| + |
CREBBP | up-regulates activity 
acetylation
|
STAT2 |
0.549 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217891 |
Lys390 |
QKTLTPEkGQSQGLI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17923090 |
STAT2 is another important component of ISGF3 complex, and its acetylation was similar to IFNaR2 and IRF9 acetylation in many respects: CBP downregulation largely abolished STAT2 acetylation induction by IFNa (Figure 6A), and CBP was more potent than transferases tested in catalyzing STAT2 acetylation (Figure 6B). [...] Figure 6 (I) STAT2-K390R substitution has reduced activity in ISGF3 complex formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GSK3B | down-regulates quantity by destabilization 
phosphorylation
|
STAT2 |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276763 |
Ser381 |
RKFNILTsNQKTLTP |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31843895 |
GSK3α/β are critical kinases to regulate STAT2 protein stability mediated by FBXW7.The 4-point mutant (STAT2-4A) of STAT2 at S381A/T385A/E389A/S393A inhibited GSK3α/β-mediated STAT2 phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276764 |
Ser393 |
LTPEKGQsQGLIWDF |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31843895 |
GSK3α/β are critical kinases to regulate STAT2 protein stability mediated by FBXW7.The 4-point mutant (STAT2-4A) of STAT2 at S381A/T385A/E389A/S393A inhibited GSK3α/β-mediated STAT2 phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276765 |
Thr385 |
ILTSNQKtLTPEKGQ |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31843895 |
GSK3α/β are critical kinases to regulate STAT2 protein stability mediated by FBXW7.The 4-point mutant (STAT2-4A) of STAT2 at S381A/T385A/E389A/S393A inhibited GSK3α/β-mediated STAT2 phosphorylation. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
GSK3A | down-regulates quantity by destabilization
phosphorylation
|
STAT2 |
0.266 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276760 |
Ser381 |
RKFNILTsNQKTLTP |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31843895 |
GSK3α/β are critical kinases to regulate STAT2 protein stability mediated by FBXW7.The 4-point mutant (STAT2-4A) of STAT2 at S381A/T385A/E389A/S393A inhibited GSK3α/β-mediated STAT2 phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276762 |
Ser393 |
LTPEKGQsQGLIWDF |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31843895 |
GSK3α/β are critical kinases to regulate STAT2 protein stability mediated by FBXW7.The 4-point mutant (STAT2-4A) of STAT2 at S381A/T385A/E389A/S393A inhibited GSK3α/β-mediated STAT2 phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276761 |
Thr385 |
ILTSNQKtLTPEKGQ |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31843895 |
GSK3α/β are critical kinases to regulate STAT2 protein stability mediated by FBXW7.The 4-point mutant (STAT2-4A) of STAT2 at S381A/T385A/E389A/S393A inhibited GSK3α/β-mediated STAT2 phosphorylation. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PTPRG | up-regulates activity
dephosphorylation
|
STAT2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254728 |
Tyr690 |
NLQERRKyLKHRLIV |
in vitro |
|
| pmid |
sentence |
| 25624455 |
PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
JAK1 | up-regulates activity
phosphorylation
|
STAT2 |
0.76 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251344 |
Tyr690 |
NLQERRKyLKHRLIV |
|
|
| pmid |
sentence |
| 9020188 |
STAT2 plays a pivotal role in IFN-a signaling. It is recruited to the activated receptor first and, after phosphorylation by JAK kinases on tyrosine 690, provides a docking site for the SH2 domain of STAT1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-88285 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9020188 |
The stat1 and stat2 proteins are present in the cytoplasm of untreated cells;upon stimulation with ifn-?, They become rapidly activated by tyrosine phosphorylation at a single site catalyzed by receptor associated jak (janus) kinases. |
|
| Publications: |
2 |
Organism: |
, Homo Sapiens |
| + |
SCF-FBW7 | down-regulates quantity by destabilization
ubiquitination
|
STAT2 |
0.291 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276766 |
|
|
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 31843895 |
These results demonstrate that the interaction between STAT2 and FBXW7 is involved in the SCF complex containing cullin 1 and RBX1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STAT2 | form complex 
binding
|
ISGF3 complex |
0.726 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240603 |
|
|
in vitro |
|
| pmid |
sentence |
| 8943351 |
The first STAT-containing transcription factor to be studied, the alpha-interferon-induced ISGF3, is composed of a Stat1:2 heterodimer and a weak DNA-binding protein, p48. The p48 and Stat1:2 heterodimer do not associate stably in the absence of DNA, but we show that amino acids approximately 150 to 250 of Stat1 and a COOH-terminal portion of p48 exhibit physical interaction, implying contact that stabilizes ISGF3 |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STAT2 | up-regulates activity
binding
|
STAT1 |
0.534 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217957 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17923090 |
We then examined STAT2 acetylation within the b-barrel DBD. A direct interaction between the STAT2-DBD (315485) and STAT1 was detected (Figure 6E) (Li et al., 1997). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ZNF804A | up-regulates activity
binding
|
STAT2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269460 |
|
|
Homo sapiens |
SH-EP Cell |
| pmid |
sentence |
| 34364876 |
Together these results indicate the formation of ZNF804A:STAT2 protein complex and its translocation from the cytoplasm into the nucleus upon IFN stimulation, suggesting that it may function as a signal transducer that activates IFN-mediated gene expression programs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IRF9 | up-regulates activity
binding
|
STAT2 |
0.919 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-217806 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 9242679 |
Coimmunoprecipitation assays demonstrate p48 association with STAT2 but not STAT1.The studies demonstrate the in vivo existence of a STAT2.p48 complex and a distinct STAT2.STAT1 complex after IFN-alpha stimulation. Data suggest that distinct bipartite complexes STAT2.p48 and STAT2.STAT1 translocate to the nucleus and associate on the DNA target site as ISGF3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
STAT2
- 
- 