LRP1_MOUSE - dbPTM
LRP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRP1_MOUSE
UniProt AC Q91ZX7
Protein Name Prolow-density lipoprotein receptor-related protein 1
Gene Name Lrp1 {ECO:0000312|EMBL:AAL09566.1}
Organism Mus musculus (Mouse).
Sequence Length 4545
Subcellular Localization Low-density lipoprotein receptor-related protein 1 85 kDa subunit: Cell membrane
Single-pass type I membrane protein. Membrane, coated pit.
Low-density lipoprotein receptor-related protein 1 515 kDa subunit: Cell membrane
Peripheral membrane protein
E
Protein Description Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. [PubMed: 1423604 Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission. Acts as an alpha-2-macroglobulin receptor (By similarity; (Microbial infection) Functions as a receptor for Vibrio cholerae cholix toxin and for Pseudomonas aeruginosa exotoxin A.]
Protein Sequence MLTPPLLLLLPLLSALVSGATMDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEAPEICPQSKAQRCPPNEHSCLGTELCVPMSRLCNGIQDCMDGSDEGAHCRELRANCSRMGCQHHCVPTPSGPTCYCNSSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFTCGCVEGYLLQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANETVCWVHVGDSAAQTQLKCARMPGLKGFVDEHTINISLSLHHVEQMAIDWLTGNFYFVDDIDDRIFVCNRNGDTCVTLLDLELYNPKGIALDPAMGKVFFTDYGQIPKVERCDMDGQNRTKLVDSKIVFPHGITLDLVSRLVYWADAYLDYIEVVDYEGKGRQTIIQGILIEHLYGLTVFENYLYATNSDNANTQQKTSVIRVNRFNSTEYQVVTRVDKGGALHIYHQRRQPRVRSHACENDQYGKPGGCSDICLLANSHKARTCRCRSGFSLGSDGKSCKKPEHELFLVYGKGRPGIIRGMDMGAKVPDEHMIPIENLMNPRALDFHAETGFIYFADTTSYLIGRQKIDGTERETILKDGIHNVEGVAVDWMGDNLYWTDDGPKKTISVARLEKAAQTRKTLIEGKMTHPRAIVVDPLNGWMYWTDWEEDPKDSRRGRLERAWMDGSHRDIFVTSKTVLWPNGLSLDIPAGRLYWVDAFYDRIETILLNGTDRKIVYEGPELNHAFGLCHHGNYLFWTEYRSGSVYRLERGVAGAPPTVTLLRSERPPIFEIRMYDAQQQQVGTNKCRVNNGGCSSLCLATPGSRQCACAEDQVLDTDGVTCLANPSYVPPPQCQPGEFACANNRCIQERWKCDGDNDCLDNSDEAPALCHQHTCPSDRFKCENNRCIPNRWLCDGDNDCGNSEDESNATCSARTCPPNQFSCASGRCIPISWTCDLDDDCGDRSDESASCAYPTCFPLTQFTCNNGRCININWRCDNDNDCGDNSDEAGCSHSCSSTQFKCNSGRCIPEHWTCDGDNDCGDYSDETHANCTNQATRPPGGCHSDEFQCRLDGLCIPLRWRCDGDTDCMDSSDEKSCEGVTHVCDPNVKFGCKDSARCISKAWVCDGDSDCEDNSDEENCEALACRPPSHPCANNTSVCLPPDKLCDGKDDCGDGSDEGELCDQCSLNNGGCSHNCSVAPGEGIVCSCPLGMELGSDNHTCQIQSYCAKHLKCSQKCDQNKFSVKCSCYEGWVLEPDGESCRSLDPFKPFIIFSNRHEIRRIDLHKGDYSVLVPGLRNTIALDFHLSQSALYWTDVVEDKIYRGKLLDNGALTSFEVVIQYGLATPEGLAVDWIAGNIYWVESNLDQIEVAKLDGTLRTTLLAGDIEHPRAIALDPRDGILFWTDWDASLPRIEAASMSGAGRRTIHRETGSGGWPNGLTVDYLEKRILWIDARSDAIYSARYDGSGHMEVLRGHEFLSHPFAVTLYGGEVYWTDWRTNTLAKANKWTGHNVTVVQRTNTQPFDLQVYHPSRQPMAPNPCEANGGRGPCSHLCLINYNRTVSCACPHLMKLHKDNTTCYEFKKFLLYARQMEIRGVDLDAPYYNYIISFTVPDIDNVTVLDYDAREQRVYWSDVRTQAIKRAFINGTGVETVVSADLPNAHGLAVDWVSRNLFWTSYDTNKKQINVARLDGSFKNAVVQGLEQPHGLVVHPLRGKLYWTDGDNISMANMDGSNHTLLFSGQKGPVGLAIDFPESKLYWISSGNHTINRCNLDGSELEVIDTMRSQLGKATALAIMGDKLWWADQVSEKMGTCNKADGSGSVVLRNSTTLVMHMKVYDESIQLEHEGTNPCSVNNGDCSQLCLPTSETTRSCMCTAGYSLRSGQQACEGVGSFLLYSVHEGIRGIPLDPNDKSDALVPVSGTSLAVGIDFHAENDTIYWVDMGLSTISRAKRDQTWREDVVTNGIGRVEGIAVDWIAGNIYWTDQGFDVIEVARLNGSFRYVVISQGLDKPRAITVHPEKGYLFWTEWGHYPRIERSRLDGTERVVLVNVSISWPNGISVDYQGGKLYWCDARMDKIERIDLETGENREVVLSSNNMDMFSVSVFEDFIYWSDRTHANGSIKRGCKDNATDSVPLRTGIGVQLKDIKVFNRDRQKGTNVCAVANGGCQQLCLYRGGGQRACACAHGMLAEDGASCREYAGYLLYSERTILKSIHLSDERNLNAPVQPFEDPEHMKNVIALAFDYRAGTSPGTPNRIFFSDIHFGNIQQINDDGSGRTTIVENVGSVEGLAYHRGWDTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLDECQNLMFWTNWNELHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRAEKLYFSDATLDKIERCEYDGSHRYVILKSEPVHPFGLAVYGEHIFWTDWVRRAVQRANKYVGSDMKLLRVDIPQQPMGIIAVANDTNSCELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQEDFTCRAVNSSCRAQDEFECANGECISFSLTCDGVSHCKDKSDEKPSYCNSRRCKKTFRQCNNGRCVSNMLWCNGVDDCGDGSDEIPCNKTACGVGEFRCRDGSCIGNSSRCNQFVDCEDASDEMNCSATDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPGVKRPRCPLNYFACPSGRCIPMSWTCDKEDDCENGEDETHCNKFCSEAQFECQNHRCISKQWLCDGSDDCGDGSDEAAHCEGKTCGPSSFSCPGTHVCVPERWLCDGDKDCTDGADESVTAGCLYNSTCDDREFMCQNRLCIPKHFVCDHDRDCADGSDESPECEYPTCGPNEFRCANGRCLSSRQWECDGENDCHDHSDEAPKNPHCTSPEHKCNASSQFLCSSGRCVAEALLCNGQDDCGDGSDERGCHVNECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCADLDECSTTFPCSQLCINTHGSYKCLCVEGYAPRGGDPHSCKAVTDEEPFLIFANRYYLRKLNLDGSNYTLLKQGLNNAVALDFDYREQMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVGGNLYWCDKGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQNGYLYWTDWGDHSLIGRIGMDGSGRSIIVDTKITWPNGLTVDYVTERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLFEDYVYWTDWETKSINRAHKTTGANKTLLISTLHRPMDLHVFHALRQPDVPNHPCKVNNGGCSNLCLLSPGGGHKCACPTNFYLGGDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCGDHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKCTNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCVDGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQFRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDCADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQCNNTLCKPLAWKCDGEDDCGDNSDENPEECARFICPPNRPFRCKNDRVCLWIGRQCDGVDNCGDGTDEEDCEPPTAQNPHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSIDPKLTSCATNASMCGDEARCVRTEKAAYCACRSGFHTVPGQPGCQDINECLRFGTCSQLCNNTKGGHLCSCARNFMKTHNTCKAEGSEYQVLYIADDNEIRSLFPGHPHSAYEQTFQGDESVRIDAMDVHVKAGRVYWTNWHTGTISYRSLPPAAPPTTSNRHRRQIDRGVTHLNISGLKMPRGIAIDWVAGNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLRGTMYWSDWGNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHNERLYWADAKLSVIGSIRLNGTDPIVAADSKRGLSHPFSIDVFEDYIYGVTYINNRVFKIHKFGHSPLINLTGGLSHASDVVLYHQHKQPEVTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCVPVPSPTPPPDAPRPGTCTLQCFNGGSCFLNARRQPKCRCQPRYTGDKCELDQCWEYCHNGGTCAASPSGMPTCRCPTGFTGPKCTAQVCAGYCSNNSTCTVNQGNQPQCRCLPGFLGDRCQYRQCSGFCENFGTCQMAADGSRQCRCTVYFEGPRCEVNKCSRCLQGACVVNKQTGDVTCNCTDGRVAPSCLTCIDHCSNGGSCTMNSKMMPECQCPPHMTGPRCEEQVVSQQQPGHMASILIPLLLLLLLLLVAGVVFWYKRRVRGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPTNFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA
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
3Phosphorylation-----MLTPPLLLLL
-----CCCHHHHHHH		34.42-
58PhosphorylationERDCPDGSDEAPEIC
CCCCCCCCCCCCCCC		39.3926525534
115N-linked_GlycosylationHCRELRANCSRMGCQ
HHHHHHHHHHCCCCC		20.19-
137N-linked_GlycosylationSGPTCYCNSSFQLQA
CCCCCEECCCEEEEC		17.76-
186N-linked_GlycosylationGYLLQPDNRSCKAKN
EEEECCCCCCCCCCC		44.44-
240N-linked_GlycosylationAMDFSYANETVCWVH
CEECCCCCCEEEEEE		36.92-
275N-linked_GlycosylationFVDEHTINISLSLHH
CCCCCEEEEEEEEHH		20.96-
358N-linked_GlycosylationRCDMDGQNRTKLVDS
EECCCCCCCCEEECC		60.15-
447N-linked_GlycosylationVIRVNRFNSTEYQVV
EEEEECCCCCEEEEE		44.8019349973
730N-linked_GlycosylationRIETILLNGTDRKIV
HHHHHCCCCCCCEEE		48.1219656770
808GlutathionylationQQVGTNKCRVNNGGC
CCCCCCCCCCCCCCC		6.7824333276
808S-palmitoylationQQVGTNKCRVNNGGC
CCCCCCCCCCCCCCC		6.7826165157
884PhosphorylationDNDCLDNSDEAPALC
CCCCCCCCCCCCHHC		36.1726525534
924PhosphorylationGDNDCGNSEDESNAT
CCCCCCCCCCCCCCE		31.5426525534
929N-linked_GlycosylationGNSEDESNATCSART
CCCCCCCCCEECCCC		36.90-
1007PhosphorylationDNDCGDNSDEAGCSH
CCCCCCCCCCCCCCC		41.3826525534
1051N-linked_GlycosylationYSDETHANCTNQATR
CCCCCCCCCCCCCCC		26.07-
1076S-palmitoylationQCRLDGLCIPLRWRC
EEECCCEEEEEEEEE		3.5428526873
1087PhosphorylationRWRCDGDTDCMDSSD
EEEECCCCCCCCCCC		36.3126525534
1092PhosphorylationGDTDCMDSSDEKSCE
CCCCCCCCCCCHHCC		16.8926525534
1093PhosphorylationDTDCMDSSDEKSCEG
CCCCCCCCCCHHCCC		45.5926525534
1110AcetylationHVCDPNVKFGCKDSA
CCCCCCCCCCCCCCC		42.5522826441
1155N-linked_GlycosylationPPSHPCANNTSVCLP
CCCCCCCCCCCEECC		60.06-
1156N-linked_GlycosylationPSHPCANNTSVCLPP
CCCCCCCCCCEECCH		18.40-
1196N-linked_GlycosylationNNGGCSHNCSVAPGE
CCCCCCCCCCCCCCC		11.94-
1219N-linked_GlycosylationGMELGSDNHTCQIQS
CCCCCCCCCEEHHHH		33.78-
1287UbiquitinationIRRIDLHKGDYSVLV
EEEEECCCCCEEEEC		61.8522790023
1405PhosphorylationRDGILFWTDWDASLP
CCCEEEEECCCCCCC		21.6321454597
1410PhosphorylationFWTDWDASLPRIEAA
EEECCCCCCCHHHHH		36.1121454597
1420PhosphorylationRIEAASMSGAGRRTI
HHHHHHCCCCCCCEE		24.0121454597
1512N-linked_GlycosylationANKWTGHNVTVVQRT
HCCCCCCCEEEEEEC		32.28-
1514PhosphorylationKWTGHNVTVVQRTNT
CCCCCCEEEEEECCC		21.92-
1541GlutathionylationQPMAPNPCEANGGRG
CCCCCCCCCCCCCCC		11.0924333276
1559N-linked_GlycosylationHLCLINYNRTVSCAC
CEEEEECCCEEECCC		28.76-
1566GlutathionylationNRTVSCACPHLMKLH
CCEEECCCHHHHHHC		2.2724333276
1576N-linked_GlycosylationLMKLHKDNTTCYEFK
HHHHCCCCCCHHHHH		41.93-
1617N-linked_GlycosylationFTVPDIDNVTVLDYD
EECCCCCCCEEECCC		31.52-
1646N-linked_GlycosylationAIKRAFINGTGVETV
HHHHHHHCCCCCEEE		35.20-
1724N-linked_GlycosylationLYWTDGDNISMANMD
EEEECCCCEEEEECC		33.49-
1734N-linked_GlycosylationMANMDGSNHTLLFSG
EEECCCCCCEEEECC		37.38-
1764N-linked_GlycosylationLYWISSGNHTINRCN
EEEEECCCCEEEEEC		30.95-
1826N-linked_GlycosylationSGSVVLRNSTTLVMH
CCCEEEECCCEEEEE		39.28-
1887S-palmitoylationLRSGQQACEGVGSFL
HCCCCHHHCCCCHHH		3.9826165157
1934N-linked_GlycosylationGIDFHAENDTIYWVD
EEEEECCCCEEEEEE		53.13-
1996N-linked_GlycosylationVIEVARLNGSFRYVV
EEEEEECCCCEEEEE		38.21-
2001PhosphorylationRLNGSFRYVVISQGL
ECCCCEEEEEEECCC		9.3220531401
2005PhosphorylationSFRYVVISQGLDKPR
CEEEEEEECCCCCCE		13.4420531401
2010AcetylationVISQGLDKPRAITVH
EEECCCCCCEEEEEC		41.2523806337
2049N-linked_GlycosylationTERVVLVNVSISWPN
CCEEEEEEEEEECCC		20.05-
2118N-linked_GlycosylationWSDRTHANGSIKRGC
CCCCCCCCCCCCCCC		36.82-
2128N-linked_GlycosylationIKRGCKDNATDSVPL
CCCCCCCCCCCCCCC		30.1819656770
2391UbiquitinationAIDHRAEKLYFSDAT
EECCCCCCCCCCCCC		47.72-
2473N-linked_GlycosylationMGIIAVANDTNSCEL
CEEEEEECCCCCCCC		50.47-
2503N-linked_GlycosylationLTHQGHVNCSCRGGR
EECCCCEEEEECCCE		13.30-
2518S-palmitoylationILQEDFTCRAVNSSC
ECCCCCEEEECCCCC		2.3828526873
2522N-linked_GlycosylationDFTCRAVNSSCRAQD
CCEEEECCCCCCCCC		27.50-
2560PhosphorylationDKSDEKPSYCNSRRC
CCCCCCCCCCCCHHH		54.08-
2561PhosphorylationKSDEKPSYCNSRRCK
CCCCCCCCCCCHHHH		12.27-
2564PhosphorylationEKPSYCNSRRCKKTF
CCCCCCCCHHHHHHH		19.96-
2602N-linked_GlycosylationGSDEIPCNKTACGVG
CCCCCCCCCCCCCCC		39.08-
2606S-palmitoylationIPCNKTACGVGEFRC
CCCCCCCCCCCEEEE		5.7028526873
2621N-linked_GlycosylationRDGSCIGNSSRCNQF
CCCCCCCCCCCCCCC		19.53-
2639N-linked_GlycosylationEDASDEMNCSATDCS
CCCCCCCCCCCCCCH		17.97-
2661GlutathionylationKGVLFQPCERTSLCY
CEEEEEECCCCCCEE		3.7224333276
2661S-palmitoylationKGVLFQPCERTSLCY
CEEEEEECCCCCCEE		3.7228526873
2757PhosphorylationKQWLCDGSDDCGDGS
CEEEECCCCCCCCCC		19.6126525534
2764PhosphorylationSDDCGDGSDEAAHCE
CCCCCCCCCCCCCCC		36.7026525534
2816N-linked_GlycosylationVTAGCLYNSTCDDRE
CCCCHHCCCCCCCCH		20.21-
2889PhosphorylationENDCHDHSDEAPKNP
CCCCCCCCCCCCCCC		43.1128285833
2906N-linked_GlycosylationTSPEHKCNASSQFLC
CCCCCCCCCCCCEEC		47.89-
2935PhosphorylationQDDCGDGSDERGCHV
CCCCCCCCCCCCCCH		40.8322324799
2951PhosphorylationECLSRKLSGCSQDCE
HHHHHHCCCCCCCHH		40.5730635358
3022GlutathionylationRGGDPHSCKAVTDEE
CCCCCCCCCCCCCCC		2.7424333276
3022S-palmitoylationRGGDPHSCKAVTDEE
CCCCCCCCCCCCCCC		2.7426165157
3049N-linked_GlycosylationKLNLDGSNYTLLKQG
ECCCCCCHHHHHHHH		39.0619656770
3090N-linked_GlycosylationMIRRMHLNGSNVQVL
EEEEEEECCCCCEEE		36.85-
3262PhosphorylationINRAHKTTGANKTLL
CCCHHCCCCCCCEEE		38.8228059163
3265N-linked_GlycosylationAHKTTGANKTLLIST
HHCCCCCCCEEEEEE		38.91-
3334N-linked_GlycosylationDGRTCVSNCTASQFV
CCCCCCCCCCHHHEE		13.53-
3364PhosphorylationEDDCGDHSDEPPDCP
CCCCCCCCCCCCCCC		48.7026525534
3489N-linked_GlycosylationDGSDEPANCTQMTCG
CCCCCCCCCCCCEEC		39.83-
3505PhosphorylationDEFRCKDSGRCIPAR
EEEEECCCCCEECCE		17.4028059163
3566PhosphorylationDNDCGDNSDEESCTP
CCCCCCCCCCCCCCC		51.6526525534
3577PhosphorylationSCTPRPCSESEFSCA
CCCCCCCCCCCEEEC		47.0026525534
3605PhosphorylationDHDCADGSDEKDCTP
CCCCCCCCCCCCCCC		43.0523140645
3626S-palmitoylationFQCKSGHCIPLRWRC
CCCCCCCEEECEEEE		3.8026165157
3643PhosphorylationDADCMDGSDEEACGT
CCCCCCCCCHHHCCC		37.2726525534
3663N-linked_GlycosylationPLDEFQCNNTLCKPL
CCCCCCCCCCCCCCC		33.46-
3684PhosphorylationEDDCGDNSDENPEEC
CCCCCCCCCCCHHHH		51.5526525534
3727PhosphorylationVDNCGDGTDEEDCEP
CCCCCCCCCHHHCCC		45.0026525534
3772PhosphorylationFDDCGDGSDEEDCSI
CCCCCCCCCHHHCCC		46.7326525534
3778PhosphorylationGSDEEDCSIDPKLTS
CCCHHHCCCCHHHHC		42.2026525534
3789N-linked_GlycosylationKLTSCATNASMCGDE
HHHCCCCCHHHCCCH		16.11-
3840N-linked_GlycosylationGTCSQLCNNTKGGHL
CCHHHHCCCCCCCCH		68.73-
3954N-linked_GlycosylationDRGVTHLNISGLKMP
CCCCCEEECCCCCCC		20.83-
4076N-linked_GlycosylationVIGSIRLNGTDPIVA
EEEEEECCCCCCEEE		41.28-
4078PhosphorylationGSIRLNGTDPIVAAD
EEEECCCCCCEEEEC		37.2123649490
4126N-linked_GlycosylationFGHSPLINLTGGLSH
CCCCCCEECCCCCCH		38.95-
4152GlutathionylationQPEVTNPCDRKKCEW
CCCCCCCCCHHHCEE		9.5524333276
4180N-linked_GlycosylationPNGKRLDNGTCVPVP
CCCCCCCCCCEEECC		52.87-
4256PhosphorylationASPSGMPTCRCPTGF
CCCCCCCCCCCCCCC		12.04-
4268GlutathionylationTGFTGPKCTAQVCAG
CCCCCCCEEEEEECC		4.2524333276
4279N-linked_GlycosylationVCAGYCSNNSTCTVN
EECCEECCCCEEEEC		42.80-
4280N-linked_GlycosylationCAGYCSNNSTCTVNQ
ECCEECCCCEEEECC		23.54-
4295GlutathionylationGNQPQCRCLPGFLGD
CCCCEEEECCCCCCC		7.6624333276
4334PhosphorylationRQCRCTVYFEGPRCE
CEEEEEEEEECCCEE		4.2728059163
4365N-linked_GlycosylationQTGDVTCNCTDGRVA
CCCCEEEECCCCCCC		23.51-
4400GlutathionylationKMMPECQCPPHMTGP
CCCCCCCCCCCCCCC		9.5224333276
4453UbiquitinationKRRVRGAKGFQHQRM
HHHHCCCCCCCCCCC		64.18-
4461PhosphorylationGFQHQRMTNGAMNVE
CCCCCCCCCCCEEEE		32.4627180971
4474PhosphorylationVEIGNPTYKMYEGGE
EEECCCCEEEECCCC		8.6022817900
4501PhosphorylationALDPDKPTNFTNPVY
CCCCCCCCCCCCCCE		49.0223984901
4504PhosphorylationPDKPTNFTNPVYATL
CCCCCCCCCCCEEEE		40.4523984901
4508PhosphorylationTNFTNPVYATLYMGG
CCCCCCCEEEEECCC		8.6422817900
4510PhosphorylationFTNPVYATLYMGGHG
CCCCCEEEEECCCCC		10.7523984901
4512PhosphorylationNPVYATLYMGGHGSR
CCCEEEEECCCCCCC		6.8623984901
4518PhosphorylationLYMGGHGSRHSLAST
EECCCCCCCCCCCCH		22.5823984901
4521PhosphorylationGGHGSRHSLASTDEK
CCCCCCCCCCCHHHH		25.2325521595
4524PhosphorylationGSRHSLASTDEKREL
CCCCCCCCHHHHHHH		41.5025521595
4525PhosphorylationSRHSLASTDEKRELL
CCCCCCCHHHHHHHC		42.4425521595
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

Oops, there are no upstream regulatory protein records of LRP1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRP1_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 LRP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RANB9_MOUSERanbp9physical
19251705
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LRP1_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-447, AND MASSSPECTROMETRY.
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation.";
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.;
Mol. Cell. Proteomics 8:2555-2569(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-730; ASN-2128 ANDASN-3049, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4521, AND MASSSPECTROMETRY.
"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-4521; SER-4524 ANDTHR-4525, AND MASS SPECTROMETRY.

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