DYNLL1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1CMI, 3ZKE, 3ZKF, 1F95, 1F3C, 1F96
Identifiers
Aliases	DYNLL1, DLC1, DLC8, DNCL1, DNCLC1, LC8, LC8a, PIN, hdlc1, dynein light chain LC8-type 1
External IDs	OMIM: 601562 MGI: 1861457 HomoloGene: 133063 GeneCards: DYNLL1
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q24.31 Start 120,469,850 bp[1] End 120,498,493 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5|5 F Start 115,435,169 bp[2] End 115,439,058 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in prefrontal cortex frontal pole cingulate gyrus Brodmann area 9 bronchial epithelial cell Brodmann area 10 middle frontal gyrus amygdala olfactory bulb hypothalamus Top expressed in medial ganglionic eminence endocardial cushion maxillary prominence condyle spermatid hair follicle seminiferous tubule abdominal wall fossa superior frontal gyrus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein domain specific binding protein C-terminus binding protein binding cytoskeletal motor activity cytoskeletal protein binding plus-end-directed microtubule motor activity dynein intermediate chain binding dynein light intermediate chain binding enzyme binding nitric-oxide synthase regulator activity protein homodimerization activity protein heterodimerization activity scaffold protein binding Cellular component cytoplasm cytosol centrosome membrane plasma membrane microtubule associated complex ciliary tip mitochondrion dynein complex COP9 signalosome mitotic spindle microtubule cytoskeleton extracellular exosome nucleus kinetochore cytoplasmic dynein complex cilium tertiary granule membrane ficolin-1-rich granule membrane microtubule organizing center secretory granule axon cytoplasm Biological process regulation of transcription, DNA-templated substantia nigra development antigen processing and presentation of exogenous peptide antigen via MHC class II transcription, DNA-templated endoplasmic reticulum to Golgi vesicle-mediated transport positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway G2/M transition of mitotic cell cycle microtubule-based process intraciliary retrograde transport viral process negative regulation of phosphorylation macroautophagy apoptotic process intraciliary transport involved in cilium assembly neutrophil degranulation motile cilium assembly ciliary basal body-plasma membrane docking positive regulation of non-motile cilium assembly transport along microtubule cilium assembly sister chromatid cohesion regulation of G2/M transition of mitotic cell cycle transport spermatid development positive regulation of insulin secretion involved in cellular response to glucose stimulus Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8655 56455 Ensembl ENSG00000088986 ENSMUSG00000009013 UniProt P63167 P63168 RefSeq (mRNA) NM_003746 NM_001037494 NM_001037495 NM_019682 RefSeq (protein) NP_001032583 NP_001032584 NP_003737 NP_062656 Location (UCSC) Chr 12: 120.47 – 120.5 Mb Chr 5: 115.44 – 115.44 Mb PubMed search [3] [4]
Wikidata
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Dynein light chain 1, cytoplasmic is a protein that in humans is encoded by the DYNLL1 gene.^[5][6][7][8]

Function

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.^[8]

Interactions

DYNLL1 has been shown to interact with: