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Literature summary for 3.6.4.B1 extracted from

  • Christodoulou, A.; Lederer, C.W.; Surrey, T.; Vernos, I.; Santama, N.
    Motor protein KIFC5A interacts with Nubp1 and Nubp2, and is implicated in the regulation of centrosome duplication (2006), J. Cell Sci., 119, 2035-2047.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in mouse cell Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information overexpression of KIFC5A in mouse cells causes the formation of aberrant, non-separated microtubule asters and mitotic arrest in a prometaphase-like state. KIFC5A knockdown partly rescues the phenotype caused by inhibition of plus-end directed motor Eg5 by monastrol on the mitotic spindle. Silencing also results in centrosome amplification detectable throughout the cell cycle. KIFC5A interacts with nucleotide-binding proteins 1 and 2. Knockdown of nucleotide-binding protein 1 or double knockdown of nucleotide-binding proteins 1 and 2 both phenocopy the KIFC5A silencing effect Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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isoform KIFC5A
-

Subunits

Subunits Comment Organism
More KIFC5A interacts with nucleotide-binding proteins 1 and 2. Knockdown of nucleotide-binding protein 1 or double knockdown of nucleotide-binding proteins 1 and 2 both phenocopy the KIFC5A silencing effect Mus musculus