| + |
MARK2 | up-regulates 
phosphorylation
|
UTRN |
0.433 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161915 |
Ser1258 |
TLEERMKsTEVLPEK |
Homo sapiens |
|
| pmid |
sentence |
| 19945424 |
Par-1b, interacts with the utrophin-dg complex, and positively regulates the interaction between utrophin and dg. Ser1258 within r9 is specifically phosphorylated by par-1b. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Muscle, Skeletal Muscle |
| + |
MARK2 | down-regulates activity 
phosphorylation
|
KIF13B |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262955 |
Ser1381 |
KLSRRSIsSPNVNRL |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 20194617 |
We report here the identification of GAKIN/KIF13B as a novel in vivo substrate for Par1b and present evidence that GAKIN/KIF13B plays a critical role in axon formation in neurons, which is negatively regulated by Par1b-mediated phosphorylation. Par1b phosphorylates GAKIN/KIF13B at both Ser1381 and Ser1410. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262956 |
Ser1410 |
SNKGRWEsQQDVSQT |
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 20194617 |
We report here the identification of GAKIN/KIF13B as a novel in vivo substrate for Par1b and present evidence that GAKIN/KIF13B plays a critical role in axon formation in neurons, which is negatively regulated by Par1b-mediated phosphorylation. Par1b phosphorylates GAKIN/KIF13B at both Ser1381 and Ser1410. |
|
| Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
| + |
MARK2 | down-regulates
phosphorylation
|
HDAC7 |
0.35 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-149583 |
Ser155 |
FPLRKTVsEPNLKLR |
Homo sapiens |
|
| pmid |
sentence |
| 16980613 |
We further show that emk and c-tak1 phosphorylate class iia hdacs on one of their multiple 14-3-3 binding sites and alter their subcellular localization and repressive function |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GSK3B | down-regulates activity
phosphorylation
|
MARK2 |
0.355 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276163 |
Ser212 |
KLDTFCGsPPYAAPE |
in vitro |
|
| pmid |
sentence |
| 18424437 |
MARK family kinases can be activated by phosphorylation of a conserved threonine (Thr-208 in MARK2), and inactivated by phosphorylation of a serine (Ser-212), both in the activation loop of the catalytic domain. Activation is achieved by the kinases MARKK/TAO1 or LKB1, although the inactivating kinase was unknown. We show here that GSK3beta serves the role of the inhibitory kinase. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MARK2 | up-regulates
phosphorylation
|
RAB11FIP2 |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-147118 |
Ser227 |
QRLSSAHsMSDLSGS |
Homo sapiens |
|
| pmid |
sentence |
| 16775013 |
We identified the kinase that phosphorylated rab11-fip2 as mark2/emk1/par-1balpha (mark2), and recombinant mark2 phosphorylated rab11-fip2 only on serine 227. In calcium switch assays, cells expressing rab11-fip2(s227a) showed a defect in the timely reestablishment of p120-containing junctional complexes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Kidney |
| + |
MARK2 | up-regulates quantity
phosphorylation
|
RAB11FIP1 |
0.349 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273676 |
Ser234 |
QKTPLSQsMSVLPTS |
in vitro |
|
| pmid |
sentence |
| 28396819 |
We have now found that MARK2 phosphorylates Rab11-FIP1B/C at serine 234 in a consensus site similar to that previously identified in Rab11-FIP2. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MARK2 | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.695 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275435 |
Ser267 |
RVQSKIGsLDNITHV |
in vitro |
|
| pmid |
sentence |
| 10090741 |
We have studied the relationship between the phosphorylation oftau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. By contrast, MARK and PKA phosphorylate several sites within the repeats (notably theKXGS motifs including Ser262, Ser324, and Ser356, plus Ser320); in addition PKA phosphorylates somesites in the flanking domains, notably Ser214. This type of phosphorylation strongly reduces tau’s affinityfor microtubules, and at the same time inhibits tau’s assembly into PHFs. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275437 |
Ser324 |
RHLSNVSsTGSIDMV |
in vitro |
|
| pmid |
sentence |
| 10090741 |
We have studied the relationship between the phosphorylation oftau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. By contrast, MARK and PKA phosphorylate several sites within the repeats (notably theKXGS motifs including Ser262, Ser324, and Ser356, plus Ser320); in addition PKA phosphorylates somesites in the flanking domains, notably Ser214. This type of phosphorylation strongly reduces tau’s affinityfor microtubules, and at the same time inhibits tau’s assembly into PHFs. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
MARK2 | down-regulates activity
phosphorylation
|
MAPT |
0.695 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275436 |
Ser355 |
EADLPEPsEKQPAAA |
in vitro |
|
| pmid |
sentence |
| 10090741 |
We have studied the relationship between the phosphorylation oftau by several kinases (MARK, PKA, MAPK, GSK3) and its assembly into PHFs. By contrast, MARK and PKA phosphorylate several sites within the repeats (notably theKXGS motifs including Ser262, Ser324, and Ser356, plus Ser320); in addition PKA phosphorylates somesites in the flanking domains, notably Ser214. This type of phosphorylation strongly reduces tau’s affinityfor microtubules, and at the same time inhibits tau’s assembly into PHFs. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKACA | down-regulates activity
phosphorylation
|
MARK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276870 |
Ser409 |
NPKQRRFsDQAAGPA |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 25512381 |
Here, we found the disruption of microtubule and neurite outgrowth induced by MARK2 overexpression was blocked by active PKA. The interaction between PKA and MARK2 was confirmed by coimmunoprecipitation and immunocytochemistry both in vitro and in vivo. PKA was found to inhibit MARK2 kinase activity by phosphorylating a novel site, serine 409. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MARK2 | down-regulates activity
phosphorylation
|
TNK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273867 |
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 |
| + |
MARK2 | up-regulates
phosphorylation
|
PARD3 |
0.508 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-198742 |
Ser873 |
VDDQKAGsPSRDVGP |
Homo sapiens |
|
| pmid |
sentence |
| 22883624 |
Gab1 brings par1 and par3 into a transient complex, stimulating par3 phosphorylation by par1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MARK2 | down-regulates
phosphorylation
|
ARHGEF2 |
0.518 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177096 |
Ser886 |
PVDPRRRsLPAGDAL |
Homo sapiens |
|
| pmid |
sentence |
| 22072711 |
We also show that par1b-induced serine 885/serine 959 phosphorylation inhibits rhoa-specific gef activity of gef-h1. As a consequence, gef-h1 phosphorylated on both of the serine residues loses the ability to stimulate rhoa and thereby fails to induce rhoa-dependent stress fiber formation |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-177100 |
Ser960 |
SRLSPPHsPRDFTRM |
Homo sapiens |
|
| pmid |
sentence |
| 22072711 |
We also show that par1b-induced serine 885/serine 959 phosphorylation inhibits rhoa-specific gef activity of gef-h1. As a consequence, gef-h1 phosphorylated on both of the serine residues loses the ability to stimulate rhoa and thereby fails to induce rhoa-dependent stress fiber formation |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
STK11 | up-regulates activity
phosphorylation
|
MARK2 |
0.569 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276165 |
Thr208 |
TFGNKLDtFCGSPPY |
in vitro |
|
| pmid |
sentence |
| 18424437 |
MARK family kinases can be activated by phosphorylation of a conserved threonine (Thr-208 in MARK2), and inactivated by phosphorylation of a serine (Ser-212), both in the activation loop of the catalytic domain. Activation is achieved by the kinases MARKK/TAO1 or LKB1, although the inactivating kinase was unknown. We show here that GSK3beta serves the role of the inhibitory kinase. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
TAOK1 | up-regulates activity
phosphorylation
|
MARK2 |
0.424 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276164 |
Thr208 |
TFGNKLDtFCGSPPY |
in vitro |
|
| pmid |
sentence |
| 18424437 |
MARK family kinases can be activated by phosphorylation of a conserved threonine (Thr-208 in MARK2), and inactivated by phosphorylation of a serine (Ser-212), both in the activation loop of the catalytic domain. Activation is achieved by the kinases MARKK/TAO1 or LKB1, although the inactivating kinase was unknown. We show here that GSK3beta serves the role of the inhibitory kinase. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
STK11 | up-regulates
phosphorylation
|
MARK2 |
0.569 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-122628 |
Thr208 |
TFGNKLDtFCGSPPY |
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-156126 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 17573348 |
Here we show in vitro that lkb1 phosphorylates and activates mark2 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MARK2 | up-regulates activity
phosphorylation
|
PINK1 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276401 |
Thr313 |
EGLGHGRtLFLVMKN |
in vitro |
|
| pmid |
sentence |
| 22238344 |
MARK2 phosphorylated and activated the cleaved form of PINK1 (ΔN-PINK1; amino acids 156-581). Thr-313 was the primary phosphorylation site, a residue mutated to a non-phosphorylatable form (T313M) in a frequent variant of PD. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCZ | down-regulates
phosphorylation
|
MARK2 |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-124217 |
Thr596 |
RGVSSRStFHAGQLR |
Homo sapiens |
|
| pmid |
sentence |
| 15084291 |
Hpar-1b is phosphorylated by apkc on threonine 595 importantly, phosphorylation of hpar-1b on t595 negatively regulates the kinase activity and plasma membrane localization of hpar-1b in vivo. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
MARK2
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