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P98164

- LRP2_HUMAN

UniProt

P98164 - LRP2_HUMAN

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Protein

Low-density lipoprotein receptor-related protein 2

Gene
LRP2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Acts together with cubilin to mediate HDL endocytosis By similarity. May participate in regulation of parathyroid-hormone and para-thyroid-hormone-related protein release.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1208 – 12081Calcium By similarity
Metal bindingi1210 – 12101Calcium; via carbonyl oxygen By similarity
Metal bindingi1212 – 12121Calcium By similarity
Metal bindingi1218 – 12181Calcium By similarity
Metal bindingi1219 – 12191Calcium By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. protein binding Source: UniProtKB

GO - Biological processi

  1. cell proliferation Source: Ensembl
  2. endocytosis Source: ProtInc
  3. forebrain development Source: Ensembl
  4. lipid metabolic process Source: ProtInc
  5. phototransduction, visible light Source: Reactome
  6. protein glycosylation Source: ProtInc
  7. receptor-mediated endocytosis Source: ProtInc
  8. retinoid metabolic process Source: Reactome
  9. small molecule metabolic process Source: Reactome
  10. steroid metabolic process Source: Reactome
  11. vitamin D metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_13523. Vitamin D (calciferol) metabolism.
REACT_24968. Retinoid metabolism and transport.
SignaLinkiP98164.

Names & Taxonomyi

Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein 2
Short name:
LRP-2
Alternative name(s):
Glycoprotein 330
Short name:
gp330
Megalin
Gene namesi
Name:LRP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6694. LRP2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 44234398Extracellular Reviewed predictionAdd
BLAST
Transmembranei4424 – 444623Helical; Reviewed predictionAdd
BLAST
Topological domaini4447 – 4655209Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. apical plasma membrane Source: UniProtKB
  2. brush border membrane Source: Ensembl
  3. coated pit Source: UniProtKB-SubCell
  4. endocytic vesicle Source: Ensembl
  5. endoplasmic reticulum Source: Ensembl
  6. endosome Source: Ensembl
  7. extracellular vesicular exosome Source: UniProt
  8. Golgi apparatus Source: Ensembl
  9. integral component of membrane Source: UniProtKB-KW
  10. lysosomal membrane Source: UniProtKB
  11. lysosome Source: ProtInc
  12. plasma membrane Source: Reactome
  13. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Membrane

Pathology & Biotechi

Involvement in diseasei

Donnai-Barrow syndrome (DBS) [MIM:222448]: Rare autosomal recessive disorder characterized by major malformations including agenesis of the corpus callosum, congenital diaphragmatic hernia, facial dysmorphology, ocular anomalies, sensorineural hearing loss and developmental delay. The FOAR syndrome was first described as comprising facial anomalies, ocular anomalies, sensorineural hearing loss, and proteinuria. DBS and FOAR were first described as distinct disorders but the classic distinguishing features between the 2 disorders were presence of proteinuria and absence of diaphragmatic hernia and corpus callosum anomalies in FOAR. Early reports noted that the 2 disorders shared many phenotypic features and may be identical. Although there is variability in the expression of some features (e.g., agenesis of the corpus callosum and proteinuria), DBS and FOAR are now considered to represent the same entity.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2522 – 25221Y → H in DBS. 1 Publication
VAR_037013

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi222448. phenotype.
Orphaneti2143. Donnai-Barrow syndrome.
PharmGKBiPA30452.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525 Reviewed predictionAdd
BLAST
Chaini26 – 46554630Low-density lipoprotein receptor-related protein 2PRO_0000017321Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 40 By similarity
Disulfide bondi35 ↔ 53 By similarity
Disulfide bondi47 ↔ 62 By similarity
Disulfide bondi67 ↔ 80 By similarity
Disulfide bondi74 ↔ 93 By similarity
Disulfide bondi87 ↔ 103 By similarity
Disulfide bondi108 ↔ 120 By similarity
Disulfide bondi115 ↔ 133 By similarity
Disulfide bondi127 ↔ 142 By similarity
Disulfide bondi147 ↔ 157 By similarity
Disulfide bondi152 ↔ 170 By similarity
Glycosylationi159 – 1591N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi164 ↔ 179 By similarity
Glycosylationi178 – 1781N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi183 ↔ 195 By similarity
Disulfide bondi190 ↔ 208 By similarity
Disulfide bondi202 ↔ 217 By similarity
Disulfide bondi222 ↔ 234 By similarity
Disulfide bondi229 ↔ 247 By similarity
Disulfide bondi241 ↔ 256 By similarity
Disulfide bondi266 ↔ 279 By similarity
Disulfide bondi273 ↔ 292 By similarity
Disulfide bondi286 ↔ 307 By similarity
Glycosylationi299 – 2991N-linked (GlcNAc...) Reviewed prediction
Glycosylationi300 – 3001N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi312 ↔ 321 By similarity
Disulfide bondi317 ↔ 330 By similarity
Disulfide bondi332 ↔ 346 By similarity
Glycosylationi341 – 3411N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi352 ↔ 362 By similarity
Disulfide bondi358 ↔ 371 By similarity
Disulfide bondi373 ↔ 385 By similarity
Glycosylationi388 – 3881N-linked (GlcNAc...) Reviewed prediction
Glycosylationi463 – 4631N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi663 ↔ 674 By similarity
Disulfide bondi670 ↔ 689 By similarity
Disulfide bondi691 ↔ 704 By similarity
Glycosylationi866 – 8661N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi974 ↔ 988 By similarity
Disulfide bondi984 ↔ 998 By similarity
Disulfide bondi1000 ↔ 1013 By similarity
Disulfide bondi1026 ↔ 1038 By similarity
Disulfide bondi1033 ↔ 1051 By similarity
Disulfide bondi1045 ↔ 1060 By similarity
Glycosylationi1064 – 10641N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1067 ↔ 1079 By similarity
Disulfide bondi1074 ↔ 1092 By similarity
Disulfide bondi1086 ↔ 1101 By similarity
Disulfide bondi1109 ↔ 1121 By similarity
Disulfide bondi1116 ↔ 1134 By similarity
Disulfide bondi1128 ↔ 1143 By similarity
Glycosylationi1144 – 11441N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1149 ↔ 1161 By similarity
Disulfide bondi1156 ↔ 1174 By similarity
Disulfide bondi1168 ↔ 1183 By similarity
Glycosylationi1186 – 11861N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1187 ↔ 1200 By similarity
Disulfide bondi1194 ↔ 1213 By similarity
Disulfide bondi1207 ↔ 1222 By similarity
Disulfide bondi1230 ↔ 1243 By similarity
Disulfide bondi1237 ↔ 1256 By similarity
Disulfide bondi1250 ↔ 1266 By similarity
Disulfide bondi1271 ↔ 1283 By similarity
Disulfide bondi1278 ↔ 1296 By similarity
Disulfide bondi1290 ↔ 1305 By similarity
Disulfide bondi1312 ↔ 1325 By similarity
Disulfide bondi1319 ↔ 1338 By similarity
Glycosylationi1327 – 13271N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1332 ↔ 1348 By similarity
Glycosylationi1340 – 13401N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1353 ↔ 1364 By similarity
Disulfide bondi1360 ↔ 1373 By similarity
Disulfide bondi1375 ↔ 1388 By similarity
Glycosylationi1383 – 13831N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1394 ↔ 1404 By similarity
Disulfide bondi1400 ↔ 1413 By similarity
Disulfide bondi1415 ↔ 1428 By similarity
Glycosylationi1464 – 14641N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1496 – 14961N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1550 – 15501N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1675 – 16751N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1704 ↔ 1713 By similarity
Disulfide bondi1709 ↔ 1725 By similarity
Disulfide bondi1727 ↔ 1740 By similarity
Glycosylationi1810 – 18101N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2022 ↔ 2033 By similarity
Disulfide bondi2029 ↔ 2043 By similarity
Disulfide bondi2045 ↔ 2058 By similarity
Glycosylationi2055 – 20551N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2177 – 21771N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2224 – 22241N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2346 ↔ 2357 By similarity
Disulfide bondi2353 ↔ 2368 By similarity
Disulfide bondi2370 ↔ 2382 By similarity
Glycosylationi2499 – 24991N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2547 – 25471N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2655 ↔ 2666 By similarity
Disulfide bondi2662 ↔ 2675 By similarity
Disulfide bondi2677 ↔ 2692 By similarity
Disulfide bondi2700 ↔ 2712 By similarity
Disulfide bondi2707 ↔ 2725 By similarity
Disulfide bondi2719 ↔ 2736 By similarity
Disulfide bondi2741 ↔ 2753 By similarity
Disulfide bondi2748 ↔ 2766 By similarity
Disulfide bondi2760 ↔ 2775 By similarity
Disulfide bondi2780 ↔ 2793 By similarity
Glycosylationi2781 – 27811N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2788 ↔ 2806 By similarity
Disulfide bondi2800 ↔ 2817 By similarity
Glycosylationi2809 – 28091N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2810 – 28101N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2822 ↔ 2835 By similarity
Disulfide bondi2829 ↔ 2848 By similarity
Disulfide bondi2842 ↔ 2859 By similarity
Disulfide bondi2864 ↔ 2876 By similarity
Disulfide bondi2871 ↔ 2889 By similarity
Disulfide bondi2883 ↔ 2899 By similarity
Disulfide bondi2906 ↔ 2918 By similarity
Disulfide bondi2913 ↔ 2931 By similarity
Disulfide bondi2925 ↔ 2943 By similarity
Glycosylationi2947 – 29471N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2948 ↔ 2965 By similarity
Disulfide bondi2955 ↔ 2978 By similarity
Disulfide bondi2972 ↔ 2988 By similarity
Glycosylationi2987 – 29871N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2993 ↔ 3005 By similarity
Disulfide bondi3000 ↔ 3018 By similarity
Disulfide bondi3012 ↔ 3027 By similarity
Disulfide bondi3032 ↔ 3044 By similarity
Disulfide bondi3039 ↔ 3057 By similarity
Disulfide bondi3051 ↔ 3068 By similarity
Disulfide bondi3075 ↔ 3087 By similarity
Disulfide bondi3082 ↔ 3100 By similarity
Disulfide bondi3094 ↔ 3109 By similarity
Disulfide bondi3114 ↔ 3126 By similarity
Disulfide bondi3122 ↔ 3135 By similarity
Glycosylationi3125 – 31251N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3137 ↔ 3150 By similarity
Disulfide bondi3156 ↔ 3167 By similarity
Disulfide bondi3163 ↔ 3176 By similarity
Disulfide bondi3178 ↔ 3191 By similarity
Glycosylationi3211 – 32111N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3257 – 32571N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3315 – 33151N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3355 – 33551N-linked (GlcNAc...) Reviewed prediction
Glycosylationi3446 – 34461N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3469 ↔ 3480 By similarity
Disulfide bondi3476 ↔ 3491 By similarity
Disulfide bondi3493 ↔ 3508 By similarity
Disulfide bondi3512 ↔ 3525 By similarity
Disulfide bondi3519 ↔ 3538 By similarity
Disulfide bondi3532 ↔ 3548 By similarity
Disulfide bondi3553 ↔ 3565 By similarity
Disulfide bondi3560 ↔ 3578 By similarity
Glycosylationi3564 – 35641N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3572 ↔ 3589 By similarity
Disulfide bondi3594 ↔ 3606 By similarity
Disulfide bondi3601 ↔ 3619 By similarity
Disulfide bondi3613 ↔ 3630 By similarity
Disulfide bondi3635 ↔ 3647 By similarity
Disulfide bondi3642 ↔ 3660 By similarity
Disulfide bondi3654 ↔ 3671 By similarity
Disulfide bondi3678 ↔ 3692 By similarity
Glycosylationi3680 – 36801N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3686 ↔ 3705 By similarity
Disulfide bondi3699 ↔ 3714 By similarity
Disulfide bondi3719 ↔ 3732 By similarity
Disulfide bondi3727 ↔ 3745 By similarity
Disulfide bondi3739 ↔ 3754 By similarity
Disulfide bondi3759 ↔ 3771 By similarity
Disulfide bondi3766 ↔ 3784 By similarity
Disulfide bondi3778 ↔ 3793 By similarity
Disulfide bondi3798 ↔ 3810 By similarity
Disulfide bondi3805 ↔ 3823 By similarity
Disulfide bondi3817 ↔ 3832 By similarity
Disulfide bondi3842 ↔ 3854 By similarity
Disulfide bondi3849 ↔ 3867 By similarity
Disulfide bondi3861 ↔ 3878 By similarity
Disulfide bondi3883 ↔ 3896 By similarity
Disulfide bondi3891 ↔ 3909 By similarity
Disulfide bondi3903 ↔ 3920 By similarity
Disulfide bondi3928 ↔ 3940 By similarity
Disulfide bondi3935 ↔ 3953 By similarity
Disulfide bondi3947 ↔ 3962 By similarity
Disulfide bondi3970 ↔ 3979 By similarity
Disulfide bondi3975 ↔ 3989 By similarity
Glycosylationi3978 – 39781N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi3991 ↔ 4005 By similarity
Disulfide bondi4011 ↔ 4021 By similarity
Disulfide bondi4017 ↔ 4030 By similarity
Disulfide bondi4032 ↔ 4047 By similarity
Glycosylationi4068 – 40681N-linked (GlcNAc...) Reviewed prediction
Glycosylationi4327 – 43271N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi4334 ↔ 4342 By similarity
Disulfide bondi4338 ↔ 4351 By similarity
Disulfide bondi4353 ↔ 4367 By similarity
Disulfide bondi4381 ↔ 4389 By similarity
Disulfide bondi4383 ↔ 4399 By similarity
Disulfide bondi4401 ↔ 4410 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP98164.
PaxDbiP98164.
PRIDEiP98164.

PTM databases

PhosphoSiteiP98164.

Expressioni

Tissue specificityi

Absorptive epithelia, including renal proximal tubules.

Gene expression databases

ArrayExpressiP98164.
BgeeiP98164.
CleanExiHS_LRP2.
GenevestigatoriP98164.

Organism-specific databases

HPAiHPA005980.

Interactioni

Subunit structurei

Binds plasminogen, extracellular matrix components, plasminogen activator-plasminogen activator inhibitor type I complex, apolipoprotein E-enriched beta-VLDL, lipoprotein lipase, lactoferrin, CLU/clusterin and calcium. Forms a multimeric complex together with a receptor-associated protein (RAP). Binds to ankyrin-repeat family A protein 2 (ANKRA2). Interacts with LRP2BP. Interacts (via NPXY motif) with DAB2; the interaction is not affected by tyrosine phosphorylation of the NPXY motif.4 Publications

Protein-protein interaction databases

BioGridi110216. 34 interactions.
IntActiP98164. 9 interactions.
MINTiMINT-2860496.
STRINGi9606.ENSP00000263816.

Structurei

Secondary structure

1
4655
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1111 – 11155
Beta strandi1121 – 11233
Beta strandi1129 – 11313
Beta strandi1133 – 11364
Helixi1138 – 11414

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M0PNMR-A1103-1148[»]
ProteinModelPortaliP98164.
SMRiP98164. Positions 26-1346, 1351-4373.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 6439LDL-receptor class A 1Add
BLAST
Domaini65 – 10541LDL-receptor class A 2Add
BLAST
Domaini106 – 14439LDL-receptor class A 3Add
BLAST
Domaini145 – 18137LDL-receptor class A 4Add
BLAST
Domaini182 – 21938LDL-receptor class A 5Add
BLAST
Domaini220 – 25839LDL-receptor class A 6Add
BLAST
Domaini264 – 30845LDL-receptor class A 7Add
BLAST
Domaini309 – 34739EGF-like 1Add
BLAST
Domaini348 – 38639EGF-like 2Add
BLAST
Repeati436 – 47843LDL-receptor class B 1Add
BLAST
Repeati479 – 52143LDL-receptor class B 2Add
BLAST
Repeati522 – 56847LDL-receptor class B 3Add
BLAST
Repeati569 – 61244LDL-receptor class B 4Add
BLAST
Repeati613 – 65341LDL-receptor class B 5Add
BLAST
Domaini659 – 70547EGF-like 3Add
BLAST
Repeati753 – 79543LDL-receptor class B 6Add
BLAST
Repeati796 – 83742LDL-receptor class B 7Add
BLAST
Repeati838 – 88144LDL-receptor class B 8Add
BLAST
Repeati882 – 92544LDL-receptor class B 9Add
BLAST
Domaini970 – 101445EGF-like 4Add
BLAST
Domaini1024 – 106239LDL-receptor class A 8Add
BLAST
Domaini1065 – 110339LDL-receptor class A 9Add
BLAST
Domaini1107 – 114539LDL-receptor class A 10Add
BLAST
Domaini1147 – 118539LDL-receptor class A 11Add
BLAST
Domaini1186 – 122439LDL-receptor class A 12Add
BLAST
Domaini1228 – 126841LDL-receptor class A 13Add
BLAST
Domaini1269 – 130739LDL-receptor class A 14Add
BLAST
Domaini1310 – 135041LDL-receptor class A 15Add
BLAST
Domaini1349 – 138941EGF-like 5Add
BLAST
Domaini1390 – 142940EGF-like 6; calcium-binding Reviewed predictionAdd
BLAST
Repeati1478 – 152043LDL-receptor class B 10Add
BLAST
Repeati1521 – 156343LDL-receptor class B 11Add
BLAST
Repeati1566 – 160944LDL-receptor class B 12Add
BLAST
Repeati1610 – 165445LDL-receptor class B 13Add
BLAST
Repeati1655 – 169541LDL-receptor class B 14Add
BLAST
Domaini1700 – 174142EGF-like 7Add
BLAST
Repeati1790 – 183243LDL-receptor class B 15Add
BLAST
Repeati1833 – 188250LDL-receptor class B 16Add
BLAST
Repeati1883 – 193048LDL-receptor class B 17Add
BLAST
Repeati1931 – 197141LDL-receptor class B 18Add
BLAST
Repeati1972 – 201342LDL-receptor class B 19Add
BLAST
Domaini2018 – 205942EGF-like 8Add
BLAST
Repeati2107 – 215650LDL-receptor class B 20Add
BLAST
Repeati2157 – 220145LDL-receptor class B 21Add
BLAST
Repeati2202 – 224544LDL-receptor class B 22Add
BLAST
Repeati2246 – 228944LDL-receptor class B 23Add
BLAST
Repeati2290 – 233142LDL-receptor class B 24Add
BLAST
Domaini2342 – 238342EGF-like 9Add
BLAST
Repeati2431 – 247747LDL-receptor class B 25Add
BLAST
Repeati2478 – 251841LDL-receptor class B 26Add
BLAST
Repeati2519 – 256244LDL-receptor class B 27Add
BLAST
Repeati2563 – 260341LDL-receptor class B 28Add
BLAST
Repeati2604 – 264643LDL-receptor class B 29Add
BLAST
Domaini2651 – 269343EGF-like 10Add
BLAST
Domaini2698 – 273841LDL-receptor class A 16Add
BLAST
Domaini2739 – 277739LDL-receptor class A 17Add
BLAST
Domaini2778 – 281942LDL-receptor class A 18Add
BLAST
Domaini2820 – 286142LDL-receptor class A 19Add
BLAST
Domaini2862 – 290140LDL-receptor class A 20Add
BLAST
Domaini2904 – 294542LDL-receptor class A 21Add
BLAST
Domaini2946 – 299045LDL-receptor class A 22Add
BLAST
Domaini2991 – 302939LDL-receptor class A 23Add
BLAST
Domaini3030 – 307041LDL-receptor class A 24Add
BLAST
Domaini3073 – 311038LDL-receptor class A 25Add
BLAST
Domaini3111 – 315141EGF-like 11Add
BLAST
Domaini3152 – 319241EGF-like 12; calcium-binding Reviewed predictionAdd
BLAST
Repeati3239 – 328143LDL-receptor class B 30Add
BLAST
Repeati3282 – 332443LDL-receptor class B 31Add
BLAST
Repeati3333 – 337644LDL-receptor class B 32Add
BLAST
Repeati3377 – 341842LDL-receptor class B 33Add
BLAST
Repeati3419 – 346042LDL-receptor class B 34Add
BLAST
Domaini3465 – 350945EGF-like 13Add
BLAST
Domaini3510 – 355041LDL-receptor class A 26Add
BLAST
Domaini3551 – 359141LDL-receptor class A 27Add
BLAST
Domaini3592 – 363241LDL-receptor class A 28Add
BLAST
Domaini3633 – 367341LDL-receptor class A 29Add
BLAST
Domaini3676 – 371641LDL-receptor class A 30Add
BLAST
Domaini3717 – 375640LDL-receptor class A 31Add
BLAST
Domaini3757 – 379539LDL-receptor class A 32Add
BLAST
Domaini3796 – 383439LDL-receptor class A 33Add
BLAST
Domaini3840 – 388041LDL-receptor class A 34Add
BLAST
Domaini3881 – 392242LDL-receptor class A 35Add
BLAST
Domaini3926 – 396439LDL-receptor class A 36Add
BLAST
Domaini3966 – 400641EGF-like 14Add
BLAST
Domaini4007 – 404842EGF-like 15; calcium-binding Reviewed predictionAdd
BLAST
Repeati4154 – 419643LDL-receptor class B 35Add
BLAST
Repeati4197 – 424044LDL-receptor class B 36Add
BLAST
Repeati4242 – 428342LDL-receptor class B 37Add
BLAST
Domaini4330 – 436839EGF-like 16Add
BLAST
Domaini4377 – 441135EGF-like 17Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4589 – 460214Interaction with DAB2Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi4453 – 446210SH3-binding Reviewed prediction
Motifi4521 – 45266Endocytosis signal Reviewed prediction
Motifi4593 – 45986NPXY motif
Motifi4598 – 46014SH2-binding Reviewed prediction
Motifi4611 – 462212SH3-binding Reviewed predictionAdd
BLAST

Sequence similaritiesi

Belongs to the LDLR family.
Contains 17 EGF-like domains.

Keywords - Domaini

EGF-like domain, Repeat, SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG235850.
HOGENOMiHOG000230574.
HOVERGENiHBG097941.
InParanoidiP98164.
KOiK06233.
OMAiFWADYGQ.
OrthoDBiEOG790FZT.
PhylomeDBiP98164.
TreeFamiTF315253.

Family and domain databases

Gene3Di2.120.10.30. 8 hits.
4.10.400.10. 35 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.
IPR019825. Lectin_legB_Mn/Ca_BS.
[Graphical view]
PfamiPF12662. cEGF. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00057. Ldl_recept_a. 34 hits.
PF00058. Ldl_recept_b. 14 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 15 hits.
SM00179. EGF_CA. 3 hits.
SM00192. LDLa. 36 hits.
SM00135. LY. 38 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 5 hits.
SSF57424. SSF57424. 36 hits.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 9 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 3 hits.
PS01209. LDLRA_1. 31 hits.
PS50068. LDLRA_2. 36 hits.
PS51120. LDLRB. 35 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P98164-1 [UniParc]FASTAAdd to Basket

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MDRGPAAVAC TLLLALVACL APASGQECDS AHFRCGSGHC IPADWRCDGT     50
KDCSDDADEI GCAVVTCQQG YFKCQSEGQC IPNSWVCDQD QDCDDGSDER 100
QDCSQSTCSS HQITCSNGQC IPSEYRCDHV RDCPDGADEN DCQYPTCEQL 150
TCDNGACYNT SQKCDWKVDC RDSSDEINCT EICLHNEFSC GNGECIPRAY 200
VCDHDNDCQD GSDEHACNYP TCGGYQFTCP SGRCIYQNWV CDGEDDCKDN 250
GDEDGCESGP HDVHKCSPRE WSCPESGRCI SIYKVCDGIL DCPGREDENN 300
TSTGKYCSMT LCSALNCQYQ CHETPYGGAC FCPPGYIINH NDSRTCVEFD 350
DCQIWGICDQ KCESRPGRHL CHCEEGYILE RGQYCKANDS FGEASIIFSN 400
GRDLLIGDIH GRSFRILVES QNRGVAVGVA FHYHLQRVFW TDTVQNKVFS 450
VDINGLNIQE VLNVSVETPE NLAVDWVNNK IYLVETKVNR IDMVNLDGSY 500
RVTLITENLG HPRGIAVDPT VGYLFFSDWE SLSGEPKLER AFMDGSNRKD 550
LVKTKLGWPA GVTLDMISKR VYWVDSRFDY IETVTYDGIQ RKTVVHGGSL 600
IPHPFGVSLF EGQVFFTDWT KMAVLKANKF TETNPQVYYQ ASLRPYGVTV 650
YHSLRQPYAT NPCKDNNGGC EQVCVLSHRT DNDGLGFRCK CTFGFQLDTD 700
ERHCIAVQNF LIFSSQVAIR GIPFTLSTQE DVMVPVSGNP SFFVGIDFDA 750
QDSTIFFSDM SKHMIFKQKI DGTGREILAA NRVENVESLA FDWISKNLYW 800
TDSHYKSISV MRLADKTRRT VVQYLNNPRS VVVHPFAGYL FFTDWFRPAK 850
IMRAWSDGSH LLPVINTTLG WPNGLAIDWA ASRLYWVDAY FDKIEHSTFD 900
GLDRRRLGHI EQMTHPFGLA IFGEHLFFTD WRLGAIIRVR KADGGEMTVI 950
RSGIAYILHL KSYDVNIQTG SNACNQPTHP NGDCSHFCFP VPNFQRVCGC 1000
PYGMRLASNH LTCEGDPTNE PPTEQCGLFS FPCKNGRCVP NYYLCDGVDD 1050
CHDNSDEQLC GTLNNTCSSS AFTCGHGECI PAHWRCDKRN DCVDGSDEHN 1100
CPTHAPASCL DTQYTCDNHQ CISKNWVCDT DNDCGDGSDE KNCNSTETCQ 1150
PSQFNCPNHR CIDLSFVCDG DKDCVDGSDE VGCVLNCTAS QFKCASGDKC 1200
IGVTNRCDGV FDCSDNSDEA GCPTRPPGMC HSDEFQCQED GICIPNFWEC 1250
DGHPDCLYGS DEHNACVPKT CPSSYFHCDN GNCIHRAWLC DRDNDCGDMS 1300
DEKDCPTQPF RCPSWQWQCL GHNICVNLSV VCDGIFDCPN GTDESPLCNG 1350
NSCSDFNGGC THECVQEPFG AKCLCPLGFL LANDSKTCED IDECDILGSC 1400
SQHCYNMRGS FRCSCDTGYM LESDGRTCKV TASESLLLLV ASQNKIIADS 1450
VTSQVHNIYS LVENGSYIVA VDFDSISGRI FWSDATQGKT WSAFQNGTDR 1500
RVVFDSSIIL TETIAIDWVG RNLYWTDYAL ETIEVSKIDG SHRTVLISKN 1550
LTNPRGLALD PRMNEHLLFW SDWGHHPRIE RASMDGSMRT VIVQDKIFWP 1600
CGLTIDYPNR LLYFMDSYLD YMDFCDYNGH HRRQVIASDL IIRHPYALTL 1650
FEDSVYWTDR ATRRVMRANK WHGGNQSVVM YNIQWPLGIV AVHPSKQPNS 1700
VNPCAFSRCS HLCLLSSQGP HFYSCVCPSG WSLSPDLLNC LRDDQPFLIT 1750
VRQHIIFGIS LNPEVKSNDA MVPIAGIQNG LDVEFDDAEQ YIYWVENPGE 1800
IHRVKTDGTN RTVFASISMV GPSMNLALDW ISRNLYSTNP RTQSIEVLTL 1850
HGDIRYRKTL IANDGTALGV GFPIGITVDP ARGKLYWSDQ GTDSGVPAKI 1900
ASANMDGTSV KTLFTGNLEH LECVTLDIEE QKLYWAVTGR GVIERGNVDG 1950
TDRMILVHQL SHPWGIAVHD SFLYYTDEQY EVIERVDKAT GANKIVLRDN 2000
VPNLRGLQVY HRRNAAESSN GCSNNMNACQ QICLPVPGGL FSCACATGFK 2050
LNPDNRSCSP YNSFIVVSML SAIRGFSLEL SDHSETMVPV AGQGRNALHV 2100
DVDVSSGFIY WCDFSSSVAS DNAIRRIKPD GSSLMNIVTH GIGENGVRGI 2150
AVDWVAGNLY FTNAFVSETL IEVLRINTTY RRVLLKVTVD MPRHIVVDPK 2200
NRYLFWADYG QRPKIERSFL DCTNRTVLVS EGIVTPRGLA VDRSDGYVYW 2250
VDDSLDIIAR IRINGENSEV IRYGSRYPTP YGITVFENSI IWVDRNLKKI 2300
FQASKEPENT EPPTVIRDNI NWLRDVTIFD KQVQPRSPAE VNNNPCLENN 2350
GGCSHLCFAL PGLHTPKCDC AFGTLQSDGK NCAISTENFL IFALSNSLRS 2400
LHLDPENHSP PFQTINVERT VMSLDYDSVS DRIYFTQNLA SGVGQISYAT 2450
LSSGIHTPTV IASGIGTADG IAFDWITRRI YYSDYLNQMI NSMAEDGSNR 2500
TVIARVPKPR AIVLDPCQGY LYWADWDTHA KIERATLGGN FRVPIVNSSL 2550
VMPSGLTLDY EEDLLYWVDA SLQRIERSTL TGVDREVIVN AAVHAFGLTL 2600
YGQYIYWTDL YTQRIYRANK YDGSGQIAMT TNLLSQPRGI NTVVKNQKQQ 2650
CNNPCEQFNG GCSHICAPGP NGAECQCPHE GNWYLANNRK HCIVDNGERC 2700
GASSFTCSNG RCISEEWKCD NDNDCGDGSD EMESVCALHT CSPTAFTCAN 2750
GRCVQYSYRC DYYNDCGDGS DEAGCLFRDC NATTEFMCNN RRCIPREFIC 2800
NGVDNCHDNN TSDEKNCPDR TCQSGYTKCH NSNICIPRVY LCDGDNDCGD 2850
NSDENPTYCT THTCSSSEFQ CASGRCIPQH WYCDQETDCF DASDEPASCG 2900
HSERTCLADE FKCDGGRCIP SEWICDGDND CGDMSDEDKR HQCQNQNCSD 2950
SEFLCVNDRP PDRRCIPQSW VCDGDVDCTD GYDENQNCTR RTCSENEFTC 3000
GYGLCIPKIF RCDRHNDCGD YSDERGCLYQ TCQQNQFTCQ NGRCISKTFV 3050
CDEDNDCGDG SDELMHLCHT PEPTCPPHEF KCDNGRCIEM MKLCNHLDDC 3100
LDNSDEKGCG INECHDPSIS GCDHNCTDTL TSFYCSCRPG YKLMSDKRTC 3150
VDIDECTEMP FVCSQKCENV IGSYICKCAP GYLREPDGKT CRQNSNIEPY 3200
LIFSNRYYLR NLTIDGYFYS LILEGLDNVV ALDFDRVEKR LYWIDTQRQV 3250
IERMFLNKTN KETIINHRLP AAESLAVDWV SRKLYWLDAR LDGLFVSDLN 3300
GGHRRMLAQH CVDANNTFCF DNPRGLALHP QYGYLYWADW GHRAYIGRVG 3350
MDGTNKSVII STKLEWPNGI TIDYTNDLLY WADAHLGYIE YSDLEGHHRH 3400
TVYDGALPHP FAITIFEDTI YWTDWNTRTV EKGNKYDGSN RQTLVNTTHR 3450
PFDIHVYHPY RQPIVSNPCG TNNGGCSHLC LIKPGGKGFT CECPDDFRTL 3500
QLSGSTYCMP MCSSTQFLCA NNEKCIPIWW KCDGQKDCSD GSDELALCPQ 3550
RFCRLGQFQC SDGNCTSPQT LCNAHQNCPD GSDEDRLLCE NHHCDSNEWQ 3600
CANKRCIPES WQCDTFNDCE DNSDEDSSHC ASRTCRPGQF RCANGRCIPQ 3650
AWKCDVDNDC GDHSDEPIEE CMSSAHLCDN FTEFSCKTNY RCIPKWAVCN 3700
GVDDCRDNSD EQGCEERTCH PVGDFRCKNH HCIPLRWQCD GQNDCGDNSD 3750
EENCAPRECT ESEFRCVNQQ CIPSRWICDH YNDCGDNSDE RDCEMRTCHP 3800
EYFQCTSGHC VHSELKCDGS ADCLDASDEA DCPTRFPDGA YCQATMFECK 3850
NHVCIPPYWK CDGDDDCGDG SDEELHLCLD VPCNSPNRFR CDNNRCIYSH 3900
EVCNGVDDCG DGTDETEEHC RKPTPKPCTE YEYKCGNGHC IPHDNVCDDA 3950
DDCGDWSDEL GCNKGKERTC AENICEQNCT QLNEGGFICS CTAGFETNVF 4000
DRTSCLDINE CEQFGTCPQH CRNTKGSYEC VCADGFTSMS DRPGKRCAAE 4050
GSSPLLLLPD NVRIRKYNLS SERFSEYLQD EEYIQAVDYD WDPKDIGLSV 4100
VYYTVRGEGS RFGAIKRAYI PNFESGRNNL VQEVDLKLKY VMQPDGIAVD 4150
WVGRHIYWSD VKNKRIEVAK LDGRYRKWLI STDLDQPAAI AVNPKLGLMF 4200
WTDWGKEPKI ESAWMNGEDR NILVFEDLGW PTGLSIDYLN NDRIYWSDFK 4250
EDVIETIKYD GTDRRVIAKE AMNPYSLDIF EDQLYWISKE KGEVWKQNKF 4300
GQGKKEKTLV VNPWLTQVRI FHQLRYNKSV PNLCKQICSH LCLLRPGGYS 4350
CACPQGSSFI EGSTTECDAA IELPINLPPP CRCMHGGNCY FDETDLPKCK 4400
CPSGYTGKYC EMAFSKGISP GTTAVAVLLT ILLIVVIGAL AIAGFFHYRR 4450
TGSLLPALPK LPSLSSLVKP SENGNGVTFR SGADLNMDIG VSGFGPETAI 4500
DRSMAMSEDF VMEMGKQPII FENPMYSARD SAVKVVQPIQ VTVSENVDNK 4550
NYGSPINPSE IVPETNPTSP AADGTQVTKW NLFKRKSKQT TNFENPIYAQ 4600
MENEQKESVA ATPPPSPSLP AKPKPPSRRD PTPTYSATED TFKDTANLVK 4650
EDSEV 4655
Length:4,655
Mass (Da):521,958
Last modified:November 13, 2007 - v3
Checksum:iC73C4206B8B28CE0
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti83 – 831N → S.1 Publication
Corresponds to variant rs2229263 [ dbSNP | Ensembl ].
VAR_037009
Natural varianti103 – 1031C → R Found in a renal cell carcinoma sample; somatic mutation. 1 Publication
VAR_064727
Natural varianti259 – 2591G → R.
Corresponds to variant rs34693334 [ dbSNP | Ensembl ].
VAR_061294
Natural varianti669 – 6691G → D.
Corresponds to variant rs34291900 [ dbSNP | Ensembl ].
VAR_037010
Natural varianti909 – 9091H → R.
Corresponds to variant rs36082715 [ dbSNP | Ensembl ].
VAR_037011
Natural varianti1083 – 10831H → Q.
Corresponds to variant rs2302691 [ dbSNP | Ensembl ].
VAR_037012
Natural varianti1279 – 12791D → A.
Corresponds to variant rs17848149 [ dbSNP | Ensembl ].
VAR_029182
Natural varianti1287 – 12871A → P.
VAR_005421
Natural varianti2012 – 20121R → K.
Corresponds to variant rs4667596 [ dbSNP | Ensembl ].
VAR_029183
Natural varianti2065 – 20651I → T.
Corresponds to variant rs2228168 [ dbSNP | Ensembl ].
VAR_020218
Natural varianti2522 – 25221Y → H in DBS. 1 Publication
VAR_037013
Natural varianti2632 – 26321N → D.
Corresponds to variant rs17848169 [ dbSNP | Ensembl ].
VAR_029184
Natural varianti2872 – 28721A → T.
Corresponds to variant rs2228171 [ dbSNP | Ensembl ].
VAR_005422
Natural varianti3011 – 30111R → M.
Corresponds to variant rs11674973 [ dbSNP | Ensembl ].
VAR_037014
Natural varianti3305 – 33051R → H.
Corresponds to variant rs3213760 [ dbSNP | Ensembl ].
VAR_020219
Natural varianti4094 – 40941K → E.1 Publication
Corresponds to variant rs2075252 [ dbSNP | Ensembl ].
VAR_005423
Natural varianti4210 – 42101I → L.1 Publication
Corresponds to variant rs4667591 [ dbSNP | Ensembl ].
VAR_005424
Natural varianti4272 – 42721M → V in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035996

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2724 – 27241D → G in AAB02882. 1 Publication
Sequence conflicti2773 – 27731A → T in AAB02882. 1 Publication
Sequence conflicti2827 – 28271T → P in AAB02882. 1 Publication
Sequence conflicti2880 – 28823HWY → TFGI in AAB02882. 1 Publication
Sequence conflicti2897 – 28971A → S in AAB02882. 1 Publication
Sequence conflicti2908 – 29081A → S in AAB02882. 1 Publication
Sequence conflicti2921 – 29211S → N in AAB02882. 1 Publication
Sequence conflicti2954 – 29541L → P in AAB02882. 1 Publication
Sequence conflicti2971 – 29722VC → PP in AAB02882. 1 Publication
Sequence conflicti2982 – 29821Y → H in AAB02882. 1 Publication
Sequence conflicti2985 – 29851N → I in AAB02882. 1 Publication
Sequence conflicti3615 – 36151T → S in AAB02882. 1 Publication
Sequence conflicti3738 – 37381Q → K in AAB02882. 1 Publication
Sequence conflicti3784 – 37841C → LW in AAB02882. 1 Publication
Sequence conflicti3810 – 38101C → R in AAB02882. 1 Publication
Sequence conflicti4220 – 42201R → P in AAB02882. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33837 mRNA. Translation: AAB41649.1.
AC007556 Genomic DNA. No translation available.
AC008178 Genomic DNA. No translation available.
U04441 mRNA. Translation: AAB02882.1.
S73145 mRNA. Translation: AAB30825.1.
CCDSiCCDS2232.1.
PIRiI38467.
I53413.
RefSeqiNP_004516.2. NM_004525.2.
UniGeneiHs.657729.

Genome annotation databases

EnsembliENST00000263816; ENSP00000263816; ENSG00000081479.
GeneIDi4036.
KEGGihsa:4036.
UCSCiuc002ues.3. human.

Polymorphism databases

DMDMi160332309.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U33837 mRNA. Translation: AAB41649.1 .
AC007556 Genomic DNA. No translation available.
AC008178 Genomic DNA. No translation available.
U04441 mRNA. Translation: AAB02882.1 .
S73145 mRNA. Translation: AAB30825.1 .
CCDSi CCDS2232.1.
PIRi I38467.
I53413.
RefSeqi NP_004516.2. NM_004525.2.
UniGenei Hs.657729.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2M0P NMR - A 1103-1148 [» ]
ProteinModelPortali P98164.
SMRi P98164. Positions 26-1346, 1351-4373.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110216. 34 interactions.
IntActi P98164. 9 interactions.
MINTi MINT-2860496.
STRINGi 9606.ENSP00000263816.

Chemistry

DrugBanki DB00798. Gentamicin.
DB00047. Insulin Glargine recombinant.
DB00046. Insulin Lyspro recombinant.
DB00030. Insulin recombinant.
DB00071. Insulin, porcine.
DB00013. Urokinase.

PTM databases

PhosphoSitei P98164.

Polymorphism databases

DMDMi 160332309.

Proteomic databases

MaxQBi P98164.
PaxDbi P98164.
PRIDEi P98164.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263816 ; ENSP00000263816 ; ENSG00000081479 .
GeneIDi 4036.
KEGGi hsa:4036.
UCSCi uc002ues.3. human.

Organism-specific databases

CTDi 4036.
GeneCardsi GC02M169947.
GeneReviewsi LRP2.
H-InvDB HIX0029894.
HGNCi HGNC:6694. LRP2.
HPAi HPA005980.
MIMi 222448. phenotype.
600073. gene.
neXtProti NX_P98164.
Orphaneti 2143. Donnai-Barrow syndrome.
PharmGKBi PA30452.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG235850.
HOGENOMi HOG000230574.
HOVERGENi HBG097941.
InParanoidi P98164.
KOi K06233.
OMAi FWADYGQ.
OrthoDBi EOG790FZT.
PhylomeDBi P98164.
TreeFami TF315253.

Enzyme and pathway databases

Reactomei REACT_13523. Vitamin D (calciferol) metabolism.
REACT_24968. Retinoid metabolism and transport.
SignaLinki P98164.

Miscellaneous databases

ChiTaRSi LRP2. human.
GeneWikii LRP2.
GenomeRNAii 4036.
NextBioi 15810.
PROi P98164.
SOURCEi Search...

Gene expression databases

ArrayExpressi P98164.
Bgeei P98164.
CleanExi HS_LRP2.
Genevestigatori P98164.

Family and domain databases

Gene3Di 2.120.10.30. 8 hits.
4.10.400.10. 35 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.
IPR019825. Lectin_legB_Mn/Ca_BS.
[Graphical view ]
Pfami PF12662. cEGF. 1 hit.
PF07645. EGF_CA. 2 hits.
PF00057. Ldl_recept_a. 34 hits.
PF00058. Ldl_recept_b. 14 hits.
[Graphical view ]
PRINTSi PR00261. LDLRECEPTOR.
SMARTi SM00181. EGF. 15 hits.
SM00179. EGF_CA. 3 hits.
SM00192. LDLa. 36 hits.
SM00135. LY. 38 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 5 hits.
SSF57424. SSF57424. 36 hits.
PROSITEi PS00010. ASX_HYDROXYL. 4 hits.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. 9 hits.
PS50026. EGF_3. 6 hits.
PS01187. EGF_CA. 3 hits.
PS01209. LDLRA_1. 31 hits.
PS50068. LDLRA_2. 36 hits.
PS51120. LDLRB. 35 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of human gp330, a Ca(2+)-binding receptor with potential intracellular signaling properties."
    Hjaelm G., Murray E., Crumley G., Harazim W., Lundgren S., Onyango I., Ek B., Larsson M., Juhlin C., Hellman P., Davis H., Aekerstroem G., Rask L., Morse B.
    Eur. J. Biochem. 239:132-137(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-83.
    Tissue: Kidney.
  2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Chromosomal localization of human genes for the LDL receptor family member glycoprotein 330 (LRP2) and its associated protein RAP (LRPAP1)."
    Korenberg J.R., Argraves K.M., Chen X.N., Tran H., Strickland D.K., Argraves W.S.
    Genomics 22:88-93(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2705-4453, VARIANTS GLU-4094 AND LEU-4210.
    Tissue: Kidney.
  4. "A protein involved in calcium sensing of the human parathyroid and placental cytotrophoblast cells belongs to the LDL-receptor protein superfamily."
    Lundgren S., Hjaelm G., Hellman P., Ek B., Juhlin C., Rastad J., Klareskog L., Aakerstroem G., Rask L.
    Exp. Cell Res. 212:344-350(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4139-4406.
  5. "Identification of glycoprotein 330 as an endocytic receptor for apolipoprotein J/clusterin."
    Kounnas M.Z., Loukinova E.B., Stefansson S., Harmony J.A.K., Brewer B.H., Strickland D.K., Argraves W.S.
    J. Biol. Chem. 270:13070-13075(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLU.
  6. "Cytosolic adaptor protein Dab2 is an intracellular ligand of endocytic receptor gp600/megalin."
    Oleinikov A.V., Zhao J., Makker S.P.
    Biochem. J. 347:613-621(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2.
  7. "Functional interaction of megalin with the megalin-binding protein (MegBP), a novel tetratrico peptide repeat-containing adaptor molecule."
    Petersen H.H., Hilpert J., Militz D., Zandler V., Jacobsen C., Roebroek A.J.M., Willnow T.E.
    J. Cell Sci. 116:453-461(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRP2BP.
  8. "The adaptor disabled-2 binds to the third psi xNPxY sequence on the cytoplasmic tail of megalin."
    Gallagher H., Oleinikov A.V., Fenske C., Newman D.J.
    Biochimie 86:179-182(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2.
  9. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-4272.
  10. "Mutations in LRP2, which encodes the multiligand receptor megalin, cause Donnai-Barrow and facio-oculo-acoustico-renal syndromes."
    Kantarci S., Al-Gazali L., Hill R.S., Donnai D., Black G.C.M., Bieth E., Chassaing N., Lacombe D., Devriendt K., Teebi A., Loscertales M., Robson C., Liu T., MacLaughlin D.T., Noonan K.M., Russell M.K., Walsh C.A., Donahoe P.K., Pober B.R.
    Nat. Genet. 39:957-959(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DBS HIS-2522.
  11. Cited for: VARIANT ARG-103.

Entry informationi

Entry nameiLRP2_HUMAN
AccessioniPrimary (citable) accession number: P98164
Secondary accession number(s): O00711, Q16215
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 13, 2007
Last modified: September 3, 2014
This is version 150 of the entry and version 3 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, Reference proteome

Documents

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

External Data

Dasty 3

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