LSR_MOUSE - dbPTM
LSR_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LSR_MOUSE
UniProt AC Q99KG5
Protein Name Lipolysis-stimulated lipoprotein receptor
Gene Name Lsr
Organism Mus musculus (Mouse).
Sequence Length 594
Subcellular Localization Cell membrane
Single-pass type I membrane protein .
Protein Description Probable role in the clearance of triglyceride-rich lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of free fatty acids and allows their subsequent uptake in the cells (By similarity)..
Protein Sequence MAPAASACAGAPGSHPATTIFVCLFLIIYCPDRASAIQVTVPDPYHVVILFQPVTLHCTYQMSNTLTAPIVIWKYKSFCRDRVADAFSPASVDNQLNAQLAAGNPGYNPYVECQDSVRTVRVVATKQGNAVTLGDYYQGRRITITGNADLTFEQTAWGDSGVYYCSVVSAQDLDGNNEAYAELIVLGRTSEAPELLPGFRAGPLEDWLFVVVVCLASLLFFLLLGICWCQCCPHTCCCYVRCPCCPDKCCCPEALYAAGKAATSGVPSIYAPSIYTHLSPAKTPPPPPAMIPMRPPYGYPGDFDRTSSVGGHSSQVPLLREVDGSVSSEVRSGYRIQANQQDDSMRVLYYMEKELANFDPSRPGPPNGRVERAMSEVTSLHEDDWRSRPSRAPALTPIRDEEWNRHSPRSPRTWEQEPLQEQPRGGWGSGRPRARSVDALDDINRPGSTESGRSSPPSSGRRGRAYAPPRSRSRDDLYDPDDPRDLPHSRDPHYYDDLRSRDPRADPRSRQRSHDPRDAGFRSRDPQYDGRLLEEALKKKGAGERRRVYREEEEEEEEGHYPPAPPPYSETDSQASRERRMKKNLALSRESLVV
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
113S-palmitoylationGYNPYVECQDSVRTV
CCCCCCCHHCCCEEE		3.7728526873
132PhosphorylationTKQGNAVTLGDYYQG
ECCCCEEEECCEECC		23.7117203969
256PhosphorylationCCCPEALYAAGKAAT
CCCHHHHHHHHHHHH		11.0617242355
263PhosphorylationYAAGKAATSGVPSIY
HHHHHHHHCCCCCEE		30.7626643407
264PhosphorylationAAGKAATSGVPSIYA
HHHHHHHCCCCCEEC		32.8226643407
268PhosphorylationAATSGVPSIYAPSIY
HHHCCCCCEECCCHH		26.3126643407
270PhosphorylationTSGVPSIYAPSIYTH
HCCCCCEECCCHHHC		19.4626643407
273PhosphorylationVPSIYAPSIYTHLSP
CCCEECCCHHHCCCC		21.7626643407
275PhosphorylationSIYAPSIYTHLSPAK
CEECCCHHHCCCCCC		7.7626643407
276PhosphorylationIYAPSIYTHLSPAKT
EECCCHHHCCCCCCC		18.0526643407
279PhosphorylationPSIYTHLSPAKTPPP
CCHHHCCCCCCCCCC		18.4026643407
282UbiquitinationYTHLSPAKTPPPPPA
HHCCCCCCCCCCCCC		66.0222790023
283PhosphorylationTHLSPAKTPPPPPAM
HCCCCCCCCCCCCCC		43.0425195567
288 (in isoform 2)Phosphorylation-39.99-
306PhosphorylationYPGDFDRTSSVGGHS
CCCCCCCCCCCCCCC		27.4822324799
307PhosphorylationPGDFDRTSSVGGHSS
CCCCCCCCCCCCCCC		24.7422324799
308PhosphorylationGDFDRTSSVGGHSSQ
CCCCCCCCCCCCCCC		24.9421082442
313PhosphorylationTSSVGGHSSQVPLLR
CCCCCCCCCCCCEEE		26.2421082442
314PhosphorylationSSVGGHSSQVPLLRE
CCCCCCCCCCCEEEE		29.5326643407
325PhosphorylationLLREVDGSVSSEVRS
EEEEECCCCCCHHHC		17.8625521595
327PhosphorylationREVDGSVSSEVRSGY
EEECCCCCCHHHCCE		23.6025521595
328PhosphorylationEVDGSVSSEVRSGYR
EECCCCCCHHHCCEE		37.6525521595
332PhosphorylationSVSSEVRSGYRIQAN
CCCCHHHCCEEEEEC		45.40-
349PhosphorylationDDSMRVLYYMEKELA
CCHHHHHHHHHHHHH		9.63-
353UbiquitinationRVLYYMEKELANFDP
HHHHHHHHHHHCCCC		41.3122790023
374OxidationNGRVERAMSEVTSLH
CCHHHHHHHHHHHHC		4.3717242355
375PhosphorylationGRVERAMSEVTSLHE
CHHHHHHHHHHHHCC		28.1227087446
378PhosphorylationERAMSEVTSLHEDDW
HHHHHHHHHHCCCCH		22.8627087446
379PhosphorylationRAMSEVTSLHEDDWR
HHHHHHHHHCCCCHH		32.6727087446
396PhosphorylationPSRAPALTPIRDEEW
CCCCCCCCCCCCCHH		20.8322324799
407PhosphorylationDEEWNRHSPRSPRTW
CCHHHCCCCCCCCCC		20.8325521595
410PhosphorylationWNRHSPRSPRTWEQE
HHCCCCCCCCCCCCC		23.3230352176
413PhosphorylationHSPRSPRTWEQEPLQ
CCCCCCCCCCCCCCC		36.4228973931
424MethylationEPLQEQPRGGWGSGR
CCCCCCCCCCCCCCC		56.82-
429PhosphorylationQPRGGWGSGRPRARS
CCCCCCCCCCCCCCC		25.7229472430
436PhosphorylationSGRPRARSVDALDDI
CCCCCCCCCCCCCCC		24.3027087446
448PhosphorylationDDINRPGSTESGRSS
CCCCCCCCCCCCCCC		31.5221082442
449PhosphorylationDINRPGSTESGRSSP
CCCCCCCCCCCCCCC		39.8321082442
451PhosphorylationNRPGSTESGRSSPPS
CCCCCCCCCCCCCCC		39.3321082442
454PhosphorylationGSTESGRSSPPSSGR
CCCCCCCCCCCCCCC		51.2027087446
455PhosphorylationSTESGRSSPPSSGRR
CCCCCCCCCCCCCCC		39.2027087446
458PhosphorylationSGRSSPPSSGRRGRA
CCCCCCCCCCCCCCC		49.1328609623
459PhosphorylationGRSSPPSSGRRGRAY
CCCCCCCCCCCCCCC		41.9321082442
466PhosphorylationSGRRGRAYAPPRSRS
CCCCCCCCCCCCCCC		20.48-
470UbiquitinationGRAYAPPRSRSRDDL
CCCCCCCCCCCCCCC		43.5827667366
471PhosphorylationRAYAPPRSRSRDDLY
CCCCCCCCCCCCCCC		40.1430352176
473PhosphorylationYAPPRSRSRDDLYDP
CCCCCCCCCCCCCCC		41.1125521595
478PhosphorylationSRSRDDLYDPDDPRD
CCCCCCCCCCCCCCC		32.2129899451
489PhosphorylationDPRDLPHSRDPHYYD
CCCCCCCCCCCHHHH		36.1229472430
495PhosphorylationHSRDPHYYDDLRSRD
CCCCCHHHHHHHHCC		10.4326032504
515UbiquitinationRSRQRSHDPRDAGFR
HHHHHCCCCCCCCCC		40.9727667366
517MethylationRQRSHDPRDAGFRSR
HHHCCCCCCCCCCCC		53.09-
519UbiquitinationRSHDPRDAGFRSRDP
HCCCCCCCCCCCCCC		21.9427667366
522MethylationDPRDAGFRSRDPQYD
CCCCCCCCCCCCCCC		29.84-
528PhosphorylationFRSRDPQYDGRLLEE
CCCCCCCCCHHHHHH		26.25-
531MethylationRDPQYDGRLLEEALK
CCCCCCHHHHHHHHH		32.95-
538UbiquitinationRLLEEALKKKGAGER
HHHHHHHHHCCCCCC		60.5322790023
539UbiquitinationLLEEALKKKGAGERR
HHHHHHHHCCCCCCC		58.2422790023
564UbiquitinationEEGHYPPAPPPYSET
HCCCCCCCCCCCCCC		25.4027667366
576PhosphorylationSETDSQASRERRMKK
CCCCHHHHHHHHHHH		27.34-
582UbiquitinationASRERRMKKNLALSR
HHHHHHHHHHHHHHH		36.3822790023
583UbiquitinationSRERRMKKNLALSRE
HHHHHHHHHHHHHHH		48.1022790023
588PhosphorylationMKKNLALSRESLVV-
HHHHHHHHHHHCCC-		28.5225521595
591PhosphorylationNLALSRESLVV----
HHHHHHHHCCC----		25.9225521595
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
288SPhosphorylationKinaseJNK1Q91Y86
PSP
288SPhosphorylationKinaseJNK2Q9WTU6
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LSR_MOUSE !!
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 LSR_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LSR_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LSR_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436 AND SER-473, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307; SER-379; SER-436;SER-454; SER-473; TYR-478 AND SER-591, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-132 AND SER-473, ANDMASS SPECTROMETRY.

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