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Entry version 216 (13 Nov 2019)
Sequence version 2 (11 Jan 2011)
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Protein

Prolow-density lipoprotein receptor-related protein 1

Gene

LRP1

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

Endocytic receptor involved in endocytosis and in phagocytosis of apoptotic cells. Required for early embryonic development. Involved in cellular lipid homeostasis. Involved in the plasma clearance of chylomicron remnants and activated LRPAP1 (alpha 2-macroglobulin), as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate cellular events, such as APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission (PubMed:11907044, PubMed:12888553, PubMed:12713657). Acts as an alpha-2-macroglobulin receptor (PubMed:26142438).4 Publications
(Microbial infection) Functions as a receptor for Pseudomonas aeruginosa exotoxin A.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi871Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi874Calcium 11 Publication1
Metal bindingi876Calcium 1; via carbonyl oxygen1 Publication1
Metal bindingi878Calcium 11 Publication1
Metal bindingi884Calcium 11 Publication1
Metal bindingi885Calcium 11 Publication1
Metal bindingi1032Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi1035Calcium 21 Publication1
Metal bindingi1037Calcium 2; via carbonyl oxygen1 Publication1
Metal bindingi1039Calcium 21 Publication1
Metal bindingi1045Calcium 21 Publication1
Metal bindingi1046Calcium 21 Publication1
Metal bindingi1080Calcium 3; via carbonyl oxygen1 Publication1
Metal bindingi1083Calcium 31 Publication1
Metal bindingi1085Calcium 3; via carbonyl oxygen1 Publication1
Metal bindingi1087Calcium 31 Publication1
Metal bindingi1093Calcium 31 Publication1
Metal bindingi1094Calcium 31 Publication1

<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

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
LigandCalcium, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-2168880 Scavenging of heme from plasma
R-HSA-975634 Retinoid metabolism and transport

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q07954

Protein family/group databases

Transport Classification Database

More...
TCDBi
9.B.87.1.16 the selenoprotein p receptor (selp-receptor) family

<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:
Prolow-density lipoprotein receptor-related protein 1
Short name:
LRP-1
Alternative name(s):
Alpha-2-macroglobulin receptor1 Publication
Short name:
A2MR
Apolipoprotein E receptor
Short name:
APOER
CD_antigen: CD91
Cleaved into the following 3 chains:
<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:LRP1
Synonyms:A2MR, APR
<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 12

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:6692 LRP1

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
107770 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q07954

<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 & Seán O’Donoghue; 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 domaini20 – 4419ExtracellularSequence analysisAdd BLAST4400
<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>Transmembranei4420 – 4444HelicalSequence analysisAdd BLAST25
Topological domaini4445 – 4544CytoplasmicSequence analysisAdd BLAST100

Keywords - Cellular componenti

Cell junction, Cell membrane, Coated pit, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane, Nucleus, Synapse

<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

Keratosis pilaris atrophicans (KPA)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA group of rare genodermatoses characterized by keratotic follicular papules, variable degrees of inflammation, and secondary atrophic scarring. Most cases are associated with an atopic diathesis and keratosis pilaris on the extensor extremities. KPA is comprised of three distinct clinical subtypes: keratosis pilaris atrophicans faciei, atrophoderma vermiculatum, and keratosis follicularis spinulosa decalvans. Affected individuals may present with features overlapping the 3 subtypes.
Related information in OMIM
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_0779821245K → R in KPA; reduced alpha-2 macroglobulin receptor activity; reduced protein abundance. 1 PublicationCorresponds to variant dbSNP:rs483353013EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi4460T → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4517; A-4520 and A-4523. 1 Publication1
Mutagenesisi4470 – 4473NPTY → APTA: No effect on tyrosine phosphorylation. 1 Publication4
Mutagenesisi4470N → A: No effect on interaction with GULP1. 1 Publication1
Mutagenesisi4472T → A: No detectable effect on phosphorylation. 1 Publication1
Mutagenesisi4504 – 4507NPVY → APVA: Loss of tyrosine phosphorylation. Abolishes interaction with SHC1 and GULP1. 1 Publication4
Mutagenesisi4504N → A: Loss of interaction with GULP1. 1 Publication1
Mutagenesisi4517S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4520 and A-4523. 1 Publication1
Mutagenesisi4520S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4523. 1 Publication1
Mutagenesisi4523S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4520. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
4035

MalaCards human disease database

More...
MalaCardsi
LRP1
MIMi604093 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000123384

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

More...
Orphaneti
79100 Atrophoderma vermiculata
2340 Keratosis follicularis spinulosa decalvans

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA233

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q07954

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB00025 Antihemophilic factor, human recombinant
DB00100 Coagulation Factor IX (Recombinant)
DB13152 Coagulation Factor IX Human
DB06245 Lanoteplase
DB13998 Lonoctocog alfa
DB13999 Moroctocog alfa
DB00031 Tenecteplase

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
LRP1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
317373384

<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 – 19Sequence analysisAdd BLAST19
<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_000001731720 – 4544Prolow-density lipoprotein receptor-related protein 1Add BLAST4525
ChainiPRO_000030275020 – ?3943Low-density lipoprotein receptor-related protein 1 515 kDa subunitAdd BLAST3924
ChainiPRO_0000302751?3944 – 4544Low-density lipoprotein receptor-related protein 1 85 kDa subunitAdd BLAST601
ChainiPRO_0000302752?4441 – 4544Low-density lipoprotein receptor-related protein 1 intracellular domainAdd BLAST104

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 bondi27 ↔ 40By similarity
Disulfide bondi34 ↔ 53By similarity
Disulfide bondi47 ↔ 64By similarity
Disulfide bondi72 ↔ 85By similarity
Disulfide bondi79 ↔ 98By similarity
Disulfide bondi92 ↔ 108By similarity
<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>Glycosylationi114N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi115 ↔ 124By similarity
Disulfide bondi120 ↔ 133By similarity
Disulfide bondi135 ↔ 148By similarity
Glycosylationi136N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi154 ↔ 164By similarity
Disulfide bondi160 ↔ 173By similarity
Disulfide bondi175 ↔ 188By similarity
Glycosylationi185N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi239N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi274N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi357N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi446N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi478 ↔ 493By similarity
Disulfide bondi489 ↔ 504By similarity
Disulfide bondi506 ↔ 519By similarity
Glycosylationi729N-linked (GlcNAc...) (complex) asparagine3 Publications1
Disulfide bondi807 ↔ 818By similarity
Disulfide bondi814 ↔ 827By similarity
Disulfide bondi829 ↔ 842By similarity
Disulfide bondi854 ↔ 866
Disulfide bondi861 ↔ 879
Disulfide bondi873 ↔ 890
Disulfide bondi895 ↔ 907By similarity
Disulfide bondi902 ↔ 920By similarity
Disulfide bondi914 ↔ 931By similarity
Glycosylationi928N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi936 ↔ 948
Disulfide bondi943 ↔ 961
Disulfide bondi955 ↔ 971
Disulfide bondi976 ↔ 989
Disulfide bondi984 ↔ 1002
Disulfide bondi996 ↔ 1011
Disulfide bondi1015 ↔ 1027
Disulfide bondi1022 ↔ 1040
Disulfide bondi1034 ↔ 1051
Glycosylationi1050N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1062 ↔ 1075
Disulfide bondi1069 ↔ 1088
Disulfide bondi1082 ↔ 1097
Disulfide bondi1104 ↔ 1118By similarity
Disulfide bondi1112 ↔ 1131By similarity
Disulfide bondi1125 ↔ 1140By similarity
Disulfide bondi1145 ↔ 1159By similarity
Disulfide bondi1152 ↔ 1172By similarity
Glycosylationi1154N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1155N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1166 ↔ 1182By similarity
Disulfide bondi1185 ↔ 1196By similarity
Disulfide bondi1192 ↔ 1206By similarity
Glycosylationi1195N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1208 ↔ 1221By similarity
Glycosylationi1218N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1227 ↔ 1237By similarity
Disulfide bondi1233 ↔ 1246By similarity
Disulfide bondi1248 ↔ 1261By similarity
Glycosylationi1511N-linked (GlcNAc...) (complex) asparagine2 Publications1
Disulfide bondi1540 ↔ 1553By similarity
Disulfide bondi1549 ↔ 1563By similarity
Glycosylationi1558N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1565 ↔ 1578By similarity
Glycosylationi1575N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1616N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1645N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1723N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1733N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1763N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1825N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1850 ↔ 1861By similarity
Disulfide bondi1857 ↔ 1871By similarity
Disulfide bondi1873 ↔ 1886By similarity
Glycosylationi1933N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1995N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2009N6-acetyllysineBy similarity1
Glycosylationi2048N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2117N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2127N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi2159 ↔ 2170By similarity
Disulfide bondi2166 ↔ 2180By similarity
Disulfide bondi2182 ↔ 2194By similarity
Glycosylationi2472N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2482 ↔ 2493By similarity
Disulfide bondi2489 ↔ 2503By similarity
Glycosylationi2502N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2505 ↔ 2517By similarity
Glycosylationi2521N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2524 ↔ 2537By similarity
Disulfide bondi2532 ↔ 2550By similarity
Glycosylationi2539N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2544 ↔ 2561By similarity
Disulfide bondi2566 ↔ 2578By similarity
Disulfide bondi2573 ↔ 2591By similarity
Disulfide bondi2585 ↔ 2600By similarity
Glycosylationi2601N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2605 ↔ 2617By similarity
Disulfide bondi2612 ↔ 2630By similarity
Glycosylationi2620N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2624 ↔ 2639By similarity
Glycosylationi2638N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2644 ↔ 2666By similarity
Disulfide bondi2660 ↔ 2679By similarity
Disulfide bondi2673 ↔ 2688By similarity
Disulfide bondi2696 ↔ 2708By similarity
Disulfide bondi2703 ↔ 2721By similarity
Disulfide bondi2715 ↔ 2730By similarity
Disulfide bondi2734 ↔ 2746By similarity
Disulfide bondi2741 ↔ 2759By similarity
Disulfide bondi2753 ↔ 2769By similarity
Disulfide bondi2774 ↔ 2787By similarity
Disulfide bondi2781 ↔ 2800By similarity
Disulfide bondi2794 ↔ 2812By similarity
Glycosylationi2815N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi2818 ↔ 2830By similarity
Disulfide bondi2825 ↔ 2843By similarity
Disulfide bondi2837 ↔ 2853By similarity
Disulfide bondi2858 ↔ 2870By similarity
Disulfide bondi2865 ↔ 2884By similarity
Disulfide bondi2878 ↔ 2897By similarity
Disulfide bondi2904 ↔ 2917By similarity
Glycosylationi2905N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi2912 ↔ 2930By similarity
Disulfide bondi2924 ↔ 2939By similarity
Disulfide bondi2944 ↔ 2956By similarity
Disulfide bondi2952 ↔ 2965By similarity
Disulfide bondi2967 ↔ 2980By similarity
Disulfide bondi2986 ↔ 2996By similarity
Disulfide bondi2992 ↔ 3005By similarity
Disulfide bondi3007 ↔ 3021By similarity
Glycosylationi3048N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi3089N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi3264N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3294 ↔ 3305By similarity
Disulfide bondi3301 ↔ 3315By similarity
Disulfide bondi3317 ↔ 3330By similarity
Glycosylationi3333N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3334 ↔ 3346By similarity
Disulfide bondi3341 ↔ 3359By similarity
Disulfide bondi3353 ↔ 3369By similarity
Disulfide bondi3374 ↔ 3386By similarity
Disulfide bondi3381 ↔ 3399By similarity
Disulfide bondi3393 ↔ 3408By similarity
Disulfide bondi3413 ↔ 3426By similarity
Disulfide bondi3420 ↔ 3439By similarity
Disulfide bondi3433 ↔ 3448By similarity
Disulfide bondi3453 ↔ 3466By similarity
Disulfide bondi3460 ↔ 3479By similarity
Disulfide bondi3473 ↔ 3489By similarity
Glycosylationi3488N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi3494 ↔ 3507By similarity
Disulfide bondi3501 ↔ 3520By similarity
Disulfide bondi3514 ↔ 3531By similarity
Disulfide bondi3536 ↔ 3548By similarity
Disulfide bondi3543 ↔ 3561By similarity
Disulfide bondi3555 ↔ 3570By similarity
Disulfide bondi3575 ↔ 3587By similarity
Disulfide bondi3582 ↔ 3600By similarity
Disulfide bondi3594 ↔ 3609By similarity
Disulfide bondi3613 ↔ 3625By similarity
Disulfide bondi3620 ↔ 3638By similarity
Disulfide bondi3632 ↔ 3647By similarity
Disulfide bondi3654 ↔ 3666By similarity
Disulfide bondi3661 ↔ 3679By similarity
Glycosylationi3662N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3673 ↔ 3690By similarity
Disulfide bondi3695 ↔ 3709By similarity
Disulfide bondi3703 ↔ 3722By similarity
Disulfide bondi3716 ↔ 3731By similarity
Disulfide bondi3741 ↔ 3754By similarity
Disulfide bondi3749 ↔ 3767By similarity
Disulfide bondi3761 ↔ 3776By similarity
Disulfide bondi3785 ↔ 3798By similarity
Glycosylationi3788N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi3792 ↔ 3807By similarity
Disulfide bondi3809 ↔ 3822By similarity
Disulfide bondi3828 ↔ 3838By similarity
Disulfide bondi3834 ↔ 3847By similarity
Glycosylationi3839N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi3849 ↔ 3860By similarity
Glycosylationi3953N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi4075N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi4125N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi4151 ↔ 4160By similarity
Disulfide bondi4156 ↔ 4169By similarity
Disulfide bondi4171 ↔ 4182By similarity
Glycosylationi4179N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi4200 ↔ 4210By similarity
Disulfide bondi4204 ↔ 4220By similarity
Disulfide bondi4222 ↔ 4231By similarity
Disulfide bondi4236 ↔ 4246By similarity
Disulfide bondi4240 ↔ 4256By similarity
Disulfide bondi4258 ↔ 4267By similarity
Disulfide bondi4272 ↔ 4282By similarity
Disulfide bondi4276 ↔ 4292By similarity
Glycosylationi4278N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi4279N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi4294 ↔ 4303By similarity
Disulfide bondi4308 ↔ 4318By similarity
Disulfide bondi4312 ↔ 4328By similarity
Disulfide bondi4330 ↔ 4339By similarity
Disulfide bondi4344 ↔ 4352By similarity
Disulfide bondi4347 ↔ 4363By similarity
Glycosylationi4364N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi4365 ↔ 4374By similarity
Disulfide bondi4377 ↔ 4387By similarity
Disulfide bondi4381 ↔ 4397By similarity
Disulfide bondi4399 ↔ 4408By similarity
Modified residuei4460Phosphothreonine1 Publication1
Modified residuei4507Phosphotyrosine1 Publication1
Modified residuei4517Phosphoserine1 Publication1
Modified residuei4520PhosphoserineCombined sources1
Modified residuei4523Phosphoserine1 Publication1

<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

Cleaved into a 85 kDa membrane-spanning subunit (LRP-85) and a 515 kDa large extracellular domain (LRP-515) that remains non-covalently associated. Gamma-secretase-dependent cleavage of LRP-85 releases the intracellular domain from the membrane.2 Publications
The N-terminus is blocked.
Phosphorylated on serine and threonine residues.
Phosphorylated on tyrosine residues upon stimulation with PDGF. Tyrosine phosphorylation promotes interaction with SHC1.

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...
CPTACi
CPTAC-2222
CPTAC-2223

Encyclopedia of Proteome Dynamics

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EPDi
Q07954

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q07954

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
Q07954

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q07954

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

More...
PaxDbi
Q07954

PeptideAtlas

More...
PeptideAtlasi
Q07954

PRoteomics IDEntifications database

More...
PRIDEi
Q07954

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
58559 [Q07954-1]
69639

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
Q07954

GlyConnect protein glycosylation platform

More...
GlyConnecti
1638

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q07954

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

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PhosphoSitePlusi
Q07954

<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

Most abundant in liver, brain and lung.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000123384 Expressed in 230 organ(s), highest expression level in thoracic aorta

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q07954 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q07954 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB018621
HPA004182
HPA022903

<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

Heterodimer of an 85-kDa membrane-bound carboxyl subunit and a non-covalently attached 515-kDa N-terminal subunit. Intracellular domain interacts with MAFB (By similarity).

Found in a complex with PID1/PCLI1, LRP1 and CUBNI.

Interacts with SNX17, PID1/PCLI1, PDGF and CUBN. The intracellular domain interacts with SHC1, GULP1 and DAB1.

Interacts with LRPAP1. Can weakly interact (via NPXY motif) with DAB2 (via PID domain); the interaction is enhanced by tyrosine phosphorylation of the NPXY motif.

Interacts with bacterial exotoxins.

Interacts with MDK; promotes neuronal survival (PubMed:10772929).

Interacts with uPA/PLAU and PAI1/SERPINE1, either individually or in complex with each other, leading to rapid endocytosis; this interaction is abolished in the presence of LRPAP1/RAP (PubMed:15053742).

Also interacts with tPA/PLAT alone or in complex with SERPINE1 (PubMed:15053742).

Interacts with the urokinase receptor PLAUR; this interaction leads to PLAUR internalization and is impaired in the presence of SORL1 (PubMed:14764453).

Interacts with LRPAP1; this interaction is followed by rapid internalization (PubMed:15053742).

Interacts with PDGFB (PubMed:15053742).

By similarity12 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
110215, 126 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-4310 Prolow-density lipoprotein receptor-related protein 1 complex

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q07954

Database of interacting proteins

More...
DIPi
DIP-50613N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
Q07954

Protein interaction database and analysis system

More...
IntActi
Q07954, 80 interactors

Molecular INTeraction database

More...
MINTi
Q07954

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000243077

<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

Secondary structure

14544
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q07954

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q07954

<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 <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>Domaini25 – 66LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST42
Domaini70 – 110LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST41
Domaini111 – 149EGF-like 1PROSITE-ProRule annotationAdd BLAST39
Domaini150 – 189EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
<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>Repeati292 – 334LDL-receptor class B 1Add BLAST43
Repeati335 – 378LDL-receptor class B 2Add BLAST44
Repeati379 – 422LDL-receptor class B 3Add BLAST44
Domaini474 – 520EGF-like 3PROSITE-ProRule annotationAdd BLAST47
Repeati571 – 613LDL-receptor class B 4Add BLAST43
Repeati614 – 659LDL-receptor class B 5Add BLAST46
Repeati660 – 710LDL-receptor class B 6Add BLAST51
Repeati711 – 754LDL-receptor class B 7Add BLAST44
Domaini803 – 843EGF-like 4PROSITE-ProRule annotationAdd BLAST41
Domaini852 – 892LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST41
Domaini893 – 933LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST41
Domaini934 – 973LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST40
Domaini974 – 1013LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST40
Domaini1013 – 1053LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST41
Domaini1060 – 1099LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST40
Domaini1102 – 1142LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST41
Domaini1143 – 1182LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST40
Domaini1183 – 1222EGF-like 5PROSITE-ProRule annotationAdd BLAST40
Domaini1223 – 1262EGF-like 6PROSITE-ProRule annotationAdd BLAST40
Repeati1309 – 1355LDL-receptor class B 8Add BLAST47
Repeati1356 – 1398LDL-receptor class B 9Add BLAST43
Repeati1399 – 1445LDL-receptor class B 10Add BLAST47
Repeati1446 – 1490LDL-receptor class B 11Add BLAST45
Repeati1491 – 1531LDL-receptor class B 12Add BLAST41
Domaini1536 – 1579EGF-like 7PROSITE-ProRule annotationAdd BLAST44
Repeati1627 – 1669LDL-receptor class B 13Add BLAST43
Repeati1670 – 1713LDL-receptor class B 14Add BLAST44
Repeati1714 – 1753LDL-receptor class B 15Add BLAST40
Repeati1754 – 1798LDL-receptor class B 16Add BLAST45
Domaini1846 – 1887EGF-like 8PROSITE-ProRule annotationAdd BLAST42
Repeati1934 – 1976LDL-receptor class B 17Add BLAST43
Repeati1977 – 2019LDL-receptor class B 18Add BLAST43
Repeati2020 – 2063LDL-receptor class B 19Add BLAST44
Repeati2064 – 2107LDL-receptor class B 20Add BLAST44
Domaini2155 – 2195EGF-like 9PROSITE-ProRule annotationAdd BLAST41
Repeati2253 – 2294LDL-receptor class B 21Add BLAST42
Repeati2295 – 2343LDL-receptor class B 22Add BLAST49
Repeati2344 – 2388LDL-receptor class B 23Add BLAST45
Repeati2389 – 2431LDL-receptor class B 24Add BLAST43
Repeati2432 – 2473LDL-receptor class B 25Add BLAST42
Domaini2478 – 2518EGF-like 10PROSITE-ProRule annotationAdd BLAST41
Domaini2522 – 2563LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST42
Domaini2564 – 2602LDL-receptor class A 12PROSITE-ProRule annotationAdd BLAST39
Domaini2603 – 2641LDL-receptor class A 13PROSITE-ProRule annotationAdd BLAST39
Domaini2642 – 2690LDL-receptor class A 14PROSITE-ProRule annotationAdd BLAST49
Domaini2694 – 2732LDL-receptor class A 15PROSITE-ProRule annotationAdd BLAST39
Domaini2732 – 2771LDL-receptor class A 16PROSITE-ProRule annotationAdd BLAST40
Domaini2772 – 2814LDL-receptor class A 17PROSITE-ProRule annotationAdd BLAST43
Domaini2816 – 2855LDL-receptor class A 18PROSITE-ProRule annotationAdd BLAST40
Domaini2856 – 2899LDL-receptor class A 19PROSITE-ProRule annotationAdd BLAST44
Domaini2902 – 2940LDL-receptor class A 20PROSITE-ProRule annotationAdd BLAST39
Domaini2941 – 2981EGF-like 11PROSITE-ProRule annotationAdd BLAST41
Domaini2982 – 3022EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST41
Repeati3069 – 3113LDL-receptor class B 26Add BLAST45
Repeati3114 – 3156LDL-receptor class B 27Add BLAST43
Repeati3157 – 3200LDL-receptor class B 28Add BLAST44
Repeati3201 – 3243LDL-receptor class B 29Add BLAST43
Repeati3244 – 3284LDL-receptor class B 30Add BLAST41
Domaini3290 – 3331EGF-like 13PROSITE-ProRule annotationAdd BLAST42
Domaini3332 – 3371LDL-receptor class A 21PROSITE-ProRule annotationAdd BLAST40
Domaini3372 – 3410LDL-receptor class A 22PROSITE-ProRule annotationAdd BLAST39
Domaini3411 – 3450LDL-receptor class A 23PROSITE-ProRule annotationAdd BLAST40
Domaini3451 – 3491LDL-receptor class A 24PROSITE-ProRule annotationAdd BLAST41
Domaini3492 – 3533LDL-receptor class A 25PROSITE-ProRule annotationAdd BLAST42
Domaini3534 – 3572LDL-receptor class A 26PROSITE-ProRule annotationAdd BLAST39
Domaini3573 – 3611LDL-receptor class A 27PROSITE-ProRule annotationAdd BLAST39
Domaini3611 – 3649LDL-receptor class A 28PROSITE-ProRule annotationAdd BLAST39
Domaini3652 – 3692LDL-receptor class A 29PROSITE-ProRule annotationAdd BLAST41
Domaini3693 – 3733LDL-receptor class A 30PROSITE-ProRule annotationAdd BLAST41
Domaini3739 – 3778LDL-receptor class A 31PROSITE-ProRule annotationAdd BLAST40
Domaini3781 – 3823EGF-like 14PROSITE-ProRule annotationAdd BLAST43
Domaini3824 – 3861EGF-like 15PROSITE-ProRule annotationAdd BLAST38
Repeati3912 – 3954LDL-receptor class B 31Add BLAST43
Repeati3970 – 4012LDL-receptor class B 32Add BLAST43
Repeati4013 – 4056LDL-receptor class B 33Add BLAST44
Repeati4057 – 4101LDL-receptor class B 34Add BLAST45
Domaini4147 – 4183EGF-like 16PROSITE-ProRule annotationAdd BLAST37
Domaini4196 – 4232EGF-like 17PROSITE-ProRule annotationAdd BLAST37
Domaini4232 – 4268EGF-like 18PROSITE-ProRule annotationAdd BLAST37
Domaini4268 – 4304EGF-like 19PROSITE-ProRule annotationAdd BLAST37
Domaini4304 – 4340EGF-like 20PROSITE-ProRule annotationAdd BLAST37
Domaini4340 – 4375EGF-like 21PROSITE-ProRule annotationAdd BLAST36
Domaini4373 – 4409EGF-like 22PROSITE-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>Regioni4445 – 4544Interaction with MAFBBy similarityAdd BLAST100

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>Motifi3940 – 3943Recognition site for proteolytical processingSequence analysis4
Motifi4502 – 4507NPXY motif6

<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

More...
eggNOGi
KOG1215 Eukaryota
ENOG410XP34 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157899

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000230574

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q07954

KEGG Orthology (KO)

More...
KOi
K04550

Identification of Orthologs from Complete Genome Data

More...
OMAi
EPDMENC

Database of Orthologous Groups

More...
OrthoDBi
1606at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q07954

TreeFam database of animal gene trees

More...
TreeFami
TF315253

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00112 LDLa, 31 hits

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.120.10.30, 8 hits
4.10.400.10, 29 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011042 6-blade_b-propeller_TolB-like
IPR026823 cEGF
IPR032485 DUF5050
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR009030 Growth_fac_rcpt_cys_sf
IPR036055 LDL_receptor-like_sf
IPR023415 LDLR_class-A_CS
IPR000033 LDLR_classB_rpt
IPR002172 LDrepeatLR_classA_rpt

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF12662 cEGF, 1 hit
PF16472 DUF5050, 1 hit
PF07645 EGF_CA, 2 hits
PF00057 Ldl_recept_a, 29 hits
PF00058 Ldl_recept_b, 12 hits

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, 26 hits
SM00179 EGF_CA, 7 hits
SM00192 LDLa, 31 hits
SM00135 LY, 35 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF57184 SSF57184, 4 hits
SSF57424 SSF57424, 30 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00010 ASX_HYDROXYL, 3 hits
PS00022 EGF_1, 5 hits
PS01186 EGF_2, 8 hits
PS50026 EGF_3, 6 hits
PS01187 EGF_CA, 2 hits
PS01209 LDLRA_1, 27 hits
PS50068 LDLRA_2, 31 hits
PS51120 LDLRB, 34 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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)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 describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q07954-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MLTPPLLLLL PLLSALVAAA IDAPKTCSPK QFACRDQITC ISKGWRCDGE
60 70 80 90 100
RDCPDGSDEA PEICPQSKAQ RCQPNEHNCL GTELCVPMSR LCNGVQDCMD
110 120 130 140 150
GSDEGPHCRE LQGNCSRLGC QHHCVPTLDG PTCYCNSSFQ LQADGKTCKD
160 170 180 190 200
FDECSVYGTC SQLCTNTDGS FICGCVEGYL LQPDNRSCKA KNEPVDRPPV
210 220 230 240 250
LLIANSQNIL ATYLSGAQVS TITPTSTRQT TAMDFSYANE TVCWVHVGDS
260 270 280 290 300
AAQTQLKCAR MPGLKGFVDE HTINISLSLH HVEQMAIDWL TGNFYFVDDI
310 320 330 340 350
DDRIFVCNRN GDTCVTLLDL ELYNPKGIAL DPAMGKVFFT DYGQIPKVER
360 370 380 390 400
CDMDGQNRTK LVDSKIVFPH GITLDLVSRL VYWADAYLDY IEVVDYEGKG
410 420 430 440 450
RQTIIQGILI EHLYGLTVFE NYLYATNSDN ANAQQKTSVI RVNRFNSTEY
460 470 480 490 500
QVVTRVDKGG ALHIYHQRRQ PRVRSHACEN DQYGKPGGCS DICLLANSHK
510 520 530 540 550
ARTCRCRSGF SLGSDGKSCK KPEHELFLVY GKGRPGIIRG MDMGAKVPDE
560 570 580 590 600
HMIPIENLMN PRALDFHAET GFIYFADTTS YLIGRQKIDG TERETILKDG
610 620 630 640 650
IHNVEGVAVD WMGDNLYWTD DGPKKTISVA RLEKAAQTRK TLIEGKMTHP
660 670 680 690 700
RAIVVDPLNG WMYWTDWEED PKDSRRGRLE RAWMDGSHRD IFVTSKTVLW
710 720 730 740 750
PNGLSLDIPA GRLYWVDAFY DRIETILLNG TDRKIVYEGP ELNHAFGLCH
760 770 780 790 800
HGNYLFWTEY RSGSVYRLER GVGGAPPTVT LLRSERPPIF EIRMYDAQQQ
810 820 830 840 850
QVGTNKCRVN NGGCSSLCLA TPGSRQCACA EDQVLDADGV TCLANPSYVP
860 870 880 890 900
PPQCQPGEFA CANSRCIQER WKCDGDNDCL DNSDEAPALC HQHTCPSDRF
910 920 930 940 950
KCENNRCIPN RWLCDGDNDC GNSEDESNAT CSARTCPPNQ FSCASGRCIP
960 970 980 990 1000
ISWTCDLDDD CGDRSDESAS CAYPTCFPLT QFTCNNGRCI NINWRCDNDN
1010 1020 1030 1040 1050
DCGDNSDEAG CSHSCSSTQF KCNSGRCIPE HWTCDGDNDC GDYSDETHAN
1060 1070 1080 1090 1100
CTNQATRPPG GCHTDEFQCR LDGLCIPLRW RCDGDTDCMD SSDEKSCEGV
1110 1120 1130 1140 1150
THVCDPSVKF GCKDSARCIS KAWVCDGDND CEDNSDEENC ESLACRPPSH
1160 1170 1180 1190 1200
PCANNTSVCL PPDKLCDGND DCGDGSDEGE LCDQCSLNNG GCSHNCSVAP
1210 1220 1230 1240 1250
GEGIVCSCPL GMELGPDNHT CQIQSYCAKH LKCSQKCDQN KFSVKCSCYE
1260 1270 1280 1290 1300
GWVLEPDGES CRSLDPFKPF IIFSNRHEIR RIDLHKGDYS VLVPGLRNTI
1310 1320 1330 1340 1350
ALDFHLSQSA LYWTDVVEDK IYRGKLLDNG ALTSFEVVIQ YGLATPEGLA
1360 1370 1380 1390 1400
VDWIAGNIYW VESNLDQIEV AKLDGTLRTT LLAGDIEHPR AIALDPRDGI
1410 1420 1430 1440 1450
LFWTDWDASL PRIEAASMSG AGRRTVHRET GSGGWPNGLT VDYLEKRILW
1460 1470 1480 1490 1500
IDARSDAIYS ARYDGSGHME VLRGHEFLSH PFAVTLYGGE VYWTDWRTNT
1510 1520 1530 1540 1550
LAKANKWTGH NVTVVQRTNT QPFDLQVYHP SRQPMAPNPC EANGGQGPCS
1560 1570 1580 1590 1600
HLCLINYNRT VSCACPHLMK LHKDNTTCYE FKKFLLYARQ MEIRGVDLDA
1610 1620 1630 1640 1650
PYYNYIISFT VPDIDNVTVL DYDAREQRVY WSDVRTQAIK RAFINGTGVE
1660 1670 1680 1690 1700
TVVSADLPNA HGLAVDWVSR NLFWTSYDTN KKQINVARLD GSFKNAVVQG
1710 1720 1730 1740 1750
LEQPHGLVVH PLRGKLYWTD GDNISMANMD GSNRTLLFSG QKGPVGLAID
1760 1770 1780 1790 1800
FPESKLYWIS SGNHTINRCN LDGSGLEVID AMRSQLGKAT ALAIMGDKLW
1810 1820 1830 1840 1850
WADQVSEKMG TCSKADGSGS VVLRNSTTLV MHMKVYDESI QLDHKGTNPC
1860 1870 1880 1890 1900
SVNNGDCSQL CLPTSETTRS CMCTAGYSLR SGQQACEGVG SFLLYSVHEG
1910 1920 1930 1940 1950
IRGIPLDPND KSDALVPVSG TSLAVGIDFH AENDTIYWVD MGLSTISRAK
1960 1970 1980 1990 2000
RDQTWREDVV TNGIGRVEGI AVDWIAGNIY WTDQGFDVIE VARLNGSFRY
2010 2020 2030 2040 2050
VVISQGLDKP RAITVHPEKG YLFWTEWGQY PRIERSRLDG TERVVLVNVS
2060 2070 2080 2090 2100
ISWPNGISVD YQDGKLYWCD ARTDKIERID LETGENREVV LSSNNMDMFS
2110 2120 2130 2140 2150
VSVFEDFIYW SDRTHANGSI KRGSKDNATD SVPLRTGIGV QLKDIKVFNR
2160 2170 2180 2190 2200
DRQKGTNVCA VANGGCQQLC LYRGRGQRAC ACAHGMLAED GASCREYAGY
2210 2220 2230 2240 2250
LLYSERTILK SIHLSDERNL NAPVQPFEDP EHMKNVIALA FDYRAGTSPG
2260 2270 2280 2290 2300
TPNRIFFSDI HFGNIQQIND DGSRRITIVE NVGSVEGLAY HRGWDTLYWT
2310 2320 2330 2340 2350
SYTTSTITRH TVDQTRPGAF ERETVITMSG DDHPRAFVLD ECQNLMFWTN
2360 2370 2380 2390 2400
WNEQHPSIMR AALSGANVLT LIEKDIRTPN GLAIDHRAEK LYFSDATLDK
2410 2420 2430 2440 2450
IERCEYDGSH RYVILKSEPV HPFGLAVYGE HIFWTDWVRR AVQRANKHVG
2460 2470 2480 2490 2500
SNMKLLRVDI PQQPMGIIAV ANDTNSCELS PCRINNGGCQ DLCLLTHQGH
2510 2520 2530 2540 2550
VNCSCRGGRI LQDDLTCRAV NSSCRAQDEF ECANGECINF SLTCDGVPHC
2560 2570 2580 2590 2600
KDKSDEKPSY CNSRRCKKTF RQCSNGRCVS NMLWCNGADD CGDGSDEIPC
2610 2620 2630 2640 2650
NKTACGVGEF RCRDGTCIGN SSRCNQFVDC EDASDEMNCS ATDCSSYFRL
2660 2670 2680 2690 2700
GVKGVLFQPC ERTSLCYAPS WVCDGANDCG DYSDERDCPG VKRPRCPLNY
2710 2720 2730 2740 2750
FACPSGRCIP MSWTCDKEDD CEHGEDETHC NKFCSEAQFE CQNHRCISKQ
2760 2770 2780 2790 2800
WLCDGSDDCG DGSDEAAHCE GKTCGPSSFS CPGTHVCVPE RWLCDGDKDC
2810 2820 2830 2840 2850
ADGADESIAA GCLYNSTCDD REFMCQNRQC IPKHFVCDHD RDCADGSDES
2860 2870 2880 2890 2900
PECEYPTCGP SEFRCANGRC LSSRQWECDG ENDCHDQSDE APKNPHCTSQ
2910 2920 2930 2940 2950
EHKCNASSQF LCSSGRCVAE ALLCNGQDDC GDSSDERGCH INECLSRKLS
2960 2970 2980 2990 3000
GCSQDCEDLK IGFKCRCRPG FRLKDDGRTC ADVDECSTTF PCSQRCINTH
3010 3020 3030 3040 3050
GSYKCLCVEG YAPRGGDPHS CKAVTDEEPF LIFANRYYLR KLNLDGSNYT
3060 3070 3080 3090 3100
LLKQGLNNAV ALDFDYREQM IYWTDVTTQG SMIRRMHLNG SNVQVLHRTG
3110 3120 3130 3140 3150
LSNPDGLAVD WVGGNLYWCD KGRDTIEVSK LNGAYRTVLV SSGLREPRAL
3160 3170 3180 3190 3200
VVDVQNGYLY WTDWGDHSLI GRIGMDGSSR SVIVDTKITW PNGLTLDYVT
3210 3220 3230 3240 3250
ERIYWADARE DYIEFASLDG SNRHVVLSQD IPHIFALTLF EDYVYWTDWE
3260 3270 3280 3290 3300
TKSINRAHKT TGTNKTLLIS TLHRPMDLHV FHALRQPDVP NHPCKVNNGG
3310 3320 3330 3340 3350
CSNLCLLSPG GGHKCACPTN FYLGSDGRTC VSNCTASQFV CKNDKCIPFW
3360 3370 3380 3390 3400
WKCDTEDDCG DHSDEPPDCP EFKCRPGQFQ CSTGICTNPA FICDGDNDCQ
3410 3420 3430 3440 3450
DNSDEANCDI HVCLPSQFKC TNTNRCIPGI FRCNGQDNCG DGEDERDCPE
3460 3470 3480 3490 3500
VTCAPNQFQC SITKRCIPRV WVCDRDNDCV DGSDEPANCT QMTCGVDEFR
3510 3520 3530 3540 3550
CKDSGRCIPA RWKCDGEDDC GDGSDEPKEE CDERTCEPYQ FRCKNNRCVP
3560 3570 3580 3590 3600
GRWQCDYDND CGDNSDEESC TPRPCSESEF SCANGRCIAG RWKCDGDHDC
3610 3620 3630 3640 3650
ADGSDEKDCT PRCDMDQFQC KSGHCIPLRW RCDADADCMD GSDEEACGTG
3660 3670 3680 3690 3700
VRTCPLDEFQ CNNTLCKPLA WKCDGEDDCG DNSDENPEEC ARFVCPPNRP
3710 3720 3730 3740 3750
FRCKNDRVCL WIGRQCDGTD NCGDGTDEED CEPPTAHTTH CKDKKEFLCR
3760 3770 3780 3790 3800
NQRCLSSSLR CNMFDDCGDG SDEEDCSIDP KLTSCATNAS ICGDEARCVR
3810 3820 3830 3840 3850
TEKAAYCACR SGFHTVPGQP GCQDINECLR FGTCSQLCNN TKGGHLCSCA
3860 3870 3880 3890 3900
RNFMKTHNTC KAEGSEYQVL YIADDNEIRS LFPGHPHSAY EQAFQGDESV
3910 3920 3930 3940 3950
RIDAMDVHVK AGRVYWTNWH TGTISYRSLP PAAPPTTSNR HRRQIDRGVT
3960 3970 3980 3990 4000
HLNISGLKMP RGIAIDWVAG NVYWTDSGRD VIEVAQMKGE NRKTLISGMI
4010 4020 4030 4040 4050
DEPHAIVVDP LRGTMYWSDW GNHPKIETAA MDGTLRETLV QDNIQWPTGL
4060 4070 4080 4090 4100
AVDYHNERLY WADAKLSVIG SIRLNGTDPI VAADSKRGLS HPFSIDVFED
4110 4120 4130 4140 4150
YIYGVTYINN RVFKIHKFGH SPLVNLTGGL SHASDVVLYH QHKQPEVTNP
4160 4170 4180 4190 4200
CDRKKCEWLC LLSPSGPVCT CPNGKRLDNG TCVPVPSPTP PPDAPRPGTC
4210 4220 4230 4240 4250
NLQCFNGGSC FLNARRQPKC RCQPRYTGDK CELDQCWEHC RNGGTCAASP
4260 4270 4280 4290 4300
SGMPTCRCPT GFTGPKCTQQ VCAGYCANNS TCTVNQGNQP QCRCLPGFLG
4310 4320 4330 4340 4350
DRCQYRQCSG YCENFGTCQM AADGSRQCRC TAYFEGSRCE VNKCSRCLEG
4360 4370 4380 4390 4400
ACVVNKQSGD VTCNCTDGRV APSCLTCVGH CSNGGSCTMN SKMMPECQCP
4410 4420 4430 4440 4450
PHMTGPRCEE HVFSQQQPGH IASILIPLLL LLLLVLVAGV VFWYKRRVQG
4460 4470 4480 4490 4500
AKGFQHQRMT NGAMNVEIGN PTYKMYEGGE PDDVGGLLDA DFALDPDKPT
4510 4520 4530 4540
NFTNPVYATL YMGGHGSRHS LASTDEKREL LGRGPEDEIG DPLA
Length:4,544
Mass (Da):504,606
Last modified:January 11, 2011 - 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:i5A11CC02FAB127BE
GO
Isoform 2 (identifier: Q07954-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     281-292: HVEQMAIDWLTG → LCVFSKSQQEMG
     293-4544: Missing.

Note: No experimental confirmation available.
Show »
Length:292
Mass (Da):31,631
Checksum:i82C39315F1ECEE24
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q6PJ72Q6PJ72_HUMAN
LRP1 protein
LRP1
439Annotation 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>
Q7Z7K9Q7Z7K9_HUMAN
LRP1 protein
LRP1
296Annotation 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>
H0YJ88H0YJ88_HUMAN
Prolow-density lipoprotein receptor...
LRP1
183Annotation 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>
H0YJI8H0YJI8_HUMAN
Prolow-density lipoprotein receptor...
LRP1
139Annotation 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 conflicti685D → G AA sequence (PubMed:1698775).Curated1
Sequence conflicti1743G → S AA sequence (PubMed:1698775).Curated1
Sequence conflicti2871 – 2872LS → IA AA sequence (PubMed:1698775).Curated2
Sequence conflicti3036R → M AA sequence (PubMed:1698775).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_021885166N → D. Corresponds to variant dbSNP:rs2306691Ensembl.1
Natural variantiVAR_014725217A → V. Corresponds to variant dbSNP:rs1800127Ensembl.1
Natural variantiVAR_035994869E → K in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1207947902Ensembl.1
Natural variantiVAR_0779821245K → R in KPA; reduced alpha-2 macroglobulin receptor activity; reduced protein abundance. 1 PublicationCorresponds to variant dbSNP:rs483353013EnsemblClinVar.1
Natural variantiVAR_0291812059V → L. Corresponds to variant dbSNP:rs2229278Ensembl.1
Natural variantiVAR_0475252080D → N. Corresponds to variant dbSNP:rs34577247Ensembl.1
Natural variantiVAR_0475262900Q → P3 PublicationsCorresponds to variant dbSNP:rs7397167Ensembl.1
Natural variantiVAR_0693883258H → Q Found in a patient with severe mental retardation, seizures, stereotypic behavior, high pain threshold and sleep disturbances. 1 Publication1
Natural variantiVAR_0359953760R → H in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs569866427Ensembl.1
Natural variantiVAR_0475274536E → G. Corresponds to variant dbSNP:rs17357542Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_056919281 – 292HVEQM…DWLTG → LCVFSKSQQEMG in isoform 2. 1 PublicationAdd BLAST12
Alternative sequenceiVSP_056920293 – 4544Missing in isoform 2. 1 PublicationAdd BLAST4252

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X13916 mRNA Translation: CAA32112.1
AF058427 Genomic DNA Translation: AAC64265.1
DQ314873 Genomic DNA Translation: ABC40732.1
AC023237 Genomic DNA No translation available.
AC137628 Genomic DNA No translation available.
AC137834 Genomic DNA No translation available.
BC045107 mRNA Translation: AAH45107.1
X15424 Genomic DNA Translation: CAA33464.1
Y18524 Genomic DNA Translation: CAD57169.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS8932.1 [Q07954-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
S02392

NCBI Reference Sequences

More...
RefSeqi
NP_002323.2, NM_002332.2 [Q07954-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000243077; ENSP00000243077; ENSG00000123384 [Q07954-1]
ENST00000338962; ENSP00000341264; ENSG00000123384 [Q07954-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
4035

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:4035

UCSC genome browser

More...
UCSCi
uc001snd.4 human [Q07954-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13916 mRNA Translation: CAA32112.1
AF058427 Genomic DNA Translation: AAC64265.1
DQ314873 Genomic DNA Translation: ABC40732.1
AC023237 Genomic DNA No translation available.
AC137628 Genomic DNA No translation available.
AC137834 Genomic DNA No translation available.
BC045107 mRNA Translation: AAH45107.1
X15424 Genomic DNA Translation: CAA33464.1
Y18524 Genomic DNA Translation: CAD57169.1
CCDSiCCDS8932.1 [Q07954-1]
PIRiS02392
RefSeqiNP_002323.2, NM_002332.2 [Q07954-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CR8NMR-A1059-1100[»]
1D2LNMR-A851-893[»]
1J8EX-ray1.85A1011-1054[»]
2FYJNMR-A932-1013[»]
2FYLNMR-B932-1013[»]
2KNXNMR-A2770-2817[»]
2KNYNMR-A2770-2817[»]
SMRiQ07954
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi110215, 126 interactors
ComplexPortaliCPX-4310 Prolow-density lipoprotein receptor-related protein 1 complex
CORUMiQ07954
DIPiDIP-50613N
ELMiQ07954
IntActiQ07954, 80 interactors
MINTiQ07954
STRINGi9606.ENSP00000243077

Chemistry databases

DrugBankiDB00025 Antihemophilic factor, human recombinant
DB00100 Coagulation Factor IX (Recombinant)
DB13152 Coagulation Factor IX Human
DB06245 Lanoteplase
DB13998 Lonoctocog alfa
DB13999 Moroctocog alfa
DB00031 Tenecteplase

Protein family/group databases

TCDBi9.B.87.1.16 the selenoprotein p receptor (selp-receptor) family

PTM databases

CarbonylDBiQ07954
GlyConnecti1638
iPTMnetiQ07954
PhosphoSitePlusiQ07954

Polymorphism and mutation databases

BioMutaiLRP1
DMDMi317373384

Proteomic databases

CPTACiCPTAC-2222
CPTAC-2223
EPDiQ07954
jPOSTiQ07954
MassIVEiQ07954
MaxQBiQ07954
PaxDbiQ07954
PeptideAtlasiQ07954
PRIDEiQ07954
ProteomicsDBi58559 [Q07954-1]
69639

Genome annotation databases

EnsembliENST00000243077; ENSP00000243077; ENSG00000123384 [Q07954-1]
ENST00000338962; ENSP00000341264; ENSG00000123384 [Q07954-2]
GeneIDi4035
KEGGihsa:4035
UCSCiuc001snd.4 human [Q07954-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4035
DisGeNETi4035

GeneCards: human genes, protein and diseases

More...
GeneCardsi
LRP1
HGNCiHGNC:6692 LRP1
HPAiCAB018621
HPA004182
HPA022903
MalaCardsiLRP1
MIMi107770 gene
604093 phenotype
neXtProtiNX_Q07954
OpenTargetsiENSG00000123384
Orphaneti79100 Atrophoderma vermiculata
2340 Keratosis follicularis spinulosa decalvans
PharmGKBiPA233

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1215 Eukaryota
ENOG410XP34 LUCA
GeneTreeiENSGT00940000157899
HOGENOMiHOG000230574
InParanoidiQ07954
KOiK04550
OMAiEPDMENC
OrthoDBi1606at2759
PhylomeDBiQ07954
TreeFamiTF315253

Enzyme and pathway databases

ReactomeiR-HSA-2168880 Scavenging of heme from plasma
R-HSA-975634 Retinoid metabolism and transport
SIGNORiQ07954

Miscellaneous databases

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

More...
ChiTaRSi
LRP1 human
EvolutionaryTraceiQ07954

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
LRP1

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

More...
GenomeRNAii
4035
PharosiQ07954

Protein Ontology

More...
PROi
PR:Q07954

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000123384 Expressed in 230 organ(s), highest expression level in thoracic aorta
ExpressionAtlasiQ07954 baseline and differential
GenevisibleiQ07954 HS

Family and domain databases

CDDicd00112 LDLa, 31 hits
Gene3Di2.120.10.30, 8 hits
4.10.400.10, 29 hits
InterProiView protein in InterPro
IPR011042 6-blade_b-propeller_TolB-like
IPR026823 cEGF
IPR032485 DUF5050
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR009030 Growth_fac_rcpt_cys_sf
IPR036055 LDL_receptor-like_sf
IPR023415 LDLR_class-A_CS
IPR000033 LDLR_classB_rpt
IPR002172 LDrepeatLR_classA_rpt
PfamiView protein in Pfam
PF12662 cEGF, 1 hit
PF16472 DUF5050, 1 hit
PF07645 EGF_CA, 2 hits
PF00057 Ldl_recept_a, 29 hits
PF00058 Ldl_recept_b, 12 hits
PRINTSiPR00261 LDLRECEPTOR
SMARTiView protein in SMART
SM00181 EGF, 26 hits
SM00179 EGF_CA, 7 hits
SM00192 LDLa, 31 hits
SM00135 LY, 35 hits
SUPFAMiSSF57184 SSF57184, 4 hits
SSF57424 SSF57424, 30 hits
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 3 hits
PS00022 EGF_1, 5 hits
PS01186 EGF_2, 8 hits
PS50026 EGF_3, 6 hits
PS01187 EGF_CA, 2 hits
PS01209 LDLRA_1, 27 hits
PS50068 LDLRA_2, 31 hits
PS51120 LDLRB, 34 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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 nameiLRP1_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: Q07954
Secondary accession number(s): Q2PP12, Q86SW0, Q8IVG8
<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: October 1, 1996
Last sequence update: January 11, 2011
Last modified: November 13, 2019
This is version 216 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  4. SIMILARITY comments
    Index of protein domains and families
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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