| + |
CSNK2A2 | up-regulates activity 
phosphorylation
|
WAS |
0.354 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251048 |
Ser483 |
KRSRAIHsSDEGEDQ |
Homo sapiens |
|
| pmid |
sentence |
| 12769847 |
We identify two phosphorylation sites in the VCA domain of WASP at serines 483 and 484. S483 and S484 are substrates for casein kinase 2 in vitro and in vivo. Phosphorylation of these residues increases the affinity of the VCA domain for the Arp2/3 complex 7-fold and is required for efficient in vitro actin polymerization by the full-length WASP molecule. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251049 |
Ser484 |
RSRAIHSsDEGEDQA |
Homo sapiens |
U-937 Cell |
| pmid |
sentence |
| 12769847 |
We identify two phosphorylation sites in the VCA domain of WASP at serines 483 and 484. S483 and S484 are substrates for casein kinase 2 in vitro and in vivo. Phosphorylation of these residues increases the affinity of the VCA domain for the Arp2/3 complex 7-fold and is required for efficient in vitro actin polymerization by the full-length WASP molecule. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CSNK2A1 | up-regulates
phosphorylation
|
WAS |
0.361 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101264 |
Ser483 |
KRSRAIHsSDEGEDQ |
Homo sapiens |
|
| pmid |
sentence |
| 12769847 |
Here we identify two phosphorylation sites in the vca domain of wasp at serines 483 and 484. S483 and s484 are substrates for casein kinase 2 in vitro and in vivo. Phosphorylation of these residues increases the affinity of the vca domain for the arp2/3 complex 7-fold and is required for efficient in vitro actin polymerization by the full-length wasp molecule. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101268 |
Ser484 |
RSRAIHSsDEGEDQA |
Homo sapiens |
|
| pmid |
sentence |
| 12769847 |
Here we identify two phosphorylation sites in the vca domain of wasp at serines 483 and 484. S483 and s484 are substrates for casein kinase 2 in vitro and in vivo. Phosphorylation of these residues increases the affinity of the vca domain for the arp2/3 complex 7-fold and is required for efficient in vitro actin polymerization by the full-length wasp molecule. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
LYN | up-regulates activity
phosphorylation
|
WAS |
0.387 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273959 |
Tyr291 |
AETSKLIyDFIEDQG |
Homo sapiens |
Macrophage |
| pmid |
sentence |
| 17890224 |
We demonstrated that WASP is phosphorylated on tyrosine 291 in macrophages, and the WASP phosphorylation is important for the phagocytic cup formation. In addition, we showed that WASP and WASP-interacting protein (WIP) form a complex at the phagocytic cup and that the WASP.WIP complex plays a critical role in the phagocytic cup formation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTK | up-regulates activity
phosphorylation
|
WAS |
0.732 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273958 |
Tyr291 |
AETSKLIyDFIEDQG |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10068673 |
These results demonstrate that WASP, under this experimental condition, can be tyrosine-phosphorylated by the kinase activity of Btk and that the direct interaction between WASP and the SH3 domain of Btk is required for this phosphorylation to occur. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
BTK |
phosphorylation
|
WAS |
0.732 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-86004 |
Tyr291 |
AETSKLIyDFIEDQG |
Homo sapiens |
|
| pmid |
sentence |
| 10068673 |
These results indicate that btk phosphorylates wasp on its tyrosine 291 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HCK | up-regulates activity
phosphorylation
|
WAS |
0.572 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251268 |
Tyr291 |
AETSKLIyDFIEDQG |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 12235133 |
Src family kinase Hck induces phosphorylation of WASp-Tyr(291). Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate actin polymerization and filopodium formation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273957 |
Tyr291 |
AETSKLIyDFIEDQG |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 12235133 |
Hck induces tyrosine phosphorylation of WASp. Here we show that the Src family kinase Hck induces phosphorylation of WASp-Tyr(291) independently of Cdc42 and that this causes a shift in the mobility of WASp upon SDS-PAGE. A phospho-mimicking mutant, WASp-Y291E, exhibited an enhanced ability to stimulate actin polymerization in a cell-free system and when microinjected into primary macrophages induced extensive filopodium formation with greater efficiency than wild-type WASp or a Y291F mutant. We propose that phosphorylation of Tyr(291) directly regulates WASp function. |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| + |
PTPN12 | down-regulates activity 
dephosphorylation
|
WAS |
0.456 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248660 |
Tyr291 |
AETSKLIyDFIEDQG |
Mus musculus |
|
| pmid |
sentence |
| 14707117 |
Mutation of tyrosine residue Y291, identified here as the major site of TCR-induced WASp tyrosine phosphorylation, abrogated induction of WASp tyrosine phosphorylation and its effector activities|WASp was tyrosine dephosphorylated by protein tyrosine phosphatase (PTP)-PEST |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
FYN | up-regulates activity
phosphorylation
|
WAS |
0.579 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273960 |
Tyr291 |
AETSKLIyDFIEDQG |
Mus musculus |
Lymphocyte |
| pmid |
sentence |
| 14707117 |
TCR-induced WASp tyrosine phosphorylation was also disrupted in T cells lacking Fyn, a kinase shown here to bind, colocalize with, and phosphorylate WASp. Although Fyn enhanced WASp-mediated Arp2/3 activation and was required for synapse formation, PTP-PEST combined with PSTPIP1 inhibited WASp-driven actin polymerization and synapse formation. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| Pathways: | T cell activation |
| + |
WAS | up-regulates activity
binding
|
ARP2/3 |
0.804 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261001 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 20498093 |
Members of the Wiskott-Aldrich syndrome protein (WASP) family, which includes WASP, N-WASP, WAVE (1–3), WHAMM, JMY, and WASH, control actin cytoskeletal dynamics throughout biology. They act in large part by regulating the actin nucleating activity of the ubiquitous Arp2/3 complex. WASP proteins stimulate Arp2/3 complex using a conserved C-terminal VCA (Verprolin homologous, central hydrophobic, and acidic) region. They contain distinct N-terminal elements, which facilitate integration into unique macromolecular complexes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | T cell activation |
| + |
CDC42 | up-regulates activity
binding
|
WAS |
0.956 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261869 |
|
|
Homo sapiens |
Blood Platelet |
| pmid |
sentence |
| 27871158 |
Cdc42 can induce Arp2/3-mediated filopodia formation through the activation of WASp (Wiskott-Aldrich syndrome proteins) and neuronal N-WASp (Rohatgi et al., 1999). Similarly, Rac1-enhanced lamellipodia formation is related to Arp2/3 activation by the WAVE (WASP-family verprolin-homologous) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPN12 | down-regulates
dephosphorylation
|
WAS |
0.456 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-111688 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11711533 |
Furthermore, we demonstrate that pstpip serves as a scaffold protein between ptp-pest and wasp and allows ptp-pest to dephosphorylate wasp. This finding suggests a possible mechanism for ptp-pest to directly modulate actin remodeling through the pstpip-wasp interaction. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121136 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 14707117 |
Furthermore, we demonstrate that pstpip serves as a scaffold protein between ptp-pest and wasp and allows ptp-pest to dephosphorylate wasp. This finding suggests a possible mechanism for ptp-pest to directly modulate actin remodeling through the pstpip-wasp interaction. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
3.0
WAS
- 
- 