+ |
PRKAA1 | up-regulates
phosphorylation
|
KLC2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-174681 |
Ser582 |
PRMKRASsLNFLNKS |
Homo sapiens |
|
pmid |
sentence |
21725060 |
Consistent with phosphorylation of both ser545 and ser582 of klc2 contributing to its 14-3-3 binding, a ser545ala mutant of klc2 could be phosphorylated in vitro by ampk on ser582 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
AMPK | up-regulates
phosphorylation
|
KLC2 |
0.292 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-216468 |
Ser582 |
PRMKRASsLNFLNKS |
Homo sapiens |
|
pmid |
sentence |
21725060 |
Consistent with phosphorylation of both ser545 and ser582 of klc2 contributing to its 14-3-3 binding, a ser545ala mutant of klc2 could be phosphorylated in vitro by ampk on ser582 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
KLC2 | up-regulates activity
binding
|
FYCO1 |
0.35 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260599 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
25855459 |
Interestingly, bead capture assays indicated that the middle part of FYCO1 (residues 585–1233) interacts directly with the KLC2 light chain of kinesin 1 (Fig. 3a and Extended Data Fig. 7a, b). Residues 735–773 of FYCO1 were found to be necessary for its kinesin-1 binding (Fig. 3c and Extended Data Fig. 7b, c), and FYCO1(Δ735–773)-positive LEs failed to translocate to the cell periphery (Extended Data Fig. 7e). |
|
Publications: |
1 |
Organism: |
Homo Sapiens |