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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Dynein light chain 1, cytoplasmic

UniprotKB/SwissProt ID: P63167 (P63167)

Gene Name: DYNLL1

Organism: Homo sapiens (Human)

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 (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)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Chromosome. Cytoplasm, cytoskeleton. Nucleus. Mitochondrion

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR037177 DLC_sf
IPR019763 Dynein_light_1/2_CS
IPR001372 Dynein_light_chain_typ-1/2

The S-nitrosylation sites of P63167

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 24 SEEMQQDSVE C ATQALEKYNI  CCCCCHHHCC C CCCHHHHHHH  4.68% 21278135
2 56 FDKKYNPTWH C IVGRNFGSYV  CCCCCHHHCC C CCCHHHHHHH  1.71% 19483679
21278135