| + |
PRKCQ | up-regulates activity 
phosphorylation
|
PTPN7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276045 |
Ser246 |
QYQEERRsVKHILFS |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 16479000 |
PKC θ is required for HePTP translocation to the immune synapse. PKC θ phosphorylates HePTP at S225 in primary T cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCD | up-regulates activity
phosphorylation
|
PTPN7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276048 |
Ser246 |
QYQEERRsVKHILFS |
in vitro |
|
| pmid |
sentence |
| 16479000 |
HePTP is phosphorylated by PKC isozymes at Ser-225 in vitro. While all isozymes phosphorylated Ser-225 predominantly and Ser-113 to a lesser extent (Fig. (Fig.5),5), they differed strikingly in how much 32P they incorporated into HePTP during the 30-min assay. PKC θ was the most efficient, while PKC ζ and PKC μ were clearly less potent; PKC δ, ɛ, and η were quite inefficient. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKD1 | up-regulates activity
phosphorylation
|
PTPN7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276046 |
Ser246 |
QYQEERRsVKHILFS |
in vitro |
|
| pmid |
sentence |
| 16479000 |
HePTP is phosphorylated by PKC isozymes at Ser-225 in vitro. While all isozymes phosphorylated Ser-225 predominantly and Ser-113 to a lesser extent (Fig. (Fig.5),5), they differed strikingly in how much 32P they incorporated into HePTP during the 30-min assay. PKC θ was the most efficient, while PKC ζ and PKC μ were clearly less potent; PKC δ, ɛ, and η were quite inefficient. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCE | up-regulates activity
phosphorylation
|
PTPN7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276050 |
Ser246 |
QYQEERRsVKHILFS |
in vitro |
|
| pmid |
sentence |
| 16479000 |
HePTP is phosphorylated by PKC isozymes at Ser-225 in vitro. While all isozymes phosphorylated Ser-225 predominantly and Ser-113 to a lesser extent (Fig. (Fig.5),5), they differed strikingly in how much 32P they incorporated into HePTP during the 30-min assay. PKC θ was the most efficient, while PKC ζ and PKC μ were clearly less potent; PKC δ, ɛ, and η were quite inefficient. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCH | up-regulates activity
phosphorylation
|
PTPN7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276049 |
Ser246 |
QYQEERRsVKHILFS |
in vitro |
|
| pmid |
sentence |
| 16479000 |
HePTP is phosphorylated by PKC isozymes at Ser-225 in vitro. While all isozymes phosphorylated Ser-225 predominantly and Ser-113 to a lesser extent (Fig. (Fig.5),5), they differed strikingly in how much 32P they incorporated into HePTP during the 30-min assay. PKC θ was the most efficient, while PKC ζ and PKC μ were clearly less potent; PKC δ, ɛ, and η were quite inefficient. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
PTPN7 |
0.263 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276047 |
Ser246 |
QYQEERRsVKHILFS |
in vitro |
|
| pmid |
sentence |
| 16479000 |
HePTP is phosphorylated by PKC isozymes at Ser-225 in vitro. While all isozymes phosphorylated Ser-225 predominantly and Ser-113 to a lesser extent (Fig. (Fig.5),5), they differed strikingly in how much 32P they incorporated into HePTP during the 30-min assay. PKC θ was the most efficient, while PKC ζ and PKC μ were clearly less potent; PKC δ, ɛ, and η were quite inefficient. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKACA | down-regulates 
phosphorylation
|
PTPN7 |
0.367 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-72147 |
Ser44 |
RLQERRGsNVALMLD |
Homo sapiens |
|
| pmid |
sentence |
| 10559944 |
Here we show that cyclic-amp-dependent protein kinase (pka) phosphorylates serine residue 23 in the kim of heptp in vitro and in intact cells. This modification reduces binding of map kinases to the kim, an effect that is prevented by mutation of serine 23 to alanine. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182522 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19047375 |
B2 adrenergic receptor stimulation induces the pka dependent phosphorylation of heptp and releases bound p38 mapk |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | up-regulates activity
phosphorylation
|
PTPN7 |
0.68 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249475 |
Ser93 |
ALQRQPPsPKQLEEE |
in vitro |
|
| pmid |
sentence |
| 16226275 |
First, Erk phosphorylates HePTP at residues Thr45 and Ser72. Second, HePTP dephosphorylates Erk at PTyr185.| |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249476 |
Thr66 |
EPICSVNtPREVTLH |
in vitro |
|
| pmid |
sentence |
| 16226275 |
First, Erk phosphorylates HePTP at residues Thr45 and Ser72. Second, HePTP dephosphorylates Erk at PTyr185.| |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MAPK1 | up-regulates activity
phosphorylation
|
PTPN7 |
0.805 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249436 |
Ser93 |
ALQRQPPsPKQLEEE |
in vitro |
|
| pmid |
sentence |
| 16226275 |
First, Erk phosphorylates HePTP at residues Thr45 and Ser72. Second, HePTP dephosphorylates Erk at PTyr185.| |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249437 |
Thr66 |
EPICSVNtPREVTLH |
in vitro |
|
| pmid |
sentence |
| 16226275 |
First, Erk phosphorylates HePTP at residues Thr45 and Ser72. Second, HePTP dephosphorylates Erk at PTyr185.| |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MAPK14 | down-regulates activity
phosphorylation
|
PTPN7 |
0.584 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250109 |
Ser93 |
ALQRQPPsPKQLEEE |
in vitro |
|
| pmid |
sentence |
| 10206983 |
The noncatalytic N terminus of HePTP binds Erk and p38 and is phosphorylated at Ser-72 and Thr-45 by these kinases. the N terminus of HePTP binds Erk and p38 but may release them upon phosphorylation.it is clear that phosphorylation of HePTP at Thr-45 and/or Ser-72 is not required for inhibition of MAP kinase. Rather, it seems that phosphorylation has the opposite effect, namely to lessen the inhibitory effect of HePTP. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250110 |
Thr66 |
EPICSVNtPREVTLH |
in vitro |
|
| pmid |
sentence |
| 10206983 |
The noncatalytic N terminus of HePTP binds Erk and p38 and is phosphorylated at Ser-72 and Thr-45 by these kinases. the N terminus of HePTP binds Erk and p38 but may release them upon phosphorylation.it is clear that phosphorylation of HePTP at Thr-45 and/or Ser-72 is not required for inhibition of MAP kinase. Rather, it seems that phosphorylation has the opposite effect, namely to lessen the inhibitory effect of HePTP. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PTPN7 | down-regulates activity
dephosphorylation
|
MAPK14 |
0.584 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248485 |
Tyr182 |
TDDEMTGyVATRWYR |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 10206983 |
In Jurkat cells, LC-PTP suppressed the ERK and p38 mitogen-activated protein kinase cascades |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN7 | down-regulates activity
dephosphorylation
|
MAPK1 |
0.805 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248483 |
Tyr187 |
HTGFLTEyVATRWYR |
Homo sapiens |
|
| pmid |
sentence |
| 16226275 |
First, Erk phosphorylates HePTP at residues Thr45 and Ser72. Second, HePTP dephosphorylates Erk at PTyr185 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248484 |
Tyr187 |
HTGFLTEyVATRWYR |
Homo sapiens |
|
| pmid |
sentence |
| 10702794 |
HePTP efficiently dephosphorylated active ERK2 on the tyrosine residue in the activation loop in vitro. Together, these data identify ERK2 as a specific and direct target of HePTP and are consistent with a model in which HePTP negatively regulates ERK2 activity as part of a feedback mechanism |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | up-regulates activity
phosphorylation
|
PTPN7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270202 |
|
|
in vitro |
|
| pmid |
sentence |
| 16226275 |
First, Erk phosphorylates HePTP at residues Thr45 and Ser72. Second, HePTP dephosphorylates Erk at PTyr185.| |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CD40LG | down-regulates 
|
PTPN7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182519 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 19047375 |
Coimmunoprecipitation and western blot analysis showed that heptp was phosphorylated in a pka-dependent manner, which inactivated heptp and allowed for increased free p38 mapk to be phosphorylated by the mapk cascade that was activated by cd40l |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Gbeta | up-regulates activity
phosphorylation
|
PTPN7 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270111 |
|
|
in vitro |
|
| pmid |
sentence |
| 16226275 |
First, Erk phosphorylates HePTP at residues Thr45 and Ser72. Second, HePTP dephosphorylates Erk at PTyr185.| |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PTPN7 | down-regulates
binding
|
MAPK14 |
0.584 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182525 |
|
|
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 19047375 |
Thus, beta(2)ar stimulation on a b cell phosphorylates and inactivates heptp in a gs/camp/pka-dependent manner to release bound p38 mapk, making more available for phosphorylation and subsequent ige regulation |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN7 | down-regulates
dephosphorylation
|
MAPK1 |
0.805 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-69448 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10415025 |
Lc-ptp dephosphorylated erk2 in vitro. the complex formation of lc-ptp with erk is the essential mechanism for the suppression. Taken collectively, these results indicate that lc-ptp suppresses mitogen-activated protein kinase directly in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
PTPN7
- 
- 