| + |
RNF208 | down-regulates quantity by destabilization 
ubiquitination
|
VIM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269051 |
Lys97 |
DAINTEFkNTRTNEK |
Homo sapiens |
MDA-MB-231 Cell |
| pmid |
sentence |
| 31862882 |
Here, we show that RING finger protein 208 (RNF208) decreases the stability of soluble Vimentin protein through a polyubiquitin-mediated proteasomal degradation pathway, thereby suppressing metastasis of TNBC cells |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCA | down-regulates quantity by destabilization
phosphorylation
|
VIM |
0.282 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248877 |
Ser10 |
TRSVSSSsYRRMFGG |
in vitro |
|
| pmid |
sentence |
| 2500966 |
We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248878 |
Ser22 |
FGGPGTAsRPSSSRS |
in vitro |
|
| pmid |
sentence |
| 2500966 |
We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248882 |
Ser26 |
GTASRPSsSRSYVTT |
in vitro |
|
| pmid |
sentence |
| 2500966 |
We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248879 |
Ser27 |
TASRPSSsRSYVTTS |
in vitro |
|
| pmid |
sentence |
| 2500966 |
We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248880 |
Ser34 |
SRSYVTTsTRTYSLG |
in vitro |
|
| pmid |
sentence |
| 2500966 |
We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248881 |
Ser42 |
TRTYSLGsALRPSTS |
in vitro |
|
| pmid |
sentence |
| 2500966 |
We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248883 |
Ser51 |
LRPSTSRsLYASSPG |
in vitro |
|
| pmid |
sentence |
| 2500966 |
We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248884 |
Ser66 |
GVYATRSsAVRLRSS |
in vitro |
|
| pmid |
sentence |
| 2500966 |
We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248886 |
Ser7 |
sSSSYRRM |
in vitro |
|
| pmid |
sentence |
| 2500966 |
We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248876 |
Ser9 |
STRSVSSsSYRRMFG |
in vitro |
|
| pmid |
sentence |
| 2500966 |
We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. |
|
| Publications: |
10 |
Organism: |
In Vitro |
| + |
PRKACA | down-regulates activity
phosphorylation
|
VIM |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250066 |
Ser25 |
PGTASRPsSSRSYVT |
in vitro |
|
| pmid |
sentence |
| 2500966 |
Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250067 |
Ser39 |
TTSTRTYsLGSALRP |
in vitro |
|
| pmid |
sentence |
| 2500966 |
Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250070 |
Ser47 |
LGSALRPsTSRSLYA |
in vitro |
|
| pmid |
sentence |
| 2500966 |
Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250069 |
Ser51 |
LRPSTSRsLYASSPG |
in vitro |
|
| pmid |
sentence |
| 2500966 |
Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250068 |
Ser66 |
GVYATRSsAVRLRSS |
in vitro |
|
| pmid |
sentence |
| 2500966 |
Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250071 |
Ser7 |
sSSSYRRM |
in vitro |
|
| pmid |
sentence |
| 2500966 |
Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. Domain- and sequence-specific phosphorylation of vimentin induces disassembly of the filament structure. |
|
| Publications: |
6 |
Organism: |
In Vitro |
| + |
PAK2 | down-regulates activity
phosphorylation
|
VIM |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250237 |
Ser26 |
GTASRPSsSRSYVTT |
in vitro |
|
| pmid |
sentence |
| 11895474 |
In vitro analyses revealed that vimentin served as an excellent substrate for PAK. This phosphorylated vimentin lost the potential to form 10 nm filaments. We identified Ser25, Ser38, Ser50, Ser65 and Ser72 in the amino-terminal head domain as the major phosphorylation sites on vimentin for PAK. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250239 |
Ser39 |
TTSTRTYsLGSALRP |
in vitro |
|
| pmid |
sentence |
| 11895474 |
In vitro analyses revealed that vimentin served as an excellent substrate for PAK. This phosphorylated vimentin lost the potential to form 10 nm filaments. We identified Ser25, Ser38, Ser50, Ser65 and Ser72 in the amino-terminal head domain as the major phosphorylation sites on vimentin for PAK.  |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250241 |
Ser66 |
GVYATRSsAVRLRSS |
in vitro |
|
| pmid |
sentence |
| 11895474 |
In vitro analyses revealed that vimentin served as an excellent substrate for PAK. This phosphorylated vimentin lost the potential to form 10 nm filaments. We identified Ser25, Ser38, Ser50, Ser65 and Ser72 in the amino-terminal head domain as the major phosphorylation sites on vimentin for PAK. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250243 |
Ser73 |
SAVRLRSsVPGVRLL |
in vitro |
|
| pmid |
sentence |
| 11895474 |
In vitro analyses revealed that vimentin served as an excellent substrate for PAK. This phosphorylated vimentin lost the potential to form 10 nm filaments. We identified Ser25, Ser38, Ser50, Ser65 and Ser72 in the amino-terminal head domain as the major phosphorylation sites on vimentin for PAK. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
PRKCI | up-regulates activity 
phosphorylation
|
VIM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277623 |
Ser34 |
SRSYVTTsTRTYSLG |
Homo sapiens |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 33525953 |
Results suggest that aPKCs target multiple activation sites (Ser33/39/56) on Vimentin and therefore is essential for VIF dynamics regulation during the metastasis of prostate cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCZ | up-regulates activity
phosphorylation
|
VIM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277622 |
Ser34 |
SRSYVTTsTRTYSLG |
Homo sapiens |
Prostate Cancer Cell Line |
| pmid |
sentence |
| 33525953 |
Results suggest that aPKCs target multiple activation sites (Ser33/39/56) on Vimentin and therefore is essential for VIF dynamics regulation during the metastasis of prostate cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT | up-regulates quantity by stabilization
phosphorylation
|
VIM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167971 |
Ser39 |
TTSTRTYsLGSALRP |
Homo sapiens |
|
| pmid |
sentence |
| 20856200 |
The binding of akt (tail region) to vim (head region) results in vim ser39 phosphorylation enhancing the ability of vim to induce motility and invasion while protecting vim from caspase-induced proteolysis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AKT1 | up-regulates quantity by stabilization
phosphorylation
|
VIM |
0.662 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252511 |
Ser39 |
TTSTRTYsLGSALRP |
Homo sapiens |
|
| pmid |
sentence |
| 20856200 |
The binding of akt (tail region) to vim (head region) results in vim ser39 phosphorylation enhancing the ability of vim to induce motility and invasion while protecting vim from caspase-induced proteolysis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCA | down-regulates activity
phosphorylation
|
VIM |
0.282 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248885 |
Ser39 |
TTSTRTYsLGSALRP |
|
|
| pmid |
sentence |
| 2500966 |
We reported that stoichiometric phosphorylation by either cAMP-dependent protein kinase or protein kinase C induces disassembly of vimentin filaments. In the present work, we attempted to identify the sites of vimentin phosphorylated by each protein kinase. Sequential analysis of the purified phosphopeptides, together with the known primary sequence, revealed that Ser-8, Ser-9, Ser-20, Ser-25, Ser-33, and Ser-41 were specifically phosphorylated by protein kinase C, whereas Ser-46 was phosphorylated preferentially by cAMP-dependent protein kinase. Both kinases reacted with Ser-6, Ser-24, Ser-38, Ser-50, and Ser-65. |
|
| Publications: |
1 |
| + |
CDK1 | down-regulates
phosphorylation
|
VIM |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-35492 |
Ser55 |
TSRSLYAsSPGGVYA |
Homo sapiens |
|
| pmid |
sentence |
| 7983050 |
These results strongly suggest that cdc2 kinase is the kinase which phosphorylates vimentin ser55 in the entire cytoplasm during mitosis and that the appearance of immunoreactivities with antibody 4a4 in cell staining indeed reflect the vimentin phosphorylation by cdc2 kinase. immunofluorescent evidence using antibody 4a4 and biochemical analysis using vimentin ser55 peptide showed that the degree of disassembly of vimentin filament of various cell types at early mitotic phase correlated well with the amount of mitotically activated cdc2 kinase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 |
Fatal error: Uncaught TypeError: implode(): Argument #2 ($array) must be of type ?array, string given in /home/prisca/signor/relation_result.php:2084
Stack trace:
#0 /home/prisca/signor/relation_result.php(2084): implode()
#1 {main}
thrown in /home/prisca/signor/relation_result.php on line 2084
4.0
VIM
- 
- 