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Q07954

- LRP1_HUMAN

UniProt

Q07954 - LRP1_HUMAN

Protein

Prolow-density lipoprotein receptor-related protein 1

Gene

LRP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    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.
    Functions as a receptor for Pseudomonas aeruginosa exotoxin A.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi871 – 8711Calcium 1; via carbonyl oxygen
    Metal bindingi874 – 8741Calcium 1
    Metal bindingi876 – 8761Calcium 1; via carbonyl oxygen
    Metal bindingi878 – 8781Calcium 1
    Metal bindingi884 – 8841Calcium 1
    Metal bindingi885 – 8851Calcium 1
    Metal bindingi1032 – 10321Calcium 2; via carbonyl oxygen
    Metal bindingi1035 – 10351Calcium 2
    Metal bindingi1037 – 10371Calcium 2; via carbonyl oxygen
    Metal bindingi1039 – 10391Calcium 2
    Metal bindingi1045 – 10451Calcium 2
    Metal bindingi1046 – 10461Calcium 2
    Metal bindingi1080 – 10801Calcium 3; via carbonyl oxygen
    Metal bindingi1083 – 10831Calcium 3
    Metal bindingi1085 – 10851Calcium 3; via carbonyl oxygen
    Metal bindingi1087 – 10871Calcium 3
    Metal bindingi1093 – 10931Calcium 3
    Metal bindingi1094 – 10941Calcium 3

    GO - Molecular functioni

    1. apolipoprotein binding Source: UniProtKB
    2. calcium ion binding Source: UniProtKB
    3. lipoprotein particle receptor binding Source: BHF-UCL
    4. lipoprotein transporter activity Source: UniProtKB
    5. poly(A) RNA binding Source: UniProtKB
    6. protein binding Source: IntAct
    7. protein complex binding Source: BHF-UCL
    8. receptor activity Source: ProtInc

    GO - Biological processi

    1. aging Source: Ensembl
    2. aorta morphogenesis Source: BHF-UCL
    3. apoptotic cell clearance Source: BHF-UCL
    4. beta-amyloid clearance Source: BHF-UCL
    5. cell proliferation Source: Ensembl
    6. cholesterol metabolic process Source: Ensembl
    7. lipoprotein metabolic process Source: Ensembl
    8. lipoprotein transport Source: UniProtKB
    9. negative regulation of neuron apoptotic process Source: Ensembl
    10. negative regulation of platelet-derived growth factor receptor-beta signaling pathway Source: BHF-UCL
    11. negative regulation of smooth muscle cell migration Source: BHF-UCL
    12. negative regulation of Wnt signaling pathway Source: BHF-UCL
    13. phototransduction, visible light Source: Reactome
    14. positive regulation of cholesterol efflux Source: BHF-UCL
    15. positive regulation of lipid transport Source: BHF-UCL
    16. positive regulation of protein transport Source: Ensembl
    17. protein kinase C-activating G-protein coupled receptor signaling pathway Source: Ensembl
    18. receptor-mediated endocytosis Source: Ensembl
    19. regulation of actin cytoskeleton organization Source: BHF-UCL
    20. regulation of cholesterol transport Source: BHF-UCL
    21. regulation of phospholipase A2 activity Source: BHF-UCL
    22. retinoid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Developmental protein, Receptor

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_160163. Scavenging of heme from plasma.
    REACT_24968. Retinoid metabolism and transport.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prolow-density lipoprotein receptor-related protein 1
    Short name:
    LRP-1
    Alternative name(s):
    Alpha-2-macroglobulin receptor
    Short name:
    A2MR
    Apolipoprotein E receptor
    Short name:
    APOER
    CD_antigen: CD91
    Cleaved into the following 3 chains:
    Gene namesi
    Name:LRP1
    Synonyms:A2MR, APR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:6692. LRP1.

    Subcellular locationi

    Chain Low-density lipoprotein receptor-related protein 1 intracellular domain : Cytoplasm. Nucleus
    Note: After cleavage, the intracellular domain (LRPICD) is detected both in the cytoplasm and in the nucleus.

    GO - Cellular componenti

    1. clathrin-coated vesicle Source: Ensembl
    2. coated pit Source: UniProtKB-SubCell
    3. dendrite Source: Ensembl
    4. endocytic vesicle membrane Source: Reactome
    5. endosome Source: Ensembl
    6. integral component of plasma membrane Source: UniProtKB
    7. lysosomal membrane Source: UniProtKB
    8. neuronal cell body Source: Ensembl
    9. nucleus Source: UniProtKB-SubCell
    10. plasma membrane Source: Reactome
    11. receptor complex Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Coated pit, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi4460 – 44601T → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4517; A-4520 and A-4523. 2 Publications
    Mutagenesisi4470 – 44734NPTY → APTA: No effect on tyrosine phosphorylation. 2 Publications
    Mutagenesisi4470 – 44701N → A: No effect on interaction with GULP1. 2 Publications
    Mutagenesisi4472 – 44721T → A: No detectable effect on phosphorylation. 2 Publications
    Mutagenesisi4504 – 45074NPVY → APVA: Loss of tyrosine phosphorylation. Abolishes interaction with SHC1 and GULP1. 2 Publications
    Mutagenesisi4504 – 45041N → A: Loss of interaction with GULP1. 2 Publications
    Mutagenesisi4517 – 45171S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4520 and A-4523. 2 Publications
    Mutagenesisi4520 – 45201S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4523. 2 Publications
    Mutagenesisi4523 – 45231S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4520. 2 Publications

    Organism-specific databases

    PharmGKBiPA233.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 45444525Prolow-density lipoprotein receptor-related protein 1PRO_0000017317Add
    BLAST
    Chaini20 – ?39433924Low-density lipoprotein receptor-related protein 1 515 kDa subunitPRO_0000302750Add
    BLAST
    Chaini?3944 – 4544601Low-density lipoprotein receptor-related protein 1 85 kDa subunitPRO_0000302751Add
    BLAST
    Chaini?4441 – 4544104Low-density lipoprotein receptor-related protein 1 intracellular domainPRO_0000302752Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi27 ↔ 40By similarity
    Disulfide bondi34 ↔ 53By similarity
    Disulfide bondi47 ↔ 64By similarity
    Disulfide bondi72 ↔ 85By similarity
    Disulfide bondi79 ↔ 98By similarity
    Disulfide bondi92 ↔ 108By similarity
    Glycosylationi114 – 1141N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi115 ↔ 124By similarity
    Disulfide bondi120 ↔ 133By similarity
    Disulfide bondi135 ↔ 148By similarity
    Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi154 ↔ 164By similarity
    Disulfide bondi160 ↔ 173By similarity
    Disulfide bondi175 ↔ 188By similarity
    Glycosylationi185 – 1851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi274 – 2741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi357 – 3571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi446 – 4461N-linked (GlcNAc...)2 Publications
    Disulfide bondi478 ↔ 493By similarity
    Disulfide bondi489 ↔ 504By similarity
    Disulfide bondi506 ↔ 519By similarity
    Glycosylationi729 – 7291N-linked (GlcNAc...) (complex)3 Publications
    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
    Glycosylationi928 – 9281N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi1050 – 10501N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi1154 – 11541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1155 – 11551N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1166 ↔ 1182By similarity
    Disulfide bondi1185 ↔ 1196By similarity
    Disulfide bondi1192 ↔ 1206By similarity
    Glycosylationi1195 – 11951N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1208 ↔ 1221By similarity
    Glycosylationi1218 – 12181N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1227 ↔ 1237By similarity
    Disulfide bondi1233 ↔ 1246By similarity
    Disulfide bondi1248 ↔ 1261By similarity
    Glycosylationi1511 – 15111N-linked (GlcNAc...) (complex)2 Publications
    Disulfide bondi1540 ↔ 1553By similarity
    Disulfide bondi1549 ↔ 1563By similarity
    Glycosylationi1558 – 15581N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1565 ↔ 1578By similarity
    Glycosylationi1575 – 15751N-linked (GlcNAc...)1 Publication
    Glycosylationi1616 – 16161N-linked (GlcNAc...)1 Publication
    Glycosylationi1645 – 16451N-linked (GlcNAc...)1 Publication
    Glycosylationi1723 – 17231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1733 – 17331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1763 – 17631N-linked (GlcNAc...)1 Publication
    Glycosylationi1825 – 18251N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1850 ↔ 1861By similarity
    Disulfide bondi1857 ↔ 1871By similarity
    Disulfide bondi1873 ↔ 1886By similarity
    Glycosylationi1933 – 19331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1995 – 19951N-linked (GlcNAc...)Sequence Analysis
    Modified residuei2009 – 20091N6-acetyllysineBy similarity
    Glycosylationi2048 – 20481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2117 – 21171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2127 – 21271N-linked (GlcNAc...)2 Publications
    Disulfide bondi2159 ↔ 2170By similarity
    Disulfide bondi2166 ↔ 2180By similarity
    Disulfide bondi2182 ↔ 2194By similarity
    Glycosylationi2472 – 24721N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2482 ↔ 2493By similarity
    Disulfide bondi2489 ↔ 2503By similarity
    Glycosylationi2502 – 25021N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2505 ↔ 2517By similarity
    Glycosylationi2521 – 25211N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2524 ↔ 2537By similarity
    Disulfide bondi2532 ↔ 2550By similarity
    Glycosylationi2539 – 25391N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2544 ↔ 2561By similarity
    Disulfide bondi2566 ↔ 2578By similarity
    Disulfide bondi2573 ↔ 2591By similarity
    Disulfide bondi2585 ↔ 2600By similarity
    Glycosylationi2601 – 26011N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2605 ↔ 2617By similarity
    Disulfide bondi2612 ↔ 2630By similarity
    Glycosylationi2620 – 26201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2624 ↔ 2639By similarity
    Glycosylationi2638 – 26381N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi2815 – 28151N-linked (GlcNAc...)1 Publication
    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
    Glycosylationi2905 – 29051N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi3048 – 30481N-linked (GlcNAc...)2 Publications
    Glycosylationi3089 – 30891N-linked (GlcNAc...)1 Publication
    Glycosylationi3264 – 32641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3294 ↔ 3305By similarity
    Disulfide bondi3301 ↔ 3315By similarity
    Disulfide bondi3317 ↔ 3330By similarity
    Glycosylationi3333 – 33331N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi3488 – 34881N-linked (GlcNAc...)1 Publication
    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
    Glycosylationi3662 – 36621N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi3788 – 37881N-linked (GlcNAc...)1 Publication
    Disulfide bondi3792 ↔ 3807By similarity
    Disulfide bondi3809 ↔ 3822By similarity
    Disulfide bondi3828 ↔ 3838By similarity
    Disulfide bondi3834 ↔ 3847By similarity
    Glycosylationi3839 – 38391N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3849 ↔ 3860By similarity
    Glycosylationi3953 – 39531N-linked (GlcNAc...)1 Publication
    Glycosylationi4075 – 40751N-linked (GlcNAc...)1 Publication
    Glycosylationi4125 – 41251N-linked (GlcNAc...)1 Publication
    Disulfide bondi4151 ↔ 4160By similarity
    Disulfide bondi4156 ↔ 4169By similarity
    Disulfide bondi4171 ↔ 4182By similarity
    Glycosylationi4179 – 41791N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi4278 – 42781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi4279 – 42791N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi4294 ↔ 4303By similarity
    Disulfide bondi4308 ↔ 4318By similarity
    Disulfide bondi4312 ↔ 4328By similarity
    Disulfide bondi4330 ↔ 4339By similarity
    Disulfide bondi4344 ↔ 4352By similarity
    Disulfide bondi4347 ↔ 4363By similarity
    Glycosylationi4364 – 43641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi4365 ↔ 4374By similarity
    Disulfide bondi4377 ↔ 4387By similarity
    Disulfide bondi4381 ↔ 4397By similarity
    Disulfide bondi4399 ↔ 4408By similarity
    Modified residuei4460 – 44601Phosphothreonine1 Publication
    Modified residuei4507 – 45071Phosphotyrosine1 Publication
    Modified residuei4517 – 45171Phosphoserine1 Publication
    Modified residuei4520 – 45201Phosphoserine1 Publication
    Modified residuei4523 – 45231Phosphoserine1 Publication

    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

    MaxQBiQ07954.
    PaxDbiQ07954.
    PRIDEiQ07954.

    PTM databases

    PhosphoSiteiQ07954.

    Expressioni

    Tissue specificityi

    Most abundant in liver, brain and lung.

    Gene expression databases

    ArrayExpressiQ07954.
    BgeeiQ07954.
    CleanExiHS_LRP1.
    GenevestigatoriQ07954.

    Organism-specific databases

    HPAiCAB018621.
    HPA004182.
    HPA022903.

    Interactioni

    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.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APBB1O002133EBI-1046087,EBI-81694
    FCN2Q154852EBI-1046087,EBI-7468784
    Jag1Q637224EBI-1046087,EBI-4567800From a different organism.
    MBL2P112265EBI-1046087,EBI-5325353
    Thbs2Q033502EBI-1046087,EBI-4567830From a different organism.

    Protein-protein interaction databases

    BioGridi110215. 50 interactions.
    DIPiDIP-50613N.
    IntActiQ07954. 17 interactions.
    MINTiMINT-5004471.

    Structurei

    Secondary structure

    1
    4544
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni853 – 8575
    Beta strandi859 – 8613
    Turni862 – 8643
    Beta strandi865 – 8673
    Helixi869 – 8713
    Beta strandi874 – 8763
    Turni878 – 8814
    Beta strandi934 – 9363
    Beta strandi940 – 9423
    Turni944 – 9463
    Beta strandi948 – 9503
    Beta strandi953 – 9564
    Beta strandi958 – 9614
    Turni964 – 9685
    Turni969 – 9713
    Beta strandi974 – 9763
    Beta strandi978 – 9836
    Turni985 – 9873
    Beta strandi989 – 9913
    Beta strandi995 – 10006
    Beta strandi1003 – 10075
    Beta strandi1009 – 10113
    Beta strandi1013 – 10153
    Beta strandi1019 – 10213
    Beta strandi1027 – 10293
    Helixi1030 – 10323
    Beta strandi1035 – 10373
    Beta strandi1040 – 10434
    Helixi1044 – 10463
    Helixi1048 – 10514
    Turni1070 – 10723
    Helixi1078 – 10803
    Beta strandi1081 – 10855
    Beta strandi1088 – 10914
    Turni1092 – 10965
    Beta strandi2778 – 27814
    Turni2782 – 27854
    Beta strandi2786 – 27894
    Turni2790 – 27945
    Beta strandi2795 – 27973
    Beta strandi2800 – 28034
    Helixi2804 – 28063
    Helixi2808 – 28103
    Beta strandi2813 – 28164

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ07954.
    SMRiQ07954. Positions 851-893, 932-1054, 1059-1100, 2770-2815, 2856-2896, 3571-3606.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ07954.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 44194400ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini4445 – 4544100CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei4420 – 444425HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 6642LDL-receptor class A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini70 – 11041LDL-receptor class A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini111 – 14939EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini150 – 18940EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Repeati292 – 33443LDL-receptor class B 1Add
    BLAST
    Repeati335 – 37844LDL-receptor class B 2Add
    BLAST
    Repeati379 – 42244LDL-receptor class B 3Add
    BLAST
    Domaini474 – 52047EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati571 – 61343LDL-receptor class B 4Add
    BLAST
    Repeati614 – 65946LDL-receptor class B 5Add
    BLAST
    Repeati660 – 71051LDL-receptor class B 6Add
    BLAST
    Repeati711 – 75444LDL-receptor class B 7Add
    BLAST
    Domaini803 – 84341EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini852 – 89241LDL-receptor class A 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini893 – 93341LDL-receptor class A 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini934 – 97340LDL-receptor class A 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini974 – 101340LDL-receptor class A 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1013 – 105341LDL-receptor class A 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1060 – 109940LDL-receptor class A 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1102 – 114241LDL-receptor class A 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini1143 – 118240LDL-receptor class A 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1183 – 122240EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini1223 – 126240EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Repeati1309 – 135547LDL-receptor class B 8Add
    BLAST
    Repeati1356 – 139843LDL-receptor class B 9Add
    BLAST
    Repeati1399 – 144547LDL-receptor class B 10Add
    BLAST
    Repeati1446 – 149045LDL-receptor class B 11Add
    BLAST
    Repeati1491 – 153141LDL-receptor class B 12Add
    BLAST
    Domaini1536 – 157944EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Repeati1627 – 166943LDL-receptor class B 13Add
    BLAST
    Repeati1670 – 171344LDL-receptor class B 14Add
    BLAST
    Repeati1714 – 175340LDL-receptor class B 15Add
    BLAST
    Repeati1754 – 179845LDL-receptor class B 16Add
    BLAST
    Domaini1846 – 188742EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Repeati1934 – 197643LDL-receptor class B 17Add
    BLAST
    Repeati1977 – 201943LDL-receptor class B 18Add
    BLAST
    Repeati2020 – 206344LDL-receptor class B 19Add
    BLAST
    Repeati2064 – 210744LDL-receptor class B 20Add
    BLAST
    Domaini2155 – 219541EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Repeati2253 – 229442LDL-receptor class B 21Add
    BLAST
    Repeati2295 – 234349LDL-receptor class B 22Add
    BLAST
    Repeati2344 – 238845LDL-receptor class B 23Add
    BLAST
    Repeati2389 – 243143LDL-receptor class B 24Add
    BLAST
    Repeati2432 – 247342LDL-receptor class B 25Add
    BLAST
    Domaini2478 – 251841EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini2522 – 256342LDL-receptor class A 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini2564 – 260239LDL-receptor class A 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini2603 – 264139LDL-receptor class A 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini2642 – 269049LDL-receptor class A 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini2694 – 273239LDL-receptor class A 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini2732 – 277140LDL-receptor class A 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini2772 – 281443LDL-receptor class A 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini2816 – 285540LDL-receptor class A 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini2856 – 289944LDL-receptor class A 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini2902 – 294039LDL-receptor class A 20PROSITE-ProRule annotationAdd
    BLAST
    Domaini2941 – 298141EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini2982 – 302241EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Repeati3069 – 311345LDL-receptor class B 26Add
    BLAST
    Repeati3114 – 315643LDL-receptor class B 27Add
    BLAST
    Repeati3157 – 320044LDL-receptor class B 28Add
    BLAST
    Repeati3201 – 324343LDL-receptor class B 29Add
    BLAST
    Repeati3244 – 328441LDL-receptor class B 30Add
    BLAST
    Domaini3290 – 333142EGF-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini3332 – 337140LDL-receptor class A 21PROSITE-ProRule annotationAdd
    BLAST
    Domaini3372 – 341039LDL-receptor class A 22PROSITE-ProRule annotationAdd
    BLAST
    Domaini3411 – 345040LDL-receptor class A 23PROSITE-ProRule annotationAdd
    BLAST
    Domaini3451 – 349141LDL-receptor class A 24PROSITE-ProRule annotationAdd
    BLAST
    Domaini3492 – 353342LDL-receptor class A 25PROSITE-ProRule annotationAdd
    BLAST
    Domaini3534 – 357239LDL-receptor class A 26PROSITE-ProRule annotationAdd
    BLAST
    Domaini3573 – 361139LDL-receptor class A 27PROSITE-ProRule annotationAdd
    BLAST
    Domaini3611 – 364939LDL-receptor class A 28PROSITE-ProRule annotationAdd
    BLAST
    Domaini3652 – 369241LDL-receptor class A 29PROSITE-ProRule annotationAdd
    BLAST
    Domaini3693 – 373341LDL-receptor class A 30PROSITE-ProRule annotationAdd
    BLAST
    Domaini3739 – 377840LDL-receptor class A 31PROSITE-ProRule annotationAdd
    BLAST
    Domaini3781 – 382343EGF-like 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini3824 – 386138EGF-like 15PROSITE-ProRule annotationAdd
    BLAST
    Repeati3912 – 395443LDL-receptor class B 31Add
    BLAST
    Repeati3970 – 401243LDL-receptor class B 32Add
    BLAST
    Repeati4013 – 405644LDL-receptor class B 33Add
    BLAST
    Repeati4057 – 410145LDL-receptor class B 34Add
    BLAST
    Domaini4147 – 418337EGF-like 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini4196 – 423237EGF-like 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini4232 – 426837EGF-like 18PROSITE-ProRule annotationAdd
    BLAST
    Domaini4268 – 430437EGF-like 19PROSITE-ProRule annotationAdd
    BLAST
    Domaini4304 – 434037EGF-like 20PROSITE-ProRule annotationAdd
    BLAST
    Domaini4340 – 437536EGF-like 21PROSITE-ProRule annotationAdd
    BLAST
    Domaini4373 – 440937EGF-like 22PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni4445 – 4544100Interaction with MAFBBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi3940 – 39434Recognition site for proteolytical processingSequence Analysis
    Motifi4502 – 45076NPXY motif

    Sequence similaritiesi

    Belongs to the LDLR family.Curated
    Contains 22 EGF-like domains.PROSITE-ProRule annotation
    Contains 31 LDL-receptor class A domains.PROSITE-ProRule annotation
    Contains 34 LDL-receptor class B repeats.PROSITE-ProRule annotation

    Keywords - Domaini

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

    Phylogenomic databases

    eggNOGiNOG235850.
    HOGENOMiHOG000230574.
    HOVERGENiHBG006292.
    InParanoidiQ07954.
    KOiK04550.
    OMAiAYFEGPR.
    OrthoDBiEOG790FZT.
    PhylomeDBiQ07954.
    TreeFamiTF315253.

    Family and domain databases

    Gene3Di2.120.10.30. 8 hits.
    4.10.400.10. 29 hits.
    InterProiIPR011042. 6-blade_b-propeller_TolB-like.
    IPR026823. cEGF.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR023415. LDLR_class-A_CS.
    IPR000033. LDLR_classB_rpt.
    IPR002172. LDrepeatLR_classA_rpt.
    [Graphical view]
    PfamiPF12662. cEGF. 1 hit.
    PF07645. EGF_CA. 1 hit.
    PF00057. Ldl_recept_a. 30 hits.
    PF00058. Ldl_recept_b. 16 hits.
    [Graphical view]
    PRINTSiPR00261. LDLRECEPTOR.
    SMARTiSM00181. EGF. 18 hits.
    SM00179. EGF_CA. 3 hits.
    SM00192. LDLa. 31 hits.
    SM00135. LY. 35 hits.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 9 hits.
    SSF57424. SSF57424. 30 hits.
    PROSITEiPS00010. 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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q07954-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLTPPLLLLL PLLSALVAAA IDAPKTCSPK QFACRDQITC ISKGWRCDGE     50
    RDCPDGSDEA PEICPQSKAQ RCQPNEHNCL GTELCVPMSR LCNGVQDCMD 100
    GSDEGPHCRE LQGNCSRLGC QHHCVPTLDG PTCYCNSSFQ LQADGKTCKD 150
    FDECSVYGTC SQLCTNTDGS FICGCVEGYL LQPDNRSCKA KNEPVDRPPV 200
    LLIANSQNIL ATYLSGAQVS TITPTSTRQT TAMDFSYANE TVCWVHVGDS 250
    AAQTQLKCAR MPGLKGFVDE HTINISLSLH HVEQMAIDWL TGNFYFVDDI 300
    DDRIFVCNRN GDTCVTLLDL ELYNPKGIAL DPAMGKVFFT DYGQIPKVER 350
    CDMDGQNRTK LVDSKIVFPH GITLDLVSRL VYWADAYLDY IEVVDYEGKG 400
    RQTIIQGILI EHLYGLTVFE NYLYATNSDN ANAQQKTSVI RVNRFNSTEY 450
    QVVTRVDKGG ALHIYHQRRQ PRVRSHACEN DQYGKPGGCS DICLLANSHK 500
    ARTCRCRSGF SLGSDGKSCK KPEHELFLVY GKGRPGIIRG MDMGAKVPDE 550
    HMIPIENLMN PRALDFHAET GFIYFADTTS YLIGRQKIDG TERETILKDG 600
    IHNVEGVAVD WMGDNLYWTD DGPKKTISVA RLEKAAQTRK TLIEGKMTHP 650
    RAIVVDPLNG WMYWTDWEED PKDSRRGRLE RAWMDGSHRD IFVTSKTVLW 700
    PNGLSLDIPA GRLYWVDAFY DRIETILLNG TDRKIVYEGP ELNHAFGLCH 750
    HGNYLFWTEY RSGSVYRLER GVGGAPPTVT LLRSERPPIF EIRMYDAQQQ 800
    QVGTNKCRVN NGGCSSLCLA TPGSRQCACA EDQVLDADGV TCLANPSYVP 850
    PPQCQPGEFA CANSRCIQER WKCDGDNDCL DNSDEAPALC HQHTCPSDRF 900
    KCENNRCIPN RWLCDGDNDC GNSEDESNAT CSARTCPPNQ FSCASGRCIP 950
    ISWTCDLDDD CGDRSDESAS CAYPTCFPLT QFTCNNGRCI NINWRCDNDN 1000
    DCGDNSDEAG CSHSCSSTQF KCNSGRCIPE HWTCDGDNDC GDYSDETHAN 1050
    CTNQATRPPG GCHTDEFQCR LDGLCIPLRW RCDGDTDCMD SSDEKSCEGV 1100
    THVCDPSVKF GCKDSARCIS KAWVCDGDND CEDNSDEENC ESLACRPPSH 1150
    PCANNTSVCL PPDKLCDGND DCGDGSDEGE LCDQCSLNNG GCSHNCSVAP 1200
    GEGIVCSCPL GMELGPDNHT CQIQSYCAKH LKCSQKCDQN KFSVKCSCYE 1250
    GWVLEPDGES CRSLDPFKPF IIFSNRHEIR RIDLHKGDYS VLVPGLRNTI 1300
    ALDFHLSQSA LYWTDVVEDK IYRGKLLDNG ALTSFEVVIQ YGLATPEGLA 1350
    VDWIAGNIYW VESNLDQIEV AKLDGTLRTT LLAGDIEHPR AIALDPRDGI 1400
    LFWTDWDASL PRIEAASMSG AGRRTVHRET GSGGWPNGLT VDYLEKRILW 1450
    IDARSDAIYS ARYDGSGHME VLRGHEFLSH PFAVTLYGGE VYWTDWRTNT 1500
    LAKANKWTGH NVTVVQRTNT QPFDLQVYHP SRQPMAPNPC EANGGQGPCS 1550
    HLCLINYNRT VSCACPHLMK LHKDNTTCYE FKKFLLYARQ MEIRGVDLDA 1600
    PYYNYIISFT VPDIDNVTVL DYDAREQRVY WSDVRTQAIK RAFINGTGVE 1650
    TVVSADLPNA HGLAVDWVSR NLFWTSYDTN KKQINVARLD GSFKNAVVQG 1700
    LEQPHGLVVH PLRGKLYWTD GDNISMANMD GSNRTLLFSG QKGPVGLAID 1750
    FPESKLYWIS SGNHTINRCN LDGSGLEVID AMRSQLGKAT ALAIMGDKLW 1800
    WADQVSEKMG TCSKADGSGS VVLRNSTTLV MHMKVYDESI QLDHKGTNPC 1850
    SVNNGDCSQL CLPTSETTRS CMCTAGYSLR SGQQACEGVG SFLLYSVHEG 1900
    IRGIPLDPND KSDALVPVSG TSLAVGIDFH AENDTIYWVD MGLSTISRAK 1950
    RDQTWREDVV TNGIGRVEGI AVDWIAGNIY WTDQGFDVIE VARLNGSFRY 2000
    VVISQGLDKP RAITVHPEKG YLFWTEWGQY PRIERSRLDG TERVVLVNVS 2050
    ISWPNGISVD YQDGKLYWCD ARTDKIERID LETGENREVV LSSNNMDMFS 2100
    VSVFEDFIYW SDRTHANGSI KRGSKDNATD SVPLRTGIGV QLKDIKVFNR 2150
    DRQKGTNVCA VANGGCQQLC LYRGRGQRAC ACAHGMLAED GASCREYAGY 2200
    LLYSERTILK SIHLSDERNL NAPVQPFEDP EHMKNVIALA FDYRAGTSPG 2250
    TPNRIFFSDI HFGNIQQIND DGSRRITIVE NVGSVEGLAY HRGWDTLYWT 2300
    SYTTSTITRH TVDQTRPGAF ERETVITMSG DDHPRAFVLD ECQNLMFWTN 2350
    WNEQHPSIMR AALSGANVLT LIEKDIRTPN GLAIDHRAEK LYFSDATLDK 2400
    IERCEYDGSH RYVILKSEPV HPFGLAVYGE HIFWTDWVRR AVQRANKHVG 2450
    SNMKLLRVDI PQQPMGIIAV ANDTNSCELS PCRINNGGCQ DLCLLTHQGH 2500
    VNCSCRGGRI LQDDLTCRAV NSSCRAQDEF ECANGECINF SLTCDGVPHC 2550
    KDKSDEKPSY CNSRRCKKTF RQCSNGRCVS NMLWCNGADD CGDGSDEIPC 2600
    NKTACGVGEF RCRDGTCIGN SSRCNQFVDC EDASDEMNCS ATDCSSYFRL 2650
    GVKGVLFQPC ERTSLCYAPS WVCDGANDCG DYSDERDCPG VKRPRCPLNY 2700
    FACPSGRCIP MSWTCDKEDD CEHGEDETHC NKFCSEAQFE CQNHRCISKQ 2750
    WLCDGSDDCG DGSDEAAHCE GKTCGPSSFS CPGTHVCVPE RWLCDGDKDC 2800
    ADGADESIAA GCLYNSTCDD REFMCQNRQC IPKHFVCDHD RDCADGSDES 2850
    PECEYPTCGP SEFRCANGRC LSSRQWECDG ENDCHDQSDE APKNPHCTSQ 2900
    EHKCNASSQF LCSSGRCVAE ALLCNGQDDC GDSSDERGCH INECLSRKLS 2950
    GCSQDCEDLK IGFKCRCRPG FRLKDDGRTC ADVDECSTTF PCSQRCINTH 3000
    GSYKCLCVEG YAPRGGDPHS CKAVTDEEPF LIFANRYYLR KLNLDGSNYT 3050
    LLKQGLNNAV ALDFDYREQM IYWTDVTTQG SMIRRMHLNG SNVQVLHRTG 3100
    LSNPDGLAVD WVGGNLYWCD KGRDTIEVSK LNGAYRTVLV SSGLREPRAL 3150
    VVDVQNGYLY WTDWGDHSLI GRIGMDGSSR SVIVDTKITW PNGLTLDYVT 3200
    ERIYWADARE DYIEFASLDG SNRHVVLSQD IPHIFALTLF EDYVYWTDWE 3250
    TKSINRAHKT TGTNKTLLIS TLHRPMDLHV FHALRQPDVP NHPCKVNNGG 3300
    CSNLCLLSPG GGHKCACPTN FYLGSDGRTC VSNCTASQFV CKNDKCIPFW 3350
    WKCDTEDDCG DHSDEPPDCP EFKCRPGQFQ CSTGICTNPA FICDGDNDCQ 3400
    DNSDEANCDI HVCLPSQFKC TNTNRCIPGI FRCNGQDNCG DGEDERDCPE 3450
    VTCAPNQFQC SITKRCIPRV WVCDRDNDCV DGSDEPANCT QMTCGVDEFR 3500
    CKDSGRCIPA RWKCDGEDDC GDGSDEPKEE CDERTCEPYQ FRCKNNRCVP 3550
    GRWQCDYDND CGDNSDEESC TPRPCSESEF SCANGRCIAG RWKCDGDHDC 3600
    ADGSDEKDCT PRCDMDQFQC KSGHCIPLRW RCDADADCMD GSDEEACGTG 3650
    VRTCPLDEFQ CNNTLCKPLA WKCDGEDDCG DNSDENPEEC ARFVCPPNRP 3700
    FRCKNDRVCL WIGRQCDGTD NCGDGTDEED CEPPTAHTTH CKDKKEFLCR 3750
    NQRCLSSSLR CNMFDDCGDG SDEEDCSIDP KLTSCATNAS ICGDEARCVR 3800
    TEKAAYCACR SGFHTVPGQP GCQDINECLR FGTCSQLCNN TKGGHLCSCA 3850
    RNFMKTHNTC KAEGSEYQVL YIADDNEIRS LFPGHPHSAY EQAFQGDESV 3900
    RIDAMDVHVK AGRVYWTNWH TGTISYRSLP PAAPPTTSNR HRRQIDRGVT 3950
    HLNISGLKMP RGIAIDWVAG NVYWTDSGRD VIEVAQMKGE NRKTLISGMI 4000
    DEPHAIVVDP LRGTMYWSDW GNHPKIETAA MDGTLRETLV QDNIQWPTGL 4050
    AVDYHNERLY WADAKLSVIG SIRLNGTDPI VAADSKRGLS HPFSIDVFED 4100
    YIYGVTYINN RVFKIHKFGH SPLVNLTGGL SHASDVVLYH QHKQPEVTNP 4150
    CDRKKCEWLC LLSPSGPVCT CPNGKRLDNG TCVPVPSPTP PPDAPRPGTC 4200
    NLQCFNGGSC FLNARRQPKC RCQPRYTGDK CELDQCWEHC RNGGTCAASP 4250
    SGMPTCRCPT GFTGPKCTQQ VCAGYCANNS TCTVNQGNQP QCRCLPGFLG 4300
    DRCQYRQCSG YCENFGTCQM AADGSRQCRC TAYFEGSRCE VNKCSRCLEG 4350
    ACVVNKQSGD VTCNCTDGRV APSCLTCVGH CSNGGSCTMN SKMMPECQCP 4400
    PHMTGPRCEE HVFSQQQPGH IASILIPLLL LLLLVLVAGV VFWYKRRVQG 4450
    AKGFQHQRMT NGAMNVEIGN PTYKMYEGGE PDDVGGLLDA DFALDPDKPT 4500
    NFTNPVYATL YMGGHGSRHS LASTDEKREL LGRGPEDEIG DPLA 4544
    Length:4,544
    Mass (Da):504,606
    Last modified:January 11, 2011 - v2
    Checksum:i5A11CC02FAB127BE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti685 – 6851D → G AA sequence (PubMed:1698775)Curated
    Sequence conflicti1743 – 17431G → S AA sequence (PubMed:1698775)Curated
    Sequence conflicti2871 – 28722LS → IA AA sequence (PubMed:1698775)Curated
    Sequence conflicti3036 – 30361R → M AA sequence (PubMed:1698775)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti166 – 1661N → D.
    Corresponds to variant rs2306691 [ dbSNP | Ensembl ].
    VAR_021885
    Natural varianti217 – 2171A → V.
    Corresponds to variant rs1800127 [ dbSNP | Ensembl ].
    VAR_014725
    Natural varianti869 – 8691E → K in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035994
    Natural varianti2059 – 20591V → L.
    Corresponds to variant rs2229278 [ dbSNP | Ensembl ].
    VAR_029181
    Natural varianti2080 – 20801D → N.
    Corresponds to variant rs34577247 [ dbSNP | Ensembl ].
    VAR_047525
    Natural varianti2900 – 29001Q → P.3 Publications
    Corresponds to variant rs7397167 [ dbSNP | Ensembl ].
    VAR_047526
    Natural varianti3258 – 32581H → Q Found in a patient with severe mental retardation, seizures, stereotypic behavior, high pain threshold and sleep disturbances. 1 Publication
    VAR_069388
    Natural varianti3760 – 37601R → H in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035995
    Natural varianti4536 – 45361E → G.
    Corresponds to variant rs17357542 [ dbSNP | Ensembl ].
    VAR_047527

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    X15424 Genomic DNA. Translation: CAA33464.1.
    Y18524 Genomic DNA. Translation: CAD57169.1.
    CCDSiCCDS8932.1.
    PIRiS02392.
    RefSeqiNP_002323.2. NM_002332.2.
    UniGeneiHs.162757.

    Genome annotation databases

    EnsembliENST00000243077; ENSP00000243077; ENSG00000123384.
    GeneIDi4035.
    KEGGihsa:4035.
    UCSCiuc001snd.3. human.

    Polymorphism databases

    DMDMi317373384.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    X15424 Genomic DNA. Translation: CAA33464.1 .
    Y18524 Genomic DNA. Translation: CAD57169.1 .
    CCDSi CCDS8932.1.
    PIRi S02392.
    RefSeqi NP_002323.2. NM_002332.2.
    UniGenei Hs.162757.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CR8 NMR - A 1059-1100 [» ]
    1D2L NMR - A 851-893 [» ]
    1J8E X-ray 1.85 A 1011-1054 [» ]
    2FYJ NMR - A 932-1013 [» ]
    2FYL NMR - B 932-1013 [» ]
    2KNX NMR - A 2770-2817 [» ]
    2KNY NMR - A 2770-2817 [» ]
    ProteinModelPortali Q07954.
    SMRi Q07954. Positions 851-893, 932-1054, 1059-1100, 2770-2815, 2856-2896, 3571-3606.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110215. 50 interactions.
    DIPi DIP-50613N.
    IntActi Q07954. 17 interactions.
    MINTi MINT-5004471.

    Chemistry

    DrugBanki DB00009. Alteplase.
    DB00029. Anistreplase.
    DB00025. Antihemophilic Factor.
    DB00102. Becaplermin.
    DB00100. Coagulation Factor IX.
    DB00031. Tenecteplase.

    PTM databases

    PhosphoSitei Q07954.

    Polymorphism databases

    DMDMi 317373384.

    Proteomic databases

    MaxQBi Q07954.
    PaxDbi Q07954.
    PRIDEi Q07954.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000243077 ; ENSP00000243077 ; ENSG00000123384 .
    GeneIDi 4035.
    KEGGi hsa:4035.
    UCSCi uc001snd.3. human.

    Organism-specific databases

    CTDi 4035.
    GeneCardsi GC12P057497.
    HGNCi HGNC:6692. LRP1.
    HPAi CAB018621.
    HPA004182.
    HPA022903.
    MIMi 107770. gene.
    neXtProti NX_Q07954.
    PharmGKBi PA233.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG235850.
    HOGENOMi HOG000230574.
    HOVERGENi HBG006292.
    InParanoidi Q07954.
    KOi K04550.
    OMAi AYFEGPR.
    OrthoDBi EOG790FZT.
    PhylomeDBi Q07954.
    TreeFami TF315253.

    Enzyme and pathway databases

    Reactomei REACT_160163. Scavenging of heme from plasma.
    REACT_24968. Retinoid metabolism and transport.

    Miscellaneous databases

    ChiTaRSi LRP1. human.
    EvolutionaryTracei Q07954.
    GeneWikii LRP1.
    GenomeRNAii 4035.
    NextBioi 15806.
    PROi Q07954.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q07954.
    Bgeei Q07954.
    CleanExi HS_LRP1.
    Genevestigatori Q07954.

    Family and domain databases

    Gene3Di 2.120.10.30. 8 hits.
    4.10.400.10. 29 hits.
    InterProi IPR011042. 6-blade_b-propeller_TolB-like.
    IPR026823. cEGF.
    IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR023415. LDLR_class-A_CS.
    IPR000033. LDLR_classB_rpt.
    IPR002172. LDrepeatLR_classA_rpt.
    [Graphical view ]
    Pfami PF12662. cEGF. 1 hit.
    PF07645. EGF_CA. 1 hit.
    PF00057. Ldl_recept_a. 30 hits.
    PF00058. Ldl_recept_b. 16 hits.
    [Graphical view ]
    PRINTSi PR00261. LDLRECEPTOR.
    SMARTi SM00181. EGF. 18 hits.
    SM00179. EGF_CA. 3 hits.
    SM00192. LDLa. 31 hits.
    SM00135. LY. 35 hits.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 9 hits.
    SSF57424. SSF57424. 30 hits.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor."
      Herz J., Hamann U., Rogne S., Myklebost O., Gausepohl H., Stanley K.K.
      EMBO J. 7:4119-4127(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-2900.
      Tissue: Liver.
    2. "Structure of the gene (LRP1) coding for the human alpha 2-macroglobulin receptor lipoprotein receptor-related protein."
      Van Leuven F., Stas L., Hilliker C., Lorent K., Umans L., Serneels L., Overbergh L., Torrekens S., Moechars D., De Strooper B., Van den Berghe H.
      Genomics 24:78-89(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Strategy to sequence the 89 exons of the human LRP1 gene coding for the lipoprotein receptor related protein: identification of one expressed mutation among 48 polymorphisms."
      Van Leuven F., Stas L., Thiry E., Nelissen B., Miyake Y.
      Genomics 52:138-144(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-2900.
    4. NHLBI resequencing and genotyping service (RS&G)
      Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-2900.
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "Structure of the low-density lipoprotein receptor-related protein (LRP) promoter."
      Kutt H., Herz J., Stanley K.K.
      Biochim. Biophys. Acta 1009:229-236(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
    7. Glaeser C.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
      Tissue: Blood.
    8. "Sequence identity between the alpha 2-macroglobulin receptor and low density lipoprotein receptor-related protein suggests that this molecule is a multifunctional receptor."
      Strickland D.K., Ashcom J.D., Williams S., Burgess W.H., Migliorini M., Argraves W.S.
      J. Biol. Chem. 265:17401-17404(1990) [PubMed] [Europe PMC] [Abstract]
      Tissue: Placenta.
    9. "Proteolytic processing of the 600 kd low density lipoprotein receptor-related protein (LRP) occurs in a trans-Golgi compartment."
      Herz J., Kowal R.C., Goldstein J.L., Brown M.S.
      EMBO J. 9:1769-1776(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING.
    10. "Evidence that the newly cloned low-density-lipoprotein receptor related protein (LRP) is the alpha 2-macroglobulin receptor."
      Kristensen T., Moestrup S.K., Gliemann J., Bendtsen L., Sand O., Sottrup-Jensen L.
      FEBS Lett. 276:151-155(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "The alpha 2-macroglobulin receptor/low density lipoprotein receptor-related protein binds and internalizes Pseudomonas exotoxin A."
      Kounnas M.Z., Morris R.E., Thompson M.R., FitzGerald D.J., Strickland D.K., Saelinger C.B.
      J. Biol. Chem. 267:12420-12423(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A RECEPTOR FOR P.AERUGINOSA EXOA TOXIN.
    12. "Interaction of CED-6/GULP, an adapter protein involved in engulfment of apoptotic cells with CED-1 and CD91/low density lipoprotein receptor-related protein (LRP)."
      Su H.P., Nakada-Tsukui K., Tosello-Trampont A.-C., Li Y., Bu G., Henson P.M., Ravichandran K.S.
      J. Biol. Chem. 277:11772-11779(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GULP1, MUTAGENESIS OF ASN-4470 AND ASN-4504.
    13. "Platelet-derived growth factor (PDGF)-induced tyrosine phosphorylation of the low density lipoprotein receptor-related protein (LRP). Evidence for integrated co-receptor function between LRP and the PDGF."
      Loukinova E., Ranganathan S., Kuznetsov S., Gorlatova N., Migliorini M.M., Loukinov D., Ulery P.G., Mikhailenko I., Lawrence D.A., Strickland D.K.
      J. Biol. Chem. 277:15499-15506(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-4507, MUTAGENESIS OF 4470-ASN--TYR-4473 AND 4504-ASN--TYR-4507, INTERACTION WITH PDGF.
    14. "Proteolytic processing of low density lipoprotein receptor-related protein mediates regulated release of its intracellular domain."
      May P., Reddy Y.K., Herz J.
      J. Biol. Chem. 277:18736-18743(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PROTEOLYTIC PROCESSING.
    15. "The intracellular domain of the low density lipoprotein receptor-related protein modulates transactivation mediated by amyloid precursor protein and Fe65."
      Kinoshita A., Shah T., Tangredi M.M., Strickland D.K., Hyman B.T.
      J. Biol. Chem. 278:41182-41188(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    16. "LDL receptor-related proteins in neurodevelopment."
      May P., Herz J.
      Traffic 4:291-301(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Serine and threonine phosphorylation of the low density lipoprotein receptor-related protein by protein kinase Calpha regulates endocytosis and association with adaptor molecules."
      Ranganathan S., Liu C.-X., Migliorini M.M., Von Arnim C.A.F., Peltan I.D., Mikhailenko I., Hyman B.T., Strickland D.K.
      J. Biol. Chem. 279:40536-40544(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-4460; SER-4517; SER-4520 AND SER-4523, MUTAGENESIS OF THR-4460; THR-4472; SER-4517; SER-4520 AND SER-4523, INTERACTION WITH SHC1; GULP1 AND DAB1.
    18. "Functions of sorting nexin 17 domains and recognition motif for P-selectin trafficking."
      Knauth P., Schlueter T., Czubayko M., Kirsch C., Florian V., Schreckenberger S., Hahn H., Bohnensack R.
      J. Mol. Biol. 347:813-825(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNX17.
    19. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-446; ASN-729; ASN-2127 AND ASN-3048.
      Tissue: Plasma.
    20. "Identification of the ligands of protein interaction domains through a functional approach."
      Caratu G., Allegra D., Bimonte M., Schiattarella G.G., D'Ambrosio C., Scaloni A., Napolitano M., Russo T., Zambrano N.
      Mol. Cell. Proteomics 6:333-345(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH CUBN AND PID1, INTERACTION WITH CUBN AND PID1.
    21. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-446; ASN-729; ASN-1511; ASN-1575; ASN-1616; ASN-1645; ASN-1763; ASN-2127; ASN-2815; ASN-3048; ASN-3089; ASN-3488; ASN-3788; ASN-3953; ASN-4075 AND ASN-4125.
      Tissue: Liver.
    22. Cited for: GLYCOSYLATION AT ASN-729 AND ASN-1511.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein."
      Huang W., Dolmer K., Gettins P.G.W.
      J. Biol. Chem. 274:14130-14136(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1059-1100 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS.
    25. "NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein. Evidence for specific binding to the receptor binding domain of human alpha(2)-macroglobulin."
      Dolmer K., Huang W., Gettins P.G.W.
      J. Biol. Chem. 275:3264-3269(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 851-893 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS.
    26. "Calcium coordination and pH dependence of the calcium affinity of ligand-binding repeat CR7 from the LRP. Comparison with related domains from the LRP and the LDL receptor."
      Simonovic M., Dolmer K., Huang W., Strickland D.K., Volz K., Gettins P.G.
      Biochemistry 40:15127-15134(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1012-1054 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS.
    27. "Binding site structure of one LRP-RAP complex: implications for a common ligand-receptor binding motif."
      Jensen G.A., Andersen O.M.J.J., Bonvin A.M., Bjerrum-Bohr I., Etzerodt M., Thoegersen H.C., O'Shea C., Poulsen F.M., Kragelund B.B.
      J. Mol. Biol. 362:700-716(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 932-1013 IN COMPLEX WITH LRPAP1 AND CALCIUM IONS, DISULFIDE BONDS.
    28. Cited for: VARIANTS [LARGE SCALE ANALYSIS] LYS-869 AND HIS-3760.
    29. Cited for: VARIANT GLN-3258.

    Entry informationi

    Entry nameiLRP1_HUMAN
    AccessioniPrimary (citable) accession number: Q07954
    Secondary accession number(s): Q2PP12, Q8IVG8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 164 of the entry and version 2 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

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

    Documents

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

    External Data

    Dasty 3