DYL1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DYL1_MOUSE
• UniProt AC: P63168
• Protein Name: Dynein light chain 1, cytoplasmic
• Gene Name: Dynll1
• Organism: Mus musculus (Mouse).
• Sequence Length: 89
• Subcellular Localization: Cytoplasm, cytoskeleton. Nucleus. Mitochondrion.
• 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 (By similarity).; 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
14	Phosphorylation	VIKNADMSEEMQQDS HHCCCCCCHHHHHHH	30.84	29899451
21	Phosphorylation	SEEMQQDSVECATQA CHHHHHHHHHHHHHH	18.58	28285833
31	Ubiquitination	CATQALEKYNIEKDI HHHHHHHHCCCHHHH	44.43	-
36	Acetylation	LEKYNIEKDIAAHIK HHHCCCHHHHHHHHH	51.11	23806337
36	Ubiquitination	LEKYNIEKDIAAHIK HHHCCCHHHHHHHHH	51.11	22790023
43	Ubiquitination	KDIAAHIKKEFDKKY HHHHHHHHHHHHHHC	36.06	27667366
49	Ubiquitination	IKKEFDKKYNPTWHC HHHHHHHHCCCCCEE	52.70	-
49	Acetylation	IKKEFDKKYNPTWHC HHHHHHHHCCCCCEE	52.70	22826441
50	Nitration	KKEFDKKYNPTWHCI HHHHHHHCCCCCEEE	31.92	-
56	S-nitrosocysteine	KYNPTWHCIVGRNFG HCCCCCEEEECCCCH	1.71	-
56	S-nitrosylation	KYNPTWHCIVGRNFG HCCCCCEEEECCCCH	1.71	20925432
64	Phosphorylation	IVGRNFGSYVTHETK EECCCCHHHCCCCHH	16.58	25367039
65	Phosphorylation	VGRNFGSYVTHETKH ECCCCHHHCCCCHHH	15.11	25367039
67	Phosphorylation	RNFGSYVTHETKHFI CCCHHHCCCCHHHHH	13.03	25367039
88	Phosphorylation	VAILLFKSG------ HHHHHHHCC------	42.26	15504720

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
88	S	Phosphorylation	Kinase	PAK1	O88643	PSP

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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PP2AA_HUMAN	PPP2CA	physical	20360068
UH1BL_HUMAN	UHRF1BP1L	physical	20360068
HDAC2_HUMAN	HDAC2	physical	20360068
WDR34_HUMAN	WDR34	physical	20360068
IFFO2_HUMAN	IFFO2	physical	20360068
PHOCN_HUMAN	MOB4	physical	20360068
NEK9_HUMAN	NEK9	physical	20360068
DEF1_HUMAN	DEFA1	physical	20360068
F172A_HUMAN	FAM172A	physical	20360068
DC1L2_HUMAN	DYNC1LI2	physical	20360068
WDR60_HUMAN	WDR60	physical	20360068
FA83D_HUMAN	FAM83D	physical	20360068
ZMYM3_HUMAN	ZMYM3	physical	20360068
STRN4_HUMAN	STRN4	physical	20360068
TRFL_HUMAN	LTF	physical	20360068
CT2NL_HUMAN	CTTNBP2NL	physical	20360068
KAP2_HUMAN	PRKAR2A	physical	20360068
GLCI1_HUMAN	GLCCI1	physical	20360068
TLK2_HUMAN	TLK2	physical	20360068
PP2AB_HUMAN	PPP2CB	physical	20360068
STRN_HUMAN	STRN	physical	20360068
STRN3_HUMAN	STRN3	physical	20360068
TP53B_HUMAN	TP53BP1	physical	20360068
PIP_HUMAN	PIP	physical	20360068
GEPH_HUMAN	GPHN	physical	20360068
DCAF7_HUMAN	DCAF7	physical	20360068
DYHC1_HUMAN	DYNC1H1	physical	20360068
AMRA1_HUMAN	AMBRA1	physical	20360068
DYL2_HUMAN	DYNLL2	physical	20360068
2AAA_HUMAN	PPP2R1A	physical	20360068
PAPD1_HUMAN	MTPAP	physical	20360068
MORC3_HUMAN	MORC3	physical	20360068
RCOR1_HUMAN	RCOR1	physical	20360068
DC1L1_HUMAN	DYNC1LI1	physical	20360068
STK25_HUMAN	STK25	physical	20360068
SKP1_HUMAN	SKP1	physical	20360068
KDM1A_HUMAN	KDM1A	physical	20360068
EMAL3_HUMAN	EML3	physical	20360068
SOGA1_HUMAN	SOGA1	physical	20360068
GWL_HUMAN	MASTL	physical	20360068
HMMR_HUMAN	HMMR	physical	20360068
PERM_HUMAN	MPO	physical	20360068
AGGF1_HUMAN	AGGF1	physical	20360068
PDC10_HUMAN	PDCD10	physical	20360068
MTCL1_HUMAN	MTCL1	physical	20360068
PIGR_HUMAN	PIGR	physical	20360068
STK26_HUMAN	STK26	physical	20360068
KANK1_HUMAN	KANK1	physical	20360068
DYL1_HUMAN	DYNLL1	physical	20360068
ZMYM2_HUMAN	ZMYM2	physical	20360068
TRPS1_HUMAN	TRPS1	physical	20360068
FBX30_HUMAN	FBXO30	physical	20360068
DC1I2_HUMAN	DYNC1I2	physical	20360068
SPAG5_HUMAN	SPAG5	physical	20360068
CIZ1_HUMAN	CIZ1	physical	20360068
FBX38_HUMAN	FBXO38	physical	20360068
TLK1_HUMAN	TLK1	physical	20360068
SKAP_HUMAN	KNSTRN	physical	20360068
RCOR3_HUMAN	RCOR3	physical	20360068
CR3L2_HUMAN	CREB3L2	physical	20360068
KANK2_HUMAN	KANK2	physical	20360068
DLRB1_HUMAN	DYNLRB1	physical	20360068
STRP1_HUMAN	STRIP1	physical	20360068
ZMYM4_HUMAN	ZMYM4	physical	20360068
ZN609_HUMAN	ZNF609	physical	20360068
AMRA1_MOUSE	Ambra1	physical	20921139

Drug and Disease Associations

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