dbPTM

DYL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DYL1_HUMAN
UniProt AC	P63167
Protein Name	Dynein light chain 1, cytoplasmic
Gene Name	DYNLL1
Organism	Homo sapiens (Human).
Sequence Length	89
Subcellular Localization	Cytoplasm, cytoskeleton. Nucleus. Mitochondrion. Upon induction of apoptosis translocates together with BCL2L11 to mitochondria.
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..
Protein Sequence	MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Sumoylation	CDRKAVIKNADMSEE CCCCHHHCCCCCCHH	39.21	-
9	Ubiquitination	CDRKAVIKNADMSEE CCCCHHHCCCCCCHH	39.21	-
9	Acetylation	CDRKAVIKNADMSEE CCCCHHHCCCCCCHH	39.21	23954790
9	Sumoylation	CDRKAVIKNADMSEE CCCCHHHCCCCCCHH	39.21	-
9	Malonylation	CDRKAVIKNADMSEE CCCCHHHCCCCCCHH	39.21	26320211
13	Sulfoxidation	AVIKNADMSEEMQQD HHHCCCCCCHHHHHH	5.16	21406390
14	Phosphorylation	VIKNADMSEEMQQDS HHCCCCCCHHHHHHH	30.84	25159151
17	Sulfoxidation	NADMSEEMQQDSVEC CCCCCHHHHHHHHHH	3.68	30846556
21	Phosphorylation	SEEMQQDSVECATQA CHHHHHHHHHHHHHH	18.58	29396449
24	S-nitrosylation	MQQDSVECATQALEK HHHHHHHHHHHHHHH	4.68	21278135
24	Glutathionylation	MQQDSVECATQALEK HHHHHHHHHHHHHHH	4.68	22555962
24	S-nitrosocysteine	MQQDSVECATQALEK HHHHHHHHHHHHHHH	4.68	-
26	Phosphorylation	QDSVECATQALEKYN HHHHHHHHHHHHHCC	26.49	29396449
31	Acetylation	CATQALEKYNIEKDI HHHHHHHHCCCHHHH	44.43	25038526
31	Ubiquitination	CATQALEKYNIEKDI HHHHHHHHCCCHHHH	44.43	-
36	Malonylation	LEKYNIEKDIAAHIK HHHCCCHHHHHHHHH	51.11	26320211
36	Ubiquitination	LEKYNIEKDIAAHIK HHHCCCHHHHHHHHH	51.11	21890473
36	Acetylation	LEKYNIEKDIAAHIK HHHCCCHHHHHHHHH	51.11	19608861
43	Acetylation	KDIAAHIKKEFDKKY HHHHHHHHHHHHHHC	36.06	26051181
43	Ubiquitination	KDIAAHIKKEFDKKY HHHHHHHHHHHHHHC	36.06	-
43	Sumoylation	KDIAAHIKKEFDKKY HHHHHHHHHHHHHHC	36.06	28112733
43	2-Hydroxyisobutyrylation	KDIAAHIKKEFDKKY HHHHHHHHHHHHHHC	36.06	-
43	Sumoylation	KDIAAHIKKEFDKKY HHHHHHHHHHHHHHC	36.06	-
44	Acetylation	DIAAHIKKEFDKKYN HHHHHHHHHHHHHCC	64.11	11921203
44	Ubiquitination	DIAAHIKKEFDKKYN HHHHHHHHHHHHHCC	64.11	-
48	Ubiquitination	HIKKEFDKKYNPTWH HHHHHHHHHCCCCCE	63.58	-
49	Sumoylation	IKKEFDKKYNPTWHC HHHHHHHHCCCCCEE	52.70	-
49	Acetylation	IKKEFDKKYNPTWHC HHHHHHHHCCCCCEE	52.70	25038526
49	Methylation	IKKEFDKKYNPTWHC HHHHHHHHCCCCCEE	52.70	23644510
49	Ubiquitination	IKKEFDKKYNPTWHC HHHHHHHHCCCCCEE	52.70	21906983
49	Sumoylation	IKKEFDKKYNPTWHC HHHHHHHHCCCCCEE	52.70	-
50	Phosphorylation	KKEFDKKYNPTWHCI HHHHHHHCCCCCEEE	31.92	28152594
53	Phosphorylation	FDKKYNPTWHCIVGR HHHHCCCCCEEEECC	24.97	28857561
56	S-nitrosocysteine	KYNPTWHCIVGRNFG HCCCCCEEEECCCCH	1.71	-
56	Glutathionylation	KYNPTWHCIVGRNFG HCCCCCEEEECCCCH	1.71	22555962
56	S-nitrosylation	KYNPTWHCIVGRNFG HCCCCCEEEECCCCH	1.71	19483679
64	Phosphorylation	IVGRNFGSYVTHETK EECCCCHHHCCCCHH	16.58	28152594
65	Phosphorylation	VGRNFGSYVTHETKH ECCCCHHHCCCCHHH	15.11	25159151
67	Phosphorylation	RNFGSYVTHETKHFI CCCHHHCCCCHHHHH	13.03	25884760
70	Phosphorylation	GSYVTHETKHFIYFY HHHCCCCHHHHHHEE	23.39	23186163
88	Phosphorylation	VAILLFKSG------ HHHHHHHCC------	42.26	28112733

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	Q13153	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
88	S	Phosphorylation	15193260
According to PubMed:15193260, it is phosphorylated at Ser-88 by PAK1, however, according to PubMed:18650427, the DYNLL1 dimer is not accessible for PAK1 and the phosphorylation could not be demonstrated in vitro.
88	S	Phosphorylation	15193260
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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of DYL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DC1I2_HUMAN	DYNC1I2	physical	17353931
PABP1_HUMAN	PABPC1	physical	17353931
DDX3X_HUMAN	DDX3X	physical	17353931
TP53B_HUMAN	TP53BP1	physical	15611139
CAH1_RAT	Car1	physical	14760703
LDHA_RAT	Ldha	physical	14760703
ALDOA_RAT	Aldoa	physical	14760703
MTA1_RAT	Mta1	physical	14760703
CACB1_RAT	Cacnb1	physical	14760703
GLNA_RAT	Glul	physical	14760703
ACTB_RAT	Actb	physical	14760703
ACTG_RAT	Actg1	physical	14760703
MDHC_RAT	Mdh1	physical	14760703
VIME_RAT	Vim	physical	14760703
DHE3_RAT	Glud1	physical	14760703
DNM3A_MOUSE	Dnmt3a	physical	14760703
TBA1A_RAT	Tuba1a	physical	14760703
TBB2B_RAT	Tubb2b	physical	14760703
GEPH_RAT	Gphn	physical	14760703
PFKAP_RAT	Pfkp	physical	14760703
PFKAM_RAT	Pfkm	physical	14760703
PARD3_RAT	Pard3	physical	14760703
MLP3B_RAT	Map1lc3b	physical	14760703
DYHC1_RAT	Dync1h1	physical	14760703
DLG4_RAT	Dlg4	physical	14760703
DYN3_RAT	Dnm3	physical	14760703
NMDE1_RAT	Grin2a	physical	14760703
METH_RAT	Mtr	physical	14760703
DYN2_RAT	Dnm2	physical	14760703
CLIP2_RAT	Clip2	physical	14760703
NOS1_RAT	Nos1	physical	14760703
NMD3A_RAT	Grin3a	physical	14760703
POLH_MOUSE	Polh	physical	14760703
MYO10_MOUSE	Myo10	physical	14760703
MAST1_MOUSE	Mast1	physical	14760703
SHRM1_MOUSE	Shroom1	physical	14760703
DYL1_HUMAN	DYNLL1	physical	16169070
ERG28_HUMAN	C14orf1	physical	16169070
ZHX1_HUMAN	ZHX1	physical	16169070
EF1A1_HUMAN	EEF1A1	physical	16169070
DYL1_HUMAN	DYNLL1	physical	12475239
DC1I1_HUMAN	DYNC1I1	physical	12475239
DLGP1_HUMAN	DLGAP1	physical	10844022
MYO5A_HUMAN	MYO5A	physical	10844022
DLG4_HUMAN	DLG4	physical	10844022
DLG2_HUMAN	DLG2	physical	10844022
B2L11_HUMAN	BCL2L11	physical	14561217
BMF_HUMAN	BMF	physical	14561217
B2L11_HUMAN	BCL2L11	physical	15193260
PAK1_HUMAN	PAK1	physical	15193260
IKBA_HUMAN	NFKBIA	physical	9372968
B2L11_MOUSE	Bcl2l11	physical	10198631
DC1I1_MOUSE	Dync1i1	physical	10198631
TBA1A_MOUSE	Tuba1a	physical	10198631
HDAC6_HUMAN	HDAC6	physical	15937109
LIS1_HUMAN	PAFAH1B1	physical	11056532
MYO5A_HUMAN	MYO5A	physical	11148209
DLGP1_HUMAN	DLGAP1	physical	11148209
BCAS1_HUMAN	BCAS1	physical	11148209
DC1I1_HUMAN	DYNC1I1	physical	11148209
RACK1_HUMAN	GNB2L1	physical	18420585
B2L11_HUMAN	BCL2L11	physical	12591950
PAK1_HUMAN	PAK1	physical	21988832
RACK1_HUMAN	GNB2L1	physical	22863883
RSSA_HUMAN	RPSA	physical	22863883
RS2_HUMAN	RPS2	physical	22863883
RS3_HUMAN	RPS3	physical	22863883
RS5_HUMAN	RPS5	physical	22863883
AMRA1_HUMAN	AMBRA1	physical	20921139
KANK2_HUMAN	KANK2	physical	25416956
AMOL2_HUMAN	AMOTL2	physical	25416956
IQUB_HUMAN	IQUB	physical	25416956
IHO1_HUMAN	CCDC36	physical	25416956
COF1_HUMAN	CFL1	physical	26344197
DYL2_HUMAN	DYNLL2	physical	26344197
NDKA_HUMAN	NME1	physical	26344197
PCBP1_HUMAN	PCBP1	physical	26344197
SNX3_HUMAN	SNX3	physical	26344197
CAV1_HUMAN	CAV1	physical	26496610
CD44_HUMAN	CD44	physical	26496610
DYHC1_HUMAN	DYNC1H1	physical	26496610
DC1I2_HUMAN	DYNC1I2	physical	26496610
DC1L2_HUMAN	DYNC1LI2	physical	26496610
DESP_HUMAN	DSP	physical	26496610
GOGB1_HUMAN	GOLGB1	physical	26496610
HMMR_HUMAN	HMMR	physical	26496610
PLAK_HUMAN	JUP	physical	26496610
K1C18_HUMAN	KRT18	physical	26496610
LG3BP_HUMAN	LGALS3BP	physical	26496610
PYC_HUMAN	PC	physical	26496610
PCM1_HUMAN	PCM1	physical	26496610
KAPCB_HUMAN	PRKACB	physical	26496610
KAP2_HUMAN	PRKAR2A	physical	26496610
STRN_HUMAN	STRN	physical	26496610
TP53B_HUMAN	TP53BP1	physical	26496610
TRPS1_HUMAN	TRPS1	physical	26496610
ZMYM2_HUMAN	ZMYM2	physical	26496610
ELL_HUMAN	ELL	physical	26496610
RAE1L_HUMAN	RAE1	physical	26496610
OFD1_HUMAN	OFD1	physical	26496610
LIPB1_HUMAN	PPFIBP1	physical	26496610
ZMYM4_HUMAN	ZMYM4	physical	26496610
ZMYM3_HUMAN	ZMYM3	physical	26496610
MYOME_HUMAN	PDE4DIP	physical	26496610
EPN4_HUMAN	CLINT1	physical	26496610
SBP2L_HUMAN	SECISBP2L	physical	26496610
TLK1_HUMAN	TLK1	physical	26496610
AKAP9_HUMAN	AKAP9	physical	26496610
GEPH_HUMAN	GPHN	physical	26496610
SPTC1_HUMAN	SPTLC1	physical	26496610
SPAG5_HUMAN	SPAG5	physical	26496610
TLK2_HUMAN	TLK2	physical	26496610
CP131_HUMAN	CEP131	physical	26496610
CE152_HUMAN	CEP152	physical	26496610
ZN609_HUMAN	ZNF609	physical	26496610
UH1BL_HUMAN	UHRF1BP1L	physical	26496610
N4BP3_HUMAN	N4BP3	physical	26496610
KANK1_HUMAN	KANK1	physical	26496610
MTCL1_HUMAN	MTCL1	physical	26496610
ADNP_HUMAN	ADNP	physical	26496610
CIZ1_HUMAN	CIZ1	physical	26496610
KANK2_HUMAN	KANK2	physical	26496610
STRN4_HUMAN	STRN4	physical	26496610
STRN3_HUMAN	STRN3	physical	26496610
DC1L1_HUMAN	DYNC1LI1	physical	26496610
PAPD1_HUMAN	MTPAP	physical	26496610
KI21A_HUMAN	KIF21A	physical	26496610
CEP72_HUMAN	CEP72	physical	26496610
CK5P2_HUMAN	CDK5RAP2	physical	26496610
CT2NL_HUMAN	CTTNBP2NL	physical	26496610
NEUL_HUMAN	NLN	physical	26496610
MIB1_HUMAN	MIB1	physical	26496610
FBX38_HUMAN	FBXO38	physical	26496610
FA83D_HUMAN	FAM83D	physical	26496610
DLRB1_HUMAN	DYNLRB1	physical	26496610
FBX30_HUMAN	FBXO30	physical	26496610
CCD77_HUMAN	CCDC77	physical	26496610
PHLB2_HUMAN	PHLDB2	physical	26496610
SKAP_HUMAN	KNSTRN	physical	26496610
NEK9_HUMAN	NEK9	physical	26496610
GLCI1_HUMAN	GLCCI1	physical	26496610
ADIP_HUMAN	SSX2IP	physical	26496610
FOPNL_HUMAN	FOPNL	physical	26496610
SOGA1_HUMAN	SOGA1	physical	26496610
F117B_HUMAN	FAM117B	physical	26496610
WDR90_HUMAN	WDR90	physical	26496610
EMAL3_HUMAN	EML3	physical	26496610
CCD18_HUMAN	CCDC18	physical	26496610
WDR34_HUMAN	WDR34	physical	27173435
DYL2_HUMAN	DYNLL2	physical	27173435
NEK9_HUMAN	NEK9	physical	27173435
GEPH_HUMAN	GPHN	physical	27173435
NRF1_HUMAN	NRF1	physical	27173435
RN214_HUMAN	RNF214	physical	27173435
GLYM_HUMAN	SHMT2	physical	27173435
MORC3_HUMAN	MORC3	physical	27173435
PAPD1_HUMAN	MTPAP	physical	27173435
CIZ1_HUMAN	CIZ1	physical	27173435
TLK2_HUMAN	TLK2	physical	27173435
EPN4_HUMAN	CLINT1	physical	27173435
DBLOH_HUMAN	DIABLO	physical	27173435
XIAP_HUMAN	XIAP	physical	27173435
DDHD1_HUMAN	DDHD1	physical	27173435
AMOT_HUMAN	AMOT	physical	27173435
AMRA1_HUMAN	AMBRA1	physical	27173435
DYLT1_HUMAN	DYNLT1	physical	27173435
NEK7_HUMAN	NEK7	physical	27173435
OFD1_HUMAN	OFD1	physical	27173435
TC1D2_HUMAN	TCTEX1D2	physical	27173435
DZAN1_HUMAN	DZANK1	physical	27173435
RAF1_HUMAN	RAF1	physical	27173435
FTM_HUMAN	RPGRIP1L	physical	27173435

Drug and Disease Associations

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

Regulatory Network of DYL1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Dynein light chain 1, a p21-activated kinase 1-interacting substrate,promotes cancerous phenotypes."; Vadlamudi R.K., Bagheri-Yarmand R., Yang Z., Balasenthil S.,Nguyen D., Sahin A.A., den Hollander P., Kumar R.; Cancer Cell 5:575-585(2004). Cited for: FUNCTION IN REGULATION OF BCL2L11, INTERACTION WITH PAK1 AND BCL2L11,PHOSPHORYLATION AT SER-88, AND MUTAGENESIS OF SER-88.	15193260 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-65, AND MASSSPECTROMETRY.	19534553 [Abstract]

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