P63170 · DYL1_RAT
- ProteinDynein light chain 1, cytoplasmic
- GeneDynll1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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 (PubMed:11746667, PubMed:8702622).
Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (PubMed:11746667, PubMed:8702622).
May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (PubMed:11746667, PubMed:8702622).
In addition to its role in cytoskeleton and transport, acts as a protein-protein adapter, which inhibits and/or sequesters target proteins (By similarity).
Involved in the response to DNA damage by acting as a key regulator of DNA end resection: when phosphorylated at Ser-88, recruited to DNA double-strand breaks (DSBs) by TP53BP1 and acts by disrupting MRE11 dimerization, thereby inhibiting DNA end resection (By similarity).
In a subset of DSBs, DYNLL1 remains unphosphorylated and promotes the recruitment of the Shieldin complex (By similarity).
Binds and inhibits the catalytic activity of neuronal nitric oxide synthase/NOS1 (PubMed:8864115).
Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1 (By similarity).
Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules (By similarity).
Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity (By similarity).
Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (PubMed:11746667, PubMed:8702622).
May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (PubMed:11746667, PubMed:8702622).
In addition to its role in cytoskeleton and transport, acts as a protein-protein adapter, which inhibits and/or sequesters target proteins (By similarity).
Involved in the response to DNA damage by acting as a key regulator of DNA end resection: when phosphorylated at Ser-88, recruited to DNA double-strand breaks (DSBs) by TP53BP1 and acts by disrupting MRE11 dimerization, thereby inhibiting DNA end resection (By similarity).
In a subset of DSBs, DYNLL1 remains unphosphorylated and promotes the recruitment of the Shieldin complex (By similarity).
Binds and inhibits the catalytic activity of neuronal nitric oxide synthase/NOS1 (PubMed:8864115).
Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1 (By similarity).
Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules (By similarity).
Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity (By similarity).
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDynein light chain 1, cytoplasmic
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP63170
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Upon induction of apoptosis translocates together with BCL2L11 to mitochondria. Recruited to DNA double-strand breaks (DSBs) by TP53BP1 when phosphorylated at Ser-88.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000195129 | 1-89 | Dynein light chain 1, cytoplasmic | |||
Sequence: MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG | ||||||
Modified residue | 36 | N6-acetyllysine | ||||
Sequence: K | ||||||
Cross-link | 43 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 88 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation at Ser-88 promotes recruitment to DNA double-strand breaks (DSBs) by TP53BP1 and ability to inhibit MRE11.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Weaker expression in the cerebellum and spinal cord compared with other brain regions.
Gene expression databases
Interaction
Subunit
Homodimer. Monomer; the monomeric form is incapable of binding to target proteins (By similarity).
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 (PubMed:11746667, PubMed:8702622).
The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits (PubMed:11746667, PubMed:8702622).
The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer (PubMed:11746667, PubMed:8702622).
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 (PubMed:21478148).
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 MYZAP. Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2. 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') (By similarity).
Interacts with BICD2 (By similarity).
Interacts with BCAS1 (PubMed:16133941).
Interacts with Basson/BSN. Interacts with HDAC6. Interacts with TPPP. Interacts with AMBRA1 (via TQT motifs); tethering AMBRA1 to the cytoskeleton. Interacts with FAM83D/CHICA (via C-terminus). Interacts with HMMR, SPAG5/Astrin and KNSTRN/Kinastrin. Interacts with TLK2 (By similarity).
Interacts with NOS1 (PubMed:8864115).
Interacts with WWC1, WWC2 and WWC3. Interacts with MRE11; inhibiting MRE11 homodimerization and activity (By similarity).
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 (PubMed:11746667, PubMed:8702622).
The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits (PubMed:11746667, PubMed:8702622).
The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer (PubMed:11746667, PubMed:8702622).
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 (PubMed:21478148).
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 MYZAP. Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2. 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') (By similarity).
Interacts with BICD2 (By similarity).
Interacts with BCAS1 (PubMed:16133941).
Interacts with Basson/BSN. Interacts with HDAC6. Interacts with TPPP. Interacts with AMBRA1 (via TQT motifs); tethering AMBRA1 to the cytoskeleton. Interacts with FAM83D/CHICA (via C-terminus). Interacts with HMMR, SPAG5/Astrin and KNSTRN/Kinastrin. Interacts with TLK2 (By similarity).
Interacts with NOS1 (PubMed:8864115).
Interacts with WWC1, WWC2 and WWC3. Interacts with MRE11; inhibiting MRE11 homodimerization and activity (By similarity).
(Microbial infection) Interacts with rabies virus phosphoprotein.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 67-89 | Interaction with ESR1 | ||||
Sequence: THETKHFIYFYLGQVAILLFKSG |
Sequence similarities
Belongs to the dynein light chain family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length89
- Mass (Da)10,366
- Last updated2004-09-27 v1
- ChecksumF5E7647D092BEB3A
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U66461 EMBL· GenBank· DDBJ | AAB38257.1 EMBL· GenBank· DDBJ | mRNA | ||
BC063183 EMBL· GenBank· DDBJ | AAH63183.1 EMBL· GenBank· DDBJ | mRNA |