| + |
JAK1 | up-regulates 
phosphorylation
|
TYK2 |
0.5 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-43080 |
Tyr1054 |
AVPEGHEyYRVREDG |
Homo sapiens |
|
| pmid |
sentence |
| 8702790 |
These results indicate that tyk2 is activated by phosphorylation on tyr-1054 and/or tyr-1055 and that this phosphorylation requires another kinase, most likely jak1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256221 |
Tyr1054 |
AVPEGHEyYRVREDG |
Homo sapiens |
Keratinocyte |
| pmid |
sentence |
| 30029643 |
Since Jak-STAT pathway primarily activated in IL-15-me- diated cell proliferation, we tested whether it is also participates in IL-15-mediated proliferation of FAPs. Interestingly, we found the expression of phospho-Jak3 and phospho-Tyk2, as well as their downstream, phospho- STAT3 and phospho-STAT5, was significantly upregulated |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-43084 |
Tyr1055 |
VPEGHEYyRVREDGD |
Homo sapiens |
|
| pmid |
sentence |
| 8702790 |
These results indicate that tyk2 is activated by phosphorylation on tyr-1054 and/or tyr-1055 and that this phosphorylation requires another kinase, most likely jak1. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, EBV infection, Inflammosome Activation, SARS-CoV INFLAMMATORY RESPONSE |
| + |
TYK2 | up-regulates activity
phosphorylation
|
TYK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-43088 |
Tyr1054 |
AVPEGHEyYRVREDG |
Homo sapiens |
Fibroblast |
| pmid |
sentence |
| 8702790 |
These results indicate that tyk2 is activated by phosphorylation on tyr-1054 and/or tyr-1055The K930R mutant, bearing a mutation in the ATP binding site, is catalytically inactive (Fig. 3B, lanes 5 and 6). This protein is not basally phosphorylated, while the wt and the Y1054F/Y1055F proteins are (Fig. 3A), suggesting that autophosphorylation is responsible for the basal level of phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-43092 |
Tyr1055 |
VPEGHEYyRVREDGD |
Homo sapiens |
Fibroblast |
| pmid |
sentence |
| 8702790 |
These results indicate that tyk2 is activated by phosphorylation on tyr-1054 and/or tyr-1055The K930R mutant, bearing a mutation in the ATP binding site, is catalytically inactive (Fig. 3B, lanes 5 and 6). This protein is not basally phosphorylated, while the wt and the Y1054F/Y1055F proteins are (Fig. 3A), suggesting that autophosphorylation is responsible for the basal level of phosphorylation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, EBV infection, Inflammosome Activation, SARS-CoV INFLAMMATORY RESPONSE |
| + |
PTPRC | down-regulates activity 
dephosphorylation
|
TYK2 |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248357 |
Tyr1054 |
AVPEGHEyYRVREDG |
Mus musculus |
|
| pmid |
sentence |
| 11201744 |
CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling|these results show that CD45 dephosphorylates functionally important tyrosine residues. It should be noted that, as with our phosphatase assays in vitro, Tyr 1022 and Tyr 1023 of JAK1, Tyr 1007 and Tyr 1008 of JAK2, and Tyr 1054 and Tyr 1055 of Tyk2 are indeed hyperphosphorylated in cd45-deficient cells |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248358 |
Tyr1055 |
VPEGHEYyRVREDGD |
Mus musculus |
|
| pmid |
sentence |
| 11201744 |
CD45 is a JAK phosphatase and negatively regulates cytokine receptor signalling|these results show that CD45 dephosphorylates functionally important tyrosine residues. It should be noted that, as with our phosphatase assays in vitro, Tyr 1022 and Tyr 1023 of JAK1, Tyr 1007 and Tyr 1008 of JAK2, and Tyr 1054 and Tyr 1055 of Tyk2 are indeed hyperphosphorylated in cd45-deficient cells |
|
| Publications: |
2 |
Organism: |
Mus Musculus |
| + |
TYK2 | up-regulates
phosphorylation
|
DUSP3 |
0.268 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157655 |
Tyr138 |
SPTLVIAyLMMRQKM |
Homo sapiens |
|
| pmid |
sentence |
| 17785772 |
Phosphorylation of vhr at tyr(138) was required for its phosphatase activity toward stat5. In addition, the src homology 2 domain of stat5 was required for the effective dephosphorylation of stat5 by vhr. The tyrosine kinase tyk2, which mediates the phosphorylation of stat5, was also responsible for the phosphorylation of vhr at tyr(138). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TYK2 | up-regulates activity
phosphorylation
|
IFNAR1 |
0.908 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246934 |
Tyr466 |
VFLRCINyVFFPSLK |
in vitro |
|
| pmid |
sentence |
| 8605876 |
We demonstrate that, in vitro, p135tyk2 phosphorylates two tyrosines on IFNaR1. A phosphopeptide corresponding to the major phosphorylation site (Tyr466) binds STAT2, but not STAT1, in an SH-2-dependent manner. Furthermore, only latent, non-phosphorylated STAT2 interacts with this phosphopeptide. When this phosphopeptide is introduced into permeabilized cells, the IFN alpha-dependent tyrosine phosphorylation of both STATs is blocked. Finally, mutant versions of IFNaR1, in which Tyr466 is changed to phenylalanine, can act in a dominant negative manner to inhibit phosphorylation of STAT2. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246939 |
Tyr481 |
PSSSIDEyFSEQPLK |
Homo sapiens |
|
| pmid |
sentence |
| 7526154 |
In this report, we demonstrate that the alpha subunit of the type I IFN receptor (IFN-R) corresponds to the product of a previously cloned receptor subunit cDNA and, further, that the p135tyk2 tyrosine kinase directly binds and tyrosine phosphorylates this receptor subunit.These data support the hypothesis that the Tyk2 protein functions as part of a receptor complex to initiate intracellular signaling in response to type I IFNs |
|
| Publications: |
2 |
Organism: |
In Vitro, Homo Sapiens |
| + |
TYK2 | up-regulates activity
phosphorylation
|
STAT1 |
0.768 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246943 |
Tyr701 |
DGPKGTGyIKTELIS |
in vitro |
|
| pmid |
sentence |
| 7657660 |
Co-expression of Stat1 with Tyk2, Jak1, or Jak2 resulted in the specific tyrosine phosphorylation of Stat1 at Tyr701Phosphorylation of purified Stat1 was necessary and sufficient for the acquisition of DNA binding activity. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | EBV infection |
| + |
IL15RA | up-regulates
|
TYK2 |
0.248 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256253 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30029643 |
Since Jak-STAT pathway primarily activated in IL-15-me- diated cell proliferation, we tested whether it is also participates in IL-15-mediated proliferation of FAPs. Interestingly, we found the expression of phospho-Jak3 and phospho-Tyk2, as well as their downstream, phospho- STAT3 and phospho-STAT5, was significantly upregulated |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IFNAR | up-regulates activity
binding
|
TYK2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260146 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15120645 |
Despite signaling through distinct receptor complexes, type I IFNs and IFN-lambda activate similar signaling events and biological activities, consistent with their common ability to mediate an antiviral state in cells (Fig. 6). In both cases, receptor engagement leads via the activation of the Jak kinases Jak1 and Tyk2 to the activation of the IFN-stimulated gene factor 3 (ISGF3) transcription complex, composed of latent transcriptional factors of the Signal Transducers and Activators of Transcription (STAT) family, Stat1 and Stat2, and of the interferon regulatory factor (IRF) IRF9 (ISGF3g or p48). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, EBV infection, Inflammosome Activation, SARS-CoV INFLAMMATORY RESPONSE |
| + |
IL23R | up-regulates
binding
|
TYK2 |
0.565 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87841 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 12023369 |
Il-23 activates the same jak-stat signaling molecules as il-12: jak2, tyk2, and stat1, -3, -4, and -5, but stat4 activation is substantially weaker and different dna-binding stat complexes form in response to il-23 compared with il-12. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IFNLR1 | up-regulates
binding
|
TYK2 |
0.541 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124483 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15120645 |
Despite signaling through distinct receptor complexes, type i ifns and ifn-_s activate similar signaling events and biological activities, consistent with their common ability to mediate an antiviral state in cells (fig. 6). In both cases, receptor engagement leads via the activation of the jak kinases jak1 and tyk2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TYK2 | up-regulates
phosphorylation
|
STAT3 |
0.677 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256255 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30029643 |
Since Jak-STAT pathway primarily activated in IL-15-me- diated cell proliferation, we tested whether it is also participates in IL-15-mediated proliferation of FAPs. Interestingly, we found the expression of phospho-Jak3 and phospho-Tyk2, as well as their downstream, phospho- STAT3 and phospho-STAT5, was significantly upregulated |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-71781 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10542297 |
Stat3 activation requires kinase function of tyk2. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection |
| + |
TYK2 | up-regulates activity
phosphorylation
|
ISGF3 complex |
0.721 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260148 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15120645 |
Despite signaling through distinct receptor complexes, type I IFNs and IFN-lambda activate similar signaling events and biological activities, consistent with their common ability to mediate an antiviral state in cells (Fig. 6). In both cases, receptor engagement leads via the activation of the Jak kinases Jak1 and Tyk2 to the activation of the IFN-stimulated gene factor 3 (ISGF3) transcription complex, composed of latent transcriptional factors of the Signal Transducers and Activators of Transcription (STAT) family, Stat1 and Stat2, and of the interferon regulatory factor (IRF) IRF9 (ISGF3g or p48). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | COVID-19 Causal Network, Inflammosome Activation, SARS-CoV INFLAMMATORY RESPONSE |
| + |
IFNB1 | up-regulates 
|
TYK2 |
0.534 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-80103 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10918594 |
Early events in type i ifn signaling are tyrosine phosphorylation of the type i ifn receptor subunits (ifnar1 and ifnar2), and the activation of the receptor-associated tyk-2 and jak-1 janus kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | EBV infection |
| + |
PTPN6 | down-regulates 
|
TYK2 |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119200 |
|
|
Homo sapiens |
Breast Cancer Cell, Leukemia Cell, Lymphoma Cell, JURKAT Cell, RAMOS Cell |
| pmid |
sentence |
| 14624462 |
We find, for the first time, that shp-1 down-regulates the level of tyk2 kinase in h9 cells and of jak1 kinase in htb26 cells, by accelerating their degradation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN1 | down-regulates activity
dephosphorylation
|
TYK2 |
0.627 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134564 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15780598 |
Upon ligand binding, IL-2R , IL-6R or LeptinR , IFN-_R , IFN-_R and PRLR or growth hormone (GH) receptor associated JAKs become activated. These JAKs mediate phosphorylation of specific tyrosine residues and recruit STATs. Activated STATs are released from the receptor and translocate to the nucleus. PTP1B dephosphorylates JAK2, TYK2 and STAT5 . The 45-kDa form of TC-PTP was shown to dephosphorylate JAK1 and JAK3 as well as STAT1, STAT3 and STAT5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IL22RA1 | up-regulates
binding
|
TYK2 |
0.522 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90165 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12087100 |
Il-22 activates jak1 and tyk2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
IL13RA1 | up-regulates
binding
|
TYK2 |
0.542 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-100756 |
|
|
Homo sapiens |
T-lymphocyte, Macrophage, Monocyte |
| pmid |
sentence |
| 12704343 |
IL-4R, ?c, and IL-13R1 All contain proline-rich box-1 regions that bind jak1, jak3, and tyk2, respectivelyil-4 uses the type ii receptor, and IL-13R1 Binds tyk2. Il-13 results in activation of jak1 and tyk2 in hematopoietic and nonhematopoietic cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Lung, Smooth Muscle |
| + |
IL10RB | up-regulates
binding
|
TYK2 |
0.636 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-68013 |
|
|
Homo sapiens |
Macrophage, B-lymphocyte |
| pmid |
sentence |
| 10347215 |
Specifically, il-10 effects the activation of jak1 (associated with the il-10 receptor ? Chain) and tyk2 (associated with the il-10 receptor ? Chain) and induces the activation of stat1, stat3, and, in some cells, stat5. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
TYK2
- 
- 