| + |
CAMK4 | down-regulates 
phosphorylation
|
STMN1 |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-34743 |
Ser16 |
KELEKRAsGQAFELI |
Homo sapiens |
|
| pmid |
sentence |
| 7925472 |
Serine 16 of oncoprotein 18 is a major cytosolic target for the ca2+/calmodulin-dependent kinase-gr. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2A | down-regulates
phosphorylation
|
STMN1 |
0.39 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59354 |
Ser16 |
KELEKRAsGQAFELI |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 9686569 |
Involved in the regulation of the microtubule (mt) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. In vitro, ser16 of recombinant human stathmin was phosphorylated also by purified cam kinase ii, and in vivo, cam kinase ii activity was indeed stimulated in cd2-triggered jurkat cells. Altogether, our results favor an association of cam kinase ii activity with costimulatory signals of t lymphocyte activation and phosphorylation of stathmin on ser16. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149640 |
Ser16 |
KELEKRAsGQAFELI |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 16982419 |
Involved in the regulation of the microtubule (mt) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. In vitro, ser16 of recombinant human stathmin was phosphorylated also by purified cam kinase ii, and in vivo, cam kinase ii activity was indeed stimulated in cd2-triggered jurkat cells. Altogether, our results favor an association of cam kinase ii activity with costimulatory signals of t lymphocyte activation and phosphorylation of stathmin on ser16. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKACA | down-regulates
phosphorylation
|
STMN1 |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-38318 |
Ser16 |
KELEKRAsGQAFELI |
Homo sapiens |
|
| pmid |
sentence |
| 8376365 |
Phosphorylation at either ser(16) or ser(63) strongly reduced or abolished the ability of stathmin to bind to and sequester soluble tubulin and its ability to act as a catastrophe factor by directly binding to the microtubules. The known in vivo phosphorylation sites of stathmin are ser-16 and ser-63 for cyclic amp-dependent protein kinase (pka). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36370 |
Ser16 |
KELEKRAsGQAFELI |
Homo sapiens |
T-lymphocyte, Leukemia Cell |
| pmid |
sentence |
| 8125092 |
Phosphorylation of either serine 16 or 63 is sufficient to inhibit stathmin in vitro. Phosphorylation at ser-63 reduces tubulin binding 10-fold and suppresses the mt polymerization inhibition activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-38322 |
Ser63 |
AAEERRKsHEAEVLK |
Homo sapiens |
|
| pmid |
sentence |
| 8376365 |
Phosphorylation at either ser(16) or ser(63) strongly reduced or abolished the ability of stathmin to bind to and sequester soluble tubulin and its ability to act as a catastrophe factor by directly binding to the microtubules. The known in vivo phosphorylation sites of stathmin are ser-16 and ser-63 for cyclic amp-dependent protein kinase (pka). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36374 |
Ser63 |
AAEERRKsHEAEVLK |
Homo sapiens |
|
| pmid |
sentence |
| 8125092 |
Phosphorylation of either serine 16 or 63 is sufficient to inhibit stathmin in vitro. Phosphorylation at ser-63 reduces tubulin binding 10-fold and suppresses the mt polymerization inhibition activity. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CAMK2B | down-regulates
phosphorylation
|
STMN1 |
0.509 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-59358 |
Ser16 |
KELEKRAsGQAFELI |
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 9686569 |
Stimulation via cd2 activated multiple signal transduction pathways, resulting in phosphorylation of distinct sites of stathmin. Ser16 of recombinant human stathmin was phosphorylated also by purified cam kinase ii, and in vivo, cam kinase ii activity was indeed stimulated in cd2-triggered jurkat cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 | down-regulates
phosphorylation
|
STMN1 |
0.385 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-119483 |
Ser16 |
KELEKRAsGQAFELI |
Homo sapiens |
|
| pmid |
sentence |
| 14645234 |
Pak1 phosphorylates op18/stathmin specifically at serine 16 and inactivates its catastrophe promoting activity in biochemical and time lapse microscopy microtubule assembly assays. Furthermore, phosphorylation of either serine 16 or 63 is sufficient to inhibit op18/stathmin in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183503 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
| pmid |
sentence |
| 19162178 |
The hgf-induced wave2 transport, lamellipodia formation, stathmin/op18 phosphorylation at ser38 and binding to kinesin-wave2 complex, but not stathmin/op18 phosphorylation at ser25 and microtubule growth, were abrogated by pak1 inhibitor ipa-3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-79955 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
| pmid |
sentence |
| 10913145 |
We find that, in vitro, pak1 phosphorylates op18/stathmin specifically at serine 16 and inactivates its catastrophe promoting activity in biochemical and time lapse microscopy microtubule assembly assays. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PAK4 | down-regulates activity
phosphorylation
|
STMN1 |
0.289 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280058 |
Ser16 |
KELEKRAsGQAFELI |
Homo sapiens |
|
| pmid |
sentence |
| 20805321 |
Indeed, we show here that inactivating phosphorylation of the endogenous stathmin on serine-16 is also induced by the active PAK4 in mitotic egg extract and is likely to participate in the observed stabilization of the MT asters ( xref , right). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK3 | down-regulates activity
phosphorylation
|
STMN1 |
0.569 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249482 |
Ser25 |
QAFELILsPRSKESV |
Homo sapiens |
|
| pmid |
sentence |
| 9731215 |
Stress-induced stathmin phosphorylation is not de- pendent on ERK. Stathmin is also known to be phos- phorylated by ERK on Ser-25 and Ser-38 (17). Thus, it is possible that ERK phosphorylates stathmin in 293 cells|In subsequent reports (28, 29) it was shown that phosphorylation of stathmin blocks its ability to destabilize MTs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249483 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
| pmid |
sentence |
| 9731215 |
Stress-induced stathmin phosphorylation is not de- pendent on ERK. Stathmin is also known to be phos- phorylated by ERK on Ser-25 and Ser-38 (17). Thus, it is possible that ERK phosphorylates stathmin in 293 cells|In subsequent reports (28, 29) it was shown that phosphorylation of stathmin blocks its ability to destabilize MTs. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCB | down-regulates
phosphorylation
|
STMN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-50594 |
Ser25 |
QAFELILsPRSKESV |
Homo sapiens |
|
| pmid |
sentence |
| 9271428 |
Op18 is multisite phosphorylated on four ser residues during mitosis;two of these ser residues, ser-25 and ser-38, are targets for cyclin-dependent protein kinases. our findings suggest that stathmin phosphorylation in reh6 cells could be in part mediated by pkc activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-30353 |
Ser25 |
QAFELILsPRSKESV |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 7637391 |
Op18 is multisite phosphorylated on four ser residues during mitosis;two of these ser residues, ser-25 and ser-38, are targets for cyclin-dependent protein kinases. our findings suggest that stathmin phosphorylation in reh6 cells could be in part mediated by pkc activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-30357 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
Leukemia Cell |
| pmid |
sentence |
| 7637391 |
Op18 is multisite phosphorylated on four ser residues during mitosis;two of these ser residues, ser-25 and ser-38, are targets for cyclin-dependent protein kinases. our findings suggest that stathmin phosphorylation in reh6 cells could be in part mediated by pkc activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-50598 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
| pmid |
sentence |
| 9271428 |
Op18 is multisite phosphorylated on four ser residues during mitosis;two of these ser residues, ser-25 and ser-38, are targets for cyclin-dependent protein kinases. our findings suggest that stathmin phosphorylation in reh6 cells could be in part mediated by pkc activation. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
MAPK13 | down-regulates
phosphorylation
|
STMN1 |
0.403 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-37848 |
Ser25 |
QAFELILsPRSKESV |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 8325880 |
Serine 25 of oncoprotein 18 is a major cytosolic target for the mitogen-activated protein kinase|The present study shows that the MAP kinase has a 20-fold preference for Ser25 as opposed to Ser38 of Op18, while cdc2 kinases have a 5-fold preference for the Ser38 residue. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-36362 |
Ser25 |
QAFELILsPRSKESV |
Homo sapiens |
T-lymphocyte, Leukemia Cell |
| pmid |
sentence |
| 8125092 |
Serine 25 of oncoprotein 18 is a major cytosolic target for the mitogen-activated protein kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-25826 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 8325880 |
Serine 25 of oncoprotein 18 is a major cytosolic target for the mitogen-activated protein kinase. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CDK1 | up-regulates activity 
phosphorylation
|
STMN1 |
0.634 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279803 |
Ser25 |
QAFELILsPRSKESV |
Homo sapiens |
|
| pmid |
sentence |
| 8125092 |
|
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279802 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
| pmid |
sentence |
| 8125092 |
|
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
UHMK1 | down-regulates
phosphorylation
|
STMN1 |
0.52 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182489 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
| pmid |
sentence |
| 19033656 |
This promigratory phenotype resulted from increased stathmin protein levels, caused by a lack of kis-mediated stathmin phosphorylation at serine 38 and diminished stathmin protein degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK10 | down-regulates
phosphorylation
|
STMN1 |
0.307 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166690 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
| pmid |
sentence |
| 20630875 |
Involved in the regulation of the microtubule (mt) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Here we show that in response to hyperosmotic stress, jnk phosphorylates a key cytoplasmic microtubule regulatory protein, stathmin (stmn), on conserved ser-25 and ser-38 residues. In in vitro biochemical studies, we identified stmn ser-38 as the critical residue required for efficient phosphorylation by jnk and identified a novel kinase interaction domain in stmn required for recognition by jnk. We revealed that jnk was required for microtubule stabilization in response to hyperosmotic stress. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK8 | down-regulates
phosphorylation
|
STMN1 |
0.324 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166694 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
| pmid |
sentence |
| 20630875 |
Involved in the regulation of the microtubule (mt) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Here we show that in response to hyperosmotic stress, jnk phosphorylates a key cytoplasmic microtubule regulatory protein, stathmin (stmn), on conserved ser-25 and ser-38 residues. In in vitro biochemical studies, we identified stmn ser-38 as the critical residue required for efficient phosphorylation by jnk and identified a novel kinase interaction domain in stmn required for recognition by jnk. We revealed that jnk was required for microtubule stabilization in response to hyperosmotic stress. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5 | down-regulates
phosphorylation
|
STMN1 |
0.387 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166682 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
| pmid |
sentence |
| 20630875 |
Involved in the regulation of the microtubule (mt) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. The kinases involved in phosphorylating stmn ser-16 and ser-63 include camp-dependent protein kinase (pka) and pak1, whereas stmn ser-25 and ser-38 have been shown to be targets for proline-directed serine/threonine kinases such as cyclin-dependent kinases, erk1/2, and members of the p38 mapk subfamily. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK9 | down-regulates
phosphorylation
|
STMN1 |
0.26 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166698 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
| pmid |
sentence |
| 20630875 |
Involved in the regulation of the microtubule (mt) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Here we show that in response to hyperosmotic stress, jnk phosphorylates a key cytoplasmic microtubule regulatory protein, stathmin (stmn), on conserved ser-25 and ser-38 residues. In in vitro biochemical studies, we identified stmn ser-38 as the critical residue required for efficient phosphorylation by jnk and identified a novel kinase interaction domain in stmn required for recognition by jnk. We revealed that jnk was required for microtubule stabilization in response to hyperosmotic stress. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK1 | down-regulates
phosphorylation
|
STMN1 |
0.445 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166686 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
| pmid |
sentence |
| 20630875 |
Involved in the regulation of the microtubule (mt) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. The kinases involved in phosphorylating stmn ser-16 and ser-63 include camp-dependent protein kinase (pka) and pak1, whereas stmn ser-25 and ser-38 have been shown to be targets for proline-directed serine/threonine kinases such as cyclin-dependent kinases, erk1/2, and members of the p38 mapk subfamily. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
JNK | down-regulates
phosphorylation
|
STMN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269982 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20630875 |
Involved in the regulation of the microtubule (mt) filament system by destabilizing microtubules. Prevents assembly and promotes disassembly of microtubules. Here we show that in response to hyperosmotic stress, jnk phosphorylates a key cytoplasmic microtubule regulatory protein, stathmin (stmn), on conserved ser-25 and ser-38 residues. In in vitro biochemical studies, we identified stmn ser-38 as the critical residue required for efficient phosphorylation by jnk and identified a novel kinase interaction domain in stmn required for recognition by jnk. We revealed that jnk was required for microtubule stabilization in response to hyperosmotic stress. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERK1/2 | down-regulates activity
phosphorylation
|
STMN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270182 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 9731215 |
Stress-induced stathmin phosphorylation is not de- pendent on ERK. Stathmin is also known to be phos- phorylated by ERK on Ser-25 and Ser-38 (17). Thus, it is possible that ERK phosphorylates stathmin in 293 cells|In subsequent reports (28, 29) it was shown that phosphorylation of stathmin blocks its ability to destabilize MTs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
Gbeta | down-regulates activity
phosphorylation
|
STMN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270082 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 9731215 |
Stress-induced stathmin phosphorylation is not de- pendent on ERK. Stathmin is also known to be phos- phorylated by ERK on Ser-25 and Ser-38 (17). Thus, it is possible that ERK phosphorylates stathmin in 293 cells|In subsequent reports (28, 29) it was shown that phosphorylation of stathmin blocks its ability to destabilize MTs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
STMN1 | down-regulates
binding
|
TTL |
0.401 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-193465 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23624152 |
Stathmin depresses ttl tubulin tyrosination activityin vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AURKA | down-regulates activity
phosphorylation
|
STMN1 |
0.399 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278913 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33037191 |
Inhibition of AURKA activity activates stathmin function via reduced phosphorylation and facilitates microtubule destabilization in RB1 -/- cells, heavily impacting the bipolar spindle formation and inducing mitotic cell death selectively in RB1 -/- cells.|Two serine phosphorylation sites, Ser16 and Ser63, in stathmin contain a consensus sequence for AURKA phosphorylation and the mutations in these two serine sites abolished stathmin phosphorylation by AURKA, suggesting that stathmin is a substrate of AURKA for phosphorylation xref , xref . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
STMN1
- 
- 