| + |
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 |
| + |
MARK2 | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.706 |
| 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 |
| + |
MAPK3 | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.499 |
| 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 |
| + |
PRKCB | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.259 |
| 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) |
0.266 |
| 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 |
| + |
PRKCG | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.271 |
| 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 |
| + |
PRKCE | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.271 |
| 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 |
| + |
PRKCZ | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.269 |
| 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 |
| + |
PRKCI | down-regulates activity
phosphorylation
|
MAPT (isoform 2) |
0.266 |
| 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 |
3.0
MAPT
- 
- 