LDLR_HUMAN - dbPTM
LDLR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LDLR_HUMAN
UniProt AC P01130
Protein Name Low-density lipoprotein receptor
Gene Name LDLR
Organism Homo sapiens (Human).
Sequence Length 860
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Membrane, clathrin-coated pit . Golgi apparatus . Early endosome . Late endosome . Lysosome . Rapidly endocytosed upon ligand binding.
Protein Description Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits.; (Microbial infection) Acts as a receptor for hepatitis C virus in hepatocytes, but not through a direct interaction with viral proteins.; (Microbial infection) Acts as a receptor for Vesicular stomatitis virus.; (Microbial infection) In case of HIV-1 infection, may function as a receptor for extracellular Tat in neurons, mediating its internalization in uninfected cells..
Protein Sequence MGPWGWKLRWTVALLLAAAGTAVGDRCERNEFQCQDGKCISYKWVCDGSAECQDGSDESQETCLSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCPPKTCSQDEFRCHDGKCISRQFVCDSDRDCLDGSDEASCPVLTCGPASFQCNSSTCIPQLWACDNDPDCEDGSDEWPQRCRGLYVFQGDSSPCSAFEFHCLSGECIHSSWRCDGGPDCKDKSDEENCAVATCRPDEFQCSDGNCIHGSRQCDREYDCKDMSDEVGCVNVTLCEGPNKFKCHSGECITLDKVCNMARDCRDWSDEPIKECGTNECLDNNGGCSHVCNDLKIGYECLCPDGFQLVAQRRCEDIDECQDPDTCSQLCVNLEGGYKCQCEEGFQLDPHTKACKAVGSIAYLFFTNRHEVRKMTLDRSEYTSLIPNLRNVVALDTEVASNRIYWSDLSQRMICSTQLDRAHGVSSYDTVISRDIQAPDGLAVDWIHSNIYWTDSVLGTVSVADTKGVKRKTLFRENGSKPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIYSLVTENIQWPNGITLDLLSGRLYWVDSKLHSISSIDVNGGNRKTILEDEKRLAHPFSLAVFEDKVFWTDIINEAIFSANRLTGSDVNLLAENLLSPEDMVLFHNLTQPRGVNWCERTTLSNGGCQYLCLPAPQINPHSPKFTCACPDGMLLARDMRSCLTEAEAAVATQETSTVRLKVSSTAVRTQHTTTRPVPDTSRLPGATPGLTTVEIVTMSHQALGDVAGRGNEKKPSSVRALSIVLPIVLLVFLCLGVFLLWKNWRLKNINSINFDNPVYQKTTEDEVHICHNQDGYSYPSRQMVSLEDDVA
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
38UbiquitinationEFQCQDGKCISYKWV
CEECCCCCEEEEEEE		36.36-
97N-linked_GlycosylationDGQVDCDNGSDEQGC
CCEEECCCCCCCCCC		59.19UniProtKB CARBOHYD
108O-linked_GlycosylationEQGCPPKTCSQDEFR
CCCCCCCCCCCCCEE		24.14OGP
110PhosphorylationGCPPKTCSQDEFRCH
CCCCCCCCCCCEECC		45.9925159151
156N-linked_GlycosylationGPASFQCNSSTCIPQ
CCCEEECCCCCCCCE		28.3619520913
188PhosphorylationPQRCRGLYVFQGDSS
CCCCCEEEEECCCCC		11.3130576142
194PhosphorylationLYVFQGDSSPCSAFE
EEEECCCCCCCCEEE		42.9030576142
212PhosphorylationLSGECIHSSWRCDGG
CCCCEECCCEECCCC		16.2230576142
235O-linked_GlycosylationEENCAVATCRPDEFQ
CCCEEEEEECCCEEE		11.49OGP
272N-linked_GlycosylationSDEVGCVNVTLCEGP
CCCCCCEEEEEECCC		25.7319520913
390UbiquitinationFQLDPHTKACKAVGS
CCCCCCCHHHHHHHH		49.07-
397PhosphorylationKACKAVGSIAYLFFT
HHHHHHHHHHHHCCC		9.4620068231
400PhosphorylationKAVGSIAYLFFTNRH
HHHHHHHHHCCCCHH		11.4520068231
404PhosphorylationSIAYLFFTNRHEVRK
HHHHHCCCCHHHHHE		24.8220068231
463PhosphorylationLDRAHGVSSYDTVIS
CHHHCCCCCCCEECC		27.9827050516
464PhosphorylationDRAHGVSSYDTVISR
HHHCCCCCCCEECCC		25.3127050516
465PhosphorylationRAHGVSSYDTVISRD
HHCCCCCCCEECCCC		14.23-
470PhosphorylationSSYDTVISRDIQAPD
CCCCEECCCCCCCCC		21.40-
515N-linked_GlycosylationRKTLFRENGSKPRAI
EEEEECCCCCCCCEE		56.64UniProtKB CARBOHYD
517PhosphorylationTLFRENGSKPRAIVV
EEECCCCCCCCEEEE		51.5820363803
596UbiquitinationDVNGGNRKTILEDEK
ECCCCCCCCCCCCHH		43.87-
603UbiquitinationKTILEDEKRLAHPFS
CCCCCCHHHHCCCCC		66.10-
657N-linked_GlycosylationEDMVLFHNLTQPRGV
HHEEEEECCCCCCCC		37.1312754519
713PhosphorylationRDMRSCLTEAEAAVA
HHHHHHHHHHHHHHH		37.16-
721O-linked_GlycosylationEAEAAVATQETSTVR
HHHHHHHCCCCCEEE		21.9755826599
724O-linked_GlycosylationAAVATQETSTVRLKV
HHHHCCCCCEEEEEE		21.6334870707
724PhosphorylationAAVATQETSTVRLKV
HHHHCCCCCEEEEEE		21.63-
725O-linked_GlycosylationAVATQETSTVRLKVS
HHHCCCCCEEEEEEE		24.9355826611
726O-linked_GlycosylationVATQETSTVRLKVSS
HHCCCCCEEEEEEEC		19.6455826617
730UbiquitinationETSTVRLKVSSTAVR
CCCEEEEEEECCEEE		29.52-
732O-linked_GlycosylationSTVRLKVSSTAVRTQ
CEEEEEEECCEEEEE		22.0034866975
733O-linked_GlycosylationTVRLKVSSTAVRTQH
EEEEEEECCEEEEEE		24.312494263
734O-linked_GlycosylationVRLKVSSTAVRTQHT
EEEEEECCEEEEEEE		22.9744922071
738O-linked_GlycosylationVSSTAVRTQHTTTRP
EECCEEEEEEECCCC		20.3628510447
741O-linked_GlycosylationTAVRTQHTTTRPVPD
CEEEEEEECCCCCCC		21.7555833371
742O-linked_GlycosylationAVRTQHTTTRPVPDT
EEEEEEECCCCCCCC		20.7755833375
743O-linked_GlycosylationVRTQHTTTRPVPDTS
EEEEEECCCCCCCCC		33.8428510447
749O-linked_GlycosylationTTRPVPDTSRLPGAT
CCCCCCCCCCCCCCC		15.07OGP
750O-linked_GlycosylationTRPVPDTSRLPGATP
CCCCCCCCCCCCCCC		38.9255833383
756O-linked_GlycosylationTSRLPGATPGLTTVE
CCCCCCCCCCCEEEE		24.65OGP
760O-linked_GlycosylationPGATPGLTTVEIVTM
CCCCCCCEEEEEEEE		34.41OGP
761O-linked_GlycosylationGATPGLTTVEIVTMS
CCCCCCEEEEEEEEC		22.60OGP
766O-linked_GlycosylationLTTVEIVTMSHQALG
CEEEEEEEECHHHHH		20.72OGP
768O-linked_GlycosylationTVEIVTMSHQALGDV
EEEEEEECHHHHHCC		11.77OGP
820PhosphorylationWRLKNINSINFDNPV
CCCCCCCCCCCCCCC		18.3421945579
828PhosphorylationINFDNPVYQKTTEDE
CCCCCCCEECCCCCC		12.9221945579
830UbiquitinationFDNPVYQKTTEDEVH
CCCCCEECCCCCCEE		39.46-
831PhosphorylationDNPVYQKTTEDEVHI
CCCCEECCCCCCEEE		21.6421945579
832PhosphorylationNPVYQKTTEDEVHIC
CCCEECCCCCCEEEE		48.7721945579
845PhosphorylationICHNQDGYSYPSRQM
EEECCCCCCCCCCCE		17.2021945579
846PhosphorylationCHNQDGYSYPSRQMV
EECCCCCCCCCCCEE		35.7821945579
847PhosphorylationHNQDGYSYPSRQMVS
ECCCCCCCCCCCEEE		9.2021945579
849PhosphorylationQDGYSYPSRQMVSLE
CCCCCCCCCCEEECC		27.2321945579
854PhosphorylationYPSRQMVSLEDDVA-
CCCCCEEECCCCCC-		22.2423090842
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
-KUbiquitinationE3 ubiquitin ligaseMYLIPQ8WY64
PMID:19688294
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LDLR_HUMAN !!
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 LDLR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DAB1_HUMANDAB1physical
10827173
AP1M2_HUMANAP1M2physical
11157985
AMRP_HUMANLRPAP1physical
7822276
SNX17_HUMANSNX17physical
12169628
MYLIP_HUMANMYLIPphysical
21734303
GRP78_HUMANHSPA5physical
16257961
ENPL_HUMANHSP90B1physical
16257961
PDIA4_HUMANPDIA4physical
16257961
CALX_HUMANCANXphysical
16257961
MAP4_HUMANMAP4physical
21988832
PCSK9_HUMANPCSK9physical
23085658
MYLIP_HUMANMYLIPphysical
26666640
UBP2_HUMANUSP2physical
26666640
Drug and Disease Associations
Kegg Disease
H00155 Hypercholesterolemia, including: Hypercholesterolemia, autosomal dominant; Hyperlipoproteinemia, typ
OMIM Disease
143890Familial hypercholesterolemia (FH)
Kegg Drug
D00887 Atorvastatin calcium (USAN); Lipitor (TN)
D02258 Atorvastatin calcium hydrate (JP16); Lipitor (TN)
D07474 Atorvastatin (INN); Lipitor (TN); Sortis (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LDLR_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-657, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-657, AND MASSSPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-657.
Phosphorylation
ReferencePubMed
"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-845 AND TYR-847, ANDMASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-845, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-845, AND MASSSPECTROMETRY.

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