| + |
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 |
0.29 |
| 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 |
0.312 |
| 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 |
0.31 |
| 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 |
| + |
AKT1 | up-regulates quantity by stabilization 
phosphorylation
|
VIM |
0.629 |
| 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 |
0.29 |
| 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 |
| + |
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 |
| + |
CDK1 | down-regulates
phosphorylation
|
VIM |
0.369 |
| 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 |
phosphorylation
|
VIM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-134520 |
Ser56 |
SRSLYASsPGGVYAT |
Homo sapiens |
|
| pmid |
sentence |
| 15766329 |
In the present study, pak1 was able to phosphorylate vimentin on ser-56 in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| + |
ROCK1 | down-regulates activity
phosphorylation
|
VIM |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248998 |
Ser72 |
SSAVRLRsSVPGVRL |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 9565595 |
We found that vimentin, the most widely expressed intermediate filament protein, served as an excellent substrate for Rho-associated kinase (Rho-kinase) and that vimentin phosphorylated by Rho-kinase lost its ability to form filaments in vitro. Two amino-terminal sites on vimentin, Ser38 and Ser71, were identified as the major phosphorylation sites for Rho-kinase, and Ser71 was the most favored and unique phosphorylation site for Rho-kinase in vitro. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
AURKB | down-regulates
phosphorylation
|
VIM |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-96057 |
Ser73 |
SAVRLRSsVPGVRLL |
Homo sapiens |
|
| pmid |
sentence |
| 12458200 |
By identifying eight aurora-b phosphorylation sites on vimentin in vitro, we have demonstrated that vimentin-ser-72 is an in vitrophosphorylation site of aurora-b. in vitro analyses revealed that aurora-b phosphorylates vimentin at approximately 2 mol phosphate/mol of substrate for 30 min and that this phosphorylation dramatically inhibits vimentin filament formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PLK1 | up-regulates
phosphorylation
|
VIM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159386 |
Ser83 |
GVRLLQDsVDFSLAD |
Homo sapiens |
Breast Cancer Cell |
| pmid |
sentence |
| 18056432 |
We observed that plk1 phosphorylates vimentin on ser82, which in turn regulates cell surface levels of 1 integrin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2D |
phosphorylation
|
VIM |
0.332 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250690 |
Ser83 |
GVRLLQDsVDFSLAD |
|
Vero Cell |
| pmid |
sentence |
| 16140754 |
Interestingly, viral DNA replication also resulted in the activation of calcium calmodulin-dependent protein kinase II (CaM kinase II) and phosphorylation of the N-terminal domain of vimentin on serine 82. Immunostaining showed that vimentin within the cage was phosphorylated on serine 82. |
|
| Publications: |
1 |
| + |
TOR1AIP1 | up-regulates activity
binding
|
VIM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261313 |
|
|
Homo sapiens |
Fibroblast |
| pmid |
sentence |
| 16361107 |
Co-immune precipitation studies revealed association between vimentin and torsinA in a complex. these studies suggest that mutant torsinA interferes with cytoskeletal events involving vimentin, possibly by restricting movement of these particles/filaments, and hence may affect development of neuronal pathways in the brain. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK | down-regulates activity
phosphorylation
|
VIM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269975 |
|
|
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: |
1 |
Organism: |
In Vitro |
| + |
ETV4 | up-regulates quantity by expression 
transcriptional regulation
|
VIM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254070 |
|
|
Homo sapiens |
MCF-7 Cell, MDA-MB-231 Cell |
| pmid |
sentence |
| 8895512 |
Our results suggest that PEA3 specifically transactivates vimentin promoter through PEA3 site. Among members of the ETS transcription factor family only Erg showed ability to transactivate vimentin promoter besides PEA3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERG | up-regulates quantity by expression
transcriptional regulation
|
VIM |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254069 |
|
|
Homo sapiens |
MCF-7 Cell, MDA-MB-231 Cell |
| pmid |
sentence |
| 8895512 |
Our results suggest that PEA3 specifically transactivates vimentin promoter through PEA3 site. Among members of the ETS transcription factor family only Erg showed ability to transactivate vimentin promoter besides PEA3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
VIM
- 
- 