PLS1_HUMAN - dbPTM
PLS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
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 Orthologous
Protein Cluster
51UbiquitinationVSYPPPPAGHSGPGP
CCCCCCCCCCCCCCC
33.8233845483
69PhosphorylationPVPNQPVYNQPVYNQ
CCCCCCCCCCCCCCC
18.1122817900
74PhosphorylationPVYNQPVYNQPVGAA
CCCCCCCCCCCCCCC
18.1122817900
125UbiquitinationEVLTGFETNNKYEIK
HHHHCCCCCCCEEEE
41.6633845483
132UbiquitinationTNNKYEIKNSFGQRV
CCCCEEEECCCCCEE
34.3029901268
142UbiquitinationFGQRVYFAAEDTDCC
CCCEEEEEECCCCCC
7.7027667366
142UbiquitinationFGQRVYFAAEDTDCC
CCCEEEEEECCCCCC
7.7021890473
148S-palmitoylationFAAEDTDCCTRNCCG
EEECCCCCCCCCCCC
2.5029575903
149S-palmitoylationAAEDTDCCTRNCCGP
EECCCCCCCCCCCCC
4.4529575903
153S-palmitoylationTDCCTRNCCGPSRPF
CCCCCCCCCCCCCCE
2.2729575903
154S-palmitoylationDCCTRNCCGPSRPFT
CCCCCCCCCCCCCEE
11.6629575903
161PhosphorylationCGPSRPFTLRIIDNM
CCCCCCEEEEEECCC
20.1510770950
177UbiquitinationQEVITLERPLRCSSC
CEEEEECCCCCCCCC
38.3722817900
177UbiquitinationQEVITLERPLRCSSC
CEEEEECCCCCCCCC
38.37-
180UbiquitinationITLERPLRCSSCCCP
EEECCCCCCCCCCCC
22.4321890473
180UbiquitinationITLERPLRCSSCCCP
EEECCCCCCCCCCCC
22.4321890473
184S-palmitoylationRPLRCSSCCCPCCLQ
CCCCCCCCCCCCEEE
1.2712564925
185S-palmitoylationPLRCSSCCCPCCLQE
CCCCCCCCCCCEEEE
2.9112564925
186S-palmitoylationLRCSSCCCPCCLQEI
CCCCCCCCCCEEEEE
3.2012564925
188S-palmitoylationCSSCCCPCCLQEIEI
CCCCCCCCEEEEEEE
1.9512564925
189S-palmitoylationSSCCCPCCLQEIEIQ
CCCCCCCEEEEEEEE
2.3812564925
207UbiquitinationGVPIGYVIQTWHPCL
CCCEEEEEEECCCCC
1.9721963094
207UbiquitinationGVPIGYVIQTWHPCL
CCCEEEEEEECCCCC
1.97-
209UbiquitinationPIGYVIQTWHPCLPK
CEEEEEEECCCCCCE
18.0222817900
213S-palmitoylationVIQTWHPCLPKFTIQ
EEEECCCCCCEEEEC
7.0329575903
216UbiquitinationTWHPCLPKFTIQNEK
ECCCCCCEEEECCCC
42.0427667366
2232-HydroxyisobutyrylationKFTIQNEKREDVLKI
EEEECCCCHHCEEEE
69.50-
223UbiquitinationKFTIQNEKREDVLKI
EEEECCCCHHCEEEE
69.5021906983
249PhosphorylationDVDFEIKSLDEQCVV
CCCEEEEECCCCEEH
46.8725159151
251UbiquitinationDFEIKSLDEQCVVGK
CEEEEECCCCEEHHH
51.5222817900
254UbiquitinationIKSLDEQCVVGKISK
EEECCCCEEHHHHHH
2.2321890473
258UbiquitinationDEQCVVGKISKHWTG
CCCEEHHHHHHHHHH
32.0027667366
261UbiquitinationCVVGKISKHWTGILR
EEHHHHHHHHHHHHH
46.7821906983
281UbiquitinationADNFGIQFPLDLDVK
CHHCCCCCCCCCCHH
6.4921963094
283UbiquitinationNFGIQFPLDLDVKMK
HCCCCCCCCCCHHHH
12.3322817900
288UbiquitinationFPLDLDVKMKAVMIG
CCCCCCHHHHHHHHH
34.0621963094
290UbiquitinationLDLDVKMKAVMIGAC
CCCCHHHHHHHHHHH
31.9222817900

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
69YPhosphorylationKinaseABL1P00519
PhosphoELM
69YPhosphorylationKinaseABLP00520
PSP
69YPhosphorylationKinaseSRCP12931
PSP
69YPhosphorylationKinaseABL-FAMILY-GPS
69YPhosphorylationKinaseSRC64-PhosphoELM
74YPhosphorylationKinaseABL1P00519
PhosphoELM
74YPhosphorylationKinaseABLP00520
PSP
74YPhosphorylationKinaseSRCP12931
PSP
74YPhosphorylationKinaseABL-FAMILY-GPS
74YPhosphorylationKinaseSRC64-PhosphoELM
161TPhosphorylationKinasePRKCDQ05655
Uniprot
161TPhosphorylationKinasePRKCDP09215
GPS
161TPhosphorylationKinasePKC-FAMILY-GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
161TPhosphorylation

10770950

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 Domain-Domain Interactions
CPSF6_HUMANCPSF6physical
16189514
RASD1_HUMANRASD1physical
16189514
6PGL_HUMANPGLSphysical
16189514
DTX2_HUMANDTX2physical
16189514
DLK2_HUMANDLK2physical
16189514
SPG7_HUMANSPG7physical
16189514
NET4_HUMANNTN4physical
16189514
YIPF3_HUMANYIPF3physical
16189514
PHLA1_HUMANPHLDA1physical
16189514
SF01_HUMANSF1physical
16189514
CCD33_HUMANCCDC33physical
16189514
VISTA_HUMANC10orf54physical
16189514
FBLN4_HUMANEFEMP2physical
16189514
NOC4L_HUMANNOC4Lphysical
16189514
K1683_HUMANKIAA1683physical
16189514
ENKD1_HUMANENKD1physical
16189514
ATG12_HUMANATG12physical
16189514
NEUR4_HUMANNEU4physical
16189514
MED15_HUMANMED15physical
16189514
IP6K2_HUMANIP6K2physical
16189514
FXL18_HUMANFBXL18physical
16189514
NECP2_HUMANNECAP2physical
16189514
DEPP_HUMANC10orf10physical
16189514
RAM_HUMANFAM103A1physical
16189514
PLS4_HUMANPLSCR4physical
16189514
INT11_HUMANCPSF3Lphysical
16189514
PED1A_HUMANPCED1Aphysical
16189514
KR412_HUMANKRTAP4-12physical
16189514
GRIN2_HUMANGPRIN2physical
16189514
SPY2_HUMANSPRY2physical
16189514
VASP_HUMANVASPphysical
16189514
BORG5_HUMANCDC42EP1physical
16189514
ZN581_HUMANZNF581physical
16189514
HEY2_HUMANHEY2physical
16189514
PLS3_HUMANPLSCR3physical
16189514
TFG_HUMANTFGphysical
16189514
ATL4_HUMANADAMTSL4physical
16189514
NPDC1_HUMANNPDC1physical
16189514
CCER1_HUMANCCER1physical
16189514
ZN764_HUMANZNF764physical
16189514
MUT7_HUMANEXD3physical
16189514
GLRX3_HUMANGLRX3physical
16189514
DHRS1_HUMANDHRS1physical
16189514
DAZP2_HUMANDAZAP2physical
16189514
ZN638_HUMANZNF638physical
16189514
S35A2_HUMANSLC35A2physical
16189514
ZBT16_HUMANZBTB16physical
16189514
CJ062_HUMANC10orf62physical
16189514
EGFR_HUMANEGFRphysical
12009895
A4_HUMANAPPphysical
21832049
RBL1_HUMANRBL1physical
21988832
PML_HUMANPMLphysical
21988832
RGS3_HUMANRGS3physical
25416956
SMRC1_HUMANSMARCC1physical
25416956
STK16_HUMANSTK16physical
25416956
CHRD_HUMANCHRDphysical
25416956
DAZP2_HUMANDAZAP2physical
25416956
GLRX3_HUMANGLRX3physical
25416956
FRS3_HUMANFRS3physical
25416956
DEFI6_HUMANDEF6physical
25416956
PRR13_HUMANPRR13physical
25416956
VP37C_HUMANVPS37Cphysical
25416956
DMRT3_HUMANDMRT3physical
25416956
SCNM1_HUMANSCNM1physical
25416956
GDPD5_HUMANGDPD5physical
25416956
KRA92_HUMANKRTAP9-2physical
25416956
ZN587_HUMANZNF587physical
25416956
KRA42_HUMANKRTAP4-2physical
25416956
LONF1_HUMANLONRF1physical
25416956
CTSR1_HUMANCATSPER1physical
25416956
SPAT8_HUMANSPATA8physical
25416956
MGT5B_HUMANMGAT5Bphysical
25416956
ZN417_HUMANZNF417physical
25416956
LCE4A_HUMANLCE4Aphysical
25416956
BCL6B_HUMANBCL6Bphysical
25416956
TRI42_HUMANTRIM42physical
25416956
LCE2D_HUMANLCE2Dphysical
25416956
LCE3C_HUMANLCE3Cphysical
25416956
KR109_HUMANKRTAP10-9physical
25416956
KR10B_HUMANKRTAP10-11physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
KRA56_HUMANKRTAP5-6physical
25416956
KR411_HUMANKRTAP4-11physical
25416956
LEG9C_HUMANLGALS9Cphysical
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

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.

TOP