| + |
MARK1 | down-regulates activity 
phosphorylation
|
MAP4 |
0.451 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250169 |
Ser1073 |
KAQAKVGsLDNVGHL |
in vitro |
|
| pmid |
sentence |
| 8631898 |
Here we show that p110mark phosphorylates analogous KXGS sites in the microtubule binding domains of the neuronal MAP2 and the ubiquitous MAP4. Phosphorylation in vitro leads to the dissociation of MAP2 and MAP4 from microtubules and to a pronounced increase in dynamic instability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250170 |
Ser928 |
SRLATNTsAPDLKNV |
in vitro |
|
| pmid |
sentence |
| 8631898 |
Here we show that p110mark phosphorylates analogous KXGS sites in the microtubule binding domains of the neuronal MAP2 and the ubiquitous MAP4. Phosphorylation in vitro leads to the dissociation of MAP2 and MAP4 from microtubules and to a pronounced increase in dynamic instability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250171 |
Ser941 |
NVRSKVGsTENIKHQ |
in vitro |
|
| pmid |
sentence |
| 8631898 |
Here we show that p110mark phosphorylates analogous KXGS sites in the microtubule binding domains of the neuronal MAP2 and the ubiquitous MAP4. Phosphorylation in vitro leads to the dissociation of MAP2 and MAP4 from microtubules and to a pronounced increase in dynamic instability. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
MARK1 | down-regulates activity
phosphorylation
|
MAP2 |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250163 |
Ser1540 |
KSPEKRSsLPRPSSI |
in vitro |
|
| pmid |
sentence |
| 8631898 |
Here we show that p110mark phosphorylates analogous KXGS sites in the microtubule binding domains of the neuronal MAP2 and the ubiquitous MAP4. Phosphorylation in vitro leads to the dissociation of MAP2 and MAP4 from microtubules and to a pronounced increase in dynamic instability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250164 |
Ser1679 |
NVKSKIGsTDNIKYQ |
in vitro |
|
| pmid |
sentence |
| 8631898 |
Here we show that p110mark phosphorylates analogous KXGS sites in the microtubule binding domains of the neuronal MAP2 and the ubiquitous MAP4. Phosphorylation in vitro leads to the dissociation of MAP2 and MAP4 from microtubules and to a pronounced increase in dynamic instability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250165 |
Ser1710 |
HVTSKCGsLKNIRHR |
in vitro |
|
| pmid |
sentence |
| 8631898 |
Here we show that p110mark phosphorylates analogous KXGS sites in the microtubule binding domains of the neuronal MAP2 and the ubiquitous MAP4. Phosphorylation in vitro leads to the dissociation of MAP2 and MAP4 from microtubules and to a pronounced increase in dynamic instability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250166 |
Ser1795 |
VASPRRLsNVSSSGS |
in vitro |
|
| pmid |
sentence |
| 8631898 |
Here we show that p110mark phosphorylates analogous KXGS sites in the microtubule binding domains of the neuronal MAP2 and the ubiquitous MAP4. Phosphorylation in vitro leads to the dissociation of MAP2 and MAP4 from microtubules and to a pronounced increase in dynamic instability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250167 |
Ser1799 |
RRLSNVSsSGSINLL |
in vitro |
|
| pmid |
sentence |
| 8631898 |
Here we show that p110mark phosphorylates analogous KXGS sites in the microtubule binding domains of the neuronal MAP2 and the ubiquitous MAP4. Phosphorylation in vitro leads to the dissociation of MAP2 and MAP4 from microtubules and to a pronounced increase in dynamic instability. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250168 |
Ser1802 |
SNVSSSGsINLLESP |
in vitro |
|
| pmid |
sentence |
| 8631898 |
Here we show that p110mark phosphorylates analogous KXGS sites in the microtubule binding domains of the neuronal MAP2 and the ubiquitous MAP4. Phosphorylation in vitro leads to the dissociation of MAP2 and MAP4 from microtubules and to a pronounced increase in dynamic instability. |
|
| Publications: |
6 |
Organism: |
In Vitro |
| + |
MARK1 | down-regulates activity
phosphorylation
|
TNK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273866 |
Ser502 |
RMKGISRsLESVLSL |
Homo sapiens |
A-549 Cell |
| pmid |
sentence |
| 34504101 |
We also discover a MARK-mediated phosphorylation on TNK1 at S502 that promotes an interaction between TNK1 and 14-3-3, which sequesters TNK1 and inhibits its kinase activity.Phosphorylation of TNK1 at S502 within the proline rich domain is required for TNK1 binding to 14-3-3.MARKs mediate phosphorylation at S502 and 14-3-3 binding to TNK1, which restrains the movement of TNK1 into heavy membrane-associated clusters. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MARK1 | down-regulates
phosphorylation
|
MAPT |
0.442 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171050 |
Ser579 |
NVKSKIGsTENLKHQ |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
Mark and pka phosphorylate several sites within the repeats (notably the kxgs motifs including ser262, ser324, and ser356, plus ser320)tau pseudophosphorylation at specific sites such as s262, s293, s324 and s356 was reported to induce tau conformational change and attenuate tau binding to microtubules (fischer et al., 2009). Then, newly soluble tau proteins are targeted by post-translational modifications that directly or indirectly alter tau conformation, promoting tau dimerization in an anti-parallel manner. Stable tau dimers form tau oligomers, which continue in the aggregation process |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171054 |
Ser641 |
KVTSKCGsLGNIHHK |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
Mark and pka phosphorylate several sites within the repeats (notably the kxgs motifs including ser262, ser324, and ser356, plus ser320)tau pseudophosphorylation at specific sites such as s262, s293, s324 and s356 was reported to induce tau conformational change and attenuate tau binding to microtubules (fischer et al., 2009). Then, newly soluble tau proteins are targeted by post-translational modifications that directly or indirectly alter tau conformation, promoting tau dimerization in an anti-parallel manner. Stable tau dimers form tau oligomers, which continue in the aggregation process |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171058 |
Ser673 |
RVQSKIGsLDNITHV |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
Mark and pka phosphorylate several sites within the repeats (notably the kxgs motifs including ser262, ser324, and ser356, plus ser320)tau pseudophosphorylation at specific sites such as s262, s293, s324 and s356 was reported to induce tau conformational change and attenuate tau binding to microtubules (fischer et al., 2009). Then, newly soluble tau proteins are targeted by post-translational modifications that directly or indirectly alter tau conformation, promoting tau dimerization in an anti-parallel manner. Stable tau dimers form tau oligomers, which continue in the aggregation process |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
MARK1 | down-regulates activity
phosphorylation
|
MAPT |
0.442 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250172 |
Ser579 |
NVKSKIGsTENLKHQ |
in vitro |
|
| pmid |
sentence |
| 10090741 |
We have studied the relationship between the phosphorylation of tau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. MARK and PKA phosphorylate several sites within the repeats (notably the KXGS motifs including Ser262, Ser324, and Ser356, plus Ser320). This type of phosphorylation strongly reduces tau's affinity for microtubules, and at the same time inhibits tau's assembly into PHFs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250173 |
Ser637 |
VDLSKVTsKCGSLGN |
in vitro |
|
| pmid |
sentence |
| 10090741 |
We have studied the relationship between the phosphorylation of tau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. MARK and PKA phosphorylate several sites within the repeats (notably the KXGS motifs including Ser262, Ser324, and Ser356, plus Ser320). This type of phosphorylation strongly reduces tau's affinity for microtubules, and at the same time inhibits tau's assembly into PHFs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250174 |
Ser641 |
KVTSKCGsLGNIHHK |
in vitro |
|
| pmid |
sentence |
| 10090741 |
We have studied the relationship between the phosphorylation of tau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. MARK and PKA phosphorylate several sites within the repeats (notably the KXGS motifs including Ser262, Ser324, and Ser356, plus Ser320). This type of phosphorylation strongly reduces tau's affinity for microtubules, and at the same time inhibits tau's assembly into PHFs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250175 |
Ser673 |
RVQSKIGsLDNITHV |
in vitro |
|
| pmid |
sentence |
| 10090741 |
We have studied the relationship between the phosphorylation of tau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. MARK and PKA phosphorylate several sites within the repeats (notably the KXGS motifs including Ser262, Ser324, and Ser356, plus Ser320). This type of phosphorylation strongly reduces tau's affinity for microtubules, and at the same time inhibits tau's assembly into PHFs. |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
STK11 | up-regulates 
phosphorylation
|
MARK1 |
0.421 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122545 |
Thr215 |
TVGNKLDtFCGSPPY |
Homo sapiens |
|
| pmid |
sentence |
| 14976552 |
Lkb1 is a master kinase that activates 13 kinases of the ampk subfamily, including mark/par-1we recently demonstrated that the lkb1 tumour suppressor kinase, in complex with the pseudokinase strad and the scaffolding protein mo25, phosphorylates and activates amp-activated protein kinase (ampk). A total of 12 human kinases (nuak1, nuak2, brsk1, brsk2, qik, qsk, sik, mark1, mark2, mark3, mark4 and melk) are related to ampk. Here we demonstrate that lkb1 can phosphorylate the t-loop of all the members of this subfamily, apart from melk, increasing their activity >50-fold |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
MARK1
- 
- 