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Literature summary for 5.6.1.3 extracted from
- Motor domain phosphorylation modulates kinesin-1 transport (2013), J. Biol. Chem., 288, 32612-32621.
Application
| Application | Comment | Organism |
|---|---|---|
| pharmacology | a bias that favors motion toward the minus-end of microtubules might be used to tune transport in healthy cells when properly regulated but contribute to a disease state when misregulated | Mus musculus |
| pharmacology | a bias that favors motion toward the minus-end of microtubules, cf. EC 3.6.4.5, might be used to tune transport in healthy cells when properly regulated but contribute to a disease state when misregulated | Homo sapiens |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression of C-terminally His-and biotin-tagged heavy chain residues 1-432 in Escherichia coli strain BL21 | Homo sapiens |
| recombinant expression of mouse KIF5B kinesin heavy chain, truncated at alanine 888 with a C-terminal biotin tag and N-terminal His6-tagged enzyme KIF5B, expression of C-terminally FLAG-tagged K888 heavy chain wild-type and mutants in Spodoptera frugiperda Sf9 cells using a baculovirus expression system | Mus musculus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| S175A | site-directed mutagenesis, modifying residue 175 decreases the kinesin stall force and its velocity while working against a load | Mus musculus |
| S175D | site-directed mutagenesis, modifying residue 175 decreases the kinesin stall force and its velocity while working against a load | Mus musculus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | kinesin performs autoinhibition, addition of a negative charge at Ser175 favors the autoinhibited conformation of kinesin | Mus musculus |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | microtubule-activated ATPase kinetics of wild-type and mutant enzymes | Mus musculus | |
| 0.035 | - |
ATP | recombinant wild-type K888, pH and temperature not specified in the publication | Mus musculus |  |
| 0.044 | - |
ATP | recombinant K888 mutants S175A and S175D, pH and temperature not specified in the publication | Mus musculus | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| microtubule | - |
Homo sapiens | 5874 | - |
| microtubule | - |
Mus musculus | 5874 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Homo sapiens | |
| Mg2+ | required | Mus musculus | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + a kinesin associated with a microtubule at position n | Homo sapiens | - |
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end) | - |
? | |
| ATP + H2O + a kinesin associated with a microtubule at position n | Mus musculus | - |
ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end) | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | Q12756 | - |
- |
| Mus musculus | Q61768 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | phosphorylation at serine 175/176 via c-Jun N-terminal kinase-3. Phosphorylation of kinesin-1 light chains affects the association of cargo with the motor | Homo sapiens |
| phosphoprotein | phosphorylation at serine 175/176 via c-Jun N-terminal kinase-3. Phosphorylation of kinesin-1 light chains affects the association of cargo with the motor | Mus musculus |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant C-terminally FLAG-tagged K888 heavy chain wild-type and mutants from Sf9 cells by affinity chromatography | Mus musculus |
| recombinant heavy chain residues 1-432 from Escherichia coli strain BL21 by nickel affinity chormatography | Homo sapiens |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| neuron | - |
Homo sapiens | - |
| neuron | - |
Mus musculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + a kinesin associated with a microtubule at position n | - |
Homo sapiens | ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end) | - |
? | |
| ATP + H2O + a kinesin associated with a microtubule at position n | - |
Mus musculus | ADP + phosphate + a kinesin associated with a microtubule at position n+1 (toward the plus end) | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| K888 | - |
Homo sapiens |
| KIF1A | - |
Homo sapiens |
| KIF5B | - |
Mus musculus |
| kinesin-1 | - |
Homo sapiens |
| kinesin-1 | - |
Mus musculus |
| kinesin-1 heavy chain | - |
Mus musculus |
| kinesin-888 | - |
Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | disruptions in microtubule motor transport are associated with a variety of neurodegenerative diseases. Phosphorylation at serine 175/176 via c-Jun N-terminal kinase-3 is associated with Huntington disease and spinal and bulbar muscular atrophy | Homo sapiens |
| malfunction | disruptions in microtubule motor transport are associated with a variety of neurodegenerative diseases. Phosphorylation at serine 175/176 via c-Jun N-terminal kinase-3 is associated with Huntington disease and spinal and bulbar muscular atrophy. The ATPase, microtubule-binding affinity, and processivity are unchanged between a phosphomimetic S175D and a nonphosphorylatable S175A construct of kinesin. Placement of negative charge at Ser175, through phosphorylation or mutation, leads to a lower stall force and decreased velocity, addition of a negative charge at Ser175 favors the autoinhibited conformation of kinesin | Mus musculus |
| metabolism | a bias that favors motion toward the minus-end of microtubules might be used to tune transport in healthy cells when properly regulated but contribute to a disease state when misregulated | Mus musculus |
| additional information | residue 175 does not fall within the microtubule-binding domain or the ATP-binding domain of kinesin | Homo sapiens |
| additional information | residue 175 does not fall within the microtubule-binding domain or the ATPbinding domain of kinesin | Mus musculus |
| physiological function | the motor domain of kinesin-1 play a role in impaired fast axonal transport. When cargo is transported by both dynein and phosphorylated kinesin, a common occurrence in the cell, there may be a bias that favors motion toward the minus-end of microtubules | Mus musculus |
| physiological function | the motor domain of kinesin-1 play a role in impaired fast axonal transport. When cargo is transported by both dynein and phosphorylated kinesin, a common occurrence in the cell, there may be a bias that favors motion toward the minus-end of microtubules, cf. EC 3.6.4.5 | Homo sapiens |
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