| + |
MAPK9 | down-regulates 
phosphorylation
|
YWHAZ |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124031 |
Ser184 |
FYYEILNsPEKACSL |
Homo sapiens |
|
| pmid |
sentence |
| 15071501 |
Jnk phosphorylates 14-3-3zetaat ser-184 and 14-3-3sigmaat ser-188 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK10 | down-regulates
phosphorylation
|
YWHAZ |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124009 |
Ser184 |
FYYEILNsPEKACSL |
Homo sapiens |
|
| pmid |
sentence |
| 15071501 |
Jnk phosphorylates 14-3-3zetaat ser-184 and 14-3-3sigmaat ser-190 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK8 | down-regulates
phosphorylation
|
YWHAZ |
0.38 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124020 |
Ser184 |
FYYEILNsPEKACSL |
Homo sapiens |
|
| pmid |
sentence |
| 15071501 |
Jnk phosphorylated 14-3-3 at ser-184 and 14-3-3 at ser-186 both in vitro and in vivo, and such phosphorylation reduced the affinity of 14-3-3 proteins for bax |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | SAPK/JNK Signaling |
| + |
PRKCD | down-regulates activity
phosphorylation
|
YWHAZ |
0.456 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249222 |
Ser58 |
VVGARRSsWRVVSSI |
Homo sapiens |
|
| pmid |
sentence |
| 12861023 |
We confirmed that MAPKAPK2 interacted with and phosphorylated 14-3-3zeta in vitro and in HEK293 cells. | Experimentally, S58D mutation significantly impaired both 14-3-3zeta dimerization and binding to Raf-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPKAPK2 | down-regulates activity
phosphorylation
|
YWHAZ |
0.606 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250151 |
Ser58 |
VVGARRSsWRVVSSI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12861023 |
We confirmed that MAPKAPK2 interacted with and phosphorylated 14-3-3zeta in vitro and in HEK293 cells. Mutation analysis showed that MAPKAPK2 phosphorylated 14-3-3zeta at Ser-58. S58D mutation significantly impaired both 14-3-3zeta dimerization and binding to Raf-1. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | down-regulates activity
phosphorylation
|
YWHAZ |
0.541 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143373 |
Ser58 |
VVGARRSsWRVVSSI |
Homo sapiens |
|
| pmid |
sentence |
| 16376338 |
Phosphorylation by pka leads to modulation of 14-3-3zeta dimerization and affect its interaction with partner proteins. Substitution of ser58 to ala completely abolished phosphorylation of 14-3-3zeta by pka. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT1 |
phosphorylation
|
YWHAZ |
0.656 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-116587 |
Ser58 |
VVGARRSsWRVVSSI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11956222 |
Ese data indicate that pkb/akt phosphorylates ser-58 on 14-3-3zeta both in vitro and in intact cells. The functional relevance of this phosphorylation remains to be determined. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT |
phosphorylation
|
YWHAZ |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244381 |
Ser58 |
VVGARRSsWRVVSSI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11956222 |
Ese data indicate that pkb/akt phosphorylates ser-58 on 14-3-3zeta both in vitro and in intact cells. The functional relevance of this phosphorylation remains to be determined. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CSNK1A1 | down-regulates activity
phosphorylation
|
YWHAZ |
0.556 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250796 |
Thr232 |
LTLWTSDtQGDEAEA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 9360956 |
This protein kinase has been identified as casein kinase Ialpha (CKIalpha) by peptide mapping analysis and sequencing. Among mammalian 14-3-3, only 14-3-3 tau possesses a phosphorylatable residue at the same position (Ser-233), and we show that this residue is also phosphorylated by CKI. In addition, we show that 14-3-3 zeta is exclusively phosphorylated on Thr-233 in human embryonic kidney 293 cells. The residue 233 is located within a region shown to be important for the association of 14-3-3 to target proteins. | We have now shown that in vivo phosphorylation of 14-3-3 zeta at the CKIalpha site (Thr-233) negatively regulates its binding to c-Raf, and may be important in Raf-mediated signal transduction. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BCR |
phosphorylation
|
YWHAZ |
0.336 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250595 |
Thr232 |
LTLWTSDtQGDEAEA |
in vitro |
|
| pmid |
sentence |
| 16045749 |
We show here that BCR interacts with at least five isoforms of 14-3-3 in vivo and phosphorylates 14-3-3tau on Ser233 and to a lesser extent 14-3-3zeta on Thr233 |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
JNK | down-regulates
phosphorylation
|
YWHAZ |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269980 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15071501 |
Jnk phosphorylates 14-3-3zetaat ser-184 and 14-3-3sigmaat ser-190 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
YWHAZ | up-regulates quantity by stabilization 
binding
|
GEM |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261725 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 14701738 |
In order to address whether Gem binds specific isoforms of 14-3-3, we determined the coassociation of Gem and 14-3-3 in the neuroblastoma cell line SY5Y. 14-3-3ζ, -γ, -τ, and -β were observed to bind to Gem. 14-3-3-bound Gem has a twofold-longer half-life than nonbound Gem (Fig. (Fig.6).6). A similar increase in protein stability following 14-3-3 binding has been described for the Wee1 kinase |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261715 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 14701738 |
In order to address whether Gem binds specific isoforms of 14-3-3, we determined the coassociation of Gem and 14-3-3 in the neuroblastoma cell line SY5Y. 14-3-3ζ, -γ, -τ, and -β were observed to bind to Gem. 14-3-3-bound Gem has a twofold-longer half-life than nonbound Gem (Fig. (Fig.6).6). A similar increase in protein stability following 14-3-3 binding has been described for the Wee1 kinase |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| + |
YWHAZ | down-regulates activity
binding
|
NEFL |
0.282 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252397 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23230147 |
These results suggest the important role of 14-3-3 in the dynamic regulation of NF-L assembly, and in the capacity to prevent the formation of NF-L aggregates. all seven isoforms specifically interacted with NF-L, but not NF-M or NF-H. specific interaction of 14-3-3 proteins with phosphorylated NF-L subunits also indicated the role of 14-3-3 and NF-L phosphorylation in the disassembly of neurofilaments. What is more, binding of 14-3-3 to phosphorylated NF-L subunits may prevent the dephosphorylation of these subunits by phosphatases, maintaining the hyperphosphorylation state of the subunits, which facilitates the disassembly of neurofilaments. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
YWHAZ
- 
- 