Search Results

Overview

Uniprot IDP63167
Protein NameDynein light chain 1, cytoplasmic
Gene NameDYNLL1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
36 LEKYNIEKDIAAHIK
43 KDIAAHIKKEFDKKY
44 DIAAHIKKEFDKKYN
49 IKKEFDKKYNPTWHC
9 CDRKAVIKNADMSEE

Function

Component of dynein, a family of motor proteins essential for movement along microtubules (By similarity). Required for structural and functional integrity of cilia (By similarity). 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 (By similarity). Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules (By similarity). May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity). In addition to its role in cytoskeleton and transport, acts as a protein-protein adapter, which inhibits and/or sequesters target proteins (PubMed:10198631, PubMed:15193260, PubMed:15891768, PubMed:16684779, PubMed:30464262, PubMed:37696958). 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 (PubMed:30464262, PubMed:37696958). In a subset of DSBs, DYNLL1 remains unphosphorylated and promotes the recruitment of the Shieldin complex (PubMed:37696958). Binds and inhibits the catalytic activity of neuronal nitric oxide synthase/NOS1 (By similarity). Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1 (PubMed:15891768, PubMed:16684779). Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules (PubMed:10198631, PubMed:15193260). Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity (PubMed:10198631, PubMed:15193260)

Protein Sequence

10 MCDRKAVIKN 20 ADMSEEMQQD 30 SVECATQALE 40 KYNIEKDIAA 50 HIKKEFDKKY 60 NPTWHCIVGR 70 NFGSYVTHET 80 KHFIYFYLGQ VAILLFKSG

Gene Ontology

Classification GO ID Description
Cellular Component GO:1904115 axon cytoplasm
Cellular Component GO:0005813 centrosome
Cellular Component GO:0097542 ciliary tip
Cellular Component GO:0005929 cilium
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005868 cytoplasmic dynein complex
Cellular Component GO:0005856 cytoskeleton
Cellular Component GO:0005829 cytosol
Cellular Component GO:0101003 ficolin-1-rich granule membrane
Cellular Component GO:0000776 kinetochore
Cellular Component GO:0001673 male germ cell nucleus
Cellular Component GO:0016020 membrane
Cellular Component GO:0005874 microtubule
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0072686 mitotic spindle
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0035861 site of double-strand break
Cellular Component GO:0070821 tertiary granule membrane
Molecular Function GO:0045505 dynein intermediate chain binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0004857 enzyme inhibitor activity
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0036487 nitric-oxide synthase inhibitor activity
Molecular Function GO:0044877 protein-containing complex binding
Molecular Function GO:0097110 scaffold protein binding
Biological Process GO:0006915 apoptotic process
Biological Process GO:0006974 DNA damage response
Biological Process GO:0006351 DNA-templated transcription
Biological Process GO:0035721 intraciliary retrograde transport
Biological Process GO:0044458 motile cilium assembly
Biological Process GO:0110027 negative regulation of DNA strand resection involved in replication fork processing
Biological Process GO:0042326 negative regulation of phosphorylation
Biological Process GO:0035774 positive regulation of insulin secretion involved in cellular response to glucose stimulus
Biological Process GO:0032388 positive regulation of intracellular transport
Biological Process GO:0090267 positive regulation of mitotic cell cycle spindle assembly checkpoint
Biological Process GO:0007286 spermatid development
Biological Process GO:0021762 substantia nigra development

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[3] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.