| + |
CyclinE/CDK2 | down-regulates 
phosphorylation
|
ID2 |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-216698 |
Ser5 |
sPVRSVRK |
Homo sapiens |
|
| pmid |
sentence |
| 9029153 |
Id2 acts by forming heterodimers that are unable to bind to specific (e-box) dna sequences. Here we show that this activity can be overcome by phosphorylation of a serine residue within a consensus target site for cyclin-dependent kinases (cdks). In vitro, id2 can be phosphorylated by either cyclin e-cdk2 or cyclin a-cdk2_ |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CyclinA2/CDK2 | down-regulates
phosphorylation
|
ID2 |
0.356 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217320 |
Ser5 |
sPVRSVRK |
Homo sapiens |
|
| pmid |
sentence |
| 9029153 |
Id2 acts by forming heterodimers that are unable to bind to specific (e-box) dna sequences. Here we show that this activity can be overcome by phosphorylation of a serine residue within a consensus target site for cyclin-dependent kinases (cdks). In vitro, id2 can be phosphorylated by either cyclin e-cdk2 or cyclin a-cdk2_ |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK2 | down-regulates
phosphorylation
|
ID2 |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-46397 |
Ser5 |
sPVRSVRK |
Homo sapiens |
|
| pmid |
sentence |
| 9029153 |
Id2 acts by forming heterodimers that are unable to bind to specific (e-box) dna sequences. Here we show that this activity can be overcome by phosphorylation of a serine residue within a consensus target site for cyclin-dependent kinases (cdks). In vitro, id2 can be phosphorylated by either cyclin e-cdk2 or cyclin a-cdk2_ |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DYRK1B | down-regulates activity
phosphorylation
|
ID2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279033 |
Thr27 |
LGISRSKtPVDDPMS |
Homo sapiens |
|
| pmid |
sentence |
| 26735018 |
Phosphorylation of Thr27 of ID2 by DYRK1 blocks ID2-VHL interaction and preserves HIF2α ubiquitylation.|We report that DYRK1A and DYRK1B kinases phosphorylate ID2 on Threonine-27 (T27). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ASB4 | down-regulates quantity by destabilization
polyubiquitination
|
ID2 |
0.333 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272053 |
|
|
Homo sapiens |
Placental Cell Line |
| pmid |
sentence |
| 24586788 |
Using JAR placental cells, we determined that ASB4 ubiquitinates and represses ID2 expression in a proteasome-dependent fashion. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POU5F1 | down-regulates quantity by repression 
transcriptional regulation
|
ID2 |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254937 |
|
|
Homo sapiens |
Embryonic Stem Cell |
| pmid |
sentence |
| 17068183 |
To enhance our understanding of the molecular basis of this differentiation event in humans, we used a functional genomics approach involving RNA interference-mediated suppression of OCT4 function in a human ESC line and analysis of the resulting transcriptional profiles to identify OCT4-dependent genes in human cells. We detected altered expression of >1,000 genes, including targets regulated directly by OCT4 either positively (NANOG, SOX2, REX1, LEFTB, LEFTA/EBAF DPPA4, THY1, and TDGF1) or negatively (CDX2, EOMES, BMP4, TBX18, Brachyury [T], DKK1, HLX1, GATA6, ID2, and DLX5), as well as targets for the OCT4-associated stem cell regulators SOX2 and NANOG. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ID2 | down-regulates activity
binding
|
TCF3 |
0.57 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241140 |
|
|
Mus musculus |
C3H10T1/2 Cell |
| pmid |
sentence |
| 9242638 |
All three Ids bound with high affinity to E proteins .Each Id was able to disrupt the ability of E protein-MyoD complexes to transactivate from a muscle creatine kinase reporter construct in vivo. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
GDNF | up-regulates quantity by expression 
transcriptional regulation
|
ID2 |
0.246 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252180 |
|
|
Rattus norvegicus |
Neural Stem Cell |
| pmid |
sentence |
| 15212950 |
We characterize the network of 43 genes induced by GDNF overproduction of neuronal progenitor cells (ST14A), which mainly regulate migration and differentiation of neuronal progenitor cells.Laminin, Mpl3, Alcam, Bin1, Id1, Id2, Id3, neuregulin1, the ephrinB2-receptor, neuritin, focal adhesion kinase (FAK), Tc10, Pdpk1, clusterin, GTP-cyclooxygenase1, and follistatin are genes up-regulated by GDNF overexpression. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
ID2 | down-regulates activity
binding
|
MYOD1 |
0.527 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240268 |
|
|
Mus musculus |
Myoblast |
| pmid |
sentence |
| 8380166 |
Id1 and Id2 interacted strongly with MyoD and Myf-5.Each Id was able to disrupt the ability of E protein-MyoD complexes to transactivate from a muscle creatine kinase reporter construct in vivo. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ID2 | down-regulates activity
binding
|
MYOD/HEB |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241143 |
|
|
Mus musculus |
C3H10T1/2 Cell |
| pmid |
sentence |
| 9242638 |
All three Ids bound with high affinity to E proteins .Each Id was able to disrupt the ability of E protein-MyoD complexes to transactivate from a muscle creatine kinase reporter construct in vivo. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ID2 | down-regulates activity
binding
|
TCF4 |
0.58 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241376 |
|
|
Mus musculus |
C3H10T1/2 Cell |
| pmid |
sentence |
| 9242638 |
All three Ids bound with high affinity to E proteins .Each Id was able to disrupt the ability of E protein-MyoD complexes to transactivate from a muscle creatine kinase reporter construct in vivo. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ID2 | down-regulates activity
binding
|
MYOD/E2-2 |
0.554 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241146 |
|
|
Mus musculus |
C3H10T1/2 Cell |
| pmid |
sentence |
| 9242638 |
All three Ids bound with high affinity to E proteins .Each Id was able to disrupt the ability of E protein-MyoD complexes to transactivate from a muscle creatine kinase reporter construct in vivo. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
ID2 | down-regulates activity
binding
|
TCF12 |
0.537 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241131 |
|
|
Mus musculus |
C3H10T1/2 Cell |
| pmid |
sentence |
| 9242638 |
All three Ids bound with high affinity to E proteins .Each Id was able to disrupt the ability of E protein-MyoD complexes to transactivate from a muscle creatine kinase reporter construct in vivo. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
BMP2 | up-regulates quantity by expression
transcriptional regulation
|
ID2 |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282534 |
|
|
Homo sapiens |
Pancreatic Ductal Carcinoma Cell |
| pmid |
sentence |
| 40993391 |
BMP2 treatment led to a rapid induction of the BMP target genes Id1, Id2 and Id3 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PML-RARalpha | up-regulates quantity by expression
transcriptional regulation
|
ID2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255727 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18025157 |
Also comparable with ID1, RARα, RXR, PML, PLZF-RARα, and RARα/RXR did not transactivate the ID2 promoter, whereas PML-RARα did. Together, these data show that like ID1, ID2 may also be transactivated by PML-RARα without direct DNA binding of the fusion protein. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ID2 | down-regulates activity
binding
|
MYOD/E12E47 |
0.549 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-241149 |
|
|
Mus musculus |
C3H10T1/2 Cell |
| pmid |
sentence |
| 9242638 |
All three Ids bound with high affinity to E proteins .Each Id was able to disrupt the ability of E protein-MyoD complexes to transactivate from a muscle creatine kinase reporter construct in vivo. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
4.0
ID2
- 
- 