| + |
GSK3B | down-regulates activity 
phosphorylation
|
NOTCH2 |
0.484 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251254 |
Ser2070 |
DEYNVTPsPPGTVLT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12794074 |
Ser-2093 is efficiently phosphorylated by GSK-3β and, to a minor extent, residues Thr-2068 and/or Ser-2070 and Thr-2074 of Notch2 are also targets for GSK-3β-dependent phosphorylation. We also find that GSK-3β-dependent phosphorylation of Notch2 is inhibiting transcriptional activation of different Notch target genes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251253 |
Ser2093 |
GPNRSFLsLKHTPMG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12794074 |
Ser-2093 is efficiently phosphorylated by GSK-3β and, to a minor extent, residues Thr-2068 and/or Ser-2070 and Thr-2074 of Notch2 are also targets for GSK-3β-dependent phosphorylation. We also find that GSK-3β-dependent phosphorylation of Notch2 is inhibiting transcriptional activation of different Notch target genes. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101570 |
Thr2068 |
LLDEYNVtPSPPGTV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12794074 |
We show that gsk-3beta directly binds at c-terminal of the notch2 ankyrin repeats and phosphorylates thr-2068 and/or ser-2070, thr-2074, and thr-2093. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101574 |
Thr2074 |
VTPSPPGtVLTSALS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12794074 |
We show that gsk-3beta directly binds at c-terminal of the notch2 ankyrin repeats and phosphorylates thr-2068 and/or ser-2070, thr-2074, and thr-2093. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
MAML1 | up-regulates 
binding
|
NOTCH2 |
0.807 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84835 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11101851 |
Maml1 binds to the ankyrin repeat domain of all four mammalian notch receptors, forms a dna-binding complex with icn and rbp-jkappa, and amplifies notch-induced transcription of hes1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DLL1 | up-regulates
binding
|
NOTCH2 |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-199320 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23111325 |
In this study, we demonstrate that dll1 can activate notch signaling mostly through notch2 receptor and can contribute to drug resistance to bortezomib, both in murine and human mm cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GXYLT1 | up-regulates
binding
|
NOTCH2 |
0.338 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177694 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22117070 |
We have previously identified two human genes, gxylt1 and gxylt2, encoding glucoside xylosyltransferases responsible for the transfer of xylose to o-linked glucose. The identity of the enzyme further elongating the glycan to generate the final trisaccharide xylose-xylose-glucose, however, remained unknown. Here, we describe that the human gene c3orf21 encodes a udp-xylose:alfa-xyloside alfa1,3-xylosyltransferase, acting on xylose-alfa1,3-glucosebeta1-containing acceptor structures. We have, therefore, renamed it xxylt1 (xyloside xylosyltransferase 1). Xxylt1 cannot act on a synthetic acceptor containing an alfa-linked xylose alone, but requires the presence of the underlying glucose. Activity on notch egf repeats was proven by in vitro xylosylation of a mouse notch1 fragment recombinantly produced in sf9 insect cells, a bacterially expressed egf repeat from mouse notch2 modified in vitro by rumi and gxylt2 and in vivo by co-expression of the enzyme with the notch1 fragment. The enzyme was shown to be a typical type ii membrane-bound glycosyltransferase localized in the endoplasmic reticulum. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAG1 | up-regulates
binding
|
NOTCH2 |
0.636 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179622 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18660822 |
Here we report the first x-ray structure of a functional fragment of a notch ligand, the dsl-egf3 domains of human jagged-1 (j-1dsl-egf3). The structure identifies a highly conserved face of the dsl domain and we show, by functional analysis of drosophila ligand mutants, that this surface is required for both cis- and trans-regulatory interactions with notch. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72112 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10551863 |
Here we report the first x-ray structure of a functional fragment of a notch ligand, the dsl-egf3 domains of human jagged-1 (j-1dsl-egf3). The structure identifies a highly conserved face of the dsl domain and we show, by functional analysis of drosophila ligand mutants, that this surface is required for both cis- and trans-regulatory interactions with notch. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81364 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10958687 |
Here we report the first x-ray structure of a functional fragment of a notch ligand, the dsl-egf3 domains of human jagged-1 (j-1dsl-egf3). The structure identifies a highly conserved face of the dsl domain and we show, by functional analysis of drosophila ligand mutants, that this surface is required for both cis- and trans-regulatory interactions with notch. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
NOTCH2 | down-regulates activity
binding
|
TRAF6 |
0.312 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265562 |
|
|
Homo sapiens |
Nasopharyngeal Carcinoma Cell Line |
| pmid |
sentence |
| 31699119 |
NOTCH2 attenuated the TRAF6-AKT signaling axis via an interaction between the NOTCH2 intracellular domain (N2ICD) and TRAF6, which inhibited epithelial-mesenchymal transition (EMT) and eventually suppressed NPC metastasis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GXYLT2 | up-regulates
binding
|
NOTCH2 |
0.324 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177717 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22117070 |
We have previously identified two human genes, gxylt1 and gxylt2, encoding glucoside xylosyltransferases responsible for the transfer of xylose to o-linked glucose. The identity of the enzyme further elongating the glycan to generate the final trisaccharide xylose-xylose-glucose, however, remained unknown. Here, we describe that the human gene c3orf21 encodes a udp-xylose:alfa-xyloside alfa1,3-xylosyltransferase, acting on xylose-alfa1,3-glucosebeta1-containing acceptor structures. We have, therefore, renamed it xxylt1 (xyloside xylosyltransferase 1). Xxylt1 cannot act on a synthetic acceptor containing an alfa-linked xylose alone, but requires the presence of the underlying glucose. Activity on notch egf repeats was proven by in vitro xylosylation of a mouse notch1 fragment recombinantly produced in sf9 insect cells, a bacterially expressed egf repeat from mouse notch2 modified in vitro by rumi and gxylt2 and in vivo by co-expression of the enzyme with the notch1 fragment. The enzyme was shown to be a typical type ii membrane-bound glycosyltransferase localized in the endoplasmic reticulum. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LFNG | down-regulates
binding
|
NOTCH2 |
0.696 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107705 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11346656 |
Although both manic fringe (mfng) and lunatic fringe (lfng) decreased the binding of jagged1 to notch2 and not that of delta1, the decrease by mfng was greater in degree than that by lfng. We also found that both fringe proteins reduced jagged1-triggered notch2 signaling, whereas neither affected delta1-triggered notch2 signaling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
gamma-secretase | up-regulates activity
cleavage
|
NOTCH2 |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-209723 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25610395 |
The membrane-bound Notch segment that results from this cleavage, known as Notch Intracellular Truncation domain (NEXT), is a -secretase substrate (Kopan and Ilagan, 2009). -Secretase performs the subsequent cleavage at S3 (De Strooper et al., 1999), releasing Notch intracellular domain (NICD) from the membrane and allowing for signal transduction through binding with the CBL-1, Su(H), Lag-1 (CSL; Schroeter et al., 1998; Struhl and Adachi, 1998) family of DNA binding proteins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JAG2 | up-regulates
binding
|
NOTCH2 |
0.632 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-81367 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10958687 |
Binding of delta1, jagged1, and jagged2 to notch2 rapidly induces cleavage, nuclear translocation, and hyperphosphorylation of notch2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MBD3/NuRD complex | down-regulates quantity by repression
transcriptional regulation
|
NOTCH2 |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265561 |
|
|
Homo sapiens |
Hepatoma Cell Line |
| pmid |
sentence |
| 31659254 |
Here we report that ZNF774, a novel zinc-finger protein, inhibits the proliferation and invasion of HCC cells. Molecular characterization of this protein indicated that ZNF774 acts as a transcription repressor, and interrogation of ZNF774 interactome by affinity purification-coupled mass spectrometry revealed that ZNF774 is physically associated with the Mi-2/nucleosome remodeling and deacetylase (NuRD) complex in cells. We demonstrated that ZNF774 recruits the NuRD complex to the NOTCH2 promoter and represses NOTCH2 transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
LFNG | up-regulates
binding
|
NOTCH2 |
0.696 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107702 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11346656 |
These observations indicate that the fringe proteins directly modify notch2, which is consistent with the recent finding that fringe is a glycosyltransferase that directly modifies notch. It was further indicated that lfng does this at a site from the n terminus through the 15th egf repeat of notch2, and mfng does so at a site from the 23rd through the 29th egf repeat of notch2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NOTCH2 | down-regulates
binding
|
TCF3 |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-56222 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9528794 |
In an effort to identify processes that regulate e47, and potentially b-cell development, we found that activated notch1 and notch2 effectively inhibit e47 activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MFNG | up-regulates
binding
|
NOTCH2 |
0.685 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-107708 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11346656 |
These observations indicate that the fringe proteins directly modify notch2, which is consistent with the recent finding that fringe is a glycosyltransferase that directly modifies notch (30, 31). It was further indicated that lfng does this at a site from the n terminus through the 15th egf repeat of notch2, and mfng does so at a site from the 23rd through the 29th egf repeat of notch2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MDK | up-regulates
binding
|
NOTCH2 |
0.488 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161427 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18469519 |
We showed that mk binds to the notch2 receptor in hacat keratinocytes. We further found that mk activates notch2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
POGLUT1 | up-regulates
binding
|
NOTCH2 |
0.573 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198716 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22872643 |
O-glucosylation of epidermal growth factor-like (egf) repeats in the extracellular domain of notch is essential for notch function. O-glucose can be elongated by xylose to the trisaccharide, xylalfa1-3xylalfa1-3glcbeta1-o-ser, whose synthesis is catalyzed by the consecutive action of three glycosyltransferases. A udp-glucose:protein o-glucosyltransferase (poglut/rumi) transfers o-glucose to serine within the o-glucose consensus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAML3 | up-regulates
binding
|
NOTCH2 |
0.752 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-94097 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12370315 |
We report here the cloning and characterization of two new genes, maml2 and maml3, that also function as transcriptional coactivators for notch receptors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MBD2/NuRD complex | down-regulates quantity by repression
transcriptional regulation
|
NOTCH2 |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265560 |
|
|
Homo sapiens |
Hepatoma Cell Line |
| pmid |
sentence |
| 31659254 |
Here we report that ZNF774, a novel zinc-finger protein, inhibits the proliferation and invasion of HCC cells. Molecular characterization of this protein indicated that ZNF774 acts as a transcription repressor, and interrogation of ZNF774 interactome by affinity purification-coupled mass spectrometry revealed that ZNF774 is physically associated with the Mi-2/nucleosome remodeling and deacetylase (NuRD) complex in cells. We demonstrated that ZNF774 recruits the NuRD complex to the NOTCH2 promoter and represses NOTCH2 transcription. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
NOTCH2
- 
- 