DYL1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DYL1_RAT
• UniProt AC: P63170
• Protein Name: Dynein light chain 1, cytoplasmic
• Gene Name: Dynll1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 89
• Subcellular Localization: Cytoplasm, cytoskeleton . Nucleus. Mitochondrion. Associated with microtubules.
• Protein Description: 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.; Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.; Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.; 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 (By similarity)..
• Protein Sequence: MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Acetylation	CDRKAVIKNADMSEE CCCCHHHCCCCCCHH	39.21	22902405
36	Acetylation	LEKYNIEKDIAAHIK HHHCCCHHHHHHHHH	51.11	22902405
36	Ubiquitination	LEKYNIEKDIAAHIK HHHCCCHHHHHHHHH	51.11	-
43	Acetylation	KDIAAHIKKEFDKKY HHHHHHHHHHHHHHC	36.06	22902405
43	Ubiquitination	KDIAAHIKKEFDKKY HHHHHHHHHHHHHHC	36.06	-
49	Acetylation	IKKEFDKKYNPTWHC HHHHHHHHCCCCCEE	52.70	22902405
53	Phosphorylation	FDKKYNPTWHCIVGR HHHHCCCCCEEEECC	24.97	23984901
64	Phosphorylation	IVGRNFGSYVTHETK EECCCCHHHCCCCHH	16.58	-
65	Phosphorylation	VGRNFGSYVTHETKH ECCCCHHHCCCCHHH	15.11	-
88	Phosphorylation	VAILLFKSG------ HHHHHHHCC------	42.26	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of DYL1_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
88	S	Phosphorylation	Phosphorylation at Ser-88 appears to control the dimer-monomer transition.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DYL1_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of DYL1_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.