| + |
DAPK1 |
phosphorylation
|
MCM3 |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160958 |
Ser160 |
KTIERRYsDLTTLVA |
Homo sapiens |
|
| pmid |
sentence |
| 18283219 |
Mcm3 was efficiently and specifically phosphorylated by dapk on a unique site, ser160 / the functional effects of dapk-mediated phosphorylation and any connection to these functions remain to be determined |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DAPK1 | down-regulates activity 
phosphorylation
|
STX1A |
0.345 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251083 |
Ser188 |
IIMDSSIsKQALSEI |
Homo sapiens |
HEK-293 Cell, Breast Cancer Cell Line |
| pmid |
sentence |
| 12730201 |
Syntaxin-1A phosphorylation by DAP kinase or its S188D mutant, which mimics a state of complete phosphorylation, significantly decreases syntaxin binding to Munc18-1, a syntaxin-binding protein that regulates SNARE complex formation and is required for synaptic vesicle docking. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
DAPK1 | up-regulates activity 
phosphorylation
|
MYL12A |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262842 |
Ser19 |
KRPQRATsNVFAMFD |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11485996 |
DAPK Phosphorylates Myosin II RLC in Vitro and in Vivo. Together these results show that similar to the conventional MLCKs, Ser-19 is the primary RLC residue phosphorylated by DAPK and that phosphorylation of Thr-18 is also possible. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262843 |
Thr18 |
KKRPQRAtSNVFAMF |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11485996 |
DAPK Phosphorylates Myosin II RLC in Vitro and in Vivo. Together these results show that similar to the conventional MLCKs, Ser-19 is the primary RLC residue phosphorylated by DAPK and that phosphorylation of Thr-18 is also possible. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
DAPK1 | up-regulates
phosphorylation
|
TP53 |
0.575 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153487 |
Ser20 |
PLSQETFsDLWKLLP |
Homo sapiens |
|
| pmid |
sentence |
| 17339337 |
A cell-free ser(20) phosphorylation site assay was used to identify a broad range of calcium calmodulin kinase superfamily members, including chk2, chk1, dapk-1, dapk-3, drak-1, and ampk, as ser(20) kinases.Evaluation of these calcium calmodulin kinase superfamily members as candidate ser(20) kinases in vivo has shown that only chk1 or dapk-1 can stimulate p53 transactivation and induce ser(20) phosphorylation of p53. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-153491 |
Thr18 |
EPPLSQEtFSDLWKL |
Homo sapiens |
B-lymphocyte |
| pmid |
sentence |
| 17339337 |
Dna damage-activated protein kinases like chk1/2 modify the box-i domain of p53 at thr18 and ser20 (46) by an allosteric mechanism (10). |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
DAPK1 | up-regulates activity
phosphorylation
|
TPM1 |
0.28 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262845 |
Ser283 |
HALNDMTsI |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 17895359 |
We identified, for the first time, death-associated protein kinase 1 (DAP kinase 1) as the kinase that phosphorylates tropomyosin-1 in response to ERK activation by hydrogen peroxide (H(2)O(2)). We also report that the phosphorylation of tropomyosin-1 mediated by DAP kinase occurs on Ser283. Our finding that tropomyosin-1 is phosphorylated downstream of ERK and DAP kinase and that it helps regulate the formation of stress fibers will aid understanding the role of this protein in regulating the endothelial functions associated with cytoskeletal remodeling. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DAPK1 | down-regulates activity
phosphorylation
|
DAPK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-110807 |
Ser308 |
ARKKWKQsVRLISLC |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11579085 |
The pro-apoptotic function of death-associated protein kinase is controlled by a unique inhibitory autophosphorylation-based mechanism.These results are consistent with a molecular model in which phosphorylation on ser(308) stabilizes a locked conformation of the cam-regulatory domain within the catalytic cleft and simultaneously also interferes with cam binding. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
DAPK1 | down-regulates quantity by destabilization
phosphorylation
|
PELI1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277531 |
Ser39 |
GDRGRRKsRFALFKR |
Homo sapiens |
HK-2 Cell |
| pmid |
sentence |
| 33052227 |
DAPK1, which directly binds to and phosphorylates Pellino1 at Ser39, leading to Pellino1 poly-ubiquitination and turnover. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DAPK1 | down-regulates
phosphorylation
|
CAMKK2 |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126241 |
Ser511 |
RREERSLsAPGNLLT |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15209507 |
Dapk phosphorylates camkk. S511 was identified as the phosphorylation site . a potential mechanism of action was identified on the basis of the location of s511 near the cam recognition domain of camkk and demonstrated by attenuation of cam-stimulated camkk autophosphorylation after dapk phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
DAPK1 |
phosphorylation
|
CAMKK2 |
0.287 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-126245 |
Ser511 |
RREERSLsAPGNLLT |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15209507 |
Dapk phosphorylates camkks511 was identified as the phosphorylation site |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
MAPK1 | up-regulates
phosphorylation
|
DAPK1 |
0.55 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-132614 |
Ser734 |
NSSRFPPsPLASKPT |
Homo sapiens |
|
| pmid |
sentence |
| 15616583 |
Dapk interacts with erk through a docking sequence within its death domain and is a substrate of erk. Phosphorylation of dapk at ser 735 by erk increases the catalytic activity of dapk both in vitro and in vivo |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DAPK1 | up-regulates
phosphorylation
|
BECN1 |
0.72 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-185589 |
Thr119 |
LSRRLKVtGDLFDIM |
Homo sapiens |
|
| pmid |
sentence |
| 19395874 |
We found that DAPk phosphorylates Beclin 1 on T119, a critical residue within its BH3 domain, and thus promotes Beclin 1 dissociation from Bcl-X(L) and autophagy induction. Here we report that T119 phosphorylation also reduces the interaction between Beclin 1 and Bcl-2, in line with the high degree of structural homology between the BH3 binding pockets of Bcl-2 and Bcl-X(L) proteins. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-183548 |
Thr119 |
LSRRLKVtGDLFDIM |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 19180116 |
The activated form of DAPK triggers autophagy in a beclin-1-dependent manner. DAPK phosphorylates beclin 1 on Thr 119 located at a crucial position within its BH3 domain, and thus promotes the dissociation of beclin 1 from Bcl-XL and the induction of autophagy. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
DAPK1 | down-regulates activity
phosphorylation
|
DDX58 |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277336 |
Thr667 |
ILTGRGKtNQNTGMT |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 28132841 |
DAPK1 phosphorylates RIG-I in vitro at previously reported as well as other sites that limit 5'ppp-dsRNA sensing and virtually abrogate RIG-I activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTPRF | up-regulates activity
dephosphorylation
|
DAPK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276076 |
Tyr490 |
HCAAWHGyYSVAKAL |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 17803936 |
Here, we show that the leukocyte common antigen-related (LAR) tyrosine phosphatase dephosphorylates DAPK at pY491/492 to stimulate the catalytic, proapoptotic, and antiadhesion/antimigration activities of DAPK. Conversely, Src phosphorylates DAPK at Y491/492, which induces DAPK intra-/intermolecular interaction and inactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276075 |
Tyr491 |
CAAWHGYySVAKALC |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 17803936 |
Here, we show that the leukocyte common antigen-related (LAR) tyrosine phosphatase dephosphorylates DAPK at pY491/492 to stimulate the catalytic, proapoptotic, and antiadhesion/antimigration activities of DAPK. Conversely, Src phosphorylates DAPK at Y491/492, which induces DAPK intra-/intermolecular interaction and inactivation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PTPRF | up-regulates
dephosphorylation
|
DAPK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157702 |
Tyr490 |
HCAAWHGyYSVAKAL |
Homo sapiens |
|
| pmid |
sentence |
| 17803936 |
Here, we show that the leukocyte common antigen-related (lar) tyrosine phosphatase dephosphorylates dapk at py491/492 to stimulate the catalytic, proapoptotic, and antiadhesion/antimigration activities of dapk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-157706 |
Tyr491 |
CAAWHGYySVAKALC |
Homo sapiens |
|
| pmid |
sentence |
| 17803936 |
Lar tyrosine phosphatase dephosphorylates dapk at py491/492 to stimulate the catalytic, proapoptotic, and antiadhesion/antimigration activities of dapk |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
SRC | down-regulates activity
phosphorylation
|
DAPK1 |
0.277 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276074 |
Tyr490 |
HCAAWHGyYSVAKAL |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 17803936 |
Here, we show that the leukocyte common antigen-related (LAR) tyrosine phosphatase dephosphorylates DAPK at pY491/492 to stimulate the catalytic, proapoptotic, and antiadhesion/antimigration activities of DAPK. Conversely, Src phosphorylates DAPK at Y491/492, which induces DAPK intra-/intermolecular interaction and inactivation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276073 |
Tyr491 |
CAAWHGYySVAKALC |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 17803936 |
Here, we show that the leukocyte common antigen-related (LAR) tyrosine phosphatase dephosphorylates DAPK at pY491/492 to stimulate the catalytic, proapoptotic, and antiadhesion/antimigration activities of DAPK. Conversely, Src phosphorylates DAPK at Y491/492, which induces DAPK intra-/intermolecular interaction and inactivation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
DAPK1 |
phosphorylation
|
RPL5 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160954 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18283219 |
Here we adapted this strategy to successfully screen for dapk substrates. We report the identification of two substrates, ribosomal protein l5 and mcm3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DAPK1 | down-regulates
binding
|
MAPK1 |
0.55 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-132610 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15616583 |
Conversely, dapk promotes the cytoplasmic retention of erk, thereby inhibiting erk signaling in the nucleus. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MIB1 | down-regulates quantity by destabilization
polyubiquitination
|
DAPK1 |
0.448 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272602 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 12351649 |
Transient expression of DIP-1 in HeLa cells antagonizes the anti-apoptotic function of DAPK to promote a caspase-dependent apoptosis. These studies also demonstrate that DAPK is an in vitro and in vivo target for ubiquitination by DIP-1, thereby providing a mechanism by which DAPK activities can be regulated through proteasomal degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DAPK1 | up-regulates
binding
|
MAP1B |
0.265 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-181305 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18806760 |
Dapk-1 interacts with the microtubule-associated protein map1b, in particular in conditions of amino-acid starvation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KLHL20 | down-regulates quantity by destabilization
binding
|
DAPK1 |
0.405 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271960 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 20389280 |
Here, we identify the BTB-Kelch protein KLHL20 as a negative regulator of DAPK. KLHL20 binds DAPK and Cullin 3 (Cul3) via its Kelch-repeat domain and BTB domain, respectively. The KLHL20-Cul3-ROC1 E3 ligase complex promotes DAPK polyubiquitination, thereby inducing the proteasomal degradation of DAPK. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
DAPK1
- 
- 