+ |
DYRK2 | down-regulates quantity by destabilization
phosphorylation
|
KATNA1 |
0.524 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262847 |
Ser109 |
VPVERRPsPGPRKRQ |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19287380 |
DYRK2 mediated phosphorylation is required for Katanin p60 degradation. Serine 42, serine 109 and threonine 133 are likely to be the major DYRK2 phosphorylation sites as single mutations for these sites showed reduced phosphorylation by DYRK2 and the triple mutant showed almost no DYRK2 mediated phosphorylation (Fig. 5d). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262848 |
Ser42 |
QMNKYLYsVKDTYLQ |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19287380 |
DYRK2 mediated phosphorylation is required for Katanin p60 degradation. Serine 42, serine 109 and threonine 133 are likely to be the major DYRK2 phosphorylation sites as single mutations for these sites showed reduced phosphorylation by DYRK2 and the triple mutant showed almost no DYRK2 mediated phosphorylation (Fig. 5d). |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262849 |
Thr133 |
HGNRPSTtVRVHRSS |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19287380 |
DYRK2 mediated phosphorylation is required for Katanin p60 degradation. Serine 42, serine 109 and threonine 133 are likely to be the major DYRK2 phosphorylation sites as single mutations for these sites showed reduced phosphorylation by DYRK2 and the triple mutant showed almost no DYRK2 mediated phosphorylation (Fig. 5d). |
|
Publications: |
3 |
Organism: |
Homo Sapiens |
+ |
EDVP | down-regulates quantity by destabilization
polyubiquitination
|
KATNA1 |
0.316 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271793 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
19287380 |
EDVP-DYRK2 complex regulates Katanin p60 ubiquitination. Katanin p60 was polyubiquitinated in the presence of the intact DYRK2-EDVP, but its ubiquitination was severely reduced by the depletion of DYRK2, EDD, DDB1 or VPRBP (Fig. 3d). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KATNA1 | down-regulates
|
Microtubule_polimerization |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271794 |
|
|
Homo sapiens |
|
pmid |
sentence |
19287380 |
Katanin, one of the best-characterized microtubule (MT) severing proteins, is composed of two subunits: catalytic p60-katanin, and regulatory p80-katanin. p60-katanin triggers MT reorganization by severing them. MT reorganization is essential for both mitotic cells and post-mitotic neurons in numerous vital processes such as intracellular transport, mitosis, cellular differentiation and apoptosis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KATNA1 | up-regulates activity
binding
|
KATNB1 |
0.779 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267174 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10751153 |
In its active ATP-bound state, KATNA1 forms hexameric rings capable of binding to and severing microtubule polymers. Typically, KATNA1 binding to KATNB1 enhances severing, likely due to KATNB1 increasing the stability of the KATNA1 hexamer |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KATNB1 | up-regulates quantity by stabilization
binding
|
KATNA1 |
0.779 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-267173 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10751153 |
In its active ATP-bound state, KATNA1 forms hexameric rings capable of binding to and severing microtubule polymers. Typically, KATNA1 binding to KATNB1 enhances severing, likely due to KATNB1 increasing the stability of the KATNA1 hexamer |
|
Publications: |
1 |
Organism: |
Homo Sapiens |