| + |
TERF2 | down-regulates activity 
binding
|
ATM |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263323 |
|
|
|
|
| pmid |
sentence |
| 18680434 |
It is not yet clear how the presence of TRF2 at telomeres averts the activation of the ATM kinase.> In this regard, overexpression of TRF2can dampen the activation of the ATM kinase, even at nontelomeric sites of DNA damage (95). Furthermore, TRF2 can interact with the ATM kinase as well as with the Mre11 complex |
|
| Publications: |
1 |
| + |
TERF2 | form complex 
binding
|
Shelterin complex |
0.801 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263317 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15383534 |
Telosome, a mammalian telomere-associated complex formed by multiple telomeric proteins|Gel filtration reveals a complex consisting of POT1 , RAP1, TRF1, ACD, TERF2 and TINF2 proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HNRNPH1 | down-regulates quantity
post transcriptional regulation
|
TERF2 |
0.342 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266807 |
|
|
Rattus norvegicus |
PC-12 Cell |
| pmid |
sentence |
| 27117401 |
During neuronal differentiation, use of an alternative splice site on the rat telomere repeat-binding factor 2 (TRF2) mRNA generates a short TRF2 protein isoform (TRF2-S) capable of derepressing neuronal genes. However, the RNA-binding proteins (RBPs) controlling this splicing event are unknown. Here, using affinity pull-down analysis, we identified heterogeneous nuclear ribonucleoproteins H1 and H2(HNRNPH) as RBPs specifically capable of interacting with the spliced RNA segment (exon 7) of Trf2 pre-mRNA. HNRNPH proteins prevent the production of the short isoform of Trf2 mRNA, as HNRNPH silencing selectively elevates TRF2-S levels. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
TERF2 | down-regulates 
|
Neurogenesis |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266805 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 27117401 |
During neuronal differentiation, use of an alternative splice site on the rat telomere repeat-binding factor 2 (TRF2) mRNA generates a short TRF2 protein isoform (TRF2-S) capable of derepressing neuronal genes. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
HNRNPH2 | down-regulates quantity
post transcriptional regulation
|
TERF2 |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266806 |
|
|
Rattus norvegicus |
PC-12 Cell |
| pmid |
sentence |
| 27117401 |
During neuronal differentiation, use of an alternative splice site on the rat telomere repeat-binding factor 2 (TRF2) mRNA generates a short TRF2 protein isoform (TRF2-S) capable of derepressing neuronal genes. However, the RNA-binding proteins (RBPs) controlling this splicing event are unknown. Here, using affinity pull-down analysis, we identified heterogeneous nuclear ribonucleoproteins H1 and H2(HNRNPH) as RBPs specifically capable of interacting with the spliced RNA segment (exon 7) of Trf2 pre-mRNA. HNRNPH proteins prevent the production of the short isoform of Trf2 mRNA, as HNRNPH silencing selectively elevates TRF2-S levels. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
3.0
TERF2
- 
- 