Protein detail
LDLR
Low-density lipoprotein receptor (LDL receptor)
Entry name LDLR | UniProt ID | EVMP confidence score 0.25 |
Supporting publications (n) 3 | Transmembrane count 1 | Protein classification Disease related genesHuman disease related genesMetabolic proteinsPlasma proteinsPredicted intracellular proteinsPredicted membrane proteins |
EVMP confidence score
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40Basic Information13
Protein Names
Low-density lipoprotein receptor (LDL receptor)
Protein Class (6)
Disease related genesHuman disease related genesMetabolic proteinsPlasma proteinsPredicted intracellular proteinsPredicted membrane proteins
Protein Function (6)
- Human disease related genes:Cardiovascular diseases:Vascular diseases
- Human disease related genes:Congenital disorders of metabolism:Mitochondrial diseases
- Predicted intracellular proteins
- Human disease related genes:Congenital disorders of metabolism:Congenital disorders of lipid/glycolipid metabolism
- Human disease related genes:Endocrine and metabolic diseases:Other endocrine and metabolic diseases
- Disease related genes
Transmembrane
789..810; Helical
Transmembrane Count
1
Ensembl
Entrez Gene Symbol
Gene Synonym
LDLCQ2
Gene Description
Low density lipoprotein receptor
Chromosome
19
Position
11089462-11133820
Supporting publications (n)
3
EVMP confidence score
0.25
Fluorescence & Localization6
Tissue SpecifickidneyCell SpecificAdipocytesSingle-Nuclei Brain SpecificCGE interneuronBlood Cell SpecificneutrophilBlood Lineage Specificgranulocytes
Function & Pathway8
Protein Function (6)
- Human disease related genes:Cardiovascular diseases:Vascular diseases
- Human disease related genes:Congenital disorders of metabolism:Mitochondrial diseases
- Predicted intracellular proteins
- Human disease related genes:Congenital disorders of metabolism:Congenital disorders of lipid/glycolipid metabolism
- Human disease related genes:Endocrine and metabolic diseases:Other endocrine and metabolic diseases
- Disease related genes
Cellular Component (19)
- GO:0005764 lysosome
- GO:0005769 early endosome
- GO:0005770 late endosome
- GO:0005794 Golgi apparatus
- GO:0005886 plasma membrane
- GO:0005905 clathrin-coated pit
- GO:0009897 external side of plasma membrane
- GO:0009986 cell surface
- GO:0010008 endosome membrane
- GO:0016020 membrane
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Molecular Function (12)
- GO:0001540 amyloid-beta binding
- GO:0001618 virus receptor activity
- GO:0002020 protease binding
- GO:0005041 low-density lipoprotein particle receptor activity
- GO:0005509 calcium ion binding
- GO:0005515 protein binding
- GO:0030169 low-density lipoprotein particle binding
- GO:0030229 very-low-density lipoprotein particle receptor activity
- GO:0032050 clathrin heavy chain binding
- GO:0042802 identical protein binding
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Biological Process (3)
KEGG (11)
- hsa03272 Virion - Hepatitis viruses
- KEGG:hsa04144 Endocytosis
- KEGG:hsa04913 Ovarian steroidogenesis
- KEGG:hsa04925 Aldosterone synthesis and secretion
- KEGG:hsa04927 Cortisol synthesis and secretion
- KEGG:hsa04934 Cushing syndrome
- KEGG:hsa04976 Bile secretion
- KEGG:hsa04979 Cholesterol metabolism
- KEGG:hsa05145 Toxoplasmosis
- KEGG:hsa05160 Hepatitis C
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Reactome (13)
- R-hsa-8856825 cargo recognition for clathrin mediated endocytosis
- R-hsa-8964026 chylomicron clearance
- R-hsa-8856828 clathrin mediated endocytosis
- R-hsa-8964038 ldl clearance
- R-hsa-199991 membrane trafficking
- R-hsa-6806667 metabolism of fat soluble vitamins
- R-hsa-196854 metabolism of vitamins and cofactors
- R-hsa-174824 plasma lipoprotein assembly remodeling and clearance
- R-hsa-8964043 plasma lipoprotein clearance
- R-hsa-9709957 sensory perception
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Canonical Pathways
M72 Pid nectin pathway
Mediation Categories (4)
Adhesion and uptake mediationFusion and delivery mediationImmune mediationMetabolism mediation
Relations & Evidence70
Ligand-Receptor Signaling (50)
50 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| receptor | receptor | iTALK | No | Yes | No | Yes | No |
| receptor | receptor | Almen2009 | No | Yes | No | Yes | No |
| receptor | receptor | CellCellInteractions | No | Yes | No | Yes | No |
| receptor | receptor | EMBRACE | No | Yes | No | Yes | No |
| low_density_lipoprotein | receptor | HGNC | No | Yes | No | Yes | No |
| receptor | receptor | HGNC | No | Yes | No | Yes | No |
| transmembrane | transmembrane_predicted | Phobius | No | No | No | Yes | No |
| transmembrane_phobius | transmembrane_predicted | Almen2009 | No | No | No | Yes | No |
| transmembrane_sosui | transmembrane_predicted | Almen2009 | No | No | No | Yes | No |
| transmembrane_tmhmm | transmembrane_predicted | Almen2009 | No | No | No | Yes | No |
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Regulatory Interaction Network (2)
2 records.
| Source Protein Symbol | Source UniProt ID | Target Protein Symbol | Target UniProt ID | Is Directed | Is Stimulation | Is Inhibition | Database | References |
|---|---|---|---|---|---|---|---|---|
| APOB | P04114 | LDLR | P01130 | Yes | Yes | No | iTALKKEGG-MEDICUSICELLNETSIGNORLit-BM-17HPMR_talklrHPRD_LRdbtalklrHPRDRamilowski2015_Baccin2019WangRamilowski2015HPMR_LRdbReactome_LRdbHPRD_talklrBaccin2019CellinkerSTRING_talklrEMBRACEFantom5_LRdbCellTalkDBHPMR_CellinkerconnectomeDB2020LRdb | SIGNOR:11986215HPRD:12031600Cellinker:12031600LRdb:12Cellinker:15840700CellTalkDB:11327878Lit-BM-17:24447298LRdb:11327878connectomeDB2020:12031600connectomeDB2020:11327878Baccin2019:1132787812031600Cellinker:11327878ICELLNET:24447298 |
| MYLIP | Q8WY64 | LDLR | P01130 | Yes | No | Yes | HINTSIGNORBioGRID | HINT:32727844HINT:21734303BioGRID:23382078BioGRID:26666640SIGNOR:30896554HINT:21685362 |
Protein Complex Composition (17)
17 records.
| Component Name | Component Gene Symbols | Component UniProt ID | Stoichiometry | Database | Database IDs | References |
|---|---|---|---|---|---|---|
| AP-1 adaptor complex | AFTPHAP1G2AP1S1LDLRAP1SLC18A3SYNRG | O75843P61966Q16572Q5SW96Q6ULP2Q9UMZ2 | 1:1:1:1:1:1 | Compleat | Compleat:HC1510 | 1245117297337681575802510477754 |
| HT_DM_Cluster170 | FAM43AFAM43BLDLRAP1PSMD9PTGES3STATH | O00233P02808Q15185Q5SW96Q6ZT52Q8N2R8 | 1:1:1:1:1:1 | Compleat | Compleat:HC844 | 22036573 |
| LDLR-PCSK9 complex | LDLRPCSK9 | P01130Q8NBP7 | 1:2 | ComplexPortalPDB | PDB:3m0cPDB:2w2nPDB:2w2oPDB:2w2qPDB:3p5bPDB:3gcxPDB:2w2mPDB:3bpsPDB:3p5cintact:EBI-10796271PDB:3gcwPDB:2w2pPDB:4ne9 | 2208114124440079147552921745231618250299 |
| SYT1SYT2SYT5VLDLR | O00445P21579P98155Q8N9I0 | 0:0:0:0 | hu.MAP2 | |||
| LDLRAD4LEMD3SMAD2SMAD3SMAD9ZFYVE9 | O15165O15198O95405P84022Q15796Q9Y2U8 | 0:0:0:0:0:0 | hu.MAP2 | |||
| FLCNLDLRAD4SMURF2WWC2 | O15165Q6AWC2Q8NFG4Q9HAU4 | 0:0:0:0 | hu.MAP | |||
| FLCNHECW1LDLRAD4SMURF2 | O15165Q76N89Q8NFG4Q9HAU4 | 0:0:0:0 | hu.MAP | |||
| FLCNLDLRAD4RBCK1SMURF2 | O15165Q8NFG4Q9BYM8Q9HAU4 | 0:0:0:0 | hu.MAP | |||
| LDLR | P01130 | 2 | PDB | PDB:1ijq | ||
| APOHLDLR | P01130P02749 | 1:1 | PDB | PDB:2kri |
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Isolation & Detection Technology (1)
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Size Exclusion Chromatography | Mass spectrometry | 1 | 31414377 |
Sequence, Structure & Domains17
Sequences
Length
860
Mass
95,376
Sequence
MGPWGWKLRWTVALLLAAAGTAVGDRCERNEFQCQDGKCISYKWVCDGSAECQDGSDESQETCLSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCPPKTCSQDEFRCHDGKCISRQFVCDSDRDCLDGSDEASCPVLTCGPASFQCNSSTCIPQLWACDNDPDCEDGSDEWPQRCRGLYVFQGDSSPCSAFEFHCLSGECIHSSWRCDGGPDCKDKSDEENCAVATCRPDEFQCSDGNCIHGSRQCDREYDCKDMSDEVGCVNVTLCEGPNKFKCHSGECITLDKVCNMARDCRDWSDEPIKECGTNECLDNNGGCSHVCNDLKIGYECLCPDGFQLVAQRRCEDIDECQDPDTCSQLCVNLEGGYKCQCEEGFQLDPHTKACKAVGSIAYLFFTNRHEVRKMTLDRSEYTSLIPNLRNVVALDTEVASNRIYWSDLSQRMICSTQLDRAHGVSSYDTVISRDIQAPDGLAVDWIHSNIYWTDSVLGTVSVADTKGVKRKTLFRENGSKPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIYSLVTENIQWPNGITLDLLSGRLYWVDSKLHSISSIDVNGGNRKTILEDEKRLAHPFSLAVFEDKVFWTDIINEAIFSANRLTGSDVNLLAENLLSPEDMVLFHNLTQPRGVNWCERTTLSNGGCQYLCLPAPQINPHSPKFTCACPDGMLLARDMRSCLTEAEAAVATQETSTVRLKVSSTAVRTQHTTTRPVPDTSRLPGATPGLTTVEIVTMSHQALGDVAGRGNEKKPSSVRALSIVLPIVLLVFLCLGVFLLWKNWRLKNINSINFDNPVYQKTTEDEVHICHNQDGYSYPSRQMVSLEDDVA
Alternative Products
Event=Alternative splicing; Named isoforms=6; Name=1; IsoId=P01130-1; Sequence=Displayed; Name=2; IsoId=P01130-2; Sequence=VSP_043053, VSP_043054; Name=3; IsoId=P01130-3; Sequence=VSP_055014, VSP_055015; Name=4; IsoId=P01130-4; Sequence=VSP_043595; Name=5; IsoId=P01130-5; Sequence=VSP_045525; Name=6; IsoId=P01130-6; Sequence=VSP_047413
Alternative Sequence
35..155; Missing (in isoform 6); 64..105; LSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCP -> S (in isoform 4); 105..272; Missing (in isoform 3); 106..232; Missing (in isoform 2); 273; V -> L (in isoform 3); 663..713; Missing (in isoform 2); 850..851; Missing (in isoform 5)
3D Structural Models
Turn
42..46; 60..62; 138..142; 156..158; 189..191; 205..207; 244..246; 293..296; 310..312; 348..350; 387..389; 436..439; 446..449; 483..486; 493..496; 526..529; 570..573; 580..583; 602..605; 623..626; 633..635; 826..829
Helix
56..58; 85..87; 99..101; 124..126; 143..147; 163..165; 177..179; 181..183; 212..214; 226..228; 251..253; 265..267; 317..319; 321..324; 357..359; 657..659; 673..676
Beta Strand
29..33; 35..37; 39..41; 47..49; 51..55; 65..67; 70..72; 77..79; 90..93; 95..97; 102..104; 113..115; 121..123; 129..131; 148..151; 152..154; 160..162; 168..170; 173..176; 201..204; 208..211; 217..219; 222..224; 241..243; 247..249; 254..258; 260..264; 268..270; 281..283; 289..292; 306..308; 326..330; 333..335; 337..339; 341..343; 345..347; 351..353; 363..369; 372..374; 376..378; 381..385; 392..394; 400..404; 406..413; 420..423; 427..435; 440..445; 450..455; 466..469; 478..482; 487..492; 497..502; 505..513; 519..525; 530..535; 537..539; 541..546; 552..556; 563..569; 574..579; 584..589; 596..600; 606..614; 617..622; 627..632; 640..643; 652..656; 668..672; 678..683; 693..697; 708..713; 821..824
3D Structure
Electron microscopy (4); NMR spectroscopy (13); X-ray crystallography (19)
Domain & Motif Annotations
Compositional Bias
734..744; Polar residues
Repeat
397..438; LDL-receptor class B 1; 439..485; LDL-receptor class B 2; 486..528; LDL-receptor class B 3; 529..572; LDL-receptor class B 4; 573..615; LDL-receptor class B 5; 616..658; LDL-receptor class B 6
Motif
823..828; NPXY motif
Domain (CC)
The NPXY motif mediates the interaction with the clathrin adapter DAB2 and with LDLRAP1 which are involved in receptor internalization. A few residues outside the motif also play a role in the interaction.
Domain (FT)
25..65; LDL-receptor class A 1; 66..106; LDL-receptor class A 2; 107..145; LDL-receptor class A 3; 146..186; LDL-receptor class A 4; 195..233; LDL-receptor class A 5; 234..272; LDL-receptor class A 6; 274..313; LDL-receptor class A 7; 314..353; EGF-like 1; 354..393; EGF-like 2; calcium-binding; 663..712; EGF-like 3
Region
146..233; Binding to Getah virus E1-E2 spike glycoproteins; 721..768; Clustered O-linked oligosaccharides; 734..755; Disordered; 811..860; Required for MYLIP-triggered down-regulation of LDLR
Protein Families
LDLR family
Sequence Similarities
Belongs to the LDLR family.
Clinical Relevance6
Disease Involvement
Disease variant
Drugs (31)
EPOETIN ALFATETRACYCLINEPRAVASTATIN SODIUMHEPARIN CALCIUMACTHBUTYRIC ACIDANTIBIOTICACETYLCYSTEINECOLESTIPOL HYDROCHLORIDECHEMBL:CHEMBL233611ROSUVASTATINLOMITAPIDE MESYLATEINCLISIRANATENOLOLGLUCAGON (RDNA)ANTIVIRAL AGENTPHYTOESTROGENLOVASTATINHMG-COA REDUCTASE INHIBITORALIROCUMABRECOMBINANT TRANSFORMING GROWTH FACTORSOY PROTEIN ISOLATECHOLESTYRAMINE RESINFAT EMULSIONEVINACUMABVERAPAMILHALOPERIDOL DECANOATEVITAMIN ATRIBUTYRINGEMFIBROZILMIPOMERSEN
Interaction Protein
ENSG00000163956
Interaction Count
1
Interaction Dataset
intact_biogrid
Supporting Publications3
| PMID | Title | Abstract |
|---|---|---|
| 25471207 | Intraluminal proteome and peptidome of human urinary extracellular vesicles. | No abstract available |
| 38731868 | The Deep Proteomics Approach Identified Extracellular Vesicular Proteins Correlated to Extracellular Matrix in Type One and Two Endometrial Cancer. | No abstract available |
| 40098346 | Toward Identification of Markers for Brain-Derived Extracellular Vesicles in Cerebrospinal Fluid: A Large-Scale, Unbiased Analysis Using Proximity Extension Assays. | No abstract available |