Aliases for DYNLL1 Gene
External Ids for DYNLL1 Gene
Previous HGNC Symbols for DYNLL1 Gene
Previous GeneCards Identifiers for DYNLL1 Gene
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. [provided by RefSeq, Jul 2008]
GeneCards Summary for DYNLL1 Gene
DYNLL1 (Dynein Light Chain LC8-Type 1) is a Protein Coding gene. Diseases associated with DYNLL1 include Rabies and Prostate Carcinoma In Situ. Among its related pathways are Cell Cycle, Mitotic and Macroautophagy. Gene Ontology (GO) annotations related to this gene include protein homodimerization activity and protein domain specific binding. An important paralog of this gene is DYNLL2.
UniProtKB/Swiss-Prot Summary for DYNLL1 Gene
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.
Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.
Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.
Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity.