| + |
JNK | up-regulates activity 
phosphorylation
|
KIF5C |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264063 |
Ser176 |
CTERFVSsPEEVMDV |
Homo sapiens |
|
| pmid |
sentence |
| 27013971 |
JNK phosphorylates KIF5C on S176 in the motor domain; a site that we show is phosphorylated in brain. In the peroxisome cargo-bound state, S176 phosphorylated KIF5C(1-560) transports to microtubule plus ends, whereas dephosphorylated KIF5C(1-560) is bound tightly to microtubules resulting in an immobile state. As a consequence, phosphorylation of S176 can facilitate plus-end cargo transport by KIF5C(1-560). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
MAPK10 | down-regulates activity 
phosphorylation
|
KIF5C |
0.326 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262950 |
Ser176 |
CTERFVSsPEEVMDV |
in vitro |
|
| pmid |
sentence |
| 19525941 |
Mass spectrometry identified a residue in the kinesin-1 motor domain that was phosphorylated by JNK3 and this modification reduced kinesin-1 binding to microtubules. JNK3 phosphorylates kinesin-1 at Ser176 |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
KIF5C | up-regulates 
|
Plus-end directed sliding movement |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272518 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19773780 |
In general, N-kinesins and C-kinesins drive microtubule plus end- and minus end-directed motilities, respectively, and M-kinesins depolymerize microtubules1,9 (Box 1).|Forty-five genes that encode kinesin superfamily proteins (also known as KIFs) have been discovered in the mouse and human genomes.|KIFs are molecular motors that directionally transport various cargos, including membranous organelles, protein complexes and mRNAs, along the microtubule system. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HAP1 | up-regulates activity
binding
|
KIF5C |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264062 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31757889 |
HAP1 and GRIP1 are kinesin-1 adaptors that have been implicated individually in the transport of vesicular cargoes in the dendrites of neurons. We find that HAP1a and GRIP1 form a protein complex in the brain, and co-operate to activate the kinesin-1 subunit KIF5C in vitro |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KIF5C | up-regulates activity
binding
|
TRAK2 |
0.566 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264064 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 24161670 |
Trafficking kinesin proteins (TRAKs) are kinesin adaptors. They bind the cargo binding domain of kinesin-1 motor proteins forming a link between the motor and their cargoes. This supports the idea that the KIF5A–TRAK2 interaction is multivalent and could act to ensure stable motor-cargo interaction during intracellular trafficking; dimerization of both motor and adaptor molecules further enhances this stability (Fig. 6). A similar multivalent profile was found for the TRAK2 binding site within the kinesin-1 isoform, KIF5C. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KIF5C | up-regulates
|
Organelle_transport |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264066 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 9438838 |
The kinesin superfamily of proteins plays a major role in this complex organelle transport. Kinesin is primarily associated with anterogradely transported membranous organelles in nerve axons. KIF5B and HsuKHC are expressed ubiquitously in many tissues, whereas KIF5A, KIF5C, and HsnKHC are specific to nerve tissue. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
GRIP1 | up-regulates activity
binding
|
KIF5C |
0.33 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264061 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31757889 |
HAP1 and GRIP1 are kinesin-1 adaptors that have been implicated individually in the transport of vesicular cargoes in the dendrites of neurons. We find that HAP1a and GRIP1 form a protein complex in the brain, and co-operate to activate the kinesin-1 subunit KIF5C in vitro |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
3.0
KIF5C
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