Protein:ETV1 |
Protein Summary |
 Gene summary |
| Gene name: ETV1 | ASpdb.0 ID: 2115 | Gene | Gene symbol | ETV1 | Gene ID | 2115 |
| Gene name | ETS variant transcription factor 1 |
| Synonyms | ER81 |
| Cytomap | 7p21.2 |
| Type of gene | protein-coding |
| Description | ETS translocation variant 1ets variant gene 1ets-related protein 81 |
| Modification date | 20240403 |
| UniProtAcc | P50549 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | ETV1 | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding | 12750007 |
| Gene | ETV1 | GO:0001228 | DNA-binding transcription activator activity, RNA polymerase II-specific | 12750007 |
| Gene | ETV1 | GO:0045944 | positive regulation of transcription by RNA polymerase II | 12750007 |
| Gene | ETV1 | GO:1990837 | sequence-specific double-stranded DNA binding | 28473536 |
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 |
| P50549-1 | P50549-1_5ils_A.pdb | 5ILS | X-ray | 1.4 | A | 334 | 434 |
| 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 |
| P50549 | ETV1 | P50549-1 | P50549-2 | 477 | 459 | 61 | 79 | Substitution | AQVPDNDEQFVPDYQAESL | V | 61 | 61 |
| P50549 | ETV1 | P50549-1 | P50549-3 | 477 | 454 | 268 | 290 | Deletion | none | none | 267 | 267 |
| P50549 | ETV1 | P50549-1 | P50549-4 | 477 | 374 | 1 | 60 | Substitution | MDGFYDQQVPYMVTNSQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAE | MLQDLSASVFFPPCSQHRTL | 1 | 20 |
| P50549 | ETV1 | P50549-1 | P50549-4 | 477 | 374 | 122 | 184 | Deletion | none | none | 81 | 81 |
| P50549 | ETV1 | P50549-1 | P50549-5 | 477 | 419 | 1 | 60 | Substitution | MDGFYDQQVPYMVTNSQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAE | MLQDLSASVFFPPCSQHRTL | 1 | 20 |
| P50549 | ETV1 | P50549-1 | P50549-5 | 477 | 419 | 61 | 79 | Substitution | AQVPDNDEQFVPDYQAESL | V | 21 | 21 |
| P50549 | ETV1 | P50549-1 | P50549-6 | 477 | 437 | 1 | 60 | Substitution | MDGFYDQQVPYMVTNSQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAE | MLQDLSASVFFPPCSQHRTL | 1 | 20 |
| Multiple sequence alignment of our canonical and alternatively spliced ETV1 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of ETV1 |
| UniProt-id | ENSG | ENST | ENSP |
| P50549-1 | ENSG00000006468.15 | ENST00000405218.6 | ENSP00000385551.2 |
| P50549-1 | ENSG00000006468.15 | ENST00000430479.6 | ENSP00000405327.1 |
| P50549-2 | ENSG00000006468.15 | ENST00000242066.10 | ENSP00000242066.5 |
| P50549-2 | ENSG00000006468.15 | ENST00000403685.5 | ENSP00000385686.1 |
| P50549-3 | ENSG00000006468.15 | ENST00000405192.6 | ENSP00000385381.2 |
| P50549-4 | ENSG00000006468.15 | ENST00000443608.6 | ENSP00000394710.2 |
| P50549-5 | ENSG00000006468.15 | ENST00000438956.6 | ENSP00000393078.2 |
| P50549-6 | ENSG00000006468.15 | ENST00000403527.6 | ENSP00000384138.1 |
| UniProt-id | NM ID | NP ID |
| P50549-1 | NM_004956.4 | NP_004947.2 |
| P50549-1 | XM_011515168.2 | XP_011513470.1 |
| P50549-2 | NM_001163148.1 | NP_001156620.1 |
| P50549-2 | NM_001163149.1 | NP_001156621.1 |
| P50549-3 | NM_001163147.1 | NP_001156619.1 |
| P50549-4 | NM_001163152.1 | NP_001156624.1 |
| P50549-5 | NM_001163151.1 | NP_001156623.1 |
| P50549-6 | NM_001163150.1 | NP_001156622.1 |
| Amino acid sequences of our canonical and alternatively spliced ETV1 |
| accession_id | Protein sequence |
| P50549-1 | MDGFYDQQVPYMVTNSQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAEAQVPDNDEQFVPDYQAESLAFHGLPLKIKK EPHSPCSEISSACSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPSNPPTPSSTPVSPLHHASPNSTHTPKPDRAFPAHLPPSQSIPDSSY PMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHDPVYEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVP SCHSIYMRQEGFLAHPSRTEGCMFEKGPRQFYDDTCVVPEKFDGDIKQEPGMYREGPTYQRRGSLQLWQFLVALLDDPSNSHFIAWTGRG MEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCDPEALFSMAFPDNQRPLLKTDMERHINEEDTVPL |
| P50549-2 | MDGFYDQQVPYMVTNSQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAEVAFHGLPLKIKKEPHSPCSEISSACSQEQP FKFSYGEKCLYNVSAYDQKPQVGMRPSNPPTPSSTPVSPLHHASPNSTHTPKPDRAFPAHLPPSQSIPDSSYPMDHRFRRQLSEPCNSFP PLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHDPVYEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSR TEGCMFEKGPRQFYDDTCVVPEKFDGDIKQEPGMYREGPTYQRRGSLQLWQFLVALLDDPSNSHFIAWTGRGMEFKLIEPEEVARRWGIQ KNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCDPEALFSMAFPDNQRPLLKTDMERHINEEDTVPLSHFDESMAYMPEGGCCNP |
| P50549-3 | MDGFYDQQVPYMVTNSQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAEAQVPDNDEQFVPDYQAESLAFHGLPLKIKK EPHSPCSEISSACSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPSNPPTPSSTPVSPLHHASPNSTHTPKPDRAFPAHLPPSQSIPDSSY PMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHDPVYEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSGCM FEKGPRQFYDDTCVVPEKFDGDIKQEPGMYREGPTYQRRGSLQLWQFLVALLDDPSNSHFIAWTGRGMEFKLIEPEEVARRWGIQKNRPA MNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCDPEALFSMAFPDNQRPLLKTDMERHINEEDTVPLSHFDESMAYMPEGGCCNPHPYNE |
| P50549-4 | MLQDLSASVFFPPCSQHRTLAQVPDNDEQFVPDYQAESLAFHGLPLKIKKEPHSPCSEISSACSQEQPFKFSYGEKCLYNVRFRRQLSEP CNSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHDPVYEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFL AHPSRTEGCMFEKGPRQFYDDTCVVPEKFDGDIKQEPGMYREGPTYQRRGSLQLWQFLVALLDDPSNSHFIAWTGRGMEFKLIEPEEVAR RWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCDPEALFSMAFPDNQRPLLKTDMERHINEEDTVPLSHFDESMAYMPEG |
| P50549-5 | MLQDLSASVFFPPCSQHRTLVAFHGLPLKIKKEPHSPCSEISSACSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPSNPPTPSSTPVSPL HHASPNSTHTPKPDRAFPAHLPPSQSIPDSSYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHDPVYEH NTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRTEGCMFEKGPRQFYDDTCVVPEKFDGDIKQEPGMYREGPT YQRRGSLQLWQFLVALLDDPSNSHFIAWTGRGMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCDP |
| P50549-6 | MLQDLSASVFFPPCSQHRTLAQVPDNDEQFVPDYQAESLAFHGLPLKIKKEPHSPCSEISSACSQEQPFKFSYGEKCLYNVSAYDQKPQV GMRPSNPPTPSSTPVSPLHHASPNSTHTPKPDRAFPAHLPPSQSIPDSSYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNI PFPPQGFKQEYHDPVYEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRTEGCMFEKGPRQFYDDTCVVPE KFDGDIKQEPGMYREGPTYQRRGSLQLWQFLVALLDDPSNSHFIAWTGRGMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKG |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| ETV1 (go to UniProt):P50549 |
| 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 |
| P50549 | Region | 128 | 179 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=122;End=184 |
| P50549 | Compositional bias | 145 | 159 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=122;End=184 |
Gene Isoform Structures and Expression Levels for ETV1 |
| Gene structures of our canonical and alternative spliced genes of ETV1 * 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 P50549-1 |
| 3D view using mol* of P50549-2 |
| 3D view using mol* of P50549-3 |
| 3D view using mol* of P50549-4 |
| 3D view using mol* of P50549-5 |
| 3D view using mol* of P50549-6 |
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 P50549-1 |
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| pLDDT distribution across the protein length of P50549-2 |
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| pLDDT distribution across the protein length of P50549-3 |
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| pLDDT distribution across the protein length of P50549-4 |
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| pLDDT distribution across the protein length of P50549-5 |
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| pLDDT distribution across the protein length of P50549-6 |
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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 P50549-1 |
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| Ramachandran plot of P50549-2 |
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| Ramachandran plot of P50549-3 |
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| Ramachandran plot of P50549-5 |
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| Ramachandran plot of P50549-6 |
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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 |
| P50549-1 | 0.629 | 26 | 0.58 | 97.069 | 0.732 | 0.62 | 0.792 | 0.414 | 0.832 | 0.497 | 3.167 | 336,338,395,396,399,401,423,424,426,427,429,431
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| P50549-2 | 1.061 | 199 | 1.109 | 724.416 | 0.543 | 0.724 | 0.971 | 0.853 | 0.815 | 1.046 | 1.129 | 56,57,59,60,61,64,66,68,310,311,312,313,314,315,31 6,317,318,320,321,360,361,362,381,383,396,397,398, 403,406,407,408,409,410,412,414,415,417 |
| P50549-3 | 1.019 | 238 | 1.061 | 643.468 | 0.562 | 0.679 | 0.887 | 0.751 | 0.876 | 0.857 | 1.18 | 36,39,40,43,44,46,47,48,303,304,305,306,307,308,30 9,311,312,313,315,316,317,320,351,354,355,357,377, 378,393,394,397,401,402,403,404,405,406,407,409,41 0,411,412,413 |
| P50549-4 | 1.037 | 112 | 1.124 | 306.985 | 0.683 | 0.619 | 0.802 | 1.169 | 0.575 | 2.032 | 0.758 | 9,10,11,12,13,14,235,236,239,242,243,253,256,257,2 58,310,311,312,313,314,318,321,322 |
| P50549-5 | 1.04 | 124 | 1.111 | 344.372 | 0.615 | 0.652 | 0.88 | 1.077 | 0.674 | 1.598 | 1.554 | 8,9,10,11,12,13,14,280,281,284,286,287,288,289,290 ,292,293,296,297,298,302,303,355,356,357,358,363,3 66,367,369 |
| P50549-6 | 0.902 | 70 | 0.964 | 206.486 | 0.745 | 0.585 | 0.766 | 1.291 | 0.534 | 2.419 | 0.825 | 1,2,4,5,6,9,11,12,13,14,16,319,320,321,373,374,375 ,376,377,378,381,382,384,385,386,392 |
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 P50549-1_P50549-1_5ils_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 P50549-1_5ils_A_P50549-2.pdb |
| 3D view using mol* of P50549-1_5ils_A_P50549-3.pdb |
| 3D view using mol* of P50549-1_5ils_A_P50549-4.pdb |
| 3D view using mol* of P50549-1_5ils_A_P50549-5.pdb |
| 3D view using mol* of P50549-1_5ils_A_P50549-6.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P50549-1_P50549-2.pdb |
| 3D view using mol* of P50549-1_P50549-3.pdb |
| 3D view using mol* of P50549-1_P50549-4.pdb |
| 3D view using mol* of P50549-1_P50549-5.pdb |
| 3D view using mol* of P50549-1_P50549-6.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/P50549-1_vs_P50549-2.png |
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| ./stats/secondary_structure/figure/P50549-1_vs_P50549-3.png |
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| ./stats/secondary_structure/figure/P50549-1_vs_P50549-4.png |
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| ./stats/secondary_structure/figure/P50549-1_vs_P50549-5.png |
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| ./stats/secondary_structure/figure/P50549-1_vs_P50549-6.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/P50549-1_vs_P50549-2.png |
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| ./stats/relative_asa/P50549-1_vs_P50549-3.png |
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| ./stats/relative_asa/P50549-1_vs_P50549-4.png |
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| ./stats/relative_asa/P50549-1_vs_P50549-5.png |
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| ./stats/relative_asa/P50549-1_vs_P50549-6.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 ETV1 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to ETV1 |
| Previous studies relating to the alternative splicing of ETV1 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| ETV1 | 10597226 | Characterization of the human and mouse ETV1/ER81 transcription factor genes: role of the two alternatively spliced isoforms in the human. | The Ets transcription factors of the PEA3 group--E1AF/PEA3, ETV1/ER81 and ERM--are almost identical in the ETS DNA-binding and the transcriptional acidic domains. To accelerate our understanding of the molecular basis of putative diseases linked to ETV1 such as Ewing's sarcoma we characterized the human ETV1 and the mouse ER81 genes. We showed that these genes are both encoded by 13 exons in more than 90 kbp genomic DNA, and that the classical acceptor and donor splicing sites are present in each junction except for the 5' donor site of intron 9 where GT is replaced by TT. The genomic organization of the ETS and acidic domains in the human ETV1 and mouse ER81 (localized to chromosome 12) genes is similar to that observed in human ERM and human E1AF/PEA3 genes. Moreover, as in human ERM and human E1AF/PEA3 genes, a first untranslated exon is upstream from the first methionine, and the mouse ER81 gene transcription is regulated by a 1.8 kbp of genomic DNA upstream from this exon. In human, the alternative splicing of the ETV1 gene leads to the presence (ETV1 alpha) or the absence (ETV1 beta) of exon 5 encoding the C-terminal part of the transcriptional acidic domain, but without affecting the alpha helix previously described as crucial for transactivation. We demonstrated here that the truncated isoform (human ETV1 beta) and the full-length isoform (human ETV1 alpha) bind similarly specific DNA Ets binding sites. Moreover, they both activate transcription similarly through the PKA-transduction pathway, so suggesting that this alternative splicing is not crucial for the function of this protein as a transcription factor. The comparison of human ETV1 alpha and human ETV1 beta expression in the same tissues, such as the adrenal gland or the bladder, showed no clear-cut differences. Altogether, these data open a new avenue of investigation leading to a better understanding of the functional role of this transcription factor. | D002277 | Carcinoma |
| ETV1 | 10597226 | Characterization of the human and mouse ETV1/ER81 transcription factor genes: role of the two alternatively spliced isoforms in the human. | The Ets transcription factors of the PEA3 group--E1AF/PEA3, ETV1/ER81 and ERM--are almost identical in the ETS DNA-binding and the transcriptional acidic domains. To accelerate our understanding of the molecular basis of putative diseases linked to ETV1 such as Ewing's sarcoma we characterized the human ETV1 and the mouse ER81 genes. We showed that these genes are both encoded by 13 exons in more than 90 kbp genomic DNA, and that the classical acceptor and donor splicing sites are present in each junction except for the 5' donor site of intron 9 where GT is replaced by TT. The genomic organization of the ETS and acidic domains in the human ETV1 and mouse ER81 (localized to chromosome 12) genes is similar to that observed in human ERM and human E1AF/PEA3 genes. Moreover, as in human ERM and human E1AF/PEA3 genes, a first untranslated exon is upstream from the first methionine, and the mouse ER81 gene transcription is regulated by a 1.8 kbp of genomic DNA upstream from this exon. In human, the alternative splicing of the ETV1 gene leads to the presence (ETV1 alpha) or the absence (ETV1 beta) of exon 5 encoding the C-terminal part of the transcriptional acidic domain, but without affecting the alpha helix previously described as crucial for transactivation. We demonstrated here that the truncated isoform (human ETV1 beta) and the full-length isoform (human ETV1 alpha) bind similarly specific DNA Ets binding sites. Moreover, they both activate transcription similarly through the PKA-transduction pathway, so suggesting that this alternative splicing is not crucial for the function of this protein as a transcription factor. The comparison of human ETV1 alpha and human ETV1 beta expression in the same tissues, such as the adrenal gland or the bladder, showed no clear-cut differences. Altogether, these data open a new avenue of investigation leading to a better understanding of the functional role of this transcription factor. | D007680 | Kidney Neoplasms |
Clinically important variants in ETV1 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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