| + |
SGK1 | down-regulates 
phosphorylation
|
MAPT |
0.337 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-161288 |
Ser214 |
GGKERPGsKEEVDED |
Homo sapiens |
|
| pmid |
sentence |
| 16982696 |
Second, sgk1 indirectly depolymerized mts through the phosphorylation of tau at ser214 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKAA1 | down-regulates activity
phosphorylation
|
MAPT |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275439 |
Ser214 |
GGKERPGsKEEVDED |
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-275440 |
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: |
2 |
Organism: |
In Vitro |
| + |
AMPK | down-regulates activity
phosphorylation
|
MAPT |
0.258 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273926 |
Ser214 |
GGKERPGsKEEVDED |
in vitro |
|
| pmid |
sentence |
| 21204788 |
AMPK phosphorylation inhibits tau binding of microtubules. In order to study further the phosphorylation of tau by AMPK, we compared phosphorylation of tau by MARK4 or AMPK using a panel of phospho-tau antibodies (Figure 2A). Five phosphorylation sites common to both kinases were identified (Thr231, Ser262, Ser356, Ser396 and Ser422). In addition, AMPK, but not MARK4, was capable of phosphorylating Ser214 (Figure 2A). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273930 |
Ser396 |
DDKKAKTsTRSSAKT |
in vitro |
|
| pmid |
sentence |
| 21204788 |
AMPK phosphorylation inhibits tau binding of microtubules. In order to study further the phosphorylation of tau by AMPK, we compared phosphorylation of tau by MARK4 or AMPK using a panel of phospho-tau antibodies (Figure 2A). Five phosphorylation sites common to both kinases were identified (Thr231, Ser262, Ser356, Ser396 and Ser422). In addition, AMPK, but not MARK4, was capable of phosphorylating Ser214 (Figure 2A). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273931 |
Ser420 |
KHPTPGSsDPLIQPS |
in vitro |
|
| pmid |
sentence |
| 21204788 |
AMPK phosphorylation inhibits tau binding of microtubules. In order to study further the phosphorylation of tau by AMPK, we compared phosphorylation of tau by MARK4 or AMPK using a panel of phospho-tau antibodies (Figure 2A). Five phosphorylation sites common to both kinases were identified (Thr231, Ser262, Ser356, Ser396 and Ser422). In addition, AMPK, but not MARK4, was capable of phosphorylating Ser214 (Figure 2A). |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CDK5 | down-regulates
phosphorylation
|
MAPT |
0.754 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171018 |
Ser235 |
SPQDSPPsKASPAQD |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
Cdk5 regulates app (amyloid precursor protein) processing and tau hyperphosphorylationtau phosphorylation at t231, s235 and s262 also contributes to the dissociation of tau from microtubules |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-92603 |
Ser519 |
SGYSSPGsPGTPGSR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12226093 |
Phosphopeptide mapping revealed enhanced phosphorylation of ser(202)/thr(205) residues by p25-cdk5 considering the fact that phosphorylation of ser(202)/thr(205) antagonizes the tau-mediated nucleation of tubulin, p25-cdk5 may play a pivotal role in neuronal cell death in alzheimer's disease. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-92607 |
Thr522 |
SSPGSPGtPGSRSRT |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12226093 |
Phosphopeptide mapping revealed enhanced phosphorylation of ser(202)/thr(205) residues by p25-cdk5 considering the fact that phosphorylation of ser(202)/thr(205) antagonizes the tau-mediated nucleation of tubulin, p25-cdk5 may play a pivotal role in neuronal cell death in alzheimer's disease. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171022 |
Thr548 |
KKVAVVRtPPKSPSS |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
However, other kinases, such as cdk5, p38 and pka, also phosphorylate tau at t231tau phosphorylation at t231, s235 and s262 also contributes to the dissociation of tau from microtubules |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CDK5/CDK5R1 | down-regulates
phosphorylation
|
MAPT |
0.695 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251587 |
Ser235 |
SPQDSPPsKASPAQD |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
Cdk5 regulates app (amyloid precursor protein) processing and tau hyperphosphorylationtau phosphorylation at t231, s235 and s262 also contributes to the dissociation of tau from microtubules |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251599 |
Ser519 |
SGYSSPGsPGTPGSR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12226093 |
Phosphopeptide mapping revealed enhanced phosphorylation of ser(202)/thr(205) residues by p25-cdk5 considering the fact that phosphorylation of ser(202)/thr(205) antagonizes the tau-mediated nucleation of tubulin, p25-cdk5 may play a pivotal role in neuronal cell death in alzheimer's disease. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251600 |
Thr522 |
SSPGSPGtPGSRSRT |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12226093 |
Phosphopeptide mapping revealed enhanced phosphorylation of ser(202)/thr(205) residues by p25-cdk5 considering the fact that phosphorylation of ser(202)/thr(205) antagonizes the tau-mediated nucleation of tubulin, p25-cdk5 may play a pivotal role in neuronal cell death in alzheimer's disease. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251601 |
Thr548 |
KKVAVVRtPPKSPSS |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
However, other kinases, such as cdk5, p38 and pka, also phosphorylate tau at t231tau phosphorylation at t231, s235 and s262 also contributes to the dissociation of tau from microtubules |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
MARK4 | down-regulates activity
phosphorylation
|
MAPT (isoform 5) |
0.429 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273933 |
Ser262 |
NVKSKIGsTENLKHQ |
in vitro |
|
| pmid |
sentence |
| 21204788 |
AMPK phosphorylation inhibits tau binding of microtubules. In order to study further the phosphorylation of tau by AMPK, we compared phosphorylation of tau by MARK4 or AMPK using a panel of phospho-tau antibodies (Figure 2A). Five phosphorylation sites common to both kinases were identified (Thr231, Ser262, Ser356, Ser396 and Ser422). In addition, AMPK, but not MARK4, was capable of phosphorylating Ser214 (Figure 2A). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273932 |
Thr231 |
KKVAVVRtPPKSPSS |
in vitro |
|
| pmid |
sentence |
| 21204788 |
AMPK phosphorylation inhibits tau binding of microtubules. In order to study further the phosphorylation of tau by AMPK, we compared phosphorylation of tau by MARK4 or AMPK using a panel of phospho-tau antibodies (Figure 2A). Five phosphorylation sites common to both kinases were identified (Thr231, Ser262, Ser356, Ser396 and Ser422). In addition, AMPK, but not MARK4, was capable of phosphorylating Ser214 (Figure 2A). |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
AMPK | down-regulates activity
phosphorylation
|
MAPT (isoform 5) |
0.258 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273928 |
Ser262 |
NVKSKIGsTENLKHQ |
in vitro |
|
| pmid |
sentence |
| 21204788 |
AMPK phosphorylation inhibits tau binding of microtubules. In order to study further the phosphorylation of tau by AMPK, we compared phosphorylation of tau by MARK4 or AMPK using a panel of phospho-tau antibodies (Figure 2A). Five phosphorylation sites common to both kinases were identified (Thr231, Ser262, Ser356, Ser396 and Ser422). In addition, AMPK, but not MARK4, was capable of phosphorylating Ser214 (Figure 2A). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273927 |
Thr231 |
KKVAVVRtPPKSPSS |
in vitro |
|
| pmid |
sentence |
| 21204788 |
AMPK phosphorylation inhibits tau binding of microtubules. In order to study further the phosphorylation of tau by AMPK, we compared phosphorylation of tau by MARK4 or AMPK using a panel of phospho-tau antibodies (Figure 2A). Five phosphorylation sites common to both kinases were identified (Thr231, Ser262, Ser356, Ser396 and Ser422). In addition, AMPK, but not MARK4, was capable of phosphorylating Ser214 (Figure 2A). |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKAA1 | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275438 |
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. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MAPK3 | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.483 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275434 |
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. |
|
| 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 |
| + |
PRKCG | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275445 |
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: |
1 |
Organism: |
In Vitro |
| + |
PRKCI | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275446 |
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: |
1 |
Organism: |
In Vitro |
| + |
PRKCZ | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.272 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275447 |
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: |
1 |
Organism: |
In Vitro |
| + |
PRKCE | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.275 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275444 |
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: |
1 |
Organism: |
In Vitro |
| + |
PRKCB | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.261 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275443 |
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275442 |
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 |
| + |
PRKCA | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275441 |
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: |
1 |
Organism: |
In Vitro |
| + |
AMPK | down-regulates activity
phosphorylation
|
MAPT (isoform 4) |
0.258 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273929 |
Ser352 |
PRHLSNVsSTGSIDM |
in vitro |
|
| pmid |
sentence |
| 21204788 |
AMPK phosphorylation inhibits tau binding of microtubules. In order to study further the phosphorylation of tau by AMPK, we compared phosphorylation of tau by MARK4 or AMPK using a panel of phospho-tau antibodies (Figure 2A). Five phosphorylation sites common to both kinases were identified (Thr231, Ser262, Ser356, Ser396 and Ser422). In addition, AMPK, but not MARK4, was capable of phosphorylating Ser214 (Figure 2A). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
MARK4 | down-regulates activity
phosphorylation
|
MAPT (isoform 4) |
0.429 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273934 |
Ser353 |
RHLSNVSsTGSIDMV |
in vitro |
|
| pmid |
sentence |
| 21204788 |
AMPK phosphorylation inhibits tau binding of microtubules. In order to study further the phosphorylation of tau by AMPK, we compared phosphorylation of tau by MARK4 or AMPK using a panel of phospho-tau antibodies (Figure 2A). Five phosphorylation sites common to both kinases were identified (Thr231, Ser262, Ser356, Ser396 and Ser422). In addition, AMPK, but not MARK4, was capable of phosphorylating Ser214 (Figure 2A). |
|
| Publications: |
1 |
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 |
| + |
MARK4 | down-regulates activity
phosphorylation
|
MAPT |
0.429 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273935 |
Ser396 |
DDKKAKTsTRSSAKT |
in vitro |
|
| pmid |
sentence |
| 21204788 |
AMPK phosphorylation inhibits tau binding of microtubules. In order to study further the phosphorylation of tau by AMPK, we compared phosphorylation of tau by MARK4 or AMPK using a panel of phospho-tau antibodies (Figure 2A). Five phosphorylation sites common to both kinases were identified (Thr231, Ser262, Ser356, Ser396 and Ser422). In addition, AMPK, but not MARK4, was capable of phosphorylating Ser214 (Figure 2A). |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273936 |
Ser420 |
KHPTPGSsDPLIQPS |
in vitro |
|
| pmid |
sentence |
| 21204788 |
AMPK phosphorylation inhibits tau binding of microtubules. In order to study further the phosphorylation of tau by AMPK, we compared phosphorylation of tau by MARK4 or AMPK using a panel of phospho-tau antibodies (Figure 2A). Five phosphorylation sites common to both kinases were identified (Thr231, Ser262, Ser356, Ser396 and Ser422). In addition, AMPK, but not MARK4, was capable of phosphorylating Ser214 (Figure 2A). |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
GSK3B | down-regulates
phosphorylation
|
MAPT |
0.728 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167286 |
Ser396 |
DDKKAKTsTRSSAKT |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 20679343 |
Alzheimer disease neurons are characterized by extraneuronal plaques formed by aggregated amyloid-? Peptide and by intraneuronal tangles composed of fibrillar aggregates of the microtubule-associated tau protein. Tau is mostly found in a hyperphosphorylated form in these tangleswe find that three residues can be phosphorylated (ser-396, ser-400, and ser-404) by gsk3? |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167290 |
Ser400 |
AKTSTRSsAKTLKNR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 20679343 |
Alzheimer disease neurons are characterized by extraneuronal plaques formed by aggregated amyloid-? Peptide and by intraneuronal tangles composed of fibrillar aggregates of the microtubule-associated tau protein. Tau is mostly found in a hyperphosphorylated form in these tangleswe find that three residues can be phosphorylated (ser-396, ser-400, and ser-404) by gsk3? |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164651 |
Ser516 |
GDRSGYSsPGSPGTP |
Homo sapiens |
|
| pmid |
sentence |
| 20308788 |
Abnormal hyperphosphorylation of tau appears to be crucial in neurofibrillary degeneration in alzheimer's disease (ad). Gsk-3beta phosphorylated tau at many sites, with ser199, thr205, and ser396 being the most favorable sites in cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150360 |
Ser519 |
SGYSSPGsPGTPGSR |
Homo sapiens |
|
| pmid |
sentence |
| 17078951 |
Here, we found that prephosphorylation by pka promotes gsk-3beta-catalyzed tau phosphorylation at thr181, ser199, ser202, thr205, thr217, thr231, ser396 and ser422 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171042 |
Ser579 |
NVKSKIGsTENLKHQ |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
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-60655 |
Ser579 |
NVKSKIGsTENLKHQ |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 9771888 |
Tau is phosphorylated by gsk-3 at several sites found in alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by a-kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167294 |
Ser721 |
PVVSGDTsPRHLSNV |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 20679343 |
Alzheimer disease neurons are characterized by extraneuronal plaques formed by aggregated amyloid-? Peptide and by intraneuronal tangles composed of fibrillar aggregates of the microtubule-associated tau protein. Tau is mostly found in a hyperphosphorylated form in these tangleswe find that three residues can be phosphorylated (ser-396, ser-400, and ser-404) by gsk3? |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164655 |
Thr522 |
SSPGSPGtPGSRSRT |
Homo sapiens |
|
| pmid |
sentence |
| 20308788 |
Abnormal hyperphosphorylation of tau appears to be crucial in neurofibrillary degeneration in alzheimer's disease (ad). Gsk-3beta phosphorylated tau at many sites, with ser199, thr205, and ser396 being the most favorable sites in cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-150364 |
Thr534 |
SRTPSLPtPPTREPK |
Homo sapiens |
|
| pmid |
sentence |
| 17078951 |
Here, we found that prephosphorylation by pka promotes gsk-3beta-catalyzed tau phosphorylation at thr181, ser199, ser202, thr205, thr217, thr231, ser396 and ser422 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171046 |
Thr548 |
KKVAVVRtPPKSPSS |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
Gsk3b phosphorylates tau at t231tau phosphorylation at t231, s235 and s262 also contributes to the dissociation of tau from microtubules |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255486 |
|
|
|
|
| pmid |
sentence |
| 21443865 |
The MAPT H1 haplotype and subhaplotypes may be associated with sporadic tauopathies including AD. And that, tau's phosphorylation is regulated by many protein kinases, including glycogen synthase kinase 3beta (GSK3B). |
|
| Publications: |
11 |
Organism: |
Homo Sapiens, |
| Tissue: |
Brain |
| Pathways: | Alzheimer |
| + |
CSNK1D | down-regulates
phosphorylation
|
MAPT |
0.382 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121709 |
Ser396 |
DDKKAKTsTRSSAKT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14761950 |
Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules.Here we characterized the contribution of one ck1 isoform, ckidelta, to the phosphorylation of tau at residues ser202/thr205 and ser396/ser404 in human embryonic kidney 293 cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121705 |
Ser519 |
SGYSSPGsPGTPGSR |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14761950 |
Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules.Here we characterized the contribution of one ck1 isoform, ckidelta, to the phosphorylation of tau at residues ser202/thr205 and ser396/ser404 in human embryonic kidney 293 cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121713 |
Ser721 |
PVVSGDTsPRHLSNV |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14761950 |
Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules.Here we characterized the contribution of one ck1 isoform, ckidelta, to the phosphorylation of tau at residues ser202/thr205 and ser396/ser404 in human embryonic kidney 293 cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121717 |
Thr522 |
SSPGSPGtPGSRSRT |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14761950 |
Casein kinase 1 delta phosphorylates tau and disrupts its binding to microtubules.Here we characterized the contribution of one ck1 isoform, ckidelta, to the phosphorylation of tau at residues ser202/thr205 and ser396/ser404 in human embryonic kidney 293 cells. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
GSK3B | down-regulates activity
phosphorylation
|
MAPT |
0.728 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249353 |
Ser512 |
PPKSGDRsGYSSPGS |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 9771888 |
Sequencing of 32P-labeled trypsin phosphopeptides from tau prephosphorylated by A-kinase (using unlabeled ATP) and further phosphorylated by GSK-3 in the presence of [gamma-32P]ATP revealed that Ser-195, Ser-198, Ser-199, Ser-202, Thr-205, Thr-231, Ser-235, Ser-262, Ser-356 and Ser-404 are phosphorylated, whereas if tau is not prephosphorylated by A-kinase, GSK-3 phosphorylates it at Thr-181, Ser-184, Ser-262, Ser-356 and Ser-400. These data suggest that (i) prephosphorylation of tau by A-kinase makes additional and different sites accessible for phosphorylation by GSK-3; (ii) phosphorylation of tau at these additional sites further inhibits the biological activity of tau in its ability to bind to microtubules and promote microtubule assembly. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249354 |
Ser515 |
SGDRSGYsSPGSPGT |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 9832145 |
Sequencing of 32P-labeled trypsin phosphopeptides from tau prephosphorylated by A-kinase (using unlabeled ATP) and further phosphorylated by GSK-3 in the presence of [gamma-32P]ATP revealed that Ser-195, Ser-198, Ser-199, Ser-202, Thr-205, Thr-231, Ser-235, Ser-262, Ser-356 and Ser-404 are phosphorylated, whereas if tau is not prephosphorylated by A-kinase, GSK-3 phosphorylates it at Thr-181, Ser-184, Ser-262, Ser-356 and Ser-400. These data suggest that (i) prephosphorylation of tau by A-kinase makes additional and different sites accessible for phosphorylation by GSK-3; (ii) phosphorylation of tau at these additional sites further inhibits the biological activity of tau in its ability to bind to microtubules and promote microtubule assembly. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249352 |
Ser516 |
GDRSGYSsPGSPGTP |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249343 |
Ser519 |
SGYSSPGsPGTPGSR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249344 |
Ser531 |
GSRSRTPsLPTPPTR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249345 |
Ser713 |
GAEIVYKsPVVSGDT |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249355 |
Ser717 |
VYKSPVVsGDTSPRH |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
Sequencing of 32P-labeled trypsin phosphopeptides from tau prephosphorylated by A-kinase (using unlabeled ATP) and further phosphorylated by GSK-3 in the presence of [gamma-32P]ATP revealed that Ser-195, Ser-198, Ser-199, Ser-202, Thr-205, Thr-231, Ser-235, Ser-262, Ser-356 and Ser-404 are phosphorylated, whereas if tau is not prephosphorylated by A-kinase, GSK-3 phosphorylates it at Thr-181, Ser-184, Ser-262, Ser-356 and Ser-400. These data suggest that (i) prephosphorylation of tau by A-kinase makes additional and different sites accessible for phosphorylation by GSK-3; (ii) phosphorylation of tau at these additional sites further inhibits the biological activity of tau in its ability to bind to microtubules and promote microtubule assembly. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249346 |
Ser721 |
PVVSGDTsPRHLSNV |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249351 |
Thr498 |
KTPPAPKtPPSSGEP |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249347 |
Thr522 |
SSPGSPGtPGSRSRT |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249348 |
Thr529 |
TPGSRSRtPSLPTPP |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249349 |
Thr534 |
SRTPSLPtPPTREPK |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249350 |
Thr548 |
KKVAVVRtPPKSPSS |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Publications: |
13 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
TTBK1 | down-regulates
phosphorylation
|
MAPT |
0.463 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148966 |
Ser515 |
SGDRSGYsSPGSPGT |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16923168 |
Direct tau phosphorylation by ttbk1 at ser198, ser199, ser202 and ser422, which are also phosphorylated in phfs. Ttbk1 also induces tau aggregation in human neuronal cells in a dose-dependent manner. We conclude that ttbk1 is a neuron-specific dual kinase involved in tau phosphorylation at ad-related sites and is also associated with tau aggregation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148970 |
Ser516 |
GDRSGYSsPGSPGTP |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16923168 |
Direct tau phosphorylation by ttbk1 at ser198, ser199, ser202 and ser422, which are also phosphorylated in phfs. Ttbk1 also induces tau aggregation in human neuronal cells in a dose-dependent manner. We conclude that ttbk1 is a neuron-specific dual kinase involved in tau phosphorylation at ad-related sites and is also associated with tau aggregation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148974 |
Ser519 |
SGYSSPGsPGTPGSR |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16923168 |
Direct tau phosphorylation by ttbk1 at ser198, ser199, ser202 and ser422, which are also phosphorylated in phfs. Ttbk1 also induces tau aggregation in human neuronal cells in a dose-dependent manner. We conclude that ttbk1 is a neuron-specific dual kinase involved in tau phosphorylation at ad-related sites and is also associated with tau aggregation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-148978 |
Ser739 |
GSIDMVDsPQLATLA |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16923168 |
Direct tau phosphorylation by ttbk1 at ser198, ser199, ser202 and ser422, which are also phosphorylated in phfs. Ttbk1 also induces tau aggregation in human neuronal cells in a dose-dependent manner. We conclude that ttbk1 is a neuron-specific dual kinase involved in tau phosphorylation at ad-related sites and is also associated with tau aggregation. |
|
| Publications: |
4 |
Organism: |
Homo Sapiens |
| + |
CDK5/CDK5R1 | down-regulates activity
phosphorylation
|
MAPT |
0.695 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251598 |
Ser516 |
GDRSGYSsPGSPGTP |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251588 |
Ser519 |
SGYSSPGsPGTPGSR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251589 |
Ser531 |
GSRSRTPsLPTPPTR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251590 |
Ser552 |
VVRTPPKsPSSAKSR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251591 |
Ser713 |
GAEIVYKsPVVSGDT |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251592 |
Ser721 |
PVVSGDTsPRHLSNV |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251597 |
Thr498 |
KTPPAPKtPPSSGEP |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251593 |
Thr522 |
SSPGSPGtPGSRSRT |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251594 |
Thr529 |
TPGSRSRtPSLPTPP |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251595 |
Thr534 |
SRTPSLPtPPTREPK |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251596 |
Thr548 |
KKVAVVRtPPKSPSS |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Publications: |
11 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
PP2B | up-regulates 
dephosphorylation
|
MAPT |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164659 |
Ser516 |
GDRSGYSsPGSPGTP |
Homo sapiens |
|
| pmid |
sentence |
| 20308788 |
Among the sites studied, thr205, thr212, ser214, and ser262 were the most favorable sites, and ser199 and ser404 were the least favorable sites for pp2a in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164663 |
Ser579 |
NVKSKIGsTENLKHQ |
Homo sapiens |
|
| pmid |
sentence |
| 20308788 |
Among the sites studied, thr205, thr212, ser214, and ser262 were the most favorable sites, and ser199 and ser404 were the least favorable sites for pp2a in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164667 |
Ser721 |
PVVSGDTsPRHLSNV |
Homo sapiens |
|
| pmid |
sentence |
| 20308788 |
Among the sites studied, thr205, thr212, ser214, and ser262 were the most favorable sites, and ser199 and ser404 were the least favorable sites for pp2a in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164671 |
Thr522 |
SSPGSPGtPGSRSRT |
Homo sapiens |
|
| pmid |
sentence |
| 20308788 |
Among the sites studied, thr205, thr212, ser214, and ser262 were the most favorable sites, and ser199 and ser404 were the least favorable sites for pp2a in vitro. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-164675 |
Thr529 |
TPGSRSRtPSLPTPP |
Homo sapiens |
|
| pmid |
sentence |
| 20308788 |
Among the sites studied, thr205, thr212, ser214, and ser262 were the most favorable sites, and ser199 and ser404 were the least favorable sites for pp2a in vitro. |
|
| Publications: |
5 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
CDK5 | down-regulates activity
phosphorylation
|
MAPT |
0.754 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249327 |
Ser516 |
GDRSGYSsPGSPGTP |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249317 |
Ser519 |
SGYSSPGsPGTPGSR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249318 |
Ser531 |
GSRSRTPsLPTPPTR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249319 |
Ser552 |
VVRTPPKsPSSAKSR |
Homo sapiens |
|
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249320 |
Ser713 |
GAEIVYKsPVVSGDT |
Homo sapiens |
|
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249321 |
Ser721 |
PVVSGDTsPRHLSNV |
Homo sapiens |
|
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249326 |
Thr498 |
KTPPAPKtPPSSGEP |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249322 |
Thr522 |
SSPGSPGtPGSRSRT |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249323 |
Thr529 |
TPGSRSRtPSLPTPP |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249324 |
Thr534 |
SRTPSLPtPPTREPK |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249325 |
Thr548 |
KKVAVVRtPPKSPSS |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 12387894 |
We found that cdk5 phosphorylated tau(441) at Thr-181, Ser-199, Ser-202, Thr-205, Thr-212, Ser-214, Thr-217, Thr-231, Ser-235, Ser-396, and Ser-404, but not at Ser-262, Ser-400, Thr-403, Ser-409, Ser-413, or Ser-422. GSK-3beta phosphorylated all the cdk5-catalyzed sites above except Ser-235. |
|
| Publications: |
11 |
Organism: |
Homo Sapiens |
| + |
MAPK12 | down-regulates activity
phosphorylation
|
MAPT |
0.504 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250084 |
Ser519 |
SGYSSPGsPGTPGSR |
in vitro |
|
| pmid |
sentence |
| 9199504 |
Phosphorylation of tau by SAPK3 and SAPK4 markedly reduced the ability of tau to promote microtubule assembly. SAPK3 (also called ERK6 and p38) and SAPK4 phosphorylate recombinant tau protein at multiple Ser/Thr-Pro sites that are hyperphosphorylated in PHF-tau, with SAPK4 and SAPK3 being the most effective. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250085 |
Ser637 |
VDLSKVTsKCGSLGN |
in vitro |
|
| pmid |
sentence |
| 9199504 |
Phosphorylation of tau by SAPK3 and SAPK4 markedly reduced the ability of tau to promote microtubule assembly. SAPK3 (also called ERK6 and p38) and SAPK4 phosphorylate recombinant tau protein at multiple Ser/Thr-Pro sites that are hyperphosphorylated in PHF-tau, with SAPK4 and SAPK3 being the most effective. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250086 |
Thr498 |
KTPPAPKtPPSSGEP |
in vitro |
|
| pmid |
sentence |
| 9199504 |
Phosphorylation of tau by SAPK3 and SAPK4 markedly reduced the ability of tau to promote microtubule assembly. SAPK3 (also called ERK6 and p38) and SAPK4 phosphorylate recombinant tau protein at multiple Ser/Thr-Pro sites that are hyperphosphorylated in PHF-tau, with SAPK4 and SAPK3 being the most effective. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250087 |
Thr522 |
SSPGSPGtPGSRSRT |
in vitro |
|
| pmid |
sentence |
| 9199504 |
Phosphorylation of tau by SAPK3 and SAPK4 markedly reduced the ability of tau to promote microtubule assembly. SAPK3 (also called ERK6 and p38) and SAPK4 phosphorylate recombinant tau protein at multiple Ser/Thr-Pro sites that are hyperphosphorylated in PHF-tau, with SAPK4 and SAPK3 being the most effective. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250088 |
Thr548 |
KKVAVVRtPPKSPSS |
in vitro |
|
| pmid |
sentence |
| 9199504 |
Phosphorylation of tau by SAPK3 and SAPK4 markedly reduced the ability of tau to promote microtubule assembly. SAPK3 (also called ERK6 and p38) and SAPK4 phosphorylate recombinant tau protein at multiple Ser/Thr-Pro sites that are hyperphosphorylated in PHF-tau, with SAPK4 and SAPK3 being the most effective. |
|
| Publications: |
5 |
Organism: |
In Vitro |
| + |
MAPK1 | down-regulates activity
phosphorylation
|
MAPT |
0.552 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249416 |
Ser519 |
SGYSSPGsPGTPGSR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 10737616 |
Using nanoelectrospray mass spectrometry, we have undertaken an extensive comparison of phosphorylation in vitro by several candidate tau kinases, namely, JNK, p38, ERK2, and glycogen synthase kinase 3beta (GSK3beta). Between 10 and 15 sites were identified for each kinase. The three MAP kinases phosphorylated Ser202 and Thr205 but not detectably Ser199, whereas conversely GSK3beta phosphorylated Ser199 but not detectably Ser202 or Thr205. Phosphorylated Ser404 was found with all of these kinases except JNK. The MAP kinases may not be strictly proline specific: p38 phosphorylated the nonproline sites Ser185, Thr245, Ser305, and Ser356, whereas ERK2 was the most strict. All of the sites detected except Thr245 and Ser305 are known or suspected phosphorylation sites in paired helical filament-tau extracted from Alzheimer brains. Thus, the three MAP kinases and GSK3beta are importantly all strong candidates as tau kinases that may be involved in the pathogenic hyperphosphorylation of tau in Alzheimer's disease. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249418 |
Ser721 |
PVVSGDTsPRHLSNV |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 10737616 |
Using nanoelectrospray mass spectrometry, we have undertaken an extensive comparison of phosphorylation in vitro by several candidate tau kinases, namely, JNK, p38, ERK2, and glycogen synthase kinase 3beta (GSK3beta). Between 10 and 15 sites were identified for each kinase. The three MAP kinases phosphorylated Ser202 and Thr205 but not detectably Ser199, whereas conversely GSK3beta phosphorylated Ser199 but not detectably Ser202 or Thr205. Phosphorylated Ser404 was found with all of these kinases except JNK. The MAP kinases may not be strictly proline specific: p38 phosphorylated the nonproline sites Ser185, Thr245, Ser305, and Ser356, whereas ERK2 was the most strict. All of the sites detected except Thr245 and Ser305 are known or suspected phosphorylation sites in paired helical filament-tau extracted from Alzheimer brains. Thus, the three MAP kinases and GSK3beta are importantly all strong candidates as tau kinases that may be involved in the pathogenic hyperphosphorylation of tau in Alzheimer's disease. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249417 |
Thr522 |
SSPGSPGtPGSRSRT |
Homo sapiens |
|
| pmid |
sentence |
| 10737616 |
Using nanoelectrospray mass spectrometry, we have undertaken an extensive comparison of phosphorylation in vitro by several candidate tau kinases, namely, JNK, p38, ERK2, and glycogen synthase kinase 3beta (GSK3beta). Between 10 and 15 sites were identified for each kinase. The three MAP kinases phosphorylated Ser202 and Thr205 but not detectably Ser199, whereas conversely GSK3beta phosphorylated Ser199 but not detectably Ser202 or Thr205. Phosphorylated Ser404 was found with all of these kinases except JNK. The MAP kinases may not be strictly proline specific: p38 phosphorylated the nonproline sites Ser185, Thr245, Ser305, and Ser356, whereas ERK2 was the most strict. All of the sites detected except Thr245 and Ser305 are known or suspected phosphorylation sites in paired helical filament-tau extracted from Alzheimer brains. Thus, the three MAP kinases and GSK3beta are importantly all strong candidates as tau kinases that may be involved in the pathogenic hyperphosphorylation of tau in Alzheimer's disease. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
DYRK1A | down-regulates
phosphorylation
|
MAPT |
0.439 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171030 |
Ser519 |
SGYSSPGsPGTPGSR |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
Dyrk1a phosphorylates tau at least at s202, t212 and s404, but t212 phosphorylation is known to initiate tau hyperphosphorylation by gsk3b (ryoo et al., 2007;woods et al., 2001) and has been demonstrated to have a role in alternative splicing of taumrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171034 |
Ser721 |
PVVSGDTsPRHLSNV |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
Dyrk1a phosphorylates tau at least at s202, t212 and s404, but t212 phosphorylation is known to initiate tau hyperphosphorylation by gsk3b (ryoo et al., 2007;woods et al., 2001) and has been demonstrated to have a role in alternative splicing of taumrna |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171038 |
Thr529 |
TPGSRSRtPSLPTPP |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
Dyrk1a phosphorylates tau at least at s202, t212 and s404, but t212 phosphorylation is known to initiate tau hyperphosphorylation by gsk3b (ryoo et al., 2007;woods et al., 2001) and has been demonstrated to have a role in alternative splicing of taumrna |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKACA | down-regulates activity
phosphorylation
|
MAPT |
0.443 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250006 |
Ser531 |
GSRSRTPsLPTPPTR |
in vitro |
|
| pmid |
sentence |
| 9614189 |
S214 can be rapidly and selectively phosphorylated in vitro by PKA, and this single site strongly affects tau's ability to bind and stabilize microtubules. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250008 |
Ser579 |
NVKSKIGsTENLKHQ |
in vitro |
|
| pmid |
sentence |
| 12435421 |
Ser214, Ser262, Ser356, and Ser409 of tau441‚ were phosphorylated by PKA. tau in PHF is abnormally hyperphosphorylated and lacks its normal activity to bind to microtubules and to stimulate their assembly |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250007 |
Ser673 |
RVQSKIGsLDNITHV |
in vitro |
|
| pmid |
sentence |
| 12435421 |
Ser214, Ser262, Ser356, and Ser409 of tau441‚ were phosphorylated by PKA. tau in PHF is abnormally hyperphosphorylated and lacks its normal activity to bind to microtubules and to stimulate their assembly |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250009 |
Ser726 |
DTSPRHLsNVSSTGS |
in vitro |
|
| pmid |
sentence |
| 12435421 |
Ser214, Ser262, Ser356, and Ser409 of tau441‚ were phosphorylated by PKA. tau in PHF is abnormally hyperphosphorylated and lacks its normal activity to bind to microtubules and to stimulate their assembly |
|
| Publications: |
4 |
Organism: |
In Vitro |
| + |
CAMK2A | down-regulates activity
phosphorylation
|
MAPT |
0.578 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249316 |
Ser552 |
VVRTPPKsPSSAKSR |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 10090741 |
We found that when tau was first phosphorylated by A-kinase, C-kinase, cdk5, or CaM kinase II and then by GSK-3, its binding to microtubules was inhibited by 45, 61, 78, and 79%, respectively. Further, the kinase combinations cdk5/GSK-3 and CaM kinase II/GSK-3 rapidly phosphorylated the sites Thr 231 and Ser 235. When these sites were individually replaced by Ala and the phosphorylation experiments repeated, tau binding to microtubules was inhibited by 54 and 71%, respectively. By comparison, when Ser 262 was replaced by Ala, tau binding to microtubules was inhibited by only 8% after phosphorylation by CaM kinase II. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249314 |
Ser579 |
NVKSKIGsTENLKHQ |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 10090741 |
We found that when tau was first phosphorylated by A-kinase, C-kinase, cdk5, or CaM kinase II and then by GSK-3, its binding to microtubules was inhibited by 45, 61, 78, and 79%, respectively. Further, the kinase combinations cdk5/GSK-3 and CaM kinase II/GSK-3 rapidly phosphorylated the sites Thr 231 and Ser 235. When these sites were individually replaced by Ala and the phosphorylation experiments repeated, tau binding to microtubules was inhibited by 54 and 71%, respectively. By comparison, when Ser 262 was replaced by Ala, tau binding to microtubules was inhibited by only 8% after phosphorylation by CaM kinase II. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249315 |
Thr548 |
KKVAVVRtPPKSPSS |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 10090741 |
We found that when tau was first phosphorylated by A-kinase, C-kinase, cdk5, or CaM kinase II and then by GSK-3, its binding to microtubules was inhibited by 45, 61, 78, and 79%, respectively. Further, the kinase combinations cdk5/GSK-3 and CaM kinase II/GSK-3 rapidly phosphorylated the sites Thr 231 and Ser 235. When these sites were individually replaced by Ala and the phosphorylation experiments repeated, tau binding to microtubules was inhibited by 54 and 71%, respectively. By comparison, when Ser 262 was replaced by Ala, tau binding to microtubules was inhibited by only 8% after phosphorylation by CaM kinase II. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PHKG1 | down-regulates activity
phosphorylation
|
MAPT |
0.318 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250283 |
Ser554 |
RTPPKSPsSAKSRLQ |
in vitro |
|
| pmid |
sentence |
| 8999860 |
Muscle phosphorylase kinase phosphorylates Ser237, Ser262, Ser285, Ser305, and Ser352 of human tau. in vitro phosphorylation of tau on Ser262 alone strongly reduced the ability of tau to bind microtubules whereas the phosphorylation of many Ser/Thr-Pro motif sites of tau showed moderate effects on the binding of tau to microtubules |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250284 |
Ser579 |
NVKSKIGsTENLKHQ |
in vitro |
|
| pmid |
sentence |
| 8999860 |
Muscle phosphorylase kinase phosphorylates Ser237, Ser262, Ser285, Ser305, and Ser352 of human tau. in vitro phosphorylation of tau on Ser262 alone strongly reduced the ability of tau to bind microtubules whereas the phosphorylation of many Ser/Thr-Pro motif sites of tau showed moderate effects on the binding of tau to microtubules |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250285 |
Ser602 |
INKKLDLsNVQSKCG |
in vitro |
|
| pmid |
sentence |
| 8999860 |
Muscle phosphorylase kinase phosphorylates Ser237, Ser262, Ser285, Ser305, and Ser352 of human tau. in vitro phosphorylation of tau on Ser262 alone strongly reduced the ability of tau to bind microtubules whereas the phosphorylation of many Ser/Thr-Pro motif sites of tau showed moderate effects on the binding of tau to microtubules |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250286 |
Ser622 |
KHVPGGGsVQIVYKP |
in vitro |
|
| pmid |
sentence |
| 8999860 |
Muscle phosphorylase kinase phosphorylates Ser237, Ser262, Ser285, Ser305, and Ser352 of human tau. in vitro phosphorylation of tau on Ser262 alone strongly reduced the ability of tau to bind microtubules whereas the phosphorylation of many Ser/Thr-Pro motif sites of tau showed moderate effects on the binding of tau to microtubules |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250287 |
Ser669 |
DFKDRVQsKIGSLDN |
in vitro |
|
| pmid |
sentence |
| 8999860 |
Muscle phosphorylase kinase phosphorylates Ser237, Ser262, Ser285, Ser305, and Ser352 of human tau. in vitro phosphorylation of tau on Ser262 alone strongly reduced the ability of tau to bind microtubules whereas the phosphorylation of many Ser/Thr-Pro motif sites of tau showed moderate effects on the binding of tau to microtubules |
|
| Publications: |
5 |
Organism: |
In Vitro |
| + |
MARK1 | down-regulates
phosphorylation
|
MAPT |
0.44 |
| 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 |
| + |
CHEK2 | down-regulates
phosphorylation
|
MAPT |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171026 |
Ser579 |
NVKSKIGsTENLKHQ |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
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: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA | down-regulates
phosphorylation
|
MAPT |
0.443 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-60659 |
Ser579 |
NVKSKIGsTENLKHQ |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 9771888 |
Tau is phosphorylated by gsk-3 at several sites found in alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by a-kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171066 |
Thr548 |
KKVAVVRtPPKSPSS |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
However, other kinases, such as cdk5, p38 and pka, also phosphorylate tau at t231tau phosphorylation at t231, s235 and s262 also contributes to the dissociation of tau from microtubules |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
MARK1 | down-regulates activity
phosphorylation
|
MAPT |
0.44 |
| 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 |
| + |
GSK3A | down-regulates
phosphorylation
|
MAPT |
0.44 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-60651 |
Ser579 |
NVKSKIGsTENLKHQ |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 9771888 |
Tau is phosphorylated by gsk-3 at several sites found in alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by a-kinase. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-29364 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 7566348 |
The ability of p42 map and p44 map kinases, glycogen synthase kinases 3 alpha and 3 beta (gsk-3 alpha and gsk-3 beta) to phosphorylate tau in transfected cos cells was investigated. Both gsk-3 alpha and gsk-3 beta phosphorylated tau to produce a phf-like state of phosphorylation but the map kinases failed to induce such a transformation in tau. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
PKN1 | down-regulates
phosphorylation
|
MAPT |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-84958 |
Ser637 |
VDLSKVTsKCGSLGN |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 11104762 |
Phosphorylation of tau is regulated by pknthere is a pkn-specific phosphorylation site, ser-320, in mbdsthus pkn serves as a regulator of microtubules by specific phosphorylation of tau, which leads to disruption of tubulin assembly. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Ovary |
| + |
GSK3A | down-regulates activity
phosphorylation
|
MAPT |
0.44 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249342 |
Ser641 |
KVTSKCGsLGNIHHK |
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 7706316 |
Microtubule-associated protein/microtubule affinity-regulating kinase (p110mark). A novel protein kinase that regulates tau-microtubule interactions and dynamic instability by phosphorylation at the Alzheimer-specific site serine 262. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
p38 | down-regulates
phosphorylation
|
MAPT |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-171062 |
Thr548 |
KKVAVVRtPPKSPSS |
Homo sapiens |
|
| pmid |
sentence |
| 21215781 |
However, other kinases, such as cdk5, p38 and pka, also phosphorylate tau at t231tau phosphorylation at t231, s235 and s262 also contributes to the dissociation of tau from microtubules |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYK | down-regulates
phosphorylation
|
MAPT |
0.479 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-159648 |
Tyr18 |
MEDHAGTyGLGDRKD |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18070606 |
We established that tyrosine 18 was the primary residue in tau phosphorylated by sykphosphorylation of tau by syk could be involved in neurite outgrowth. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FYN | down-regulates
phosphorylation
|
MAPT |
0.552 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-123099 |
Tyr18 |
MEDHAGTyGLGDRKD |
Homo sapiens |
|
| pmid |
sentence |
| 14999081 |
In this study we determined that human tau tyr18 was phosphorylated by the src family tyrosine kinase fyn. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAMK2A | down-regulates
phosphorylation
|
MAPT |
0.578 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-255490 |
|
|
|
|
| pmid |
sentence |
| 15621017 |
Thus, the increased immunoreactivity of CaMKII-α of the remaining neurons may be the consequence of the altered calcium dynamics in neurons. There is evidence indicating that CaMKII might participate in tau phosphorylation in AD. |
|
| Publications: |
1 |
| + |
CAPN3 | down-regulates activity
cleavage
|
MAPT |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251605 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25969760 |
Besides tau phosphorylation, calpain activation might play a role in tau-mediated neurodegeneration by inducing tau cleavage. In vitro studies have shown that both fetal and adult tau isoforms are rapidly proteolyzed by calpains |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
APOE | up-regulates activity
binding
|
MAPT |
0.585 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262588 |
|
|
|
|
| pmid |
sentence |
| 7566652 |
Isoform specific interactions of ApoE have been shown with the microtubule-associated protein tau, which forms the neurofibrillary tangle in this disease.|Phosphorylation of serine262 in domain I of tau decreases tau binding to microtubules and also abolishes binding by ApoE3. |
|
| Publications: |
1 |
| + |
LRRK2 | down-regulates
phosphorylation
|
MAPT |
0.544 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-195756 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22303461 |
Lrrk2 directly phosphorylates tubulin-associated tau, but not free tau;(iii) lrrk2 phosphorylates tau at thr181 as one of the target sites;. furthermore, we revealed that lrrk2-mediated phosphorylation of tau reduces its tubulin-binding ability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PPP2R1A | down-regulates
dephosphorylation
|
MAPT |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-130136 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15525651 |
Galpha12 directly interacts with pp2a: evidence for galpha12-stimulated pp2a phosphatase activity and dephosphorylation of microtubule-associated protein, tau. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPT | up-regulates 
|
Neurofibrillary tangle formation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251642 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11578751 |
Tau is a multifunctional microtubule-associated protein that plays major roles in the assembly of microtubules, the stabilization of microtubules against dynamic instability, and in bridging these polymers with other cytoskeletal filaments 43, 44, 45, 46 and 47. In normal brain, the equilibrium between phosphorylations and dephosphorylations of tau modulates the stability of the cytoskeleton and consequently axonal morphology. The earliest modification found in Alzheimer brains consists of hyperphosphorylations on tau by the action of different protein kinase and phosphatase systems that appear to lead to structural and conformational changes in this protein, thus affecting its binding with tubulin and the capacity to promote microtubule assembly |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
ALPL | down-regulates activity
dephosphorylation
|
MAPT |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277097 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24646911 |
TNAP dephosphorylates overphosphorylated tau once it is released upon neuronal death. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPT | down-regulates 
|
Neurofibrillary tangle formation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251639 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11578751 |
Tau is a multifunctional microtubule-associated protein that plays major roles in the assembly of microtubules, the stabilization of microtubules against dynamic instability, and in bridging these polymers with other cytoskeletal filaments 43, 44, 45, 46 and 47. In normal brain, the equilibrium between phosphorylations and dephosphorylations of tau modulates the stability of the cytoskeleton and consequently axonal morphology. The earliest modification found in Alzheimer brains consists of hyperphosphorylations on tau by the action of different protein kinase and phosphatase systems that appear to lead to structural and conformational changes in this protein, thus affecting its binding with tubulin and the capacity to promote microtubule assembly |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
CAPN1 | down-regulates activity
cleavage
|
MAPT |
0.34 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251584 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
Besides tau phosphorylation, calpain activation might play a role in tau-mediated neurodegeneration by inducing tau cleavage. In vitro studies have shown that both fetal and adult tau isoforms are rapidly proteolyzed by calpains |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Alzheimer |
| + |
MAPK14 | up-regulates
phosphorylation
|
MAPT |
0.322 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-166611 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20626350 |
A large number of cytosolic proteins can be phosphorylated by p38 mapks, including phospholipase a2, the microtubule-associated protein tau, nhe-1, cyclin d1, cdk inhibitors, bcl2 family proteins, growth factor receptors or keratins. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | P38 Signaling |
| + |
CAPN2 | down-regulates activity
cleavage
|
MAPT |
0.445 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251611 |
|
|
Homo sapiens |
Alzheimer Disease Specific Cell Type |
| pmid |
sentence |
| 25969760 |
Besides tau phosphorylation, calpain activation might play a role in tau-mediated neurodegeneration by inducing tau cleavage. In vitro studies have shown that both fetal and adult tau isoforms are rapidly proteolyzed by calpains |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PTEN | up-regulates activity
dephosphorylation
|
MAPT |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-277079 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 27221467 |
Reduced phosphorylation of PTEN can dramatically increase tau phosphorylation and impair the ability of tau to bind to microtubules . |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
MAPT
- 
- 