 inclusion | Type=Deletion;Start=1;End=24 |
| O95319 | Region | 357 | 508 | Note=Necessary for RNA-binding%2C TNNT2 exon 5 and NMDA R1 exon 21 inclusion | Type=Substitution;Start=358;End=358 |
| O95319 | Region | 357 | 508 | Note=Necessary for RNA-binding%2C TNNT2 exon 5 and NMDA R1 exon 21 inclusion | Type=Substitution;Start=358;End=358 |
| O95319 | Region | 357 | 508 | Note=Necessary for RNA-binding%2C TNNT2 exon 5 and NMDA R1 exon 21 inclusion | Type=Substitution;Start=358;End=358 |
| O95319 | Region | 357 | 508 | Note=Necessary for RNA-binding%2C TNNT2 exon 5 and NMDA R1 exon 21 inclusion | Type=Substitution;Start=359;End=359 |
Gene Isoform Structures and Expression Levels for CELF2 |
| Gene structures of our canonical and alternative spliced genes of CELF2 * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of O95319-1 |
| 3D view using mol* of O95319-2 |
| 3D view using mol* of O95319-3 |
| 3D view using mol* of O95319-4 |
| 3D view using mol* of O95319-5 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of O95319-1 |
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| pLDDT distribution across the protein length of O95319-2 |
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| pLDDT distribution across the protein length of O95319-3 |
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| pLDDT distribution across the protein length of O95319-4 |
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| pLDDT distribution across the protein length of O95319-5 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of O95319-1 |
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| Ramachandran plot of O95319-2 |
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| Ramachandran plot of O95319-3 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| O95319-1 | 0.613 | 32 | 0.466 | 65.513 | 0.689 | 0.595 | 0.818 | 0.078 | 1.296 | 0.061 | 0.421 | 418,421,422,423,424,498,499,500,501,502
|
| O95319-2 | 0.726 | 57 | 0.704 | 117.992 | 0.741 | 0.556 | 0.733 | 0.106 | 1.04 | 0.102 | 0.502 | 403,404,406,408,410,479,480,481,482,483,484,486
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| O95319-3 | 0.718 | 33 | 0.702 | 164.983 | 0.802 | 0.64 | 0.706 | 0.389 | 0.683 | 0.569 | 0.927 | 422,423,424,425,427,428,429,430,449,450,453,462,46 3,464,465,466,481 |
| O95319-4 | 0.66 | 16 | 0.395 | 54.88 | 0.652 | 0.847 | 1.238 | 0 | 1.501 | 0 | 0.531 | 417,418,419,425,452,454,469,471,500
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| O95319-5 | 0.6 | 26 | 0.533 | 110.103 | 0.743 | 0.617 | 0.811 | 0.246 | 0.972 | 0.253 | 1.621 | 106,109,111,152,185,186,187,188,189
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Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of O95319-1_O95319-1_4lmz_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of O95319-1_4lmz_A_O95319-2.pdb |
| 3D view using mol* of O95319-1_4lmz_A_O95319-3.pdb |
| 3D view using mol* of O95319-1_4lmz_A_O95319-4.pdb |
| 3D view using mol* of O95319-1_4lmz_A_O95319-5.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of O95319-1_O95319-2.pdb |
| 3D view using mol* of O95319-1_O95319-3.pdb |
| 3D view using mol* of O95319-1_O95319-4.pdb |
| 3D view using mol* of O95319-1_O95319-5.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/O95319-1_vs_O95319-2.png |
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| ./stats/secondary_structure/figure/O95319-1_vs_O95319-3.png |
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| ./stats/secondary_structure/figure/O95319-1_vs_O95319-4.png |
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| ./stats/secondary_structure/figure/O95319-1_vs_O95319-5.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/O95319-1_vs_O95319-2.png |
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| ./stats/relative_asa/O95319-1_vs_O95319-3.png |
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| ./stats/relative_asa/O95319-1_vs_O95319-4.png |
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| ./stats/relative_asa/O95319-1_vs_O95319-5.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to CELF2 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to CELF2 |
| Previous studies relating to the alternative splicing of CELF2 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| CELF2 | 9887331 | Cardiac elav-type RNA-binding protein (ETR-3) binds to RNA CUG repeats expanded in myotonic dystrophy. | Myotonic dystrophy (DM) is a neuromuscular disorder associated with CTG triplet repeat expansion in the myotonin protein kinase gene ( DMPK ). We previously proposed a hypothesis suggesting that the expanded CUG repeats sequester specific RNA-binding proteins and that such a sequestration results in abnormal RNA processing of several RNAs containing CUG repeats in multiple tissues affected in patients with DM. One of the members of the CUG-binding proteins, CUG-BP, has been identified previously. Here we describe the second member of this family, elav -type ribonucleoprotein (ETR-3), which is highly expressed in heart and is able to interact with CUG repeats. Screening of a mouse liver cDNA library with a CUG-BP probe identified two mETR-3 cDNAs. Two additional cDNAs from mouse heart were amplified by RT-PCR. These cDNAs differ by several insertions/deletions and might be generated via alternative splicing. Mouse ETR-3 has a mol. wt of 50 kDa and displays a high level of homology to CUG-BP protein. The organization of the RNA-binding domains (RBDs) within the ETR-3 molecule is similar to one within CUG-BP. A study of mETR-3 RNA-binding activity showed that the mETR-3 binds to (CUG)8repeats. Sequence analysis of mETR-3 indicates the presence of several CUG repeats within the mETR-3 mRNA. Both CUG-BP and mETR-3 bind to mETR-3 mRNA via CUG repeats, suggesting the possible involvement of CUG-BP-like proteins in the regulation of mETR-3 processing. Analysis of the tissue distribution of ETR-3 showed that in human cells, ETR-3 mRNA is highly expressed in heart, but is undetectable in other tissues examined. Our results suggest the existence of a family of proteins that bind to CUG repeats and might be affected in DM by expansion of CUG repeats. | D009223 | Myotonic Dystrophy |
Clinically important variants in CELF2 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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