dbPTM

PLS1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PLS1_HUMAN
UniProt AC	O15162
Protein Name	Phospholipid scramblase 1
Gene Name	PLSCR1
Organism	Homo sapiens (Human).
Sequence Length	318
Subcellular Localization	Cell membrane Single-pass type II membrane protein. Membrane Lipid-anchor Cytoplasmic side. Nucleus.
Protein Description	May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system.; May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. May contribute to cytokine-regulated cell proliferation and differentiation..
Protein Sequence	MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAGFPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVLTGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLRCSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCCGDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLIDFMFFESTGSQEQKSGVW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
51	Ubiquitination	VSYPPPPAGHSGPGP CCCCCCCCCCCCCCC	33.82	33845483
69	Phosphorylation	PVPNQPVYNQPVYNQ CCCCCCCCCCCCCCC	18.11	22817900
74	Phosphorylation	PVYNQPVYNQPVGAA CCCCCCCCCCCCCCC	18.11	22817900
125	Ubiquitination	EVLTGFETNNKYEIK HHHHCCCCCCCEEEE	41.66	33845483
132	Ubiquitination	TNNKYEIKNSFGQRV CCCCEEEECCCCCEE	34.30	29901268
142	Ubiquitination	FGQRVYFAAEDTDCC CCCEEEEEECCCCCC	7.70	27667366
142	Ubiquitination	FGQRVYFAAEDTDCC CCCEEEEEECCCCCC	7.70	21890473
148	S-palmitoylation	FAAEDTDCCTRNCCG EEECCCCCCCCCCCC	2.50	29575903
149	S-palmitoylation	AAEDTDCCTRNCCGP EECCCCCCCCCCCCC	4.45	29575903
153	S-palmitoylation	TDCCTRNCCGPSRPF CCCCCCCCCCCCCCE	2.27	29575903
154	S-palmitoylation	DCCTRNCCGPSRPFT CCCCCCCCCCCCCEE	11.66	29575903
161	Phosphorylation	CGPSRPFTLRIIDNM CCCCCCEEEEEECCC	20.15	10770950
177	Ubiquitination	QEVITLERPLRCSSC CEEEEECCCCCCCCC	38.37	22817900
177	Ubiquitination	QEVITLERPLRCSSC CEEEEECCCCCCCCC	38.37	-
180	Ubiquitination	ITLERPLRCSSCCCP EEECCCCCCCCCCCC	22.43	21890473
180	Ubiquitination	ITLERPLRCSSCCCP EEECCCCCCCCCCCC	22.43	21890473
184	S-palmitoylation	RPLRCSSCCCPCCLQ CCCCCCCCCCCCEEE	1.27	12564925
185	S-palmitoylation	PLRCSSCCCPCCLQE CCCCCCCCCCCEEEE	2.91	12564925
186	S-palmitoylation	LRCSSCCCPCCLQEI CCCCCCCCCCEEEEE	3.20	12564925
188	S-palmitoylation	CSSCCCPCCLQEIEI CCCCCCCCEEEEEEE	1.95	12564925
189	S-palmitoylation	SSCCCPCCLQEIEIQ CCCCCCCEEEEEEEE	2.38	12564925
207	Ubiquitination	GVPIGYVIQTWHPCL CCCEEEEEEECCCCC	1.97	21963094
207	Ubiquitination	GVPIGYVIQTWHPCL CCCEEEEEEECCCCC	1.97	-
209	Ubiquitination	PIGYVIQTWHPCLPK CEEEEEEECCCCCCE	18.02	22817900
213	S-palmitoylation	VIQTWHPCLPKFTIQ EEEECCCCCCEEEEC	7.03	29575903
216	Ubiquitination	TWHPCLPKFTIQNEK ECCCCCCEEEECCCC	42.04	27667366
223	2-Hydroxyisobutyrylation	KFTIQNEKREDVLKI EEEECCCCHHCEEEE	69.50	-
223	Ubiquitination	KFTIQNEKREDVLKI EEEECCCCHHCEEEE	69.50	21906983
249	Phosphorylation	DVDFEIKSLDEQCVV CCCEEEEECCCCEEH	46.87	25159151
251	Ubiquitination	DFEIKSLDEQCVVGK CEEEEECCCCEEHHH	51.52	22817900
254	Ubiquitination	IKSLDEQCVVGKISK EEECCCCEEHHHHHH	2.23	21890473
258	Ubiquitination	DEQCVVGKISKHWTG CCCEEHHHHHHHHHH	32.00	27667366
261	Ubiquitination	CVVGKISKHWTGILR EEHHHHHHHHHHHHH	46.78	21906983
281	Ubiquitination	ADNFGIQFPLDLDVK CHHCCCCCCCCCCHH	6.49	21963094
283	Ubiquitination	NFGIQFPLDLDVKMK HCCCCCCCCCCHHHH	12.33	22817900
288	Ubiquitination	FPLDLDVKMKAVMIG CCCCCCHHHHHHHHH	34.06	21963094
290	Ubiquitination	LDLDVKMKAVMIGAC CCCCHHHHHHHHHHH	31.92	22817900

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
69	Y	Phosphorylation	Kinase	ABL1	P00519	PhosphoELM
69	Y	Phosphorylation	Kinase	ABL	P00520	PSP
69	Y	Phosphorylation	Kinase	SRC	P12931	PSP
69	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
69	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
74	Y	Phosphorylation	Kinase	ABL1	P00519	PhosphoELM
74	Y	Phosphorylation	Kinase	ABL	P00520	PSP
74	Y	Phosphorylation	Kinase	SRC	P12931	PSP
74	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
74	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
161	T	Phosphorylation	Kinase	PRKCD	Q05655	Uniprot
161	T	Phosphorylation	Kinase	PRKCD	P09215	GPS
161	T	Phosphorylation	Kinase	PKC-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
161	T	Phosphorylation		10770950
Phosphorylation at Thr-161 by PKC/PKCD increases its phospholipid scramblase activity during both cell stimulation and apoptosis.

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 PLS1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CPSF6_HUMAN	CPSF6	physical	16189514
RASD1_HUMAN	RASD1	physical	16189514
6PGL_HUMAN	PGLS	physical	16189514
DTX2_HUMAN	DTX2	physical	16189514
DLK2_HUMAN	DLK2	physical	16189514
SPG7_HUMAN	SPG7	physical	16189514
NET4_HUMAN	NTN4	physical	16189514
YIPF3_HUMAN	YIPF3	physical	16189514
PHLA1_HUMAN	PHLDA1	physical	16189514
SF01_HUMAN	SF1	physical	16189514
CCD33_HUMAN	CCDC33	physical	16189514
VISTA_HUMAN	C10orf54	physical	16189514
FBLN4_HUMAN	EFEMP2	physical	16189514
NOC4L_HUMAN	NOC4L	physical	16189514
K1683_HUMAN	KIAA1683	physical	16189514
ENKD1_HUMAN	ENKD1	physical	16189514
ATG12_HUMAN	ATG12	physical	16189514
NEUR4_HUMAN	NEU4	physical	16189514
MED15_HUMAN	MED15	physical	16189514
IP6K2_HUMAN	IP6K2	physical	16189514
FXL18_HUMAN	FBXL18	physical	16189514
NECP2_HUMAN	NECAP2	physical	16189514
DEPP_HUMAN	C10orf10	physical	16189514
RAM_HUMAN	FAM103A1	physical	16189514
PLS4_HUMAN	PLSCR4	physical	16189514
INT11_HUMAN	CPSF3L	physical	16189514
PED1A_HUMAN	PCED1A	physical	16189514
KR412_HUMAN	KRTAP4-12	physical	16189514
GRIN2_HUMAN	GPRIN2	physical	16189514
SPY2_HUMAN	SPRY2	physical	16189514
VASP_HUMAN	VASP	physical	16189514
BORG5_HUMAN	CDC42EP1	physical	16189514
ZN581_HUMAN	ZNF581	physical	16189514
HEY2_HUMAN	HEY2	physical	16189514
PLS3_HUMAN	PLSCR3	physical	16189514
TFG_HUMAN	TFG	physical	16189514
ATL4_HUMAN	ADAMTSL4	physical	16189514
NPDC1_HUMAN	NPDC1	physical	16189514
CCER1_HUMAN	CCER1	physical	16189514
ZN764_HUMAN	ZNF764	physical	16189514
MUT7_HUMAN	EXD3	physical	16189514
GLRX3_HUMAN	GLRX3	physical	16189514
DHRS1_HUMAN	DHRS1	physical	16189514
DAZP2_HUMAN	DAZAP2	physical	16189514
ZN638_HUMAN	ZNF638	physical	16189514
S35A2_HUMAN	SLC35A2	physical	16189514
ZBT16_HUMAN	ZBTB16	physical	16189514
CJ062_HUMAN	C10orf62	physical	16189514
EGFR_HUMAN	EGFR	physical	12009895
A4_HUMAN	APP	physical	21832049
RBL1_HUMAN	RBL1	physical	21988832
PML_HUMAN	PML	physical	21988832
RGS3_HUMAN	RGS3	physical	25416956
SMRC1_HUMAN	SMARCC1	physical	25416956
STK16_HUMAN	STK16	physical	25416956
CHRD_HUMAN	CHRD	physical	25416956
DAZP2_HUMAN	DAZAP2	physical	25416956
GLRX3_HUMAN	GLRX3	physical	25416956
FRS3_HUMAN	FRS3	physical	25416956
DEFI6_HUMAN	DEF6	physical	25416956
PRR13_HUMAN	PRR13	physical	25416956
VP37C_HUMAN	VPS37C	physical	25416956
DMRT3_HUMAN	DMRT3	physical	25416956
SCNM1_HUMAN	SCNM1	physical	25416956
GDPD5_HUMAN	GDPD5	physical	25416956
KRA92_HUMAN	KRTAP9-2	physical	25416956
ZN587_HUMAN	ZNF587	physical	25416956
KRA42_HUMAN	KRTAP4-2	physical	25416956
LONF1_HUMAN	LONRF1	physical	25416956
CTSR1_HUMAN	CATSPER1	physical	25416956
SPAT8_HUMAN	SPATA8	physical	25416956
MGT5B_HUMAN	MGAT5B	physical	25416956
ZN417_HUMAN	ZNF417	physical	25416956
LCE4A_HUMAN	LCE4A	physical	25416956
BCL6B_HUMAN	BCL6B	physical	25416956
TRI42_HUMAN	TRIM42	physical	25416956
LCE2D_HUMAN	LCE2D	physical	25416956
LCE3C_HUMAN	LCE3C	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR10B_HUMAN	KRTAP10-11	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
KRA56_HUMAN	KRTAP5-6	physical	25416956
KR411_HUMAN	KRTAP4-11	physical	25416956
LEG9C_HUMAN	LGALS9C	physical	25416956

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 PLS1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Regulation of phospholipid scramblase activity during apoptosis andcell activation by protein kinase Cdelta."; Frasch S.C., Henson P.M., Kailey J.M., Richter D.A., Janes M.S.,Fadok V.A., Bratton D.L.; J. Biol. Chem. 275:23065-23073(2000). Cited for: PHOSPHORYLATION AT THR-161, AND MUTAGENESIS.	10770950 [Abstract]
"c-Abl tyrosine kinase binds and phosphorylates phospholipidscramblase 1."; Sun J., Zhao J., Schwartz M.A., Wang J.Y., Wiedmer T., Sims P.J.; J. Biol. Chem. 276:28984-28990(2001). Cited for: PHOSPHORYLATION AT TYR-69 AND TYR-74, AND MUTAGENESIS.	11390389 [Abstract]

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