| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P14921 | Domain | 51 | 136 | Note=PNT;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00762 | Type=Deletion;Start=28;End=243 |
| P14921 | DNA binding | 335 | 415 | Note=ETS;Ontology_term=ECO:0000255;evidence=ECO:0000255|PROSITE-ProRule:PRU00237 | Type=Deletion;Start=273;End=441 |
| P14921 | Region | 130 | 243 | Note=Activation domain%3B required for transcription activation;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:11909962;Dbxref=PMID:11909962 | Type=Deletion;Start=28;End=243 |
| P14921 | Region | 304 | 312 | Note=Helix HI-1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27577 | Type=Deletion;Start=244;End=330 |
| P14921 | Region | 304 | 312 | Note=Helix HI-1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27577 | Type=Deletion;Start=273;End=441 |
| P14921 | Region | 323 | 330 | Note=Helix HI-2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27577 | Type=Deletion;Start=244;End=330 |
| P14921 | Region | 323 | 330 | Note=Helix HI-2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27577 | Type=Deletion;Start=273;End=441 |
| P14921 | Region | 418 | 422 | Note=Helix H4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27577 | Type=Deletion;Start=273;End=441 |
| P14921 | Region | 426 | 432 | Note=Helix H5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P27577 | Type=Deletion;Start=273;End=441 |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| P14921-1 | 1.029 | 97 | 1.071 | 263.081 | 0.522 | 0.702 | 0.976 | 1.039 | 0.845 | 1.229 | 1.261 | 305,307,308,309,311,312,313,314,315,316,318,319,32
0,322,325,346,347,348,424,432,433
|
| P14921-2 | 1.069 | 103 | 1.137 | 272.342 | 0.639 | 0.698 | 0.892 | 1.26 | 0.683 | 1.847 | 0.945 | 45,48,49,51,52,87,88,124,229,230,232,235,236,237,2
38,239,240,249,250,251,309,312,314,329,330,331,334
|
| P14921-3 | 1.046 | 276 | 1.101 | 702.121 | 0.574 | 0.692 | 0.922 | 1.132 | 0.78 | 1.452 | 2.004 | 78,80,81,82,83,85,86,88,89,90,92,93,94,96,132,133,
134,135,154,158,159,161,162,163,164,165,166,167,16
8,170,171,174,175,178,179,364,365,366,369,370,372,
373,374,375,376,380,382,383,464,465,466,468
|
| P14921-4 | 1.058 | 154 | 1.116 | 279.545 | 0.523 | 0.702 | 0.957 | 1.248 | 0.753 | 1.657 | 0.757 | 14,15,16,17,18,19,20,21,22,23,24,116,118,119,120,1
21,159,163,168,172,173,175,176,179,180,183
|
| P14921-5 | 0.784 | 65 | 0.713 | 180.418 | 0.693 | 0.587 | 0.798 | 0.038 | 1.217 | 0.031 | 1.877 | 50,53,54,56,57,60,66,67,68,71,128,131,132,135,136,
138,139,140,141
|
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| ETS1 | 8231246 | Quantitative and qualitative variation of ETS-1 transcripts in hematologic malignancies. | The ETS family proteins have a conserved DNA-binding domain and act as transcription factors. Three domains have been recently defined in human ETS-1 proteins and their role could depend upon the nature of alternative transcripts according to whether they possess or lack DNA binding and/or transcriptional activation domain and also point mutation that could affect these important domains. Expression of ETS-1 gene is very complex and is controlled at several levels: the initiation of transcription, alternative splicing, post-translational modification, and protein stability. As a selection apparently exists for ETS-1 gene activation in hematopoietic cells, we investigated a relation between quantitative and qualitative ETS-1 expression and leukemogenesis. Using Northern blot, polymerase chain reaction (PCR), and single strand conformation polymorphism (SSCP) methods, we analyzed quantitative and qualitative ETS-1 expression in a variety of hematological pathologies and cell lines of different origin. Two ETS-1 transcripts of 6.8 and 2.7 kb, resulting from differential polyadenylation site utilization and exhibiting different stability, were observed. We identified, in a great number of patients, the four alternative ETS-1 products, but the relative extent significance of the four transcripts was very different from one patient to another. A non-conservative mutation observed in one case of T-cell acute lymphoblastic leukemia (T-ALL) and in the ETS-1 transactivation domain raised the question of suppressor activity for some ETS-1 products, as it is now known that activators and repressors can be encoded by the same gene and consistently co-expressed in vivo. | D007938 | Leukemia |
| ETS1 | 12850290 | Ets-1 activates parathyroid hormone-related protein gene expression in tumorigenic breast epithelial cells. | Parathyroid hormone-related protein (PTHrP) is produced by many tumors not associated with humoral hypercalcemia, including breast cancers. In this study, we used three human immortalized mammary epithelial cell lines that differ in tumorigenicity and PTHrP expression. Using RT-PCR we investigated 5' and 3' alternative splicing of PTHrP transcripts and promoter usage in the lines. Increased levels of P3-derived transcripts and the 1-139 mRNA isoform were observed in the most tumorigenic cell line. Transient transfection experiments identified elements close to P3 promoter that appeared to account for a portion of differential PTHrP expression among the three cell lines. Using site-directed mutagenesis, a previously described Ets-1/Sp1 binding site upstream of P3 was determined to be crucial for full activity of this promoter. RT-PCR and western blot evaluation of Ets family member expression found that Ese-1 was present in all three lines, but that appreciable levels of Ets-1 protein were present exclusively in the most tumorigenic line. Cotransfection of Ets-1 expression vectors activated PTHrP reporter constructs in the most tumorigenic line but not in the other cell lines. These findings suggest a potential mechanism by which PTHrP transcription may be regulated as a consequence of events that promote tumorigenic behavior in breast epithelial cells. | D001943 | Breast Neoplasms |
| ETS1 | 12850290 | Ets-1 activates parathyroid hormone-related protein gene expression in tumorigenic breast epithelial cells. | Parathyroid hormone-related protein (PTHrP) is produced by many tumors not associated with humoral hypercalcemia, including breast cancers. In this study, we used three human immortalized mammary epithelial cell lines that differ in tumorigenicity and PTHrP expression. Using RT-PCR we investigated 5' and 3' alternative splicing of PTHrP transcripts and promoter usage in the lines. Increased levels of P3-derived transcripts and the 1-139 mRNA isoform were observed in the most tumorigenic cell line. Transient transfection experiments identified elements close to P3 promoter that appeared to account for a portion of differential PTHrP expression among the three cell lines. Using site-directed mutagenesis, a previously described Ets-1/Sp1 binding site upstream of P3 was determined to be crucial for full activity of this promoter. RT-PCR and western blot evaluation of Ets family member expression found that Ese-1 was present in all three lines, but that appreciable levels of Ets-1 protein were present exclusively in the most tumorigenic line. Cotransfection of Ets-1 expression vectors activated PTHrP reporter constructs in the most tumorigenic line but not in the other cell lines. These findings suggest a potential mechanism by which PTHrP transcription may be regulated as a consequence of events that promote tumorigenic behavior in breast epithelial cells. | D002471 | Cell Transformation, Neoplastic |
| ETS1 | 19377509 | Ets-1 p27: a novel Ets-1 isoform with dominant-negative effects on the transcriptional properties and the subcellular localization of Ets-1 p51. | The transcription factor Ets-1 is implicated in various physiological processes and invasive pathologies. We identified a novel variant of ets-1, ets-1Delta(III-VI), resulting from the alternative splicing of exons III to VI. This variant encodes a 27 kDa isoform, named Ets-1 p27. Ets-1 p27 lacks the threonine-38 residue, the Pointed domain and the transactivation domain, all of which are required for the transactivation of Ets-1 target genes. Both inhibitory domains surrounding the DNA-binding domain are conserved, suggesting that Ets-1 p27, like the full-length Ets-1 p51 isoform, is autoinhibited for DNA binding. We showed that Ets-1 p27 binds DNA in the same way as Ets-1 p51 does and that it acts both at a transcriptional and a subcellular localization level, thereby constituting a dual-acting dominant negative of Ets-1 p51. Ets-1 p27 blocks Ets-1 p51-mediated transactivation of target genes and induces the translocation of Ets-1 p51 from the nucleus to the cytoplasm. Furthermore, Ets-1 p27 overexpression represses the tumor properties of MDA-MB-231 mammary carcinoma cells in correlation with the known implication of Ets-1 in various cellular mechanisms. Thus the dual-acting dominant-negative function of Ets-1 p27 gives to the Ets-1 p27/Ets-1 p51 ratio a determining effect on cell fate. | D000230 | Adenocarcinoma |
| ETS1 | 19377509 | Ets-1 p27: a novel Ets-1 isoform with dominant-negative effects on the transcriptional properties and the subcellular localization of Ets-1 p51. | The transcription factor Ets-1 is implicated in various physiological processes and invasive pathologies. We identified a novel variant of ets-1, ets-1Delta(III-VI), resulting from the alternative splicing of exons III to VI. This variant encodes a 27 kDa isoform, named Ets-1 p27. Ets-1 p27 lacks the threonine-38 residue, the Pointed domain and the transactivation domain, all of which are required for the transactivation of Ets-1 target genes. Both inhibitory domains surrounding the DNA-binding domain are conserved, suggesting that Ets-1 p27, like the full-length Ets-1 p51 isoform, is autoinhibited for DNA binding. We showed that Ets-1 p27 binds DNA in the same way as Ets-1 p51 does and that it acts both at a transcriptional and a subcellular localization level, thereby constituting a dual-acting dominant negative of Ets-1 p51. Ets-1 p27 blocks Ets-1 p51-mediated transactivation of target genes and induces the translocation of Ets-1 p51 from the nucleus to the cytoplasm. Furthermore, Ets-1 p27 overexpression represses the tumor properties of MDA-MB-231 mammary carcinoma cells in correlation with the known implication of Ets-1 in various cellular mechanisms. Thus the dual-acting dominant-negative function of Ets-1 p27 gives to the Ets-1 p27/Ets-1 p51 ratio a determining effect on cell fate. | D001859 | Bone Neoplasms |
| ETS1 | 19377509 | Ets-1 p27: a novel Ets-1 isoform with dominant-negative effects on the transcriptional properties and the subcellular localization of Ets-1 p51. | The transcription factor Ets-1 is implicated in various physiological processes and invasive pathologies. We identified a novel variant of ets-1, ets-1Delta(III-VI), resulting from the alternative splicing of exons III to VI. This variant encodes a 27 kDa isoform, named Ets-1 p27. Ets-1 p27 lacks the threonine-38 residue, the Pointed domain and the transactivation domain, all of which are required for the transactivation of Ets-1 target genes. Both inhibitory domains surrounding the DNA-binding domain are conserved, suggesting that Ets-1 p27, like the full-length Ets-1 p51 isoform, is autoinhibited for DNA binding. We showed that Ets-1 p27 binds DNA in the same way as Ets-1 p51 does and that it acts both at a transcriptional and a subcellular localization level, thereby constituting a dual-acting dominant negative of Ets-1 p51. Ets-1 p27 blocks Ets-1 p51-mediated transactivation of target genes and induces the translocation of Ets-1 p51 from the nucleus to the cytoplasm. Furthermore, Ets-1 p27 overexpression represses the tumor properties of MDA-MB-231 mammary carcinoma cells in correlation with the known implication of Ets-1 in various cellular mechanisms. Thus the dual-acting dominant-negative function of Ets-1 p27 gives to the Ets-1 p27/Ets-1 p51 ratio a determining effect on cell fate. | D001943 | Breast Neoplasms |
| ETS1 | 19377509 | Ets-1 p27: a novel Ets-1 isoform with dominant-negative effects on the transcriptional properties and the subcellular localization of Ets-1 p51. | The transcription factor Ets-1 is implicated in various physiological processes and invasive pathologies. We identified a novel variant of ets-1, ets-1Delta(III-VI), resulting from the alternative splicing of exons III to VI. This variant encodes a 27 kDa isoform, named Ets-1 p27. Ets-1 p27 lacks the threonine-38 residue, the Pointed domain and the transactivation domain, all of which are required for the transactivation of Ets-1 target genes. Both inhibitory domains surrounding the DNA-binding domain are conserved, suggesting that Ets-1 p27, like the full-length Ets-1 p51 isoform, is autoinhibited for DNA binding. We showed that Ets-1 p27 binds DNA in the same way as Ets-1 p51 does and that it acts both at a transcriptional and a subcellular localization level, thereby constituting a dual-acting dominant negative of Ets-1 p51. Ets-1 p27 blocks Ets-1 p51-mediated transactivation of target genes and induces the translocation of Ets-1 p51 from the nucleus to the cytoplasm. Furthermore, Ets-1 p27 overexpression represses the tumor properties of MDA-MB-231 mammary carcinoma cells in correlation with the known implication of Ets-1 in various cellular mechanisms. Thus the dual-acting dominant-negative function of Ets-1 p27 gives to the Ets-1 p27/Ets-1 p51 ratio a determining effect on cell fate. | D012516 | Osteosarcoma |
Gene summary
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