| + |
ILK | up-regulates 
phosphorylation
|
NACA |
0.401 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-127631 |
Ser1906 |
PELEEQDsTQATTQQ |
Homo sapiens |
|
| pmid |
sentence |
| 15299025 |
The inactivation of gsk3? In response to adhesion and ilk activation (6) would then result in a thr-159-hypophosphorylated ?-Nac that would become unavailable for proteasome degradation but would become a substrate for the ilk kinase activity on residue ser-43. The ser-43-phosphorylated ?-Nac would preferentially interact with c-jun (30), translocate to the nucleus, and potentiate transcription |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ILK | up-regulates activity
phosphorylation
|
MYL12B |
0.319 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106423 |
Ser20 |
KRPQRATsNVFAMFD |
Homo sapiens |
|
| pmid |
sentence |
| 11278951 |
Integrin-linked kinase cdna was cloned, sequenced, expressed in e. coli, and shown to phosphorylate myosin light chain in the absence of ca(2+) at ser(19) and thr(18). Smooth muscle contraction follows an increase in cytosolic Ca(2+) concentration, activation of myosin light chain kinase, and phosphorylation of the 20-kDa light chain of myosin at Ser(19). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106427 |
Thr19 |
KKRPQRAtSNVFAMF |
Homo sapiens |
|
| pmid |
sentence |
| 11278951 |
Integrin-linked kinase cdna was cloned, sequenced, expressed in e. coli, and shown to phosphorylate myosin light chain in the absence of ca(2+) at ser(19) and thr(18). Smooth muscle contraction follows an increase in cytosolic Ca(2+) concentration, activation of myosin light chain kinase, and phosphorylation of the 20-kDa light chain of myosin at Ser(19).Smooth muscle contraction follows an increase in cytosolic Ca(2+) concentration, activa |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PAK1 | up-regulates
phosphorylation
|
ILK |
0.421 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154303 |
Ser246 |
CPRLRIFsHPNVLPV |
Homo sapiens |
|
| pmid |
sentence |
| 17420447 |
We found that pak1 phosphorylates ilk at threonine-173 and serine-246 in vitro and in vivo. together, these results suggest that ilk is a pak1 substrate, undergoes phosphorylation-dependent shuttling between the cell nucleus and cytoplasm, and interacts with gene-regulatory chromatin. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-154307 |
Thr173 |
DTFWKGTtRTRPRNG |
Homo sapiens |
|
| pmid |
sentence |
| 17420447 |
We found that pak1 phosphorylates ilk at threonine-173 and serine-246 in vitro and in vivo. together, these results suggest that ilk is a pak1 substrate, undergoes phosphorylation-dependent shuttling between the cell nucleus and cytoplasm, and interacts with gene-regulatory chromatin. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ILK | down-regulates 
phosphorylation
|
CFL1 |
0.357 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160756 |
Ser3 |
sGVAVSDG |
Homo sapiens |
|
| pmid |
sentence |
| 18252715 |
Actin (de)polymerization is regulated by cofilin, the ser(3) phosphorylation (ps(3)cofilin) of which inhibits its actin-severing activity. To determine how ilk regulates ps(3)cofilin, we examined the effects of ilk on ps(3)cofilin using normal rie1 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ILK | up-regulates activity
phosphorylation
|
ILK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-106838 |
Ser343 |
SMADVKFsFQCPGRM |
Homo sapiens |
|
| pmid |
sentence |
| 11313365 |
Although ilk has been shown to autophosphorylate serine 343 (s343) is in the hydrophobic motif fsf within the activation loop of the kinase domain and has previously been suggested to be the target of autophosphorylation (9). Mutation of serine 343 to alanine (s343a) resulted in the inability of ilk to stimulate phosphorylation of pkb/akt in cos cells (9). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
ILK | up-regulates
phosphorylation
|
NACA |
0.401 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-127694 |
Ser43 |
PELEEQDsTQATTQQ |
Homo sapiens |
|
| pmid |
sentence |
| 15299025 |
Ilk phosphorylated alpha-nac on residue ser-43. Ilk-dependent phosphorylation of alpha-nac induced the nuclear accumulation of the coactivator and that phosphorylation of alpha-nac by ilk is required for the potentiation of c-jun-mediated responses by the kinase. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ILK | up-regulates activity
phosphorylation
|
AKT |
0.771 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250261 |
Ser473 |
RPHFPQFsYSASGTA |
in vitro |
|
| pmid |
sentence |
| 11313365 |
ILK Phosphorylates PKB/Akt on Serine 473 To become fully activated, PKB/Akt requires phosphorylation at two sites, threonine 308 and serine 473, in a phosphatidylinositol (PI) 3-kinase-dependent manner. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Integrin Signaling |
| + |
ILK | up-regulates
phosphorylation
|
AKT |
0.771 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-60115 |
Ser473 |
RPHFPQFsYSASGTA |
Homo sapiens |
|
| pmid |
sentence |
| 9736715 |
Ilk can phosphorylate pkb-akt on serine-473, whereas kinase-deficient ilk severely inhibits endogenous phosphorylation of pkb-akt on serine-473, demonstrating that ilk is involved in agonist stimulated, pi(3)k-dependent, pkb-akt activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Integrin Signaling |
| + |
ILK | up-regulates
phosphorylation
|
AKT1 |
0.771 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252597 |
Ser473 |
RPHFPQFsYSASGTA |
Homo sapiens |
|
| pmid |
sentence |
| 9736715 |
Ilk can phosphorylate pkb-akt on serine-473, whereas kinase-deficient ilk severely inhibits endogenous phosphorylation of pkb-akt on serine-473, demonstrating that ilk is involved in agonist stimulated, pi(3)k-dependent, pkb-akt activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ILK | up-regulates activity
phosphorylation
|
AKT1 |
0.771 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252596 |
Ser473 |
RPHFPQFsYSASGTA |
in vitro |
|
| pmid |
sentence |
| 11313365 |
ILK Phosphorylates PKB/Akt on Serine 473 To become fully activated, PKB/Akt requires phosphorylation at two sites, threonine 308 and serine 473, in a phosphatidylinositol (PI) 3-kinase-dependent manner. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ILK | up-regulates activity
phosphorylation
|
PPP1R14A |
0.531 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90828 |
Thr38 |
QKRHARVtVKYDRRE |
Homo sapiens |
|
| pmid |
sentence |
| 12144526 |
Phosphopeptide mapping, phospho amino acid analysis and immunoblotting using phospho-specific antibodies indicated that ilk predominantly phosphorylated the site critical for potent inhibition, i.e. Thr(38) of cpi-17 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ILK | down-regulates activity
phosphorylation
|
PPP1R12A |
0.566 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262884 |
Thr500 |
RLAYVAPtIPRRLAS |
in vitro |
|
| pmid |
sentence |
| 12030846 |
MYPT1 was phosphorylated by ILK and phosphorylation sites in the N- and C-terminal fragments of MYPT1 were detected. From sequence analyses, three sites were identified: a primary site at Thr(709), and two other sites at Thr(695) and Thr(495). ILK produced an intermediate level of inhibition |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262886 |
Thr696 |
ARQSRRStQGVTLTD |
in vitro |
|
| pmid |
sentence |
| 12030846 |
MYPT1 was phosphorylated by ILK and phosphorylation sites in the N- and C-terminal fragments of MYPT1 were detected. From sequence analyses, three sites were identified: a primary site at Thr(709), and two other sites at Thr(695) and Thr(495). ILK produced an intermediate level of inhibition |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262885 |
Thr710 |
DLQEAEKtIGRSRST |
in vitro |
|
| pmid |
sentence |
| 12030846 |
MYPT1 was phosphorylated by ILK and phosphorylation sites in the N- and C-terminal fragments of MYPT1 were detected. From sequence analyses, three sites were identified: a primary site at Thr(709), and two other sites at Thr(695) and Thr(495). ILK produced an intermediate level of inhibition |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
ILK | up-regulates activity
phosphorylation
|
PPP1R14B |
0.371 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265741 |
Thr57 |
VRRQGKVtVKYDRKE |
in vitro |
|
| pmid |
sentence |
| 12144526 |
We conclude that ILK may activate smooth-muscle contraction both directly, via phosphorylation of myosin, and indirectly, via phosphorylation and activation of CPI-17 and PHI-1, leading to inhibition of MLCP.|CPI-17 and PHI-1 thiophosphorylated by ILK at Thr(38) or Thr(57) respectively inhibited myosin light-chain phosphatase (MLCP) activity bound to myosin |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
ILK | down-regulates
phosphorylation
|
PPP1R12A |
0.566 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87924 |
Thr696 |
ARQSRRStQGVTLTD |
Homo sapiens |
|
| pmid |
sentence |
| 12030846 |
Mypt1 was phosphorylated by ilk and phosphorylation sites in the n- and c-terminal fragments of mypt1 were detected. From sequence analyses, three sites were identified: a primary site at thr(709), and two other sites at thr(695) and thr(495) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-87928 |
Thr710 |
DLQEAEKtIGRSRST |
Homo sapiens |
|
| pmid |
sentence |
| 12030846 |
Mypt1 was phosphorylated by ilk and phosphorylation sites in the n- and c-terminal fragments of mypt1 were detected. From sequence analyses, three sites were identified: a primary site at thr(709), and two other sites at thr(695) and thr(495). phosphorylation of the various sites indicated that thr695 was the major inhibitory site, thr709 had only a slight inhibitory effect |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
ILK | up-regulates activity
phosphorylation
|
PPP1R14C |
0.528 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-101835 |
Thr73 |
RHQQGKVtVKYDRKE |
Homo sapiens |
|
| pmid |
sentence |
| 12804574 |
Pka predominantly phosphorylated a site distinct from the inhibitory t73 in kepi. Integrin-linked kinase phosphorylated KEPI (T73) and this dramatically increased inhibition of PP1c |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PXN | up-regulates
binding
|
ILK |
0.792 |
| 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 |
| + |
ILK | form complex 
binding
|
IPP complex |
0.894 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265762 |
|
|
|
|
| pmid |
sentence |
| 16493410 |
Integrin-linked kinase (ILK), PINCH and parvin form a ternary complex (the IPP complex) that binds to ECM-ligated integrins. This complex regulates signalling pathways and connects the ECM with the actin cytoskeleton. |
|
| Publications: |
1 |
| + |
TWIST2 | down-regulates quantity by repression 
transcriptional regulation
|
ILK |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255504 |
|
|
Homo sapiens |
HGC-27 Cell |
| pmid |
sentence |
| 19051271 |
we performed microarray analysis to compare the gene expression profiles in HGC-27 cells, with or without small interfering RNA (siRNA)-mediated depletion of TWIST. Our results showed that NF1, RAP1A, SRPX, RBL2, PFDN4, ILK, F2R, ERBB3, and MYB were up-regulated, whereas AKR1C2, FOS, GDF15, NR2F1, ATM, and CTPS were down-regulated after TWIST depletion |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TWIST1 | down-regulates quantity by repression
transcriptional regulation
|
ILK |
0.286 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255528 |
|
|
Homo sapiens |
HGC-27 Cell |
| pmid |
sentence |
| 19051271 |
we performed microarray analysis to compare the gene expression profiles in HGC-27 cells, with or without small interfering RNA (siRNA)-mediated depletion of TWIST. Our results showed that NF1, RAP1A, SRPX, RBL2, PFDN4, ILK, F2R, ERBB3, and MYB were up-regulated, whereas AKR1C2, FOS, GDF15, NR2F1, ATM, and CTPS were down-regulated after TWIST depletion |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ILK
- 
- 