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Q07954

- LRP1_HUMAN

UniProt

Q07954 - LRP1_HUMAN

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Protein
Prolow-density lipoprotein receptor-related protein 1
Gene
LRP1, A2MR, APR
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.5 Publications
Functions as a receptor for Pseudomonas aeruginosa exotoxin A.5 Publications

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 Wnt signaling pathway Source: BHF-UCL
  10. negative regulation of neuron apoptotic process Source: Ensembl
  11. negative regulation of platelet-derived growth factor receptor-beta signaling pathway Source: BHF-UCL
  12. negative regulation of smooth muscle cell migration 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
Complete GO annotation...

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 85 kDa subunit : Cell membrane; Single-pass type I membrane protein. Membranecoated pit 1 Publication
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.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 44194400Extracellular Reviewed prediction
Add
BLAST
Transmembranei4420 – 444425Helical; Reviewed prediction
Add
BLAST
Topological domaini4445 – 4544100Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

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. 1 Publication
Mutagenesisi4470 – 44734NPTY → APTA: No effect on tyrosine phosphorylation. 2 Publications
Mutagenesisi4470 – 44701N → A: No effect on interaction with GULP1. 1 Publication
Mutagenesisi4472 – 44721T → A: No detectable effect on phosphorylation. 1 Publication
Mutagenesisi4504 – 45074NPVY → APVA: Loss of tyrosine phosphorylation. Abolishes interaction with SHC1 and GULP1. 2 Publications
Mutagenesisi4504 – 45041N → A: Loss of interaction with GULP1. 1 Publication
Mutagenesisi4517 – 45171S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4520 and A-4523. 1 Publication
Mutagenesisi4520 – 45201S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4523. 1 Publication
Mutagenesisi4523 – 45231S → A: Strongly reduced phosphorylation and loss of interaction with SHC1; when associated with A-4460; A-4517 and A-4520. 1 Publication

Organism-specific databases

PharmGKBiPA233.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 Reviewed prediction
Add
BLAST
Chaini20 – 45444525Prolow-density lipoprotein receptor-related protein 1
PRO_0000017317Add
BLAST
Chaini20 – ?39433924Low-density lipoprotein receptor-related protein 1 515 kDa subunit
PRO_0000302750Add
BLAST
Chaini?3944 – 4544601Low-density lipoprotein receptor-related protein 1 85 kDa subunit
PRO_0000302751Add
BLAST
Chaini?4441 – 4544104Low-density lipoprotein receptor-related protein 1 intracellular domain
PRO_0000302752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 40 By similarity
Disulfide bondi34 ↔ 53 By similarity
Disulfide bondi47 ↔ 64 By similarity
Disulfide bondi72 ↔ 85 By similarity
Disulfide bondi79 ↔ 98 By similarity
Disulfide bondi92 ↔ 108 By similarity
Glycosylationi114 – 1141N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi115 ↔ 124 By similarity
Disulfide bondi120 ↔ 133 By similarity
Disulfide bondi135 ↔ 148 By similarity
Glycosylationi136 – 1361N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi154 ↔ 164 By similarity
Disulfide bondi160 ↔ 173 By similarity
Disulfide bondi175 ↔ 188 By similarity
Glycosylationi185 – 1851N-linked (GlcNAc...) Reviewed prediction
Glycosylationi239 – 2391N-linked (GlcNAc...) Reviewed prediction
Glycosylationi274 – 2741N-linked (GlcNAc...) Reviewed prediction
Glycosylationi357 – 3571N-linked (GlcNAc...) Reviewed prediction
Glycosylationi446 – 4461N-linked (GlcNAc...)2 Publications
Disulfide bondi478 ↔ 493 By similarity
Disulfide bondi489 ↔ 504 By similarity
Disulfide bondi506 ↔ 519 By similarity
Glycosylationi729 – 7291N-linked (GlcNAc...) (complex)3 Publications
Disulfide bondi807 ↔ 818 By similarity
Disulfide bondi814 ↔ 827 By similarity
Disulfide bondi829 ↔ 842 By similarity
Disulfide bondi854 ↔ 8664 Publications
Disulfide bondi861 ↔ 8794 Publications
Disulfide bondi873 ↔ 8904 Publications
Disulfide bondi895 ↔ 907 By similarity
Disulfide bondi902 ↔ 920 By similarity
Disulfide bondi914 ↔ 931 By similarity
Glycosylationi928 – 9281N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi936 ↔ 9484 Publications
Disulfide bondi943 ↔ 9614 Publications
Disulfide bondi955 ↔ 9714 Publications
Disulfide bondi976 ↔ 9894 Publications
Disulfide bondi984 ↔ 10024 Publications
Disulfide bondi996 ↔ 10114 Publications
Disulfide bondi1015 ↔ 10274 Publications
Disulfide bondi1022 ↔ 10404 Publications
Disulfide bondi1034 ↔ 10514 Publications
Glycosylationi1050 – 10501N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1062 ↔ 10754 Publications
Disulfide bondi1069 ↔ 10884 Publications
Disulfide bondi1082 ↔ 10974 Publications
Disulfide bondi1104 ↔ 1118 By similarity
Disulfide bondi1112 ↔ 1131 By similarity
Disulfide bondi1125 ↔ 1140 By similarity
Disulfide bondi1145 ↔ 1159 By similarity
Disulfide bondi1152 ↔ 1172 By similarity
Glycosylationi1154 – 11541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1155 – 11551N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1166 ↔ 1182 By similarity
Disulfide bondi1185 ↔ 1196 By similarity
Disulfide bondi1192 ↔ 1206 By similarity
Glycosylationi1195 – 11951N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1208 ↔ 1221 By similarity
Glycosylationi1218 – 12181N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1227 ↔ 1237 By similarity
Disulfide bondi1233 ↔ 1246 By similarity
Disulfide bondi1248 ↔ 1261 By similarity
Glycosylationi1511 – 15111N-linked (GlcNAc...) (complex)2 Publications
Disulfide bondi1540 ↔ 1553 By similarity
Disulfide bondi1549 ↔ 1563 By similarity
Glycosylationi1558 – 15581N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1565 ↔ 1578 By similarity
Glycosylationi1575 – 15751N-linked (GlcNAc...)1 Publication
Glycosylationi1616 – 16161N-linked (GlcNAc...)1 Publication
Glycosylationi1645 – 16451N-linked (GlcNAc...)1 Publication
Glycosylationi1723 – 17231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1733 – 17331N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1763 – 17631N-linked (GlcNAc...)1 Publication
Glycosylationi1825 – 18251N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1850 ↔ 1861 By similarity
Disulfide bondi1857 ↔ 1871 By similarity
Disulfide bondi1873 ↔ 1886 By similarity
Glycosylationi1933 – 19331N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1995 – 19951N-linked (GlcNAc...) Reviewed prediction
Modified residuei2009 – 20091N6-acetyllysine By similarity
Glycosylationi2048 – 20481N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2117 – 21171N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2127 – 21271N-linked (GlcNAc...)2 Publications
Disulfide bondi2159 ↔ 2170 By similarity
Disulfide bondi2166 ↔ 2180 By similarity
Disulfide bondi2182 ↔ 2194 By similarity
Glycosylationi2472 – 24721N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2482 ↔ 2493 By similarity
Disulfide bondi2489 ↔ 2503 By similarity
Glycosylationi2502 – 25021N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2505 ↔ 2517 By similarity
Glycosylationi2521 – 25211N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2524 ↔ 2537 By similarity
Disulfide bondi2532 ↔ 2550 By similarity
Glycosylationi2539 – 25391N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2544 ↔ 2561 By similarity
Disulfide bondi2566 ↔ 2578 By similarity
Disulfide bondi2573 ↔ 2591 By similarity
Disulfide bondi2585 ↔ 2600 By similarity
Glycosylationi2601 – 26011N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2605 ↔ 2617 By similarity
Disulfide bondi2612 ↔ 2630 By similarity
Glycosylationi2620 – 26201N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2624 ↔ 2639 By similarity
Glycosylationi2638 – 26381N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2644 ↔ 2666 By similarity
Disulfide bondi2660 ↔ 2679 By similarity
Disulfide bondi2673 ↔ 2688 By similarity
Disulfide bondi2696 ↔ 2708 By similarity
Disulfide bondi2703 ↔ 2721 By similarity
Disulfide bondi2715 ↔ 2730 By similarity
Disulfide bondi2734 ↔ 2746 By similarity
Disulfide bondi2741 ↔ 2759 By similarity
Disulfide bondi2753 ↔ 2769 By similarity
Disulfide bondi2774 ↔ 2787 By similarity
Disulfide bondi2781 ↔ 2800 By similarity
Disulfide bondi2794 ↔ 2812 By similarity
Glycosylationi2815 – 28151N-linked (GlcNAc...)1 Publication
Disulfide bondi2818 ↔ 2830 By similarity
Disulfide bondi2825 ↔ 2843 By similarity
Disulfide bondi2837 ↔ 2853 By similarity
Disulfide bondi2858 ↔ 2870 By similarity
Disulfide bondi2865 ↔ 2884 By similarity
Disulfide bondi2878 ↔ 2897 By similarity
Disulfide bondi2904 ↔ 2917 By similarity
Glycosylationi2905 – 29051N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2912 ↔ 2930 By similarity
Disulfide bondi2924 ↔ 2939 By similarity
Disulfide bondi2944 ↔ 2956 By similarity
Disulfide bondi2952 ↔ 2965 By similarity
Disulfide bondi2967 ↔ 2980 By similarity
Disulfide bondi2986 ↔ 2996 By similarity
Disulfide bondi2992 ↔ 3005 By similarity
Disulfide bondi3007 ↔ 3021 By similarity
Glycosylationi3048 – 30481N-linked (GlcNAc...)2 Publications
Glycosylationi3089 – 30891N-linked (GlcNAc...)1 Publication
Glycosylationi3264 – 32641N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3294 ↔ 3305 By similarity
Disulfide bondi3301 ↔ 3315 By similarity
Disulfide bondi3317 ↔ 3330 By similarity
Glycosylationi3333 – 33331N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3334 ↔ 3346 By similarity
Disulfide bondi3341 ↔ 3359 By similarity
Disulfide bondi3353 ↔ 3369 By similarity
Disulfide bondi3374 ↔ 3386 By similarity
Disulfide bondi3381 ↔ 3399 By similarity
Disulfide bondi3393 ↔ 3408 By similarity
Disulfide bondi3413 ↔ 3426 By similarity
Disulfide bondi3420 ↔ 3439 By similarity
Disulfide bondi3433 ↔ 3448 By similarity
Disulfide bondi3453 ↔ 3466 By similarity
Disulfide bondi3460 ↔ 3479 By similarity
Disulfide bondi3473 ↔ 3489 By similarity
Glycosylationi3488 – 34881N-linked (GlcNAc...)1 Publication
Disulfide bondi3494 ↔ 3507 By similarity
Disulfide bondi3501 ↔ 3520 By similarity
Disulfide bondi3514 ↔ 3531 By similarity
Disulfide bondi3536 ↔ 3548 By similarity
Disulfide bondi3543 ↔ 3561 By similarity
Disulfide bondi3555 ↔ 3570 By similarity
Disulfide bondi3575 ↔ 3587 By similarity
Disulfide bondi3582 ↔ 3600 By similarity
Disulfide bondi3594 ↔ 3609 By similarity
Disulfide bondi3613 ↔ 3625 By similarity
Disulfide bondi3620 ↔ 3638 By similarity
Disulfide bondi3632 ↔ 3647 By similarity
Disulfide bondi3654 ↔ 3666 By similarity
Disulfide bondi3661 ↔ 3679 By similarity
Glycosylationi3662 – 36621N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3673 ↔ 3690 By similarity
Disulfide bondi3695 ↔ 3709 By similarity
Disulfide bondi3703 ↔ 3722 By similarity
Disulfide bondi3716 ↔ 3731 By similarity
Disulfide bondi3741 ↔ 3754 By similarity
Disulfide bondi3749 ↔ 3767 By similarity
Disulfide bondi3761 ↔ 3776 By similarity
Disulfide bondi3785 ↔ 3798 By similarity
Glycosylationi3788 – 37881N-linked (GlcNAc...)1 Publication
Disulfide bondi3792 ↔ 3807 By similarity
Disulfide bondi3809 ↔ 3822 By similarity
Disulfide bondi3828 ↔ 3838 By similarity
Disulfide bondi3834 ↔ 3847 By similarity
Glycosylationi3839 – 38391N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3849 ↔ 3860 By similarity
Glycosylationi3953 – 39531N-linked (GlcNAc...)1 Publication
Glycosylationi4075 – 40751N-linked (GlcNAc...)1 Publication
Glycosylationi4125 – 41251N-linked (GlcNAc...)1 Publication
Disulfide bondi4151 ↔ 4160 By similarity
Disulfide bondi4156 ↔ 4169 By similarity
Disulfide bondi4171 ↔ 4182 By similarity
Glycosylationi4179 – 41791N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi4200 ↔ 4210 By similarity
Disulfide bondi4204 ↔ 4220 By similarity
Disulfide bondi4222 ↔ 4231 By similarity
Disulfide bondi4236 ↔ 4246 By similarity
Disulfide bondi4240 ↔ 4256 By similarity
Disulfide bondi4258 ↔ 4267 By similarity
Disulfide bondi4272 ↔ 4282 By similarity
Disulfide bondi4276 ↔ 4292 By similarity
Glycosylationi4278 – 42781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi4279 – 42791N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi4294 ↔ 4303 By similarity
Disulfide bondi4308 ↔ 4318 By similarity
Disulfide bondi4312 ↔ 4328 By similarity
Disulfide bondi4330 ↔ 4339 By similarity
Disulfide bondi4344 ↔ 4352 By similarity
Disulfide bondi4347 ↔ 4363 By similarity
Glycosylationi4364 – 43641N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi4365 ↔ 4374 By similarity
Disulfide bondi4377 ↔ 4387 By similarity
Disulfide bondi4381 ↔ 4397 By similarity
Disulfide bondi4399 ↔ 4408 By similarity
Modified residuei4460 – 44601Phosphothreonine Inferred
Modified residuei4507 – 45071Phosphotyrosine1 Publication
Modified residuei4517 – 45171Phosphoserine Inferred
Modified residuei4520 – 45201Phosphoserine Inferred
Modified residuei4523 – 45231Phosphoserine Inferred

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.
The N-terminus is blocked.
Phosphorylated on serine and threonine residues.2 Publications
Phosphorylated on tyrosine residues upon stimulation with PDGF. Tyrosine phosphorylation promotes interaction with SHC1.2 Publications

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.5 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.
IntActiQ07954. 17 interactions.
MINTiMINT-5004471.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ07954.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4445 – 4544100Interaction with MAFB By similarity
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3940 – 39434Recognition site for proteolytical processing Reviewed prediction
Motifi4502 – 45076NPXY motif

Sequence similaritiesi

Belongs to the LDLR family.
Contains 22 EGF-like domains.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti685 – 6851D → G AA sequence 1 Publication
Sequence conflicti1743 – 17431G → S AA sequence 1 Publication
Sequence conflicti2871 – 28722LS → IA AA sequence 1 Publication
Sequence conflicti3036 – 30361R → M AA sequence 1 Publication

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.
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 163 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

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