DYNLL1 Back

dynein, light chain, LC8-type 1

External References:      Wikipedia GeneCards HUGO COSMIC Google Scholar

NCBI Description of DYNLL1
Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized.

Community Annotation of DYNLL1 Add / Edit DYNLL1: Annotations

No community annotations yet for DYNLL1.
Sort mutations by: Tumor type  Mutation type  Position  
Straightedge cursor Expand

Figure notes


• "Mouse over" a mutation to see details.
• Missense green saturation indicates evolutionary conservation of the mutated positions.
• Red hashes in protein strip are splice sites.
• Blue-white-red bars are log2 copy ratio distributions (–1 to +1) from Zack et al. (2013).


Legend

DYNLL1 is highly significantly mutated in
(none)
DYNLL1 is significantly mutated in
(none)
DYNLL1 is near significance in
(none)

Click on a tumor type to see its full list of significant genes.

Data details


• Mutation list for DYNLL1