| + |
KIF5B | up-regulates 
|
Organelle_transport |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264068 |
|
|
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 |
| + |
KIF5B | up-regulates activity 
relocalization
|
JAKMIP1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260989 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 17532644 |
Marlin-1 is associated with kinesin-I and suggest that the movement of Marlin-1 is mediated by plus end microtubuledependent molecular motors |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
KIF5B | up-regulates
|
Plus-end directed sliding movement |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272520 |
|
|
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 |
| + |
KIF5B | up-regulates activity
relocalization
|
GABBR1 |
0.255 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260990 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 17532644 |
GABABR1 co-immunoprecipitated with Marlin-1 and kinesin-I, providing evidence for the existence of a complex between these proteins. Kinesin-I modulates GABAB receptor transport. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
KIF5B | up-regulates activity
relocalization
|
SYBU |
0.564 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264811 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15459722 |
Conventional kinesin I heavy chain binds to syntabulin and associates with syntabulin-linked syntaxin vesicles in vivo. These findings suggest that syntabulin functions as a linker molecule that attaches syntaxin-cargo vesicles to kinesin I, enabling the transport of syntaxin-1 to neuronal processes. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DISC1 | up-regulates activity
binding
|
KIF5B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-252161 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 17202468 |
We identified Kinesin-1, a microtubule-dependent and plus-end directed motor, as a DISC1-interacting molecule. Our results show that DISC1 links Kinesin-1 to the NUDEL/LIS1/14-3-3ε complex, serves as the cargo receptor, and regulates the transport of the complex to axons, leading to axon elongation. DISC1 directly interacted with kinesin heavy chain of Kinesin-1. Kinesin-1 interacted with the NUDEL/LIS1/14-3-3ε complex through DISC1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
KTN1 | up-regulates
binding
|
KIF5B |
0.607 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-128092 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 15316074 |
This study demonstrated the effect of kinectin-kinesin interaction on lysosome dynamics and observed that the kinesin-binding domain of kinectin can significantly enhance the mt-stimulated atpase activity of kinesin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
DOP1A-MON2, golgi-endosome traffic complex | up-regulates activity
binding
|
KIF5B |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-281441 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31324770 |
Here, we find that Dopey1 and Mon2 assemble into a complex and localize to the Golgi, endolysosome and endoplasmic reticulum exit site. The Golgi localization of Dopey1 and Mon2 requires their binding to phosphatidylinositol-4-phosphate and phosphatidic acid, respectively, two lipids known for the biogenesis of membrane carriers and the specification of organelle identities. The N-terminus of Dopey1 further interacts with kinesin-1, a plus-end or centrifugal-direction microtubule motor. Dopey1-Mon2 complex functions as a dual-lipid-regulated cargo-adaptor to recruit kinesin-1 to secretory and endocytic organelles or membrane carriers for centrifugally biased bidirectional transport. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
KIF5B
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