DYNLL1

DYNLL1

Identifiers Symbols DYNLL1; DLC1; DLC8; DNCL1; DNCLC1; LC8; LC8a; PIN; hdlc1 External IDs OMIM: 601562 MGI: 1861457 HomoloGene: 133063 GeneCards: DYNLL1 Gene

Gene Ontology
Molecular function	• motor activity • protein binding
Cellular component	• nucleus • cytoplasm • mitochondrion • centrosome • cytosol • cytoplasmic dynein complex • microtubule • plasma membrane • signalosome
Biological process	• G2/M transition of mitotic cell cycle • mitotic cell cycle • transcription, DNA-dependent • regulation of transcription, DNA-dependent • transport • apoptotic process • microtubule-based process • female gamete generation • anatomical structure morphogenesis • virus-host interaction • antigen processing and presentation of exogenous peptide antigen via MHC class II • actin cytoskeleton organization • negative regulation of phosphorylation
Sources: Amigo / QuickGO

RNA expression pattern More reference expression data Orthologs Species Human Mouse Entrez 8655 56455 Ensembl ENSG00000088986 ENSMUSG00000009013 UniProt P63167 P63168 RefSeq (mRNA) NM_001037494 NM_019682 RefSeq (protein) NP_001032583 NP_062656 Location (UCSC) Chr 12:
120.91 – 120.94 Mb Chr 5:
115.3 – 115.3 Mb PubMed search

Dynein light chain 1, cytoplasmic is a protein that in humans is encoded by the 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.