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Protein

Low-density lipoprotein receptor-related protein 5

Gene

LRP5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Acts as a coreceptor with members of the frizzled family of seven-transmembrane spanning receptors to transduce signal by Wnt proteins (PubMed:11336703, PubMed:11448771, PubMed:15778503, PubMed:11719191, PubMed:15908424, PubMed:16252235). Activates the canonical Wnt signaling pathway that controls cell fate determination and self-renewal during embryonic development and adult tissue regeneration (PubMed:11336703, PubMed:11719191). In particular, may play an important role in the development of the posterior patterning of the epiblast during gastrulation (By similarity). During bone development, regulates osteoblast proliferation and differentiation thus determining bone mass (PubMed:11719191). Mechanistically, the formation of the signaling complex between Wnt ligand, frizzled receptor and LRP5 coreceptor promotes the recruitment of AXIN1 to LRP5, stabilizing beta-catenin/CTNNB1 and activating TCF/LEF-mediated transcriptional programs (PubMed:11336703, PubMed:25920554, PubMed:24706814, PubMed:14731402). Acts as a coreceptor for non-Wnt proteins, such as norrin/NDP. Binding of norrin/NDP to frizzled 4/FZD4-LRP5 receptor complex triggers beta-catenin/CTNNB1-dependent signaling known to be required for retinal vascular development (PubMed:27228167, PubMed:16252235). Plays a role in controlling postnatal vascular regression in retina via macrophage-induced endothelial cell apoptosis (By similarity).By similarity10 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • coreceptor activity involved in canonical Wnt signaling pathway Source: ParkinsonsUK-UCL
  • coreceptor activity involved in Wnt signaling pathway Source: ParkinsonsUK-UCL
  • Wnt-activated receptor activity Source: ParkinsonsUK-UCL
  • Wnt-protein binding Source: ParkinsonsUK-UCL

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDevelopmental protein, Receptor
Biological processEndocytosis, Wnt signaling pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-201681 TCF dependent signaling in response to WNT
R-HSA-3772470 Negative regulation of TCF-dependent signaling by WNT ligand antagonists
R-HSA-4641262 Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-HSA-4641263 Regulation of FZD by ubiquitination
R-HSA-5339717 Misspliced LRP5 mutants have enhanced beta-catenin-dependent signaling
R-HSA-5340588 RNF mutants show enhanced WNT signaling and proliferation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
O75197

SIGNOR Signaling Network Open Resource

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SIGNORi
O75197

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein 51 Publication
Short name:
LRP-51 Publication
Alternative name(s):
Low-density lipoprotein receptor-related protein 7By similarity
Short name:
LRP-7
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:LRP51 PublicationImported
Synonyms:LR31 Publication, LRP7By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000162337.11

Human Gene Nomenclature Database

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HGNCi
HGNC:6697 LRP5

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603506 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_O75197

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini32 – 1384ExtracellularSequence analysisAdd BLAST1353
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei1385 – 1407HelicalSequence analysisAdd BLAST23
Topological domaini1408 – 1615CytoplasmicSequence analysisAdd BLAST208

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Vitreoretinopathy, exudative 1 (EVR1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery. In many ways the disease resembles retinopathy of prematurity but there is no evidence of prematurity or small birth weight in the patient history.
See also OMIM:133780
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_063948348R → W in OPPG and EVR1; reduces Norrin signal transduction. 2 PublicationsCorresponds to variant dbSNP:rs1320065036Ensembl.1
Natural variantiVAR_076548381D → N in EVR1; reduces Norrin signal transduction. 1 PublicationCorresponds to variant dbSNP:rs1332274863Ensembl.1
Natural variantiVAR_076549624R → W in EVR1; reduces Norrin signal transduction. 1 PublicationCorresponds to variant dbSNP:rs989864153Ensembl.1
Natural variantiVAR_0765501517Y → C in EVR1; decreases protein abundance. 1 PublicationCorresponds to variant dbSNP:rs201030241Ensembl.1
Vitreoretinopathy, exudative 4 (EVR4)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery.
See also OMIM:601813
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063943145L → F in EVR4. 1 PublicationCorresponds to variant dbSNP:rs80358305EnsemblClinVar.1
Natural variantiVAR_018465173T → M in EVR4; an individual with abnormal retinal vasculature and retinal folds. 2 PublicationsCorresponds to variant dbSNP:rs80358306Ensembl.1
Natural variantiVAR_071012422A → T in EVR4; the mutation results in significantly reduced Norrin signal transduction. 1 PublicationCorresponds to variant dbSNP:rs774342727Ensembl.1
Natural variantiVAR_063956441E → K in EVR4. 1 PublicationCorresponds to variant dbSNP:rs376152274Ensembl.1
Natural variantiVAR_063957444R → C in EVR4; associated in a EVR1 patient with mutation GLN-417 in FZD4. 1 PublicationCorresponds to variant dbSNP:rs80358308EnsemblClinVar.1
Natural variantiVAR_063962511D → A in EVR4. 1 PublicationCorresponds to variant dbSNP:rs1245625202Ensembl.1
Natural variantiVAR_063964522A → T in EVR4. 1 PublicationCorresponds to variant dbSNP:rs80358309Ensembl.1
Natural variantiVAR_063966535T → M in EVR4; autosomal recessive. 1 PublicationCorresponds to variant dbSNP:rs80358310Ensembl.1
Natural variantiVAR_071013540L → P in EVR4; the mutation results in significantly reduced Norrin signal transduction. 1 Publication1
Natural variantiVAR_063967550G → R in EVR4; autosomal recessive. 1 PublicationCorresponds to variant dbSNP:rs80358311Ensembl.1
Natural variantiVAR_021222570R → Q in EVR4; autosomal recessive; has significantly reduced Wnt or Norrin signal transduction. 2 PublicationsCorresponds to variant dbSNP:rs80358312EnsemblClinVar.1
Natural variantiVAR_063968610G → R in EVR4 and OPPG; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; has 60% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 2 PublicationsCorresponds to variant dbSNP:rs80358313EnsemblClinVar.1
Natural variantiVAR_063969617F → C in EVR4; autosomal recessive. 1 PublicationCorresponds to variant dbSNP:rs80358314Ensembl.1
Natural variantiVAR_021223752R → G in EVR4; autosomal recessive. 1 PublicationCorresponds to variant dbSNP:rs121908674EnsemblClinVar.1
Natural variantiVAR_063972798T → A in EVR4. 1 PublicationCorresponds to variant dbSNP:rs80358316Ensembl.1
Natural variantiVAR_063973805R → W in EVR4. 1 PublicationCorresponds to variant dbSNP:rs765952535Ensembl.1
Natural variantiVAR_071015852T → M in EVR4; de novo mutation found in a patient also carrying mutation P-540; unknown pathological significance; the mutation results in significantly reduced Norrin signal transduction. 1 PublicationCorresponds to variant dbSNP:rs1398692057Ensembl.1
Natural variantiVAR_0639771121N → D in EVR4; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs80358317EnsemblClinVar.1
Natural variantiVAR_0184661168Y → H in EVR4; an individual with total retinal detachment and retinoschisis; is unable to transduce Wnt or Norrin signal transduction. 2 PublicationsCorresponds to variant dbSNP:rs80358318Ensembl.1
Natural variantiVAR_0639781253C → F in EVR4. 1 PublicationCorresponds to variant dbSNP:rs768615287Ensembl.1
Natural variantiVAR_0184671361C → G in EVR4; autosomal dominant; has mildly reduced Wnt or Norrin signal transduction. 2 PublicationsCorresponds to variant dbSNP:rs80358320Ensembl.1
Natural variantiVAR_0212241367E → K in EVR4; autosomal recessive. 2 PublicationsCorresponds to variant dbSNP:rs28939709EnsemblClinVar.1
Osteoporosis (OSTEOP)3 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA systemic skeletal disorder characterized by decreased bone mass and deterioration of bone microarchitecture without alteration in the composition of bone. The result is fragile bones and an increased risk of fractures, even after minimal trauma. Osteoporosis is a chronic condition of multifactorial etiology and is usually clinically silent until a fracture occurs.
See also OMIM:166710
Osteoporosis-pseudoglioma syndrome (OPPG)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by congenital or infancy-onset blindness and severe juvenile-onset osteoporosis and spontaneous fractures. Additional clinical manifestations may include microphthalmos, abnormalities of the iris, lens or vitreous, cataracts, short stature, microcephaly, ligamental laxity, mental retardation and hypotonia.
See also OMIM:259770
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063945203D → N in OPPG. 1 PublicationCorresponds to variant dbSNP:rs760548029Ensembl.1
Natural variantiVAR_063946244T → M in OPPG; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 1 PublicationCorresponds to variant dbSNP:rs397514665EnsemblClinVar.1
Natural variantiVAR_063947307S → F in OPPG. 1 PublicationCorresponds to variant dbSNP:rs1219101402Ensembl.1
Natural variantiVAR_063948348R → W in OPPG and EVR1; reduces Norrin signal transduction. 2 PublicationsCorresponds to variant dbSNP:rs1320065036Ensembl.1
Natural variantiVAR_063949353R → Q in OPPG. 1 Publication1
Natural variantiVAR_063950356S → L in idiopathic osteoporosis and OPPG; appears to traffic comparably than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 2 PublicationsCorresponds to variant dbSNP:rs1158745675Ensembl.1
Natural variantiVAR_063951390T → K in OPPG; is unable to traffic normally; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 1 Publication1
Natural variantiVAR_063952400A → E in OPPG. 1 PublicationCorresponds to variant dbSNP:rs201320326Ensembl.1
Natural variantiVAR_063953404G → R in OPPG; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; has 50% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 1 PublicationCorresponds to variant dbSNP:rs750791263Ensembl.1
Natural variantiVAR_063954409T → A in OPPG. 1 PublicationCorresponds to variant dbSNP:rs1273567061Ensembl.1
Natural variantiVAR_063955434D → N in OPPG; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; has 50% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 1 PublicationCorresponds to variant dbSNP:rs757888034Ensembl.1
Natural variantiVAR_063959460E → K in OPPG. 1 PublicationCorresponds to variant dbSNP:rs866606166Ensembl.1
Natural variantiVAR_063960478W → R in OPPG. 1 PublicationCorresponds to variant dbSNP:rs1318906451Ensembl.1
Natural variantiVAR_021814494R → Q in OPPG. 2 PublicationsCorresponds to variant dbSNP:rs121908664EnsemblClinVar.1
Natural variantiVAR_063961504W → C in OPPG. 1 PublicationCorresponds to variant dbSNP:rs545508982Ensembl.1
Natural variantiVAR_063963520G → V in OPPG; appears to traffic comparably than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 1 Publication1
Natural variantiVAR_063965531N → I in OPPG. 1 Publication1
Natural variantiVAR_021815570R → W in OPPG. 2 PublicationsCorresponds to variant dbSNP:rs121908665EnsemblClinVar.1
Natural variantiVAR_063968610G → R in EVR4 and OPPG; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; has 60% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 2 PublicationsCorresponds to variant dbSNP:rs80358313EnsemblClinVar.1
Natural variantiVAR_063970683D → N in OPPG. 1 PublicationCorresponds to variant dbSNP:rs1470530779Ensembl.1
Natural variantiVAR_063971733Y → H in OPPG. 1 PublicationCorresponds to variant dbSNP:rs746701187Ensembl.1
Natural variantiVAR_0639751099D → Y in OPPG. 1 Publication1
Natural variantiVAR_0639761113R → C in OPPG. 1 PublicationCorresponds to variant dbSNP:rs377258285Ensembl.1
Natural variantiVAR_0639791401G → D in OPPG. 1 Publication1
High bone mass trait (HBM)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionRare phenotype characterized by exceptionally dense bones. HBM individuals show otherwise a completely normal skeletal structure and no other unusual clinical findings.
See also OMIM:601884
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063944154R → M in HBM. 1 Publication1
Natural variantiVAR_021809171G → V in HBM; also in HBM individuals with enlarged mandible and torus palatinus; abolishes interaction with MESD; impairs transport to cell surface; no enhancement of DKK1 binding by MESD resulting in impaired inhibition of Wnt signaling by DKK1. 4 PublicationsCorresponds to variant dbSNP:rs121908668EnsemblClinVar.1
Natural variantiVAR_063412282M → V in HBM; unknown pathological significance; lowered LRP5-mediated Wnt signaling; no effect on DKK1 binding. 1 Publication1
Endosteal hyperostosis, Worth type (WENHY)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant sclerosing bone dysplasia clinically characterized by elongation of the mandible, increased gonial angle, flattened forehead, and the presence of a slowly enlarging osseous prominence of the hard palate (torus palatinus). Serum calcium, phosphorus and alkaline phosphatase levels are normal. Radiologically, it is characterized by early thickening of the endosteum of long bones, the skull and of the mandible. With advancing age, the trabeculae of the metaphysis become thickened. WENHY becomes clinically and radiologically evident by adolescence, does not cause deformity except in the skull and mandible, and is not associated with bone pain or fracture. Affected patients have normal height, proportion, intelligence and longevity.
See also OMIM:144750
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021810214A → T in WENHY. 1 PublicationCorresponds to variant dbSNP:rs121908671EnsemblClinVar.1
Natural variantiVAR_021811214A → V in WENHY. 1 PublicationCorresponds to variant dbSNP:rs121908672EnsemblClinVar.1
Natural variantiVAR_021812242A → T in OPTA1, VBCH2 and WENHY. 1 PublicationCorresponds to variant dbSNP:rs121908670EnsemblClinVar.1
Osteopetrosis, autosomal dominant 1 (OPTA1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. Osteopetrosis occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. OPTA1 is an autosomal dominant form characterized by generalized osteosclerosis most pronounced in the cranial vault. Patients are often asymptomatic, but some suffer from pain and hearing loss. It appears to be the only type of osteopetrosis not associated with an increased fracture rate.
See also OMIM:607634
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021807111D → Y in OPTA1. 1 Publication1
Natural variantiVAR_021808171G → R in OPTA1. 1 PublicationCorresponds to variant dbSNP:rs121908669EnsemblClinVar.1
Natural variantiVAR_021812242A → T in OPTA1, VBCH2 and WENHY. 1 PublicationCorresponds to variant dbSNP:rs121908670EnsemblClinVar.1
Natural variantiVAR_021813253T → I in OPTA1. 1 PublicationCorresponds to variant dbSNP:rs121908673EnsemblClinVar.1
Van Buchem disease 2 (VBCH2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionVBCH2 is an autosomal dominant sclerosing bone dysplasia characterized by cranial osteosclerosis, thickened calvaria and cortices of long bones, enlarged mandible and normal serum alkaline phosphatase levels.
See also OMIM:607636
Polycystic liver disease 4 with or without kidney cysts (PCLD4)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of polycystic liver disease, an autosomal dominant hepatobiliary disease characterized by overgrowth of biliary epithelium and supportive connective tissue, resulting in multiple liver cysts. PCLD4 patients may also develop kidney cysts that usually do not result in clinically significant renal disease.
See also OMIM:617875
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_080857454V → M in PCLD4; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs373910016EnsemblClinVar.1
Natural variantiVAR_080935638K → E in PCLD4; unknown pathological significance; the patient carried additional PKHD1 variant. 1 PublicationCorresponds to variant dbSNP:rs758976409Ensembl.1
Natural variantiVAR_080936684V → A in PCLD4; unknown pathological significance; the patient carried additional PKHD1 variant. 1 PublicationCorresponds to variant dbSNP:rs1339222045Ensembl.1
Natural variantiVAR_080937925R → C in PCLD4; unknown pathological significance; the patient carried additional PKHD1 variant. 1 PublicationCorresponds to variant dbSNP:rs369471051Ensembl.1
Natural variantiVAR_0808611188R → W in PCLD4; the mutation results in significantly reduced WNT3A-induced signaling pathway. 1 PublicationCorresponds to variant dbSNP:rs141178995EnsemblClinVar.1
Natural variantiVAR_0808621529R → S in PCLD4; found in a family affected by polycystic liver disease; unknown pathological significance. 1 Publication1
Natural variantiVAR_0809381541T → M in PCLD4; unknown pathological significance; the patient carried additional PKHD1 variant. 1 PublicationCorresponds to variant dbSNP:rs150862227Ensembl.1
Natural variantiVAR_0808631551D → N in PCLD4; unknown pathological significance; the mutation results in significantly reduced WNT3A-induced signaling pathway. 1 PublicationCorresponds to variant dbSNP:rs724159827EnsemblClinVar.1
LRP5 variations may act as a disease modifier in autosomal dominant polycystic kidney disease (ADPKD) in patients who have causative mutations in PKD1. May contribute to the disease phenotype heterogeneity and hepatic cystogenesis.1 Publication

Keywords - Diseasei

Disease mutation, Osteogenesis imperfecta, Osteopetrosis

Organism-specific databases

DisGeNET

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DisGeNETi
4041

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
LRP5

MalaCards human disease database

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MalaCardsi
LRP5
MIMi133780 phenotype
144750 phenotype
166710 phenotype
259770 phenotype
601813 phenotype
601884 phenotype
607634 phenotype
607636 phenotype
617875 phenotype

Open Targets

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OpenTargetsi
ENSG00000162337

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
2783 Autosomal dominant osteopetrosis type 1
2790 Endosteal hyperostosis, Worth type
891 Familial exudative vitreoretinopathy
3416 Hyperostosis corticalis generalisata
2924 Isolated polycystic liver disease
498481 LRP5-related primary osteoporosis
2788 Osteoporosis-pseudoglioma syndrome
178377 Osteosclerosis-developmental delay-craniosynostosis syndrome
90050 Retinopathy of prematurity

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA30455

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
LRP5

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 31Sequence analysisAdd BLAST31
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001732832 – 1615Low-density lipoprotein receptor-related protein 5Add BLAST1584

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi93N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi138N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi299 ↔ 310PROSITE-ProRule annotation
Disulfide bondi306 ↔ 321PROSITE-ProRule annotation
Disulfide bondi323 ↔ 336PROSITE-ProRule annotation
Glycosylationi446N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi499N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi605 ↔ 616PROSITE-ProRule annotation
Disulfide bondi612 ↔ 625PROSITE-ProRule annotation
Disulfide bondi627 ↔ 640PROSITE-ProRule annotation
Glycosylationi705N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi878N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi906 ↔ 917PROSITE-ProRule annotation
Disulfide bondi913 ↔ 926PROSITE-ProRule annotation
Disulfide bondi928 ↔ 941PROSITE-ProRule annotation
Disulfide bondi1217 ↔ 1228PROSITE-ProRule annotation
Disulfide bondi1224 ↔ 1238PROSITE-ProRule annotation
Disulfide bondi1240 ↔ 1253PROSITE-ProRule annotation
Disulfide bondi1259 ↔ 1273PROSITE-ProRule annotation
Disulfide bondi1266 ↔ 1286PROSITE-ProRule annotation
Disulfide bondi1280 ↔ 1295PROSITE-ProRule annotation
Disulfide bondi1298 ↔ 1310PROSITE-ProRule annotation
Disulfide bondi1305 ↔ 1323PROSITE-ProRule annotation
Disulfide bondi1317 ↔ 1332PROSITE-ProRule annotation
Disulfide bondi1336 ↔ 1348PROSITE-ProRule annotation
Disulfide bondi1343 ↔ 1361PROSITE-ProRule annotation
Disulfide bondi1355 ↔ 1370PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation of cytoplasmic PPPSP motifs regulates the signal transduction of the Wnt signaling pathway through acting as a docking site for AXIN1.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
O75197

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
O75197

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
O75197

PeptideAtlas

More...
PeptideAtlasi
O75197

PRoteomics IDEntifications database

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PRIDEi
O75197

ProteomicsDB human proteome resource

More...
ProteomicsDBi
49865

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
1468

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
O75197

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
O75197

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely expressed, with the highest level of expression in the liver and in aorta.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000162337 Expressed in 171 organ(s), highest expression level in right lobe of liver

CleanEx database of gene expression profiles

More...
CleanExi
HS_LRP5

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
O75197 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
O75197 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB013001
HPA030505

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; disulfide-linked. Forms phosphorylated oligomer aggregates on Wnt-signaling (By similarity). Component of a Wnt-signaling complex that contains a WNT protein, a FZD protein and LRP5 or LRP6. Interacts with FZD8; the interaction is formed on WNT-binding and signaling (PubMed:11448771). Interacts (via the phosphorylated PPPSP motif domains) with AXIN1; the interaction prevents inhibition of beta-catenin phosphorylation and signaling and is enhanced in the presence of GSK3B and WNT1 or WNT3A (PubMed:11336703, PubMed:14731402). Interacts (via beta-propeller regions 3 and 4) with DKK1; the interaction, enhanced by MESD and/or KREMEN, inhibits beta-catenin signaling by preventing GSK3-mediated phosphorylation of the PPPSP motifs and subsequent, AXIN1 binding (PubMed:11448771, PubMed:15778503, PubMed:19746449). Interacts with MESD; the interaction prevents the formation of LRP5 aggregates, targets LRP5 to the plasma membrane and, when complexed with KREMEN2, increases DKK1 binding (PubMed:17488095, PubMed:19746449, PubMed:15143163). Interacts with CSNK1E (PubMed:16513652). Interacts with SOST; the interaction antagonizes canonical Wnt signaling (PubMed:15778503, PubMed:15908424). Interacts with APCDD1 (PubMed:20393562). Interacts with CAPRIN2 (PubMed:18762581).By similarity11 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
110220, 44 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
O75197

Database of interacting proteins

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DIPi
DIP-47265N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
O75197

Protein interaction database and analysis system

More...
IntActi
O75197, 10 interactors

Molecular INTeraction database

More...
MINTi
O75197

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000294304

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
O75197

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
O75197

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati75 – 119LDL-receptor class B 1Add BLAST45
Repeati78 – 81YWTD 14
Repeati120 – 162LDL-receptor class B 2Add BLAST43
Repeati123 – 126YWTD 24
Repeati163 – 206LDL-receptor class B 3Add BLAST44
Repeati166 – 169YWTD 34
Repeati207 – 247LDL-receptor class B 4Add BLAST41
Repeati248 – 290LDL-receptor class B 5Add BLAST43
Repeati251 – 254YWTD 44
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini295 – 337EGF-like 1Add BLAST43
Repeati385 – 427LDL-receptor class B 6Add BLAST43
Repeati388 – 391YWTD 54
Repeati428 – 470LDL-receptor class B 7Add BLAST43
Repeati431 – 434YWTD 64
Repeati471 – 514LDL-receptor class B 8Add BLAST44
Repeati474 – 477YWTD 74
Repeati515 – 557LDL-receptor class B 9Add BLAST43
Repeati558 – 600LDL-receptor class B 10Add BLAST43
Repeati559 – 562YWTD 84
Domaini601 – 641EGF-like 2Add BLAST41
Repeati687 – 729LDL-receptor class B 11Add BLAST43
Repeati690 – 693YWTD 94
Repeati730 – 772LDL-receptor class B 12Add BLAST43
Repeati773 – 815LDL-receptor class B 13Add BLAST43
Repeati816 – 855LDL-receptor class B 14Add BLAST40
Repeati819 – 822YWTD 104
Repeati856 – 898LDL-receptor class B 15Add BLAST43
Repeati859 – 862YWTD 114
Domaini902 – 942EGF-like 3Add BLAST41
Repeati989 – 1035LDL-receptor class B 16Add BLAST47
Repeati1036 – 1078LDL-receptor class B 17Add BLAST43
Repeati1079 – 1123LDL-receptor class B 18Add BLAST45
Repeati1124 – 1164LDL-receptor class B 19Add BLAST41
Repeati1165 – 1207LDL-receptor class B 20Add BLAST43
Domaini1213 – 1254EGF-like 4Add BLAST42
Domaini1258 – 1296LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST39
Domaini1297 – 1333LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST37
Domaini1335 – 1371LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni32 – 288Beta-propeller 1Add BLAST257
Regioni341 – 602Beta-propeller 2Add BLAST262
Regioni644 – 903Beta-propeller 3Add BLAST260
Regioni945 – 1212Beta-propeller 4Add BLAST268

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi1500 – 1506PPPSP motif A7
Motifi1538 – 1545PPPSP motif B8
Motifi1574 – 1581PPPSP motif C8
Motifi1591 – 1596PPPSP motif D6
Motifi1605 – 1612PPPSP motif E8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1495 – 1610Pro-richAdd BLAST116

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the LDLR family.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IPT4 Eukaryota
ENOG410XSY5 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156574

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000230697

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG049167

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O75197

KEGG Orthology (KO)

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KOi
K03068

Identification of Orthologs from Complete Genome Data

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OMAi
PFTGISC

Database of Orthologous Groups

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OrthoDBi
1349932at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O75197

TreeFam database of animal gene trees

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TreeFami
TF315253

Family and domain databases

Conserved Domains Database

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CDDi
cd00112 LDLa, 3 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.120.10.30, 4 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011042 6-blade_b-propeller_TolB-like
IPR000742 EGF-like_dom
IPR036055 LDL_receptor-like_sf
IPR023415 LDLR_class-A_CS
IPR000033 LDLR_classB_rpt
IPR002172 LDrepeatLR_classA_rpt
IPR017049 LRP5/6

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00057 Ldl_recept_a, 3 hits
PF00058 Ldl_recept_b, 13 hits

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF036314 LDL_recpt-rel_p5/6, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00261 LDLRECEPTOR

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00181 EGF, 4 hits
SM00192 LDLa, 3 hits
SM00135 LY, 20 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF57424 SSF57424, 3 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01209 LDLRA_1, 3 hits
PS50068 LDLRA_2, 3 hits
PS51120 LDLRB, 20 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

O75197-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEAAPPGPPW PLLLLLLLLL ALCGCPAPAA ASPLLLFANR RDVRLVDAGG
60 70 80 90 100
VKLESTIVVS GLEDAAAVDF QFSKGAVYWT DVSEEAIKQT YLNQTGAAVQ
110 120 130 140 150
NVVISGLVSP DGLACDWVGK KLYWTDSETN RIEVANLNGT SRKVLFWQDL
160 170 180 190 200
DQPRAIALDP AHGYMYWTDW GETPRIERAG MDGSTRKIIV DSDIYWPNGL
210 220 230 240 250
TIDLEEQKLY WADAKLSFIH RANLDGSFRQ KVVEGSLTHP FALTLSGDTL
260 270 280 290 300
YWTDWQTRSI HACNKRTGGK RKEILSALYS PMDIQVLSQE RQPFFHTRCE
310 320 330 340 350
EDNGGCSHLC LLSPSEPFYT CACPTGVQLQ DNGRTCKAGA EEVLLLARRT
360 370 380 390 400
DLRRISLDTP DFTDIVLQVD DIRHAIAIDY DPLEGYVYWT DDEVRAIRRA
410 420 430 440 450
YLDGSGAQTL VNTEINDPDG IAVDWVARNL YWTDTGTDRI EVTRLNGTSR
460 470 480 490 500
KILVSEDLDE PRAIALHPVM GLMYWTDWGE NPKIECANLD GQERRVLVNA
510 520 530 540 550
SLGWPNGLAL DLQEGKLYWG DAKTDKIEVI NVDGTKRRTL LEDKLPHIFG
560 570 580 590 600
FTLLGDFIYW TDWQRRSIER VHKVKASRDV IIDQLPDLMG LKAVNVAKVV
610 620 630 640 650
GTNPCADRNG GCSHLCFFTP HATRCGCPIG LELLSDMKTC IVPEAFLVFT
660 670 680 690 700
SRAAIHRISL ETNNNDVAIP LTGVKEASAL DFDVSNNHIY WTDVSLKTIS
710 720 730 740 750
RAFMNGSSVE HVVEFGLDYP EGMAVDWMGK NLYWADTGTN RIEVARLDGQ
760 770 780 790 800
FRQVLVWRDL DNPRSLALDP TKGYIYWTEW GGKPRIVRAF MDGTNCMTLV
810 820 830 840 850
DKVGRANDLT IDYADQRLYW TDLDTNMIES SNMLGQERVV IADDLPHPFG
860 870 880 890 900
LTQYSDYIYW TDWNLHSIER ADKTSGRNRT LIQGHLDFVM DILVFHSSRQ
910 920 930 940 950
DGLNDCMHNN GQCGQLCLAI PGGHRCGCAS HYTLDPSSRN CSPPTTFLLF
960 970 980 990 1000
SQKSAISRMI PDDQHSPDLI LPLHGLRNVK AIDYDPLDKF IYWVDGRQNI
1010 1020 1030 1040 1050
KRAKDDGTQP FVLTSLSQGQ NPDRQPHDLS IDIYSRTLFW TCEATNTINV
1060 1070 1080 1090 1100
HRLSGEAMGV VLRGDRDKPR AIVVNAERGY LYFTNMQDRA AKIERAALDG
1110 1120 1130 1140 1150
TEREVLFTTG LIRPVALVVD NTLGKLFWVD ADLKRIESCD LSGANRLTLE
1160 1170 1180 1190 1200
DANIVQPLGL TILGKHLYWI DRQQQMIERV EKTTGDKRTR IQGRVAHLTG
1210 1220 1230 1240 1250
IHAVEEVSLE EFSAHPCARD NGGCSHICIA KGDGTPRCSC PVHLVLLQNL
1260 1270 1280 1290 1300
LTCGEPPTCS PDQFACATGE IDCIPGAWRC DGFPECDDQS DEEGCPVCSA
1310 1320 1330 1340 1350
AQFPCARGQC VDLRLRCDGE ADCQDRSDEA DCDAICLPNQ FRCASGQCVL
1360 1370 1380 1390 1400
IKQQCDSFPD CIDGSDELMC EITKPPSDDS PAHSSAIGPV IGIILSLFVM
1410 1420 1430 1440 1450
GGVYFVCQRV VCQRYAGANG PFPHEYVSGT PHVPLNFIAP GGSQHGPFTG
1460 1470 1480 1490 1500
IACGKSMMSS VSLMGGRGGV PLYDRNHVTG ASSSSSSSTK ATLYPPILNP
1510 1520 1530 1540 1550
PPSPATDPSL YNMDMFYSSN IPATARPYRP YIIRGMAPPT TPCSTDVCDS
1560 1570 1580 1590 1600
DYSASRWKAS KYYLDLNSDS DPYPPPPTPH SQYLSAEDSC PPSPATERSY
1610
FHLFPPPPSP CTDSS
Length:1,615
Mass (Da):179,145
Last modified:April 12, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8BA25D07F51E02CA
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9PHY1E9PHY1_HUMAN
Low-density lipoprotein receptor-re...
LRP5
471Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YE98H0YE98_HUMAN
Low-density lipoprotein receptor-re...
LRP5
172Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti1525 – 1528Missing in AAK52433 (PubMed:11401438).Curated4

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Genetic variations in LRP5 define the bone mineral density quantitative trait locus 1 (BMND1) [MIMi:601884]. Variance in bone mineral density influences bone mass and contributes to size determination in the general population.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05858215 – 20Missing Found in a family with osteoporosis pseudoglioma syndrome; impairs protein trafficking to the endoplasmic reticulum and cell membrane. 1 Publication6
Natural variantiVAR_02180418 – 20Missing 1 Publication3
Natural variantiVAR_02180520L → LL1 Publication1
Natural variantiVAR_06394129A → T in primary osteoporosis. 1 Publication1
Natural variantiVAR_02180689Q → R2 PublicationsCorresponds to variant dbSNP:rs41494349EnsemblClinVar.1
Natural variantiVAR_06394297A → V1 PublicationCorresponds to variant dbSNP:rs143433231Ensembl.1
Natural variantiVAR_021807111D → Y in OPTA1. 1 Publication1
Natural variantiVAR_063943145L → F in EVR4. 1 PublicationCorresponds to variant dbSNP:rs80358305EnsemblClinVar.1
Natural variantiVAR_063944154R → M in HBM. 1 Publication1
Natural variantiVAR_021808171G → R in OPTA1. 1 PublicationCorresponds to variant dbSNP:rs121908669EnsemblClinVar.1
Natural variantiVAR_021809171G → V in HBM; also in HBM individuals with enlarged mandible and torus palatinus; abolishes interaction with MESD; impairs transport to cell surface; no enhancement of DKK1 binding by MESD resulting in impaired inhibition of Wnt signaling by DKK1. 4 PublicationsCorresponds to variant dbSNP:rs121908668EnsemblClinVar.1
Natural variantiVAR_018465173T → M in EVR4; an individual with abnormal retinal vasculature and retinal folds. 2 PublicationsCorresponds to variant dbSNP:rs80358306Ensembl.1
Natural variantiVAR_063945203D → N in OPPG. 1 PublicationCorresponds to variant dbSNP:rs760548029Ensembl.1
Natural variantiVAR_021810214A → T in WENHY. 1 PublicationCorresponds to variant dbSNP:rs121908671EnsemblClinVar.1
Natural variantiVAR_021811214A → V in WENHY. 1 PublicationCorresponds to variant dbSNP:rs121908672EnsemblClinVar.1
Natural variantiVAR_021812242A → T in OPTA1, VBCH2 and WENHY. 1 PublicationCorresponds to variant dbSNP:rs121908670EnsemblClinVar.1
Natural variantiVAR_063946244T → M in OPPG; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 1 PublicationCorresponds to variant dbSNP:rs397514665EnsemblClinVar.1
Natural variantiVAR_021813253T → I in OPTA1. 1 PublicationCorresponds to variant dbSNP:rs121908673EnsemblClinVar.1
Natural variantiVAR_063412282M → V in HBM; unknown pathological significance; lowered LRP5-mediated Wnt signaling; no effect on DKK1 binding. 1 Publication1
Natural variantiVAR_063947307S → F in OPPG. 1 PublicationCorresponds to variant dbSNP:rs1219101402Ensembl.1
Natural variantiVAR_063948348R → W in OPPG and EVR1; reduces Norrin signal transduction. 2 PublicationsCorresponds to variant dbSNP:rs1320065036Ensembl.1
Natural variantiVAR_063949353R → Q in OPPG. 1 Publication1
Natural variantiVAR_063950356S → L in idiopathic osteoporosis and OPPG; appears to traffic comparably than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 2 PublicationsCorresponds to variant dbSNP:rs1158745675Ensembl.1
Natural variantiVAR_076548381D → N in EVR1; reduces Norrin signal transduction. 1 PublicationCorresponds to variant dbSNP:rs1332274863Ensembl.1
Natural variantiVAR_063951390T → K in OPPG; is unable to traffic normally; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 1 Publication1
Natural variantiVAR_063952400A → E in OPPG. 1 PublicationCorresponds to variant dbSNP:rs201320326Ensembl.1
Natural variantiVAR_063953404G → R in OPPG; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; has 50% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 1 PublicationCorresponds to variant dbSNP:rs750791263Ensembl.1
Natural variantiVAR_063954409T → A in OPPG. 1 PublicationCorresponds to variant dbSNP:rs1273567061Ensembl.1
Natural variantiVAR_071012422A → T in EVR4; the mutation results in significantly reduced Norrin signal transduction. 1 PublicationCorresponds to variant dbSNP:rs774342727Ensembl.1
Natural variantiVAR_063955434D → N in OPPG; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; has 50% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 1 PublicationCorresponds to variant dbSNP:rs757888034Ensembl.1
Natural variantiVAR_063956441E → K in EVR4. 1 PublicationCorresponds to variant dbSNP:rs376152274Ensembl.1
Natural variantiVAR_063957444R → C in EVR4; associated in a EVR1 patient with mutation GLN-417 in FZD4. 1 PublicationCorresponds to variant dbSNP:rs80358308EnsemblClinVar.1
Natural variantiVAR_080857454V → M in PCLD4; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs373910016EnsemblClinVar.1
Natural variantiVAR_063958455S → L in idiopathic osteoporosis; shows an inhibitory effect on Wnt signal transduction. 1 PublicationCorresponds to variant dbSNP:rs930355318Ensembl.1
Natural variantiVAR_063959460E → K in OPPG. 1 PublicationCorresponds to variant dbSNP:rs866606166Ensembl.1
Natural variantiVAR_063960478W → R in OPPG. 1 PublicationCorresponds to variant dbSNP:rs1318906451Ensembl.1
Natural variantiVAR_021814494R → Q in OPPG. 2 PublicationsCorresponds to variant dbSNP:rs121908664EnsemblClinVar.1
Natural variantiVAR_063961504W → C in OPPG. 1 PublicationCorresponds to variant dbSNP:rs545508982Ensembl.1
Natural variantiVAR_063962511D → A in EVR4. 1 PublicationCorresponds to variant dbSNP:rs1245625202Ensembl.1
Natural variantiVAR_063963520G → V in OPPG; appears to traffic comparably than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; is unable to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 1 Publication1
Natural variantiVAR_063964522A → T in EVR4. 1 PublicationCorresponds to variant dbSNP:rs80358309Ensembl.1
Natural variantiVAR_063965531N → I in OPPG. 1 Publication1
Natural variantiVAR_063966535T → M in EVR4; autosomal recessive. 1 PublicationCorresponds to variant dbSNP:rs80358310Ensembl.1
Natural variantiVAR_071013540L → P in EVR4; the mutation results in significantly reduced Norrin signal transduction. 1 Publication1
Natural variantiVAR_063967550G → R in EVR4; autosomal recessive. 1 PublicationCorresponds to variant dbSNP:rs80358311Ensembl.1
Natural variantiVAR_080858560W → C Found in a family affected by polycystic kidney and liver disease; unknown pathological significance; the patients carried additional PKD1 variants; the mutation results in significantly reduced WNT3A-induced signaling pathway. 1 PublicationCorresponds to variant dbSNP:rs377144001EnsemblClinVar.1
Natural variantiVAR_021222570R → Q in EVR4; autosomal recessive; has significantly reduced Wnt or Norrin signal transduction. 2 PublicationsCorresponds to variant dbSNP:rs80358312EnsemblClinVar.1
Natural variantiVAR_021815570R → W in OPPG. 2 PublicationsCorresponds to variant dbSNP:rs121908665EnsemblClinVar.1
Natural variantiVAR_063968610G → R in EVR4 and OPPG; appears to traffic less well than does the wild-type protein; appears to be post-translationally modified similar to wild-type protein; has 60% of wild-type activity to transduce Wnt signal; has a significantly reduced ability to transduce Norrin signal. 2 PublicationsCorresponds to variant dbSNP:rs80358313EnsemblClinVar.1
Natural variantiVAR_063969617F → C in EVR4; autosomal recessive. 1 PublicationCorresponds to variant dbSNP:rs80358314Ensembl.1
Natural variantiVAR_076549624R → W in EVR1; reduces Norrin signal transduction. 1 PublicationCorresponds to variant dbSNP:rs989864153Ensembl.1
Natural variantiVAR_080935638K → E in PCLD4; unknown pathological significance; the patient carried additional PKHD1 variant. 1 PublicationCorresponds to variant dbSNP:rs758976409Ensembl.1
Natural variantiVAR_021816667V → M3 PublicationsCorresponds to variant dbSNP:rs4988321EnsemblClinVar.1
Natural variantiVAR_063970683D → N in OPPG. 1 PublicationCorresponds to variant dbSNP:rs1470530779Ensembl.1
Natural variantiVAR_080936684V → A in PCLD4; unknown pathological significance; the patient carried additional PKHD1 variant. 1 PublicationCorresponds to variant dbSNP:rs1339222045Ensembl.1
Natural variantiVAR_063971733Y → H in OPPG. 1 PublicationCorresponds to variant dbSNP:rs746701187Ensembl.1
Natural variantiVAR_021223752R → G in EVR4; autosomal recessive. 1 PublicationCorresponds to variant dbSNP:rs121908674EnsemblClinVar.1
Natural variantiVAR_063972798T → A in EVR4. 1 PublicationCorresponds to variant dbSNP:rs80358316Ensembl.1
Natural variantiVAR_063973805R → W in EVR4. 1 PublicationCorresponds to variant dbSNP:rs765952535Ensembl.1
Natural variantiVAR_071014816Q → P Rare polymorphism; no effect on Norrin signal transduction. 1 Publication1
Natural variantiVAR_071015852T → M in EVR4; de novo mutation found in a patient also carrying mutation P-540; unknown pathological significance; the mutation results in significantly reduced Norrin signal transduction. 1 PublicationCorresponds to variant dbSNP:rs1398692057Ensembl.1
Natural variantiVAR_080937925R → C in PCLD4; unknown pathological significance; the patient carried additional PKHD1 variant. 1 PublicationCorresponds to variant dbSNP:rs369471051Ensembl.1
Natural variantiVAR_0639741036R → Q in primary osteoporosis; unknown pathological significance; found in a patient affected by polycystic kidney disease; unknown pathological significance. 2 PublicationsCorresponds to variant dbSNP:rs61889560EnsemblClinVar.1
Natural variantiVAR_0639751099D → Y in OPPG. 1 Publication1
Natural variantiVAR_0639761113R → C in OPPG. 1 PublicationCorresponds to variant dbSNP:rs377258285Ensembl.1
Natural variantiVAR_0639771121N → D in EVR4; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs80358317EnsemblClinVar.1
Natural variantiVAR_0808591135R → C1 PublicationCorresponds to variant dbSNP:rs143396225EnsemblClinVar.1
Natural variantiVAR_0808601156Q → H Found in a patient affected by polycystic kidney disease; unknown pathological significance; the patient carried pathogenic PKD1 variant; the mutation results in significantly reduced WNT3A-induced signaling pathway. 1 PublicationCorresponds to variant dbSNP:rs724159825EnsemblClinVar.1
Natural variantiVAR_0184661168Y → H in EVR4; an individual with total retinal detachment and retinoschisis; is unable to transduce Wnt or Norrin signal transduction. 2 PublicationsCorresponds to variant dbSNP:rs80358318Ensembl.1
Natural variantiVAR_0808611188R → W in PCLD4; the mutation results in significantly reduced WNT3A-induced signaling pathway. 1 PublicationCorresponds to variant dbSNP:rs141178995EnsemblClinVar.1
Natural variantiVAR_0352081204V → L. Corresponds to variant dbSNP:rs11607268Ensembl.1
Natural variantiVAR_0639781253C → F in EVR4. 1 PublicationCorresponds to variant dbSNP:rs768615287Ensembl.1
Natural variantiVAR_0218171330A → V4 PublicationsCorresponds to variant dbSNP:rs3736228EnsemblClinVar.1
Natural variantiVAR_0184671361C → G in EVR4; autosomal dominant; has mildly reduced Wnt or Norrin signal transduction. 2 PublicationsCorresponds to variant dbSNP:rs80358320Ensembl.1
Natural variantiVAR_0212241367E → K in EVR4; autosomal recessive. 2 PublicationsCorresponds to variant dbSNP:rs28939709EnsemblClinVar.1
Natural variantiVAR_0639791401G → D in OPPG. 1 Publication1
Natural variantiVAR_0765501517Y → C in EVR1; decreases protein abundance. 1 PublicationCorresponds to variant dbSNP:rs201030241Ensembl.1
Natural variantiVAR_0212251525A → V2 PublicationsCorresponds to variant dbSNP:rs1127291EnsemblClinVar.1
Natural variantiVAR_0808621529R → S in PCLD4; found in a family affected by polycystic liver disease; unknown pathological significance. 1 Publication1
Natural variantiVAR_0639801537A → T Could be associated with idiopathic osteoporosis; does not result in a significant alteration of Wnt signal transduction. 1 PublicationCorresponds to variant dbSNP:rs144376510Ensembl.1
Natural variantiVAR_0639811540T → M1 PublicationCorresponds to variant dbSNP:rs141407040Ensembl.1
Natural variantiVAR_0809381541T → M in PCLD4; unknown pathological significance; the patient carried additional PKHD1 variant. 1 PublicationCorresponds to variant dbSNP:rs150862227Ensembl.1
Natural variantiVAR_0808631551D → N in PCLD4; unknown pathological significance; the mutation results in significantly reduced WNT3A-induced signaling pathway. 1 PublicationCorresponds to variant dbSNP:rs724159827EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF077820 mRNA Translation: AAC72791.1
AF064548 mRNA Translation: AAC36467.1
AF283321, AF283320 Genomic DNA Translation: AAK52433.1
AB017498 mRNA Translation: BAA33051.1
AP000807 Genomic DNA No translation available.
CH471076 Genomic DNA Translation: EAW74705.1
BC150595 mRNA Translation: AAI50596.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS8181.1

Protein sequence database of the Protein Information Resource

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PIRi
JE0372

NCBI Reference Sequences

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RefSeqi
NP_001278831.1, NM_001291902.1
NP_002326.2, NM_002335.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.6347

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000294304; ENSP00000294304; ENSG00000162337

Database of genes from NCBI RefSeq genomes

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GeneIDi
4041

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:4041

UCSC genome browser

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UCSCi
uc001ont.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077820 mRNA Translation: AAC72791.1
AF064548 mRNA Translation: AAC36467.1
AF283321, AF283320 Genomic DNA Translation: AAK52433.1
AB017498 mRNA Translation: BAA33051.1
AP000807 Genomic DNA No translation available.
CH471076 Genomic DNA Translation: EAW74705.1
BC150595 mRNA Translation: AAI50596.1
CCDSiCCDS8181.1
PIRiJE0372
RefSeqiNP_001278831.1, NM_001291902.1
NP_002326.2, NM_002335.3
UniGeneiHs.6347

3D structure databases

ProteinModelPortaliO75197
SMRiO75197
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110220, 44 interactors
CORUMiO75197
DIPiDIP-47265N
ELMiO75197
IntActiO75197, 10 interactors
MINTiO75197
STRINGi9606.ENSP00000294304

PTM databases

GlyConnecti1468
iPTMnetiO75197
PhosphoSitePlusiO75197

Polymorphism and mutation databases

BioMutaiLRP5

Proteomic databases

EPDiO75197
jPOSTiO75197
PaxDbiO75197
PeptideAtlasiO75197
PRIDEiO75197
ProteomicsDBi49865

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000294304; ENSP00000294304; ENSG00000162337
GeneIDi4041
KEGGihsa:4041
UCSCiuc001ont.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4041
DisGeNETi4041
EuPathDBiHostDB:ENSG00000162337.11

GeneCards: human genes, protein and diseases

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GeneCardsi
LRP5
GeneReviewsiLRP5
HGNCiHGNC:6697 LRP5
HPAiCAB013001
HPA030505
MalaCardsiLRP5
MIMi133780 phenotype
144750 phenotype
166710 phenotype
259770 phenotype
601813 phenotype
601884 phenotype
603506 gene
607634 phenotype
607636 phenotype
617875 phenotype
neXtProtiNX_O75197
OpenTargetsiENSG00000162337
Orphaneti2783 Autosomal dominant osteopetrosis type 1
2790 Endosteal hyperostosis, Worth type
891 Familial exudative vitreoretinopathy
3416 Hyperostosis corticalis generalisata
2924 Isolated polycystic liver disease
498481 LRP5-related primary osteoporosis
2788 Osteoporosis-pseudoglioma syndrome
178377 Osteosclerosis-developmental delay-craniosynostosis syndrome
90050 Retinopathy of prematurity
PharmGKBiPA30455

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IPT4 Eukaryota
ENOG410XSY5 LUCA
GeneTreeiENSGT00940000156574
HOGENOMiHOG000230697
HOVERGENiHBG049167
InParanoidiO75197
KOiK03068
OMAiPFTGISC
OrthoDBi1349932at2759
PhylomeDBiO75197
TreeFamiTF315253

Enzyme and pathway databases

ReactomeiR-HSA-201681 TCF dependent signaling in response to WNT
R-HSA-3772470 Negative regulation of TCF-dependent signaling by WNT ligand antagonists
R-HSA-4641262 Disassembly of the destruction complex and recruitment of AXIN to the membrane
R-HSA-4641263 Regulation of FZD by ubiquitination
R-HSA-5339717 Misspliced LRP5 mutants have enhanced beta-catenin-dependent signaling
R-HSA-5340588 RNF mutants show enhanced WNT signaling and proliferation
SignaLinkiO75197
SIGNORiO75197

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
LRP5 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
LRP5

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
4041

Protein Ontology

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PROi
PR:O75197

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000162337 Expressed in 171 organ(s), highest expression level in right lobe of liver
CleanExiHS_LRP5
ExpressionAtlasiO75197 baseline and differential
GenevisibleiO75197 HS

Family and domain databases

CDDicd00112 LDLa, 3 hits
Gene3Di2.120.10.30, 4 hits
InterProiView protein in InterPro
IPR011042 6-blade_b-propeller_TolB-like
IPR000742 EGF-like_dom
IPR036055 LDL_receptor-like_sf
IPR023415 LDLR_class-A_CS
IPR000033 LDLR_classB_rpt
IPR002172 LDrepeatLR_classA_rpt
IPR017049 LRP5/6
PfamiView protein in Pfam
PF00057 Ldl_recept_a, 3 hits
PF00058 Ldl_recept_b, 13 hits
PIRSFiPIRSF036314 LDL_recpt-rel_p5/6, 1 hit
PRINTSiPR00261 LDLRECEPTOR
SMARTiView protein in SMART
SM00181 EGF, 4 hits
SM00192 LDLa, 3 hits
SM00135 LY, 20 hits
SUPFAMiSSF57424 SSF57424, 3 hits
PROSITEiView protein in PROSITE
PS01209 LDLRA_1, 3 hits
PS50068 LDLRA_2, 3 hits
PS51120 LDLRB, 20 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiLRP5_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: O75197
Secondary accession number(s): Q96TD6, Q9UES7, Q9UP66
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: April 12, 2005
Last modified: January 16, 2019
This is version 187 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
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