| + |
MAPK8 | up-regulates activity 
phosphorylation
|
PXN |
0.689 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250129 |
Ser178 |
PPLPGALsPLYGVPE |
Rattus norvegicus |
NBT-II Cell |
| pmid |
sentence |
| 12853963 |
JNK1 phosphorylates serine 178 on paxillin, a focal adhesion adaptor, both in vitro and in intact cells. NBT-II cells expressing the Ser 178 --> Ala mutant of paxillin (Pax(S178A)) formed focal adhesions and exhibited the limited movement associated with such contacts in both single-cell-migration and wound-healing assays. In contrast, cells expressing wild-type paxillin moved rapidly and retained close contacts as the predominant adhesion. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PAK4 |
phosphorylation
|
PXN |
0.535 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164889 |
Ser272 |
ELDELMAsLSDFKIQ |
Homo sapiens |
Prostate Gland Cancer Cell |
| pmid |
sentence |
| 20406887 |
We find that pak4 is localised at focal adhesions, is immunoprecipitated with paxillin and phosphorylates paxillin on serine 272. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK1 |
phosphorylation
|
PXN |
0.658 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-146842 |
Ser272 |
ELDELMAsLSDFKIQ |
Homo sapiens |
|
| pmid |
sentence |
| 16717130 |
We show that p21-activated kinase (pak)-induced phosphorylation of serine 273 in paxillin is a critical regulator of this turnover. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPK14 |
phosphorylation
|
PXN |
0.336 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122108 |
Ser85 |
HQQPQSSsPVYGSSA |
Homo sapiens |
|
| pmid |
sentence |
| 14970194 |
Here, we show that paxillin is phosphorylated by p38mapk in vitro and in nerve growth factor (ngf)-induced pc-12 cells. Ser 85 (ser 83 for endogenous paxillin) is identified as one of major phosphorylation sites by phosphopeptide mapping and mass spectrometry. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5 | up-regulates activity
phosphorylation
|
PXN |
0.388 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278921 |
Ser85 |
HQQPQSSsPVYGSSA |
Homo sapiens |
|
| pmid |
sentence |
| 14970194 |
Thus, phosphorylation of paxillin is involved in NGF-induced neurite extension of PC-12 cells, probably through regulating focal adhesion organization.|cdk5 and p38MAPK phosphorylates Ser 85 on paxillin in vitro. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRG | up-regulates activity
dephosphorylation
|
PXN |
0.261 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254721 |
Tyr118 |
VGEEEHVySFPNKQK |
in vitro |
|
| pmid |
sentence |
| 25624455 |
PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254722 |
|
|
in vitro |
|
| pmid |
sentence |
| 25624455 |
a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PTK2 | up-regulates activity
phosphorylation, binding
|
PXN |
0.914 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-28243 |
Tyr118 |
VGEEEHVySFPNKQK |
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Paxillin is phosphorylated by FAK–Src on Tyr31 and Tyr118, and this can also promote SH2-mediated binding of Crk to paxillin. Overexpressing paxillin that is mutated at these phosphorylation sites inhibits the turnover of focal contacts6 and cell motility, which therefore supports the presence of multiple routes for FAK–Src-mediated signalling in modulating the dynamics of cell adhesion sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-28247 |
Tyr31 |
FLSEETPySYPTGNH |
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Paxillin is phosphorylated by FAK–Src on Tyr31 and Tyr118, and this can also promote SH2-mediated binding of Crk to paxillin. Overexpressing paxillin that is mutated at these phosphorylation sites inhibits the turnover of focal contacts6 and cell motility, which therefore supports the presence of multiple routes for FAK–Src-mediated signalling in modulating the dynamics of cell adhesion sites. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257732 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15688067 |
Focal adhesion kinase (FAK) is activated by growth factors and integrins during migration, and functions as a receptor-proximal regulator of cell motility. At contacts between cells and the extracellular matrix, FAK functions as an adaptor protein to recruit other focal contact proteins or their regulators, which affects the assembly or disassembly of focal contacts. Whereas it was first hypothesized that FAK might bind directly to the cytoplasmic tails of integrins, accumulated evidence supports an indirect association of FAK with integrins through binding to integrin-associated proteins such as paxillin and talin. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling, VEGF Signaling |
| + |
PTPRT | down-regulates activity 
dephosphorylation
|
PXN |
0.469 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263978 |
Tyr88 |
PQSSSPVyGSSAKTS |
Homo sapiens |
HT-29 Cell |
| pmid |
sentence |
| 27447856 |
To this end, using a phospho-proteomics approach, we identified and validated paxillin and STAT3 as the substrates of PTPRT [15, 16]|the PTPRT target site on paxillin is a previously uncharacterized tyrosine-88 residue (paxillin Y88)|In this study, we also show how pY88 paxillin transduces a signal to activate Akt |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates activity
phosphorylation
|
PXN |
0.809 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263977 |
Tyr88 |
PQSSSPVyGSSAKTS |
Homo sapiens |
HT-29 Cell |
| pmid |
sentence |
| 27447856 |
Here, we demonstrate that Src kinase directly phosphorylates Y88 paxillin|In this study, we also show how pY88 paxillin transduces a signal to activate Akt |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
PTPRR | down-regulates activity
dephosphorylation
|
PXN |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248720 |
Tyr88 |
PQSSSPVyGSSAKTS |
Homo sapiens |
|
| pmid |
sentence |
| 20133777 |
Here, we show that paxillin is a direct substrate of PTPRT and that PTPRT specifically regulates paxillin phosphorylation at tyrosine residue 88 (Y88) in colorectal cancer (CRC) cells. We engineered CRC cells homozygous for a paxillin Y88F knock-in mutant and found that these cells exhibit significantly reduced cell migration and impaired anchorage-independent growth, |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RNF5 | down-regulates quantity
ubiquitination
|
PXN |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271479 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 12861019 |
Here we demonstrate that the human homologue of RNF5 associates with the amino-terminal domain of paxillin, resulting in its ubiquitination. RNF5 requires intact RING and C-terminal domains to mediate paxillin ubiquitination. Concomitantly, RNF5 expression results in inhibition of cell motility. Via targeting of paxillin ubiquitination, which alters its localization, RNF5 emerges as a novel regulator of cell motility. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK2B | down-regulates quantity by destabilization
phosphorylation
|
PXN |
0.939 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279272 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15263022 |
P130Cas and paxillin can be phosphorylated by Fak or Pyk2, and bind directly to these kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PXN | up-regulates
binding
|
ILK |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106824 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11304546 |
Co-immunoprecipitation from fibroblasts confirmed that the association between paxillin and ilk occurs in vivo in both adherent cells and cells in suspension. [__] thus, paxillin binding is necessary for efficient focal adhesion targeting of ilk and may therefore impact the role of ilk in integrin-mediated signal transduction events. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Smooth Muscle |
| Pathways: | Integrin Signaling |
| + |
PXN | up-regulates activity
relocalization
|
IPP complex |
0.581 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265767 |
|
|
|
|
| pmid |
sentence |
| 16493410 |
Integrin-linked kinase (ILK), and isoforms of particularly interesting Cys-His-rich protein (PINCH) and parvin form the IPP complex (Fig. 2) in the cytoplasm, and this complex is recruited to focal adhesions through interactions with other factors, such as paxillin. |
|
| Publications: |
1 |
| + |
PXN | up-regulates 
|
Cell_migration |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261944 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18650496 |
Through the interactions of its multiple protein-protein binding modules, many of which are regulated by phosphorylation, paxillin serves as a platform for the recruitment of numerous regulatory and structural proteins that together control the dynamic changes in cell adhesion, cytoskeletal reorganization and gene expression that are necessary for cell migration and survival. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | VEGF Signaling |
| + |
MAP3K2 | down-regulates quantity
phosphorylation
|
PXN |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278955 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25190348 |
As MEKK2 kinase activity is required for this function, our findings support a model of paxillin modification wherein MEKK2 directly phosphorylates and targets paxillin for ubiquitylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PXN | up-regulates activity
|
BCAR1 |
0.918 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263979 |
|
|
Homo sapiens |
HT-29 Cell |
| pmid |
sentence |
| 27447856 |
Together, our data suggest that phosphorylation of paxillin Y88 activates AKT through the paxillin-p130Cas-p85/PI3K-AKT signaling axis and promotes colorectal tumorigenesis |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTK6 | up-regulates activity
phosphorylation
|
PXN |
0.63 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280102 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 33391524 |
It was also observed that the attenuation of BRK phosphorylation in turn inhibits BRK mediated activation of its direct targets, STAT3, SAM68, and Paxillin.|The EGF pathway also stimulates BRK 's phosphorylation of paxillin to promote migratory and invasive characteristics in breast cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
PXN
- 
- 