MitoProteome Database

New search | Record Overview | Ontology/Pathway Information | Domain Information | UniProt Annotations | Related Proteins

MT000667

UniProt Annotations

Entry Information

Gene Name	dynein, light chain, LC8-type 1
Protein Entry	DYL1_HUMAN
UniProt ID	P63167
Species	Human

Comments

Comment type	Description
Function	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.
Function	Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.
Function	Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.
Function	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.
Induction	Up-regulated by ATMIN, PAK1 and estrogen. {ECO:0000269\|PubMed:15891768, ECO:0000269\|PubMed:22167198}.
Interaction	P63244:GNB2L1; NbExp=6; IntAct=EBI-349105, EBI-296739; P0CAP1:MYZAP; NbExp=6; IntAct=EBI-349105, EBI-7929343;
Ptm	Phosphorylation at Ser-88 appears to control the dimer- monomer transition. According to PubMed:15193260, it is phosphorylated at Ser-88 by PAK1, however, according to PubMed:18650427, the DYNLL1 dimer is not accessible for PAK1 and the phosphorylation could not be demonstrated in vitro. {ECO:0000269\|PubMed:15193260}.
Similarity	Belongs to the dynein light chain family. {ECO:0000305}.
Subcellular Location	Cytoplasm, cytoskeleton. Nucleus. Mitochondrion. Note=Upon induction of apoptosis translocates together with BCL2L11 to mitochondria.
Subunit	Homodimer. Monomer; the monomeric form is incapable of binding to target proteins. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non- catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Interacts with rabies P protein (By similarity). Interacts with TXNDC17. Interacts with WWC1 and ESR1. The WWC1- DYNLL1 interaction is mandatory for the recruitment and transactivation functions of ESR1 or DYNLL1 to the target chromatin. Interacts with BCL2L11 isoform 1 and isoform 2. Interacts with BCL2; the interaction is greatly enhanced in the nucleus and in mitochondria upon induction of apoptosis. Interacts with PAK1; the interaction requires dimeric DYNLL1. Interacts with human spumaretrovirus Gag protein; this interaction is critical for intracellular microtubule-dependent viral genome transport toward the centrosome. Interacts with MYZAP. Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGOL2. Interacts with ATMIN; this interaction inhibits ATMIN transcriptional activity and hence may play a role in a feedback loop whereby DYNLL1 inhibits transactivation of its own promoter by ATMIN. Interacts with NEK9 (not phosphorylated at 'Ser-944'). {ECO:0000250, ECO:0000269\|PubMed:10198631, ECO:0000269\|PubMed:12857789, ECO:0000269\|PubMed:14607843, ECO:0000269\|PubMed:15193260, ECO:0000269\|PubMed:15891768, ECO:0000269\|PubMed:16684779, ECO:0000269\|PubMed:18084006, ECO:0000269\|PubMed:18650427, ECO:0000269\|PubMed:20412299, ECO:0000269\|PubMed:21402792, ECO:0000269\|PubMed:22167198, ECO:0000269\|PubMed:23482567}.
Tissue Specificity	Ubiquitous. {ECO:0000269\|PubMed:8628263}.