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P01130 (LDLR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 188. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Low-density lipoprotein receptor

Short name=LDL receptor
Gene names
Name:LDLR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length860 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. In case of HIV-1 infection, functions as a receptor for extracellular Tat in neurons, mediating its internalization in uninfected cells.

Subunit structure

Interacts with LDLRAP1, ARRB1, SNX17. Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Interacts with the full length immature form of PCSK9 (via C-terminus). Interacts with HCV E1/E2 heterodimer. Interacts with HIV-1 Tat. Ref.15 Ref.16 Ref.17 Ref.19 Ref.20 Ref.23 Ref.27

Subcellular location

Cell membrane; Single-pass type I membrane protein. Endomembrane system; Single-pass type I membrane protein. Membraneclathrin-coated pit; Single-pass type I membrane protein. Golgi apparatus. Early endosome. Late endosome. Cell surface. Lysosome. Note: Found distributed from the plasma membrane to intracellular compartments. Localizes to the Golgi apparatus, early and late endosomes/lysosomes and cell surface in the presence of PCSK9. Ref.23 Ref.25

Domain

The NPXY motif mediates the interaction with the clathrin adaptor DAB2 involved in receptor internalization By similarity. Ref.14

Post-translational modification

N- and O-glycosylated. Ref.18 Ref.25

Ubiquitinated by MYLIP leading to degradation. Ref.25

Involvement in disease

Familial hypercholesterolemia (FH) [MIM:143890]: Common autosomal semi-dominant disease that affects about 1 in 500 individuals. The receptor defect impairs the catabolism of LDL, and the resultant elevation in plasma LDL-cholesterol promotes deposition of cholesterol in the skin (xanthelasma), tendons (xanthomas), and coronary arteries (atherosclerosis).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.59 Ref.60 Ref.61 Ref.62 Ref.63 Ref.64 Ref.65 Ref.66 Ref.67 Ref.68 Ref.69 Ref.70 Ref.71 Ref.74 Ref.75 Ref.76 Ref.77 Ref.78 Ref.79 Ref.81

Sequence similarities

Belongs to the LDLR family.

Contains 3 EGF-like domains.

Contains 7 LDL-receptor class A domains.

Contains 6 LDL-receptor class B repeats.

Sequence caution

The sequence BAD92646.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processCholesterol metabolism
Endocytosis
Host-virus interaction
Lipid metabolism
Lipid transport
Steroid metabolism
Sterol metabolism
Transport
   Cellular componentCell membrane
Coated pit
Endosome
Golgi apparatus
LDL
Lysosome
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcholesterol homeostasis

Inferred from mutant phenotype Ref.78. Source: BHF-UCL

cholesterol import

Inferred from sequence or structural similarity. Source: BHF-UCL

cholesterol metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

cholesterol transport

Inferred from mutant phenotype Ref.78. Source: HGNC

endocytosis

Traceable author statement PubMed 12671190. Source: ProtInc

intestinal cholesterol absorption

Inferred from mutant phenotype Ref.78. Source: HGNC

lipid metabolic process

Traceable author statement PubMed 10827173PubMed 6299582. Source: ProtInc

lipoprotein catabolic process

Inferred from electronic annotation. Source: Ensembl

lipoprotein metabolic process

Traceable author statement. Source: Reactome

low-density lipoprotein particle clearance

Inferred from mutant phenotype Ref.78. Source: BHF-UCL

phospholipid transport

Inferred from sequence or structural similarity. Source: BHF-UCL

phototransduction, visible light

Traceable author statement. Source: Reactome

positive regulation of triglyceride biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

receptor-mediated endocytosis

Traceable author statement. Source: Reactome

regulation of phosphatidylcholine catabolic process

Inferred from sequence or structural similarity. Source: BHF-UCL

retinoid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.23. Source: UniProtKB

cell surface

Inferred from direct assay Ref.23. Source: UniProtKB

clathrin-coated endocytic vesicle membrane

Traceable author statement. Source: Reactome

coated pit

Inferred from direct assay PubMed 15166224. Source: BHF-UCL

early endosome

Inferred from direct assay Ref.23. Source: UniProtKB

endosome membrane

Traceable author statement. Source: Reactome

external side of plasma membrane

Inferred from direct assay PubMed 15166224. Source: BHF-UCL

integral component of plasma membrane

Traceable author statement PubMed 6327078. Source: ProtInc

late endosome

Inferred from direct assay Ref.23. Source: UniProtKB

low-density lipoprotein particle

Inferred from electronic annotation. Source: UniProtKB-KW

lysosome

Inferred from direct assay Ref.23. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

glycoprotein binding

Inferred from physical interaction PubMed 10571240. Source: BHF-UCL

low-density lipoprotein particle binding

Inferred from electronic annotation. Source: Ensembl

low-density lipoprotein receptor activity

Inferred from direct assay Ref.1PubMed 8626535. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.16Ref.23. Source: UniProtKB

very-low-density lipoprotein particle receptor activity

Inferred from direct assay PubMed 8626535. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P01130-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P01130-2)

The sequence of this isoform differs from the canonical sequence as follows:
     106-232: Missing.
     663-713: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P01130-3)

The sequence of this isoform differs from the canonical sequence as follows:
     105-272: Missing.
     273-273: V → L
Note: No experimental confirmation available.
Isoform 4 (identifier: P01130-4)

The sequence of this isoform differs from the canonical sequence as follows:
     64-105: LSVTCKSGDFSCGGRVNRCIPQFWRCDGQVDCDNGSDEQGCP → S
Note: No experimental confirmation available.
Isoform 5 (identifier: P01130-5)

The sequence of this isoform differs from the canonical sequence as follows:
     850-851: Missing.
Note: No experimental confirmation available.
Isoform 6 (identifier: P01130-6)

The sequence of this isoform differs from the canonical sequence as follows:
     35-155: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 860839Low-density lipoprotein receptor
PRO_0000017312

Regions

Topological domain22 – 788767Extracellular Potential
Transmembrane789 – 81022Helical; Potential
Topological domain811 – 86050Cytoplasmic Potential
Domain25 – 6541LDL-receptor class A 1
Domain66 – 10641LDL-receptor class A 2
Domain107 – 14539LDL-receptor class A 3
Domain146 – 18641LDL-receptor class A 4
Domain195 – 23339LDL-receptor class A 5
Domain234 – 27239LDL-receptor class A 6
Domain274 – 31340LDL-receptor class A 7
Domain314 – 35340EGF-like 1
Domain354 – 39340EGF-like 2; calcium-binding Potential
Repeat397 – 43842LDL-receptor class B 1
Repeat439 – 48547LDL-receptor class B 2
Repeat486 – 52843LDL-receptor class B 3
Repeat529 – 57244LDL-receptor class B 4
Repeat573 – 61543LDL-receptor class B 5
Repeat616 – 65843LDL-receptor class B 6
Domain663 – 71250EGF-like 3
Region721 – 76848Clustered O-linked oligosaccharides
Region811 – 86050Required for MYLIP-triggered down-regulation of LDLR
Motif823 – 8286NPXY motif

Amino acid modifications

Modified residue7241Phosphothreonine By similarity
Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation1561N-linked (GlcNAc...)
Glycosylation2721N-linked (GlcNAc...)
Glycosylation5151N-linked (GlcNAc...) Potential
Glycosylation6571N-linked (GlcNAc...) Ref.18 Ref.21 Ref.24
Disulfide bond27 ↔ 39 Ref.31 Ref.32
Disulfide bond34 ↔ 52 Ref.31 Ref.32
Disulfide bond46 ↔ 63 Ref.31 Ref.32
Disulfide bond68 ↔ 82 Ref.31 Ref.32
Disulfide bond75 ↔ 95 Ref.31 Ref.32
Disulfide bond89 ↔ 104 Ref.31 Ref.32
Disulfide bond109 ↔ 121 By similarity
Disulfide bond116 ↔ 134 Ref.31 Ref.32
Disulfide bond128 ↔ 143 Ref.31 Ref.32
Disulfide bond148 ↔ 160 Ref.31 Ref.32
Disulfide bond155 ↔ 173 Ref.31 Ref.32
Disulfide bond167 ↔ 184 Ref.31 Ref.32
Disulfide bond197 ↔ 209 Ref.31 Ref.32
Disulfide bond204 ↔ 222 Ref.31 Ref.32
Disulfide bond216 ↔ 231 Ref.31 Ref.32
Disulfide bond236 ↔ 248 Ref.31 Ref.32
Disulfide bond243 ↔ 261 Ref.31 Ref.32
Disulfide bond255 ↔ 270 Ref.31 Ref.32
Disulfide bond276 ↔ 289 Ref.31 Ref.32
Disulfide bond284 ↔ 302 Ref.31 Ref.32
Disulfide bond296 ↔ 313 Ref.31 Ref.32
Disulfide bond318 ↔ 329 Ref.31 Ref.32
Disulfide bond325 ↔ 338 Ref.31 Ref.32
Disulfide bond340 ↔ 352 Ref.31 Ref.32
Disulfide bond358 ↔ 368 Ref.31 Ref.32
Disulfide bond364 ↔ 377 Ref.31 Ref.32
Disulfide bond379 ↔ 392 Ref.31 Ref.32
Disulfide bond667 ↔ 681 Ref.31 Ref.32
Disulfide bond677 ↔ 696 Ref.31 Ref.32
Disulfide bond698 ↔ 711 Ref.31 Ref.32

Natural variations

Alternative sequence35 – 155121Missing in isoform 6.
VSP_047413
Alternative sequence64 – 10542LSVTC…EQGCP → S in isoform 4.
VSP_043595
Alternative sequence105 – 272168Missing in isoform 3.
VSP_055014
Alternative sequence106 – 232127Missing in isoform 2.
VSP_043053
Alternative sequence2731V → L in isoform 3.
VSP_055015
Alternative sequence663 – 71351Missing in isoform 2.
VSP_043054
Alternative sequence850 – 8512Missing in isoform 5.
VSP_045525
Natural variant21G → R. Ref.72
Corresponds to variant rs5931 [ dbSNP | Ensembl ].
VAR_011862
Natural variant271C → W in San Francisco.
VAR_005304
Natural variant461C → S in FH; Japanese patient. Ref.77
VAR_013949
Natural variant47 – 482Missing in FH; Cape Town-1; retards receptor transport from the endoplasmic reticulum to the cell surface.
VAR_005305
Natural variant501A → S in FH; German patient. Ref.70
Corresponds to variant rs137853960 [ dbSNP | Ensembl ].
VAR_007979
Natural variant521C → Y in Paris-4.
VAR_005306
Natural variant561S → P in FH. Ref.59
VAR_007980
Natural variant781R → C in FH.
VAR_005307
Natural variant871W → G in FH; French Canadian-4. Ref.39
VAR_005308
Natural variant891C → Y in FH. Ref.78
VAR_005309
Natural variant901D → G in London-4.
VAR_005310
Natural variant901D → N in FH.
VAR_005311
Natural variant901D → Y in FH; Durban-1. Ref.38
VAR_005312
Natural variant921Q → E in FH; Spanish patient.
VAR_005313
Natural variant951C → G in FH; Spanish patient.
VAR_005314
Natural variant1011E → K in FH; Lancashire; 6% of American English. Ref.78
VAR_005315
Natural variant1051P → S.
Corresponds to variant rs13306510 [ dbSNP | Ensembl ].
VAR_059375
Natural variant1091C → R in Munster-1.
VAR_005316
Natural variant1161C → R in FH; Spanish patient.
VAR_005317
Natural variant1341C → F in FH. Ref.74
VAR_062371
Natural variant1341C → W in FH. Ref.74
VAR_062372
Natural variant1391D → H Found in a patient with hypercholesterolemia. Ref.80
VAR_065780
Natural variant1401E → K in FH; Philippines/Durban-2/Japan. Ref.38 Ref.47
VAR_005318
Natural variant1551C → G in Germany.
VAR_005319
Natural variant1601C → Y in FH.
VAR_005320
Natural variant1681D → H in FH; Sephardic/Safed; 10% of the Sephardic Jews. Ref.42
VAR_005321
Natural variant1681D → N in FH.
VAR_005322
Natural variant1681D → Y in FH; Norwegian patient. Ref.53
VAR_005323
Natural variant1721D → H May contribute to familial hypercholesterolemia. Ref.76
VAR_013950
Natural variant1731C → R in Greece-1.
VAR_005324
Natural variant1731C → W in FH; French Canadian patient. Ref.61
VAR_005325
Natural variant1751D → N in FH; Afrikaner-3; 5-10% of Afrikaners. Ref.36
VAR_005326
Natural variant1751D → Y in FH. Ref.59
VAR_007981
Natural variant1771S → L in FH; Puerto Rico. Ref.60
VAR_005327
Natural variant1841C → Y in FH; Glasco. Ref.68
VAR_013951
Natural variant1971C → F in Shreveport.
VAR_005328
Natural variant1971C → R in FH; British patient. Ref.55
VAR_005330
Natural variant1971C → Y in El Salvador-1.
VAR_005329
Natural variant2011E → K Found in a patient with hypercholesterolemia. Ref.80
VAR_065781
Natural variant2181Missing in FH; Piscataway/Lithuania. Ref.41 Ref.60 Ref.78
VAR_005331
Natural variant2211D → G in FH; Padova. Ref.51 Ref.78
VAR_005332
Natural variant2211D → N in FH; German patient. Ref.70 Ref.78
VAR_007982
Natural variant2211D → Y in FH; Cologne patient. Ref.51
VAR_005333
Natural variant2221C → Y in FH. Ref.74
VAR_062373
Natural variant2241D → G in Italy-2.
VAR_005335
Natural variant2241D → N in Portugal.
VAR_005334
Natural variant2241D → V in FH; Cologne patient. Ref.51
VAR_005336
Natural variant2261S → P in Miami-1.
VAR_005337
Natural variant2271D → E in FH; Afrikaner-1/Maine; 65-70% of Afrikaner Americans. Ref.36
VAR_005338
Natural variant2281E → CK in Chieti-3.
VAR_005339
Natural variant2281E → K in FH; French Canadian-3/Mexico; 2% of French Canadians. Ref.39
VAR_005341
Natural variant2281E → Q in Tulsa-2.
VAR_005340
Natural variant2311C → G in FH; Norwegian patient. Ref.54
VAR_005342
Natural variant2401E → K in Charlotte.
VAR_005343
Natural variant2481C → F in Bretagne-1.
VAR_005344
Natural variant2481C → Y in FH; British patient. Ref.55
VAR_005345
Natural variant2531R → W May contribute to familial hypercholesterolemia. Ref.76
VAR_013952
Natural variant2541Q → P in FH. Ref.74 Ref.79
VAR_062374
Natural variant2551C → S Found in a patient with hypercholesterolemia. Ref.80
VAR_065782
Natural variant2561D → G in Nevers.
VAR_005346
Natural variant2611C → F in FH; rare mutation; strongly reduced receptor activity. Ref.69
VAR_013953
Natural variant2661D → E in Cincinnati-1.
VAR_005347
Natural variant2701C → Y in Miami-2.
VAR_005348
Natural variant2761C → R in FH. Ref.74
VAR_062375
Natural variant2761C → Y in FH; Syrian patient. Ref.66
VAR_005349
Natural variant2771E → K in FH; patients from Sweden and La Havana. Ref.49 Ref.52
Corresponds to variant rs148698650 [ dbSNP | Ensembl ].
VAR_005350
Natural variant2861S → R in Greece-2.
VAR_005351
Natural variant2881E → K in FH; German patient. Ref.70
VAR_007983
Natural variant3011D → A in FH; Greek patient. Ref.55
VAR_005352
Natural variant3021C → W in FH; Iraki patient. Ref.55
VAR_005354
Natural variant3021C → Y in FH; Spanish patient.
VAR_005353
Natural variant3041D → E in Baltimore-1.
VAR_005356
Natural variant3041D → N in Denver-2. Ref.80
VAR_005355
Natural variant3061S → L in Amsterdam.
Corresponds to variant rs11547917 [ dbSNP | Ensembl ].
VAR_005357
Natural variant3131C → Y in FH.
VAR_005358
Natural variant3181C → F in FH; Trieste. Ref.43
VAR_005360
Natural variant3181C → R in FH. Ref.74
VAR_062376
Natural variant3181C → Y in Mexico-1; leads to a defect in the intracellular transport of the receptor.
VAR_005359
Natural variant3271H → Y in FH.
VAR_005361
Natural variant3291C → F in FH. Ref.81
VAR_067196
Natural variant3291C → Y in FH; Chinese patient. Ref.63
VAR_005362
Natural variant3351G → S in Paris-6.
VAR_005363
Natural variant3381C → S in FH; Japanese patients. Ref.47 Ref.71
VAR_005364
Natural variant3421D → E in New York-1.
VAR_005365
Natural variant3421D → N in FH.
Corresponds to variant rs139361635 [ dbSNP | Ensembl ].
VAR_005366
Natural variant3431G → S in Picardie.
VAR_005367
Natural variant3501R → P in FH; British patient. Ref.55
VAR_005368
Natural variant3521C → Y in Mexico-2.
VAR_005369
Natural variant3541D → G in Munster-2.
VAR_005370
Natural variant3541D → V in Oklahoma.
VAR_005371
Natural variant3561D → Y in FH. Ref.59 Ref.79
VAR_007984
Natural variant3571E → K in Paris-7.
VAR_005372
Natural variant3581C → Y in FH. Ref.78 Ref.79
VAR_062377
Natural variant3641C → R in Mexico-3.
VAR_005373
Natural variant3661Q → R in FH. Ref.53
VAR_007985
Natural variant3681C → R in FH; French Canadian patient. Ref.61
VAR_005374
Natural variant3701N → T in FH. Ref.74
VAR_062378
Natural variant3791C → R in Naples-1.
VAR_005375
Natural variant3791C → Y in FH. Ref.67
VAR_007986
Natural variant3911A → T.
Corresponds to variant rs11669576 [ dbSNP | Ensembl ].
VAR_024519
Natural variant3991A → D in FH.
VAR_005376
Natural variant4011L → H in Pori. Ref.46
VAR_005377
Natural variant4011L → V in FH. Ref.59
VAR_007987
Natural variant4031F → L in FH; Japanese patient. Ref.71
VAR_008995
Natural variant4061R → Q May contribute to familial hypercholesterolemia. Ref.76
VAR_013954
Natural variant4081E → K May contribute to familial hypercholesterolemia; Algeria-1. Ref.76
VAR_005378
Natural variant4141L → R in FH; Chinese patient. Ref.63
VAR_005379
Natural variant4151D → G in FH. Ref.74
VAR_062379
Natural variant4161R → Q in FH; German patient. Ref.62
VAR_005380
Natural variant4161R → W in FH. Ref.59
VAR_005381
Natural variant4231I → T in FH; Swedish patient. Ref.49
VAR_005382
Natural variant4291V → M in FH; Afrikaner-2; 20-30% of Afrikaners and 2% of FH Dutch. Ref.36 Ref.52 Ref.62 Ref.63
Corresponds to variant rs28942078 [ dbSNP | Ensembl ].
VAR_005383
Natural variant4311A → T in FH; Algeria-2. Ref.71
Corresponds to variant rs28942079 [ dbSNP | Ensembl ].
VAR_005384
Natural variant4321L → V in FH; German patient. Ref.70
VAR_007988
Natural variant4331D → H in FH; Osaka-3. Ref.40
VAR_005385
Natural variant4341T → K in Algeria-3.
VAR_005386
Natural variant4411I → M in Rouen.
VAR_005388
Natural variant4411I → N in Russia-1.
VAR_005387
Natural variant4431W → C in North Platt.
VAR_005389
Natural variant4511I → T in FH. Ref.75 Ref.79
VAR_062380
Natural variant4681V → I. Ref.72
Corresponds to variant rs5932 [ dbSNP | Ensembl ].
VAR_011863
Natural variant4711R → G Found in a patient with hypercholesterolemia. Ref.80
VAR_065783
Natural variant4781G → R in New York-2.
VAR_005390
Natural variant4791L → P in FH. Ref.78
VAR_062381
Natural variant4821D → H in FH. Ref.78
VAR_005391
Natural variant4831W → R in FH.
VAR_005392
Natural variant4851H → R in Milan.
VAR_005394
Natural variant4871Missing in FH; Norwegian patient. Ref.50
VAR_005393
Natural variant5231V → M in Kuwait.
Corresponds to variant rs28942080 [ dbSNP | Ensembl ].
VAR_005395
Natural variant5261P → S in Cincinnati-3.
VAR_005396
Natural variant5461G → D in Saint Omer; retention in the ER. Ref.25
Corresponds to variant rs28942081 [ dbSNP | Ensembl ].
VAR_005397
Natural variant5491G → D in Genoa.
Corresponds to variant rs28941776 [ dbSNP | Ensembl ].
VAR_005398
Natural variant5641N → H in FH; French, German and Danish patients. Ref.48 Ref.57 Ref.70
Corresponds to variant rs28942086 [ dbSNP | Ensembl ].
VAR_005399
Natural variant5641N → S in FH; Sicily. Ref.60
VAR_005400
Natural variant5651G → V in Naples-2.
Corresponds to variant rs28942082 [ dbSNP | Ensembl ].
VAR_005401
Natural variant5681L → V in FH; Japanese patient. Ref.71
VAR_008996
Natural variant5791D → N in FH; Cincinnati-4; less than 2% receptor activity. Ref.49
VAR_005402
Natural variant5791D → Y in FH. Ref.74
VAR_062382
Natural variant5921G → E in FH; Sicily. Ref.60
VAR_005403
Natural variant5991L → S in London-5.
VAR_005404
Natural variant6081P → S in FH. Ref.67
VAR_007989
Natural variant6331R → C in FH.
VAR_005405
Natural variant6491P → L in FH.
VAR_005406
Natural variant6671C → Y in FH; French Canadian-2; 5% of French Canadians. Ref.39
Corresponds to variant rs28942083 [ dbSNP | Ensembl ].
VAR_005407
Natural variant6771C → R in FH; New York-3. Ref.78
VAR_005408
Natural variant6821L → P in Issoire.
VAR_005409
Natural variant6851P → L in FH; Gujerat/Zambia/Belgian/Dutch/Sweden/Japan. Ref.44 Ref.45 Ref.47 Ref.56 Ref.78
Corresponds to variant rs28942084 [ dbSNP | Ensembl ].
VAR_005410
Natural variant6991P → L May contribute to familial hypercholesterolemia. Ref.76
VAR_013955
Natural variant7001D → E in FH; Spanish patient.
VAR_005412
Natural variant7141E → K in FH; Japanese patient. Ref.71
VAR_008997
Natural variant7261T → I in Paris-9.
Corresponds to variant rs45508991 [ dbSNP | Ensembl ].
VAR_005413
Natural variant7921I → F in Russia-2.
VAR_005414
Natural variant7971V → M in FH; La Havana patient. Ref.52
VAR_005415
Natural variant799 – 8013Missing in FH; Danish patient.
VAR_005416
Natural variant8141R → Q Polymorphism that may contribute to FH. Ref.72 Ref.76
Corresponds to variant rs5928 [ dbSNP | Ensembl ].
VAR_011864
Natural variant820 – 8223Missing in FH.
VAR_005417
Natural variant8261P → S in FH. Ref.79
VAR_062383
Natural variant8271V → I in New York-5.
Corresponds to variant rs137853964 [ dbSNP | Ensembl ].
VAR_005418
Natural variant8281Y → C in FH; J.D.Bari/Syria. Ref.37
Corresponds to variant rs28942085 [ dbSNP | Ensembl ].
VAR_005419
Natural variant8441G → D in Turku. Ref.46
VAR_005420

Experimental info

Mutagenesis8111K → R: No change. No change; when associated with R-816 and R-830. Insensitive to MYLIP-triggered degradation; when associated with R-816; R-830 and A-839. Ref.14 Ref.25
Mutagenesis8161K → R: No change. No change; when associated with R-830. No change; when associated with R-811 and R-830. Insensitive to MYLIP-triggered degradation; when associated with R-830 and A-839. Insensitive to MYLIP-triggered degradation; when associated with R-811; R-830 and A-839. Ref.14 Ref.25
Mutagenesis8281Y → A: Abolishes interaction with ARRB2. Ref.14 Ref.17
Mutagenesis8301K → R: No change. No change; when associated with R-816. No change; when associated with R-811 and R-816. Insensitive to MYLIP-triggered degradation; when associated with A-839. Insensitive to MYLIP-triggered degradation; when associated with R-816 and A-839. Insensitive to MYLIP-triggered degradation; when associated with R-811; R-816 and A-839. Ref.14 Ref.25
Mutagenesis8391C → A: No change. Insensitive to MYLIP-triggered degradation; when associated with R-830. Insensitive to MYLIP-triggered degradation; when associated with R-816 and R-830. Insensitive to MYLIP-triggered degradation; when associated with R-811; R-816 and R-830. Ref.14 Ref.25
Mutagenesis8541S → A: No effect on receptor internalization. Ref.14 Ref.17
Mutagenesis8541S → D: Enhances interaction with ARRB2 and receptor internalization. Ref.14 Ref.17
Sequence conflict311E → D in BAG58495. Ref.4

Secondary structure

..................................................................................................................................................................................... 860
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: A4C28E9B8BADAD5E

FASTA86095,376
        10         20         30         40         50         60 
MGPWGWKLRW TVALLLAAAG TAVGDRCERN EFQCQDGKCI SYKWVCDGSA ECQDGSDESQ 

        70         80         90        100        110        120 
ETCLSVTCKS GDFSCGGRVN RCIPQFWRCD GQVDCDNGSD EQGCPPKTCS QDEFRCHDGK 

       130        140        150        160        170        180 
CISRQFVCDS DRDCLDGSDE ASCPVLTCGP ASFQCNSSTC IPQLWACDND PDCEDGSDEW 

       190        200        210        220        230        240 
PQRCRGLYVF QGDSSPCSAF EFHCLSGECI HSSWRCDGGP DCKDKSDEEN CAVATCRPDE 

       250        260        270        280        290        300 
FQCSDGNCIH GSRQCDREYD CKDMSDEVGC VNVTLCEGPN KFKCHSGECI TLDKVCNMAR 

       310        320        330        340        350        360 
DCRDWSDEPI KECGTNECLD NNGGCSHVCN DLKIGYECLC PDGFQLVAQR RCEDIDECQD 

       370        380        390        400        410        420 
PDTCSQLCVN LEGGYKCQCE EGFQLDPHTK ACKAVGSIAY LFFTNRHEVR KMTLDRSEYT 

       430        440        450        460        470        480 
SLIPNLRNVV ALDTEVASNR IYWSDLSQRM ICSTQLDRAH GVSSYDTVIS RDIQAPDGLA 

       490        500        510        520        530        540 
VDWIHSNIYW TDSVLGTVSV ADTKGVKRKT LFRENGSKPR AIVVDPVHGF MYWTDWGTPA 

       550        560        570        580        590        600 
KIKKGGLNGV DIYSLVTENI QWPNGITLDL LSGRLYWVDS KLHSISSIDV NGGNRKTILE 

       610        620        630        640        650        660 
DEKRLAHPFS LAVFEDKVFW TDIINEAIFS ANRLTGSDVN LLAENLLSPE DMVLFHNLTQ 

       670        680        690        700        710        720 
PRGVNWCERT TLSNGGCQYL CLPAPQINPH SPKFTCACPD GMLLARDMRS CLTEAEAAVA 

       730        740        750        760        770        780 
TQETSTVRLK VSSTAVRTQH TTTRPVPDTS RLPGATPGLT TVEIVTMSHQ ALGDVAGRGN 

       790        800        810        820        830        840 
EKKPSSVRAL SIVLPIVLLV FLCLGVFLLW KNWRLKNINS INFDNPVYQK TTEDEVHICH 

       850        860 
NQDGYSYPSR QMVSLEDDVA 

« Hide

Isoform 2 [UniParc].

Checksum: CE2D11319D31F398
Show »

FASTA68275,854
Isoform 3 [UniParc].

Checksum: 77A4DC253845DF78
Show »

FASTA69276,856
Isoform 4 [UniParc].

Checksum: F27BBF8EBEA39BEB
Show »

FASTA81990,940
Isoform 5 [UniParc].

Checksum: 8A50EA1033EB6E92
Show »

FASTA85895,092
Isoform 6 [UniParc].

Checksum: C0BFE8B8C908F9C8
Show »

FASTA73982,255

References

« Hide 'large scale' references
[1]"The human LDL receptor: a cysteine-rich protein with multiple Alu sequences in its mRNA."
Yamamoto T., Davis C.G., Brown M.S., Schneider W.J., Casey M.L., Goldstein J.L., Russell D.W.
Cell 39:27-38(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The LDL receptor gene: a mosaic of exons shared with different proteins."
Suedhof T.C., Goldstein J.L., Brown M.S., Russell D.W.
Science 228:815-822(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]Jia S., Lv L., Sun H., Wang Q., Wang H., Zhan L., Yang Z.
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3; 4 AND 6).
Tissue: Hippocampus, Placenta and Thalamus.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]Rieder M.J., da Ponte S.H., Kuldanek S.A., Rajkumar N., Smith J.D., Toth E.J., Krauss R.M., Nickerson D.A.
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Homo sapiens protein coding cDNA."
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
Tissue: Brain.
[8]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lymph.
[12]"Members of the low density lipoprotein receptor family mediate cell entry of a minor-group common cold virus."
Hofer F., Gruenberger M., Kowalski H., Machat H., Huettinger M., Kuechler E., Blaas D.
Proc. Natl. Acad. Sci. U.S.A. 91:1839-1842(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 186-210; 394-405; 441-449; 472-495; 521-541 AND 605-617.
Tissue: Cervix carcinoma.
[13]"Deletion of clustered O-linked carbohydrates does not impair function of low density lipoprotein receptor in transfected fibroblasts."
Davis C.G., Elhammer A., Russell D.W., Schneider W.J., Kornfeld S., Brown M.S., Goldstein J.L.
J. Biol. Chem. 261:2828-2838(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION OF AN O-GLYCOSYLATED SITES.
[14]"The low density lipoprotein receptor. Identification of amino acids in cytoplasmic domain required for rapid endocytosis."
Davis C.G., van Driel I.R., Russell D.W., Brown M.S., Goldstein J.L.
J. Biol. Chem. 262:4075-4082(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYTOPLASMIC DOMAIN.
[15]"Uptake of HIV-1 tat protein mediated by low-density lipoprotein receptor-related protein disrupts the neuronal metabolic balance of the receptor ligands."
Liu Y., Jones M., Hingtgen C.M., Bu G., Laribee N., Tanzi R.E., Moir R.D., Nath A., He J.J.
Nat. Med. 6:1380-1387(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 TAT.
[16]"ARH is a modular adaptor protein that interacts with the LDL receptor, clathrin, and AP-2."
He G., Gupta S., Yi M., Michaely P., Hobbs H.H., Cohen J.C.
J. Biol. Chem. 277:44044-44049(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LDLRAP1.
[17]"The adaptor protein beta-arrestin2 enhances endocytosis of the low density lipoprotein receptor."
Wu J.-H., Peppel K., Nelson C.D., Lin F.-T., Kohout T.A., Miller W.E., Exum S.T., Freedman N.J.
J. Biol. Chem. 278:44238-44245(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB1, MUTAGENESIS OF TYR-828 AND SER-854.
[18]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-657.
[19]"Infectious hepatitis C virus pseudo-particles containing functional E1-E2 envelope protein complexes."
Bartosch B., Dubuisson J., Cosset F.-L.
J. Exp. Med. 197:633-642(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HCV E1/E2 ENVELOPE HETERODIMER.
[20]"Sorting motifs in the intracellular domain of the low density lipoprotein receptor interact with a novel domain of sorting nexin-17."
Burden J.J., Sun X.-M., Garcia Garcia A.B., Soutar A.K.
J. Biol. Chem. 279:16237-16245(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX17.
[21]"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) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-657.
Tissue: Plasma.
[22]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
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) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"The cellular trafficking of the secretory proprotein convertase PCSK9 and its dependence on the LDLR."
Nassoury N., Blasiole D.A., Tebon Oler A., Benjannet S., Hamelin J., Poupon V., McPherson P.S., Attie A.D., Prat A., Seidah N.G.
Traffic 8:718-732(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PCSK9.
[24]"Glycoproteomics analysis of human liver tissue by combination of multiple 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) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-657.
Tissue: Liver.
[25]"LXR regulates cholesterol uptake through Idol-dependent ubiquitination of the LDL receptor."
Zelcer N., Hong C., Boyadjian R., Tontonoz P.
Science 325:100-104(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, CHARACTERIZATION OF VARIANT SAINT OMER ASP-546, MUTAGENESIS OF LYS-811; LYS-816; LYS-830 AND CYS-839, UBIQUITINATION.
[26]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"A two-step binding model of PCSK9 interaction with the low density lipoprotein receptor."
Yamamoto T., Lu C., Ryan R.O.
J. Biol. Chem. 286:5464-5470(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PCSK9.
[28]"Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor."
Daly N.L., Scanlon M.J., Djordjevic J.T., Kroon P.A., Smith R.
Proc. Natl. Acad. Sci. U.S.A. 92:6334-6338(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 20-67.
[29]"Three-dimensional structure of the second cysteine-rich repeat from the human low-density lipoprotein receptor."
Daly N.L., Djordjevic J.T., Kroon P.A., Smith R.
Biochemistry 34:14474-14481(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 65-104.
[30]"Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module."
Fass D., Blacklow S.C., Kim P.S., Berger J.M.
Nature 388:691-693(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 196-232.
[31]"NMR structure of a concatemer of the first and second ligand-binding modules of the human low-density lipoprotein receptor."
Kurniawan N.D., Atkins A.R., Bieri S., Brown C.J., Brereton I.M., Kroon P.A., Smith R.
Protein Sci. 9:1282-1293(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 20-104, DISULFIDE BONDS.
[32]"Structure of the LDL receptor extracellular domain at endosomal pH."
Rudenko G., Henry L., Henderson K., Ichtchenko K., Brown M.S., Goldstein J.L., Deisenhofer J.
Science 298:2353-2358(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 22-720, DISULFIDE BONDS.
[33]"Molecular genetics of the LDL receptor gene in familial hypercholesterolemia."
Hobbs H.H., Brown M.S., Goldstein J.L.
Hum. Mutat. 1:445-466(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FH VARIANTS.
[34]"Software and database for the analysis of mutations in the human LDL receptor gene."
Varret M., Rabes J.-P., Collod-Beroud G., Junien J., Boileau C., Beroud C.
Nucleic Acids Res. 25:172-180(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FH VARIANTS.
[35]"Deletion in the first cysteine-rich repeat of low density lipoprotein receptor impairs its transport but not lipoprotein binding in fibroblasts from a subject with familial hypercholesterolemia."
Leitersdorf E., Hobbs H.H., Fourie A.M., Jacobs M., van der Westhuyzen D.R., Coetzee G.A.
Proc. Natl. Acad. Sci. U.S.A. 85:7912-7916(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH 47-ASP-GLY-48 DEL.
[36]"Two common low density lipoprotein receptor gene mutations cause familial hypercholesterolemia in Afrikaners."
Leitersdorf E., van der Westhuyzen D.R., Coetzee G.A., Hobbs H.H.
J. Clin. Invest. 84:954-961(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH ASN-175; GLU-227 AND MET-429.
[37]"The J.D. mutation in familial hypercholesterolemia: amino acid substitution in cytoplasmic domain impedes internalization of LDL receptors."
Davis C.G., Lehrman M.A., Russell D.W., Anderson R.G.W., Brown M.S., Goldstein J.L.
Cell 45:15-24(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH CYS-828.
[38]"Identification of two new LDL-receptor mutations causing homozygous familial hypercholesterolemia in a South African of Indian origin."
Rubinsztein D.C., Jialal I., Leitersdorf E., Coetzee G.A., van der Westhuyzen D.R.
Biochim. Biophys. Acta 1182:75-82(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH TYR-90 AND LYS-140.
[39]"Common low-density lipoprotein receptor mutations in the French Canadian population."
Leitersdorf E., Tobin E.J., Davignon J., Hobbs H.H.
J. Clin. Invest. 85:1014-1023(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH GLY-87; LYS-228 AND TYR-667.
[40]"A point mutation of low-density-lipoprotein receptor causing rapid degradation of the receptor."
Miyake Y., Tajima S., Funahashi T., Yamamura T., Yamamoto A.
Eur. J. Biochem. 210:1-7(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH HIS-433.
[41]"A common Lithuanian mutation causing familial hypercholesterolemia in Ashkenazi Jews."
Meiner V., Landsberger D., Berkman N., Reshef A., Segal P., Seftel H.C., van der Westhuyzen D.R., Jeenah M.S., Coetzee G.A., Leitersdorf E.
Am. J. Hum. Genet. 49:443-449(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH GLY-218 DEL.
[42]"A missense mutation in the low density lipoprotein receptor gene causes familial hypercholesterolemia in Sephardic Jews."
Leitersdorf E., Reshef A., Meiner V., Dann E.J., Beigel Y., van Roggen F.G., van der Westhuyzen D.R., Coetzee G.A.
Hum. Genet. 91:141-147(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH HIS-168.
[43]"A new missense mutation (Cys297-->Phe) of the low density lipoprotein receptor in Italian patients with familial hypercholesterolemia (FHTrieste)."
Lelli N., Garuti R., Pedrazzi P., Ghisellini M., Simone M.L., Tiozzo R., Cattin L., Valenti M., Rolleri M., Bertolini S., Stefanutti C., Calandra S.
Hum. Genet. 93:538-540(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH PHE-318.
[44]"Identification of a point mutation in growth factor repeat C of the low density lipoprotein-receptor gene in a patient with homozygous familial hypercholesterolemia that affects ligand binding and intracellular movement of receptors."
Soutar A.K., Knight B.L., Patel D.D.
Proc. Natl. Acad. Sci. U.S.A. 86:4166-4170(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH LEU-685.
[45]"Identification and properties of the proline664-leucine mutant LDL receptor in South Africans of Indian origin."
Rubinsztein D.C., Coetzee G.A., Marais A.D., Leitersdorf E., Seftel H.C., van der Westhuyzen D.R.
J. Lipid Res. 33:1647-1655(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH LEU-685.
[46]"Molecular characterization of minor gene rearrangements in Finnish patients with heterozygous familial hypercholesterolemia: identification of two common missense mutations (Gly823-->Asp and Leu380-->His) and eight rare mutations of the LDL receptor gene."
Koivisto U.-M., Viikari J.S., Kontula K.
Am. J. Hum. Genet. 57:789-797(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH PORI HIS-401 AND TURKU ASP-844.
[47]"Common mutations in the low-density-lipoprotein-receptor gene causing familial hypercholesterolemia in the Japanese population."
Maruyama T., Miyake Y., Tajima S., Harada-Shiba M., Yamamura T., Tsushima M., Kishino B., Horiguchi Y., Funahashi T., Matsuzawa Y., Yamamoto A.
Arterioscler. Thromb. Vasc. Biol. 15:1713-1718(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH LYS-140; SER-338 AND LEU-685.
[48]"Identification of a mutation, N543H, in exon 11 of the low-density lipoprotein receptor gene in a French family with familial hypercholesterolemia."
Tricot-Guerber F., Saint-Jore B., Valenti K., Foulon T., Bost M., Hadjian A.J.
Hum. Mutat. 6:87-88(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH FRENCH HIS-564.
[49]"An efficient screening procedure detecting six novel mutations in the LDL receptor gene in Swedish children with hypercholesterolemia."
Ekstroem U., Abrahamson M., Sveger T., Lombardi P., Nilsson-Ehle P.
Hum. Genet. 96:147-150(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH LYS-277; THR-423 AND ASN-579.
[50]"Two novel point mutations in the EGF precursor homology domain of the LDL receptor gene causing familial hypercholesterolemia."
Leren T.P., Solberg K., Rodningen O.K., Tonstad S., Ose L.
Hum. Genet. 96:241-242(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH NORWEGIAN ASN-487 DEL.
[51]"Screening for mutations in exon 4 of the LDL receptor gene in a German population with severe hypercholesterolemia."
Geisel J., Holzem G., Oette K.
Hum. Genet. 96:301-304(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH COLOGNE GLY-221; TYR-221 AND VAL-224.
[52]"Recurrent and novel LDL receptor gene mutations causing heterozygous familial hypercholesterolemia in La Habana."
Pereira E., Ferreira R., Hermelin B., Thomas G., Bernard C., Bertrand V., Nassiff H., Mendez del Castillo D., Bereziat G., Benlian P.
Hum. Genet. 96:319-322(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH LA HABANA LYS-277; MET-429 AND MET-797.
[53]"Two novel missense mutations in the LDL receptor gene causing familial hypercholesterolemia."
Gundersen K.E., Solberg K., Rodningen O.K., Tonstad S., Ose L., Berg K., Leren T.P.
Clin. Genet. 49:85-87(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH TYR-168 AND ARG-366.
[54]"A common missense mutation (C210G) in the LDL receptor gene among Norwegian familial hypercholesterolemia subjects."
Sundvold H., Solberg K., Tonstad S., Rodningen O.K., Ose L., Berg K., Leren T.P.
Hum. Mutat. 7:70-71(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH GLY-231.
[55]"Characterization of mutations in the low density lipoprotein (LDL)-receptor gene in patients with homozygous familial hypercholesterolemia, and frequency of these mutations in FH patients in the United Kingdom."
Webb J.C., Sun X.-M., McCarthy S.N., Neuwirth C., Thompson G.R., Knigh B., Soutar A.K.
J. Lipid Res. 37:368-381(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH ARG-197; TYR-248; ALA-301; TRP-302 AND PRO-350.
[56]"Mutational and genetic origin of LDL receptor gene mutations detected in both Belgian and Dutch familial hypercholesterolemics."
Peeters A.V., van Gaal L.F., du Plessis L., Lombardi M.P.R., Havekes L.M., Kotze M.J.
Hum. Genet. 100:266-270(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH LEU-685.
[57]"Two mutations in the same low-density lipoprotein receptor allele act in synergy to reduce receptor function in heterozygous familial hypercholesterolemia."
Jensen H.K., Jensen T.G., Faergeman O., Jensen L.G., Andresen B.S., Corydon M.J., Andreasen P.H., Hansen P.S., Heath F., Bolund L., Gregersen N.
Hum. Mutat. 9:437-444(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH HIS-564 AND 799-LEU--PHE-801 DEL.
[58]"Spectrum of LDL receptor gene mutations in heterozygous familial hypercholesterolemia."
Day I.N.M., Whittall R.A., O'Dell S.D., Haddad L., Bolla M.K., Gudnason V., Humphries S.E.
Hum. Mutat. 10:116-127(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH.
[59]"Molecular genetics of familial hypercholesterolaemia in Norway."
Leren T.P., Tonstad S., Gundersen K.E., Bakken K.S., Rodningen O.K., Sundvold H., Ose L., Berg K.
J. Intern. Med. 241:185-194(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH PRO-56; TYR-175; TYR-356; VAL-401 AND TRP-416.
[60]"LDL-R and Apo-B-100 gene mutations in Polish familial hypercholesterolemias."
Gorski B., Kubalska J., Naruszewicz M., Lubinski J.
Hum. Genet. 102:562-565(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH LEU-177; GLY-218 DEL; SER-564 AND GLU-592.
[61]"Identification of three mutations in the low-density lipoprotein receptor gene causing familial hypercholesterolemia among French Canadians."
Couture P., Vohl M.-C., Gagne C., Gaudet D., Torres A.L., Lupien P.J., Despres J.-P., Labrie F., Simard J., Moorjani S.
Hum. Mutat. Suppl. 1:S226-S231(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH TRP-173 AND ARG-368.
[62]"Two novel and two known low-density lipoprotein receptor gene mutations in German patients with familial hypercholesterolemia."
Thiart R., Loubser O., de Villiers J.N.P., Marx M.P., Zaire R., Raal F.J., Kotze M.J.
Hum. Mutat. Suppl. 1:S232-S233(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH GLN-416 AND MET-429.
[63]"Possible common mutations in the low density lipoprotein receptor gene in Chinese."
Mak Y.T., Zhang J., Chan Y.S., Mak T.W.L., Tomlinson B., Masarei J.R.L., Pang C.P.
Hum. Mutat. Suppl. 1:S310-S313(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH TYR-329; ARG-414 AND MET-429.
[64]"Identification of recurrent and novel mutations in the LDL receptor gene in Spanish patients with familial hypercholesterolemia."
Cenarro A., Jensen H.K., Casao E., Civeira F., Gonzalez-Bonillo J., Rodriguez-Rey J.C., Gregersen N., Pocovi M.
Hum. Mutat. 11:413-413(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH.
[65]"Two novel mutations consisting in minor gene rearrangements in the human low density lipoprotein receptor gene in Italian patients affected by familial hypercholesterolemia."
Motti C., Bertolini S., Rampa P., Trovatello G., Liberatoscioli L., Calandra S., Federici G., Cortese C.
Hum. Mutat. 12:290-290(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH CHIETI-3 GLU-228 DELINS CYS-LYS.
[66]"A novel single amino acid substitution in exon 6 of the low-density lipoprotein receptor gene in a Syrian family."
Vergopoulos A., Bajari T., Jouma M., Aydin A., Boehring S., Luft F.C., Schuster H.
Hum. Mutat. 12:365-365(1998)
Cited for: VARIANT FH TYR-276.
[67]"Five familial hypercholesterolemic kindreds in Japan with novel mutations of the LDL receptor gene."
Hirayama T., Yamaki E., Hata A., Tsuji M., Hashimoto K., Yamamoto M., Emi M.
J. Hum. Genet. 43:250-254(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH TYR-379 AND SER-608.
[68]"Identification of a common low density lipoprotein receptor mutation (C163Y) in the west of Scotland."
Lee W.K., Haddad L., Macleod M.J., Dorrance A.M., Wilson D.J., Gaffney D., Dominiczak M.H., Packard C.J., Day I.N., Humphries S.E., Dominiczak A.F.
J. Med. Genet. 35:573-578(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH GLASCO TYR-184.
[69]"An individual with a healthy phenotype in spite of a pathogenic LDL receptor mutation (C240F)."
Ekstroem U., Abrahamson M., Floren C.-H., Tollig H., Wettrell G., Nilsson G., Sun X.-M., Soutar A.K., Nilsson-Ehle P.
Clin. Genet. 55:332-339(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH PHE-261.
[70]"Mutation analysis in 46 German families with familial hypercholesterolemia: identification of 8 new mutations."
Ebhardt M., Schmidt H., Doerk T., Tietge U., Haas R., Manns M.-P., Schmidtke J., Stuhrmann M.
Hum. Mutat. 13:257-257(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH SER-50; ASN-221; LYS-288; VAL-432 AND HIS-564.
[71]"Identification of recurrent and novel mutations in the LDL receptor gene in Japanese familial hypercholesterolemia."
Hattori H., Nagano M., Iwata F., Homma Y., Egashira T., Okada T.
Hum. Mutat. 14:87-87(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH SER-338; LEU-403; THR-431; VAL-568 AND LYS-714.
[72]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARG-2; ILE-468 AND GLN-814.
[73]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[74]"Clinical expression of familial hypercholesterolemia in clusters of mutations of the LDL receptor gene that cause a receptor-defective or receptor-negative phenotype."
Bertolini S., Cantafora A., Averna M., Cortese C., Motti C., Martini S., Pes G., Postiglione A., Stefanutti C., Blotta I., Pisciotta L., Rolleri M., Langheim S., Ghisellini M., Rabbone I., Calandra S.
Arterioscler. Thromb. Vasc. Biol. 20:E41-E52(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH PHE-134; TRP-134; TYR-222; PRO-254; ARG-276; ARG-318; THR-370; GLY-415 AND TYR-579.
[75]"Segregation of a novel LDLR gene mutation (I430T) with familial hypercholesterolaemia in a Greek pedigree."
Miltiadous G., Elisaf M., Xenophontos S., Manoli P., Cariolou M.A.
Hum. Mutat. 16:277-277(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH THR-451.
[76]"Predominance of a 6 bp deletion in exon 2 of the LDL receptor gene in Africans with familial hypercholesterolaemia."
Thiart R., Scholtz C.L., Vergotine J., Hoogendijk C.F., de Villiers J.N.P., Nissen H., Brusgaard K., Gaffney D., Hoffs M.S., Vermaak W.J.H., Kotze M.J.
J. Med. Genet. 37:514-519(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH 47-ASP-GLY-48 DEL, VARIANTS HIS-172; TRP-253; GLN-406; LYS-408; LEU-699 AND GLN-814.
[77]"A novel mutation in exon 2 of the low-density lipoprotein-receptor gene in a patient with homozygous familial hypercholesterolemia."
Takahashi M., Ikeda U., Takahashi S., Hattori H., Iwasaki T., Ishihara M., Egashira T., Honma S., Asano Y., Shimada K.A.
Clin. Genet. 59:290-292(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH SER-46.
[78]"Genetic causes of familial hypercholesterolaemia in patients in the UK: relation to plasma lipid levels and coronary heart disease risk."
Simon Broome familial hyperlipidemia register group and scientific steering committee
Humphries S.E., Whittall R.A., Hubbart C.S., Maplebeck S., Cooper J.A., Soutar A.K., Naoumova R., Thompson G.R., Seed M., Durrington P.N., Miller J.P., Betteridge D.J.B., Neil H.A.W.
J. Med. Genet. 43:943-949(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH TYR-89; LYS-101; GLY-218 DEL; GLY-221; ASN-221; TYR-358; PRO-479; HIS-482; ARG-677 AND LEU-685.
[79]"The molecular basis of familial hypercholesterolemia in Lebanon: spectrum of LDLR mutations and role of PCSK9 as a modifier gene."
Abifadel M., Rabes J.-P., Jambart S., Halaby G., Gannage-Yared M.-H., Sarkis A., Beaino G., Varret M., Salem N., Corbani S., Aydenian H., Junien C., Munnich A., Boileau C.
Hum. Mutat. 30:E682-E691(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FH PRO-254; TYR-356; TYR-358; THR-451 AND SER-826.
[80]"Analysis of sequence variations in low-density lipoprotein receptor gene among Malaysian patients with familial hypercholesterolemia."
Al-Khateeb A., Zahri M.K., Mohamed M.S., Sasongko T.H., Ibrahim S., Yusof Z., Zilfalil B.A.
BMC Med. Genet. 12:40-40(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HIS-139; LYS-201; SER-255; ASN-304 AND GLY-471.
[81]"A novel mutation (Cys308Phe) of the LDL receptor gene in families from the South-Eastern part of Poland."
Walus-Miarka M., Sanak M., Idzior-Walus B., Miarka P., Witek P., Malecki M.T., Czarnecka D.
Mol. Biol. Rep. 39:5181-5186(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FH PHE-329.
+Additional computationally mapped references.

Web resources

LDLR

LDLR mutation database

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L00352 expand/collapse EMBL AC list , L00336, L00337, L00338, L00339, L00340, L00341, L00343, L00344, L00345, L00346, L00347, L00348, L00349, L00350, L00351 Genomic DNA. Translation: AAA56833.1.
L29401 Genomic DNA. No translation available.
AY114155 mRNA. Translation: AAM56036.1.
AK295612 mRNA. Translation: BAG58495.1.
AK296312 mRNA. Translation: BAG59010.1.
AK299038 mRNA. Translation: BAG61112.1.
AK300313 mRNA. Translation: BAG62065.1.
BT007361 mRNA. Translation: AAP36025.1.
AY324609 Genomic DNA. Translation: AAP72971.1.
AB209409 mRNA. Translation: BAD92646.1. Different initiation.
FJ525879 Genomic DNA. Translation: ACN81317.1.
AC011485 Genomic DNA. No translation available.
CH471106 Genomic DNA. Translation: EAW84169.1.
BC014514 mRNA. Translation: AAH14514.1.
CCDSCCDS12254.1. [P01130-1]
CCDS56083.1. [P01130-2]
CCDS56085.1. [P01130-4]
CCDS58651.1. [P01130-5]
PIRQRHULD. A01383.
RefSeqNP_000518.1. NM_000527.4. [P01130-1]
NP_001182727.1. NM_001195798.1. [P01130-5]
NP_001182728.1. NM_001195799.1. [P01130-4]
NP_001182729.1. NM_001195800.1.
NP_001182732.1. NM_001195803.1. [P01130-2]
UniGeneHs.213289.
Hs.713981.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AJJX-ray1.70A196-232[»]
1D2JNMR-A233-272[»]
1F5YNMR-A22-104[»]
1F8ZNMR-A234-272[»]
1HJ7NMR-A314-393[»]
1HZ8NMR-A314-395[»]
1I0UNMR-A314-395[»]
1IJQX-ray1.50A/B398-713[»]
1LDLNMR-A20-67[»]
1LDRNMR-A64-104[»]
1LRXmodel-B396-659[»]
1N7DX-ray3.70A22-720[»]
1XFENMR-A272-353[»]
2FCWX-ray1.26B107-186[»]
2KRINMR-B147-186[»]
2LGPNMR-A144-235[»]
2M7PNMR-A82-104[»]
2MG9NMR-A314-339[»]
2W2MX-ray2.40E314-393[»]
2W2NX-ray2.30E314-393[»]
2W2OX-ray2.62E314-393[»]
2W2PX-ray2.62E314-393[»]
2W2QX-ray2.33E314-393[»]
3BPSX-ray2.41E314-393[»]
3GCWX-ray2.70E314-393[»]
3GCXX-ray2.70E314-393[»]
3M0CX-ray7.01C4-788[»]
3P5BX-ray3.30L316-715[»]
3P5CX-ray4.20L276-715[»]
3SO6X-ray1.37Q819-832[»]
ProteinModelPortalP01130.
SMRP01130. Positions 20-715.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110141. 18 interactions.
DIPDIP-29695N.
IntActP01130. 10 interactions.
MINTMINT-3003796.
STRING9606.ENSP00000252444.

Chemistry

BindingDBP01130.
ChEMBLCHEMBL3311.
DrugBankDB00992. Methyl aminolevulinate.
DB00707. Porfimer.

PTM databases

PhosphoSiteP01130.
UniCarbKBP01130.

Polymorphism databases

DMDM126073.

Proteomic databases

MaxQBP01130.
PaxDbP01130.
PRIDEP01130.

Protocols and materials databases

DNASU3949.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000455727; ENSP00000397829; ENSG00000130164.
ENST00000535915; ENSP00000440520; ENSG00000130164. [P01130-4]
ENST00000545707; ENSP00000437639; ENSG00000130164. [P01130-2]
ENST00000558013; ENSP00000453346; ENSG00000130164. [P01130-5]
ENST00000558518; ENSP00000454071; ENSG00000130164. [P01130-1]
GeneID3949.
KEGGhsa:3949.
UCSCuc002mqk.4. human. [P01130-1]
uc010xll.2. human. [P01130-4]
uc010xln.2. human. [P01130-2]
uc010xlo.2. human. [P01130-3]

Organism-specific databases

CTD3949.
GeneCardsGC19P011200.
GeneReviewsLDLR.
HGNCHGNC:6547. LDLR.
HPAHPA009647.
HPA013159.
MIM143890. phenotype.
606945. gene.
neXtProtNX_P01130.
Orphanet406. Heterozygous familial hypercholesterolemia.
391665. Homozygous familial hypercholesterolemia.
PharmGKBPA227.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG255913.
HOGENOMHOG000115656.
HOVERGENHBG006250.
InParanoidP01130.
KOK12473.
OrthoDBEOG7NGQ9P.
PhylomeDBP01130.
TreeFamTF351700.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

ArrayExpressP01130.
BgeeP01130.
CleanExHS_LDLR.
GenevestigatorP01130.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
4.10.400.10. 7 hits.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamPF12662. cEGF. 1 hit.
PF00057. Ldl_recept_a. 7 hits.
PF00058. Ldl_recept_b. 5 hits.
[Graphical view]
PRINTSPR00261. LDLRECEPTOR.
SMARTSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00192. LDLa. 7 hits.
SM00135. LY. 5 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 2 hits.
SSF57424. SSF57424. 7 hits.
PROSITEPS00010. ASX_HYDROXYL. 2 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
PS01209. LDLRA_1. 7 hits.
PS50068. LDLRA_2. 7 hits.
PS51120. LDLRB. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLDLR. human.
EvolutionaryTraceP01130.
GeneWikiLDL_receptor.
GenomeRNAi3949.
NextBio15493.
PROP01130.
SOURCESearch...

Entry information

Entry nameLDLR_HUMAN
AccessionPrimary (citable) accession number: P01130
Secondary accession number(s): B4DII3 expand/collapse secondary AC list , B4DJZ8, B4DR00, B4DTQ3, C0JYY8, H0YLU8, H0YNT7, Q53ZD9, Q59FQ1, Q9UDH7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 188 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM