LRP8_HUMAN - dbPTM
LRP8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRP8_HUMAN
UniProt AC Q14114
Protein Name Low-density lipoprotein receptor-related protein 8
Gene Name LRP8
Organism Homo sapiens (Human).
Sequence Length 963
Subcellular Localization Cell membrane
Single-pass type I membrane protein. Secreted. Isoforms that contain the exon coding for a furin-type cleavage site are proteolytically processed, leading to a secreted receptor fragment..
Protein Description Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation. May also function as an endocytic receptor. Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 (By similarity)..
Protein Sequence MGLPEPGPLRLLALLLLLLLLLLLQLQHLAAAAADPLLGGQGPAKDCEKDQFQCRNERCIPSVWRCDEDDDCLDHSDEDDCPKKTCADSDFTCDNGHCIHERWKCDGEEECPDGSDESEATCTKQVCPAEKLSCGPTSHKCVPASWRCDGEKDCEGGADEAGCATLCAPHEFQCGNRSCLAAVFVCDGDDDCGDGSDERGCADPACGPREFRCGGDGGGACIPERWVCDRQFDCEDRSDEAAELCGRPGPGATSAPAACATASQFACRSGECVHLGWRCDGDRDCKDKSDEADCPLGTCRGDEFQCGDGTCVLAIKHCNQEQDCPDGSDEAGCLQGLNECLHNNGGCSHICTDLKIGFECTCPAGFQLLDQKTCGDIDECKDPDACSQICVNYKGYFKCECYPGYEMDLLTKNCKAAAGKSPSLIFTNRHEVRRIDLVKRNYSRLIPMLKNVVALDVEVATNRIYWCDLSYRKIYSAYMDKASDPKEQEVLIDEQLHSPEGLAVDWVHKHIYWTDSGNKTISVATVDGGRRRTLFSRNLSEPRAIAVDPLRGFMYWSDWGDQAKIEKSGLNGVDRQTLVSDNIEWPNGITLDLLSQRLYWVDSKLHQLSSIDFSGGNRKTLISSTDFLSHPFGIAVFEDKVFWTDLENEAIFSANRLNGLEISILAENLNNPHDIVIFHELKQPRAPDACELSVQPNGGCEYLCLPAPQISSHSPKYTCACPDTMWLGPDMKRCYRAPQSTSTTTLASTMTRTVPATTRAPGTTVHRSTYQNHSTETPSLTAAVPSSVSVPRAPSISPSTLSPATSNHSQHYANEDSKMGSTVTAAVIGIIVPIVVIALLCMSGYLIWRNWKRKNTKSMNFDNPVYRKTTEEEDEDELHIGRTAQIGHVYPAAISSFDRPLWAEPCLGETREPEDPAPALKELFVLPGEPRSQLHQLPKNPLSELPVVKSKRVALSLEDDGLP
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
83 (in isoform 2)Ubiquitination-68.02-
85O-linked_GlycosylationEDDCPKKTCADSDFT
CCCCCCCCCCCCCCC		21.0355826491
118PhosphorylationCPDGSDESEATCTKQ
CCCCCCCCCCCCCCC		37.21-
123PhosphorylationDESEATCTKQVCPAE
CCCCCCCCCCCCCHH		21.84-
176N-linked_GlycosylationPHEFQCGNRSCLAAV
CCEECCCCCCEEEEE		40.08UniProtKB CARBOHYD
238PhosphorylationQFDCEDRSDEAAELC
EECCCCCCHHHHHHH		52.72-
253O-linked_GlycosylationGRPGPGATSAPAACA
CCCCCCCCCHHHHHH		31.19OGP
261O-linked_GlycosylationSAPAACATASQFACR
CHHHHHHHHHHHHCC		27.07OGP
441N-linked_GlycosylationRIDLVKRNYSRLIPM
HHHHHHHCHHHHHHH		33.15UniProtKB CARBOHYD
475PhosphorylationDLSYRKIYSAYMDKA
ECCHHHHHHHHHHCC		7.1229083192
476PhosphorylationLSYRKIYSAYMDKAS
CCHHHHHHHHHHCCC		19.1829083192
478PhosphorylationYRKIYSAYMDKASDP
HHHHHHHHHHCCCCH		10.4129083192
483PhosphorylationSAYMDKASDPKEQEV
HHHHHCCCCHHHCEE		61.2529083192
518N-linked_GlycosylationIYWTDSGNKTISVAT
EEEECCCCCEEEEEE		42.10UniProtKB CARBOHYD
520PhosphorylationWTDSGNKTISVATVD
EECCCCCEEEEEEEE		23.6023403867
522PhosphorylationDSGNKTISVATVDGG
CCCCCEEEEEEEECC		15.7823403867
525PhosphorylationNKTISVATVDGGRRR
CCEEEEEEEECCCEE		19.5823532336
538N-linked_GlycosylationRRTLFSRNLSEPRAI
EEECCCCCCCCCCEE		46.88UniProtKB CARBOHYD
5672-HydroxyisobutyrylationGDQAKIEKSGLNGVD
CCHHHHHHCCCCCCC		53.98-
595PhosphorylationGITLDLLSQRLYWVD
CEEHHHHHHHHHHHC		22.1324719451
664 (in isoform 2)Ubiquitination-5.3321906983
686 (in isoform 2)Phosphorylation-17.01-
698 (in isoform 4)Ubiquitination-49.1421906983
768PhosphorylationPGTTVHRSTYQNHST
CCCEEECCCCCCCCC		19.3124043423
769PhosphorylationGTTVHRSTYQNHSTE
CCEEECCCCCCCCCC		29.1424043423
770PhosphorylationTTVHRSTYQNHSTET
CEEECCCCCCCCCCC		14.4724043423
772N-linked_GlycosylationVHRSTYQNHSTETPS
EECCCCCCCCCCCCC		22.21UniProtKB CARBOHYD
774PhosphorylationRSTYQNHSTETPSLT
CCCCCCCCCCCCCCE		35.1724043423
775PhosphorylationSTYQNHSTETPSLTA
CCCCCCCCCCCCCEE		36.0124043423
777PhosphorylationYQNHSTETPSLTAAV
CCCCCCCCCCCEEEC		20.4724043423
779PhosphorylationNHSTETPSLTAAVPS
CCCCCCCCCEEECCC		45.8524043423
781PhosphorylationSTETPSLTAAVPSSV
CCCCCCCEEECCCCC		19.5324043423
781O-linked_GlycosylationSTETPSLTAAVPSSV
CCCCCCCEEECCCCC		19.53OGP
786PhosphorylationSLTAAVPSSVSVPRA
CCEEECCCCCCCCCC		36.4524043423
786O-linked_GlycosylationSLTAAVPSSVSVPRA
CCEEECCCCCCCCCC		36.45OGP
787PhosphorylationLTAAVPSSVSVPRAP
CEEECCCCCCCCCCC		16.6124043423
789PhosphorylationAAVPSSVSVPRAPSI
EECCCCCCCCCCCCC		28.4924043423
807N-linked_GlycosylationTLSPATSNHSQHYAN
CCCCCCCCCCHHCCC		34.18UniProtKB CARBOHYD
866PhosphorylationMNFDNPVYRKTTEEE
CCCCCCCCCCCCCCC		13.9821945579
868 (in isoform 3)Ubiquitination-41.9521906983
868 (in isoform 1)Ubiquitination-41.9521906983
868UbiquitinationFDNPVYRKTTEEEDE
CCCCCCCCCCCCCCC		41.952190698
869PhosphorylationDNPVYRKTTEEEDED
CCCCCCCCCCCCCCC		30.3723186163
870PhosphorylationNPVYRKTTEEEDEDE
CCCCCCCCCCCCCCC		44.4226471730
890 (in isoform 3)Phosphorylation-4.9727642862
921UbiquitinationEDPAPALKELFVLPG
CCCCHHHHHHCCCCC		55.25-
956PhosphorylationKSKRVALSLEDDGLP
CCCEEEEEECCCCCC		21.7029514088
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
76SPhosphorylationKinasePKA-FAMILY-GPS
-KUbiquitinationE3 ubiquitin ligaseMYLIPQ8WY64
PMID:20427281
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRP8_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 LRP8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GIPC1_HUMANGIPC1physical
10827173
JIP1_HUMANMAPK8IP1physical
10827173
DLG4_HUMANDLG4physical
10827173
JIP2_HUMANMAPK8IP2physical
10827173
SYJ2B_HUMANSYNJ2BPphysical
10827173
CAPON_HUMANNOS1APphysical
10827173
SCN3A_HUMANSCN3Aphysical
10827173
APBA2_HUMANAPBA2physical
10827173
DAB1_HUMANDAB1physical
10827173
ITBP1_HUMANITGB1BP1physical
10827173
APC10_HUMANANAPC10physical
10827173
SNX17_HUMANSNX17physical
12169628
RELN_HUMANRELNphysical
10571240
APOE_HUMANAPOEphysical
8626535
ALBU_HUMANALBphysical
26496610
PRCC_HUMANPRCCphysical
26496610
RAD51_HUMANRAD51physical
26496610
TYK2_HUMANTYK2physical
26496610
UBP11_HUMANUSP11physical
26496610
NEB1_HUMANPPP1R9Aphysical
26496610
DOCK6_HUMANDOCK6physical
26496610
CAMP3_HUMANCAMSAP3physical
26496610
CRTC3_HUMANCRTC3physical
26496610
PKRI1_HUMANPRKRIP1physical
26496610
RHG39_HUMANARHGAP39physical
26496610
GHDC_HUMANGHDCphysical
26496610
ANGE2_HUMANANGEL2physical
26496610
CS047_HUMANC19orf47physical
26496610
AMRP_HUMANLRPAP1physical
10231386
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608446Myocardial infarction 1 (MCI1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LRP8_HUMAN

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Related Literatures of Post-Translational Modification

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