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UniProtKB - Q9NZR2 (LRP1B_HUMAN)
Protein
Low-density lipoprotein receptor-related protein 1B
Gene
LRP1B
Organism
Homo sapiens (Human)
Status
Functioni
Potential cell surface proteins that bind and internalize ligands in the process of receptor-mediated endocytosis.
Miscellaneous
The gene is preferentially inactivated in one histological type of lung cancer (non-small cell lung cancer (NSCLC)). May thus play an important role in tumorigenesis of NSCLCs.
GO - Molecular functioni
- calcium ion binding Source: InterPro
- low-density lipoprotein particle receptor activity Source: GO_Central
GO - Biological processi
- protein transport Source: ProtInc
- receptor-mediated endocytosis Source: ProtInc
Keywordsi
Molecular function | Receptor |
Biological process | Endocytosis |
Ligand | Calcium |
Enzyme and pathway databases
PathwayCommonsi | Q9NZR2 |
SignaLinki | Q9NZR2 |
SIGNORi | Q9NZR2 |
Names & Taxonomyi
Protein namesi | Recommended name: Low-density lipoprotein receptor-related protein 1BShort name: LRP-1B Alternative name(s): Low-density lipoprotein receptor-related protein-deleted in tumor Short name: LRP-DIT |
Gene namesi | Name:LRP1B Synonyms:LRPDIT |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:6693, LRP1B |
MIMi | 608766, gene |
neXtProti | NX_Q9NZR2 |
VEuPathDBi | HostDB:ENSG00000168702 |
Subcellular locationi
Other locations
- Membrane Curated; Single-pass type I membrane protein Curated
Plasma Membrane
- plasma membrane Source: GO_Central
Other locations
- integral component of membrane Source: UniProtKB-KW
- receptor complex Source: MGI
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Topological domaini | 25 – 4444 | ExtracellularSequence analysisAdd BLAST | 4420 | |
Transmembranei | 4445 – 4467 | HelicalSequence analysisAdd BLAST | 23 | |
Topological domaini | 4468 – 4599 | CytoplasmicSequence analysisAdd BLAST | 132 |
Keywords - Cellular componenti
MembranePathology & Biotechi
Organism-specific databases
DisGeNETi | 53353 |
OpenTargetsi | ENSG00000168702 |
PharmGKBi | PA30451 |
Miscellaneous databases
Pharosi | Q9NZR2, Tbio |
Genetic variation databases
BioMutai | LRP1B |
DMDMi | 57015418 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 20 | Sequence analysisAdd BLAST | 20 | |
ChainiPRO_0000017319 | 21 – 4599 | Low-density lipoprotein receptor-related protein 1BAdd BLAST | 4579 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 32 ↔ 45 | By similarity | ||
Disulfide bondi | 39 ↔ 58 | By similarity | ||
Disulfide bondi | 52 ↔ 69 | By similarity | ||
Disulfide bondi | 77 ↔ 90 | By similarity | ||
Disulfide bondi | 84 ↔ 103 | By similarity | ||
Disulfide bondi | 97 ↔ 113 | By similarity | ||
Disulfide bondi | 120 ↔ 129 | By similarity | ||
Disulfide bondi | 125 ↔ 138 | By similarity | ||
Glycosylationi | 134 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 140 ↔ 153 | By similarity | ||
Disulfide bondi | 159 ↔ 169 | By similarity | ||
Disulfide bondi | 165 ↔ 178 | By similarity | ||
Disulfide bondi | 180 ↔ 193 | By similarity | ||
Glycosylationi | 190 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 220 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 313 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 360 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 443 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 725 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 758 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 798 ↔ 809 | By similarity | ||
Disulfide bondi | 805 ↔ 818 | By similarity | ||
Disulfide bondi | 820 ↔ 833 | By similarity | ||
Glycosylationi | 829 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 845 ↔ 857 | By similarity | ||
Disulfide bondi | 852 ↔ 870 | By similarity | ||
Disulfide bondi | 864 ↔ 881 | By similarity | ||
Glycosylationi | 883 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 886 ↔ 898 | By similarity | ||
Disulfide bondi | 893 ↔ 911 | By similarity | ||
Disulfide bondi | 905 ↔ 922 | By similarity | ||
Glycosylationi | 919 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 927 ↔ 939 | By similarity | ||
Disulfide bondi | 934 ↔ 952 | By similarity | ||
Disulfide bondi | 946 ↔ 962 | By similarity | ||
Disulfide bondi | 967 ↔ 980 | By similarity | ||
Disulfide bondi | 975 ↔ 993 | By similarity | ||
Disulfide bondi | 987 ↔ 1002 | By similarity | ||
Disulfide bondi | 1006 ↔ 1018 | By similarity | ||
Disulfide bondi | 1013 ↔ 1031 | By similarity | ||
Disulfide bondi | 1025 ↔ 1042 | By similarity | ||
Glycosylationi | 1041 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1053 ↔ 1066 | By similarity | ||
Disulfide bondi | 1060 ↔ 1079 | By similarity | ||
Disulfide bondi | 1073 ↔ 1088 | By similarity | ||
Glycosylationi | 1089 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1095 ↔ 1109 | By similarity | ||
Disulfide bondi | 1103 ↔ 1122 | By similarity | ||
Disulfide bondi | 1116 ↔ 1131 | By similarity | ||
Disulfide bondi | 1136 ↔ 1150 | By similarity | ||
Disulfide bondi | 1143 ↔ 1163 | By similarity | ||
Glycosylationi | 1145 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1157 ↔ 1173 | By similarity | ||
Glycosylationi | 1209 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1298 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1502 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1549 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1636 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1754 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1816 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1838 ↔ 1849 | By similarity | ||
Disulfide bondi | 1845 ↔ 1859 | By similarity | ||
Disulfide bondi | 1861 ↔ 1874 | By similarity | ||
Glycosylationi | 1921 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1983 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2105 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2147 ↔ 2158 | By similarity | ||
Disulfide bondi | 2154 ↔ 2168 | By similarity | ||
Disulfide bondi | 2170 ↔ 2182 | By similarity | ||
Glycosylationi | 2458 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2488 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 2507 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2510 ↔ 2523 | By similarity | ||
Disulfide bondi | 2518 ↔ 2536 | By similarity | ||
Disulfide bondi | 2530 ↔ 2547 | By similarity | ||
Glycosylationi | 2549 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2552 ↔ 2564 | By similarity | ||
Disulfide bondi | 2559 ↔ 2577 | By similarity | ||
Disulfide bondi | 2571 ↔ 2586 | By similarity | ||
Disulfide bondi | 2591 ↔ 2603 | By similarity | ||
Disulfide bondi | 2598 ↔ 2616 | By similarity | ||
Disulfide bondi | 2610 ↔ 2625 | By similarity | ||
Glycosylationi | 2626 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2630 ↔ 2652 | By similarity | ||
Disulfide bondi | 2646 ↔ 2665 | By similarity | ||
Glycosylationi | 2647 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2659 ↔ 2674 | By similarity | ||
Disulfide bondi | 2682 ↔ 2694 | By similarity | ||
Disulfide bondi | 2689 ↔ 2707 | By similarity | ||
Disulfide bondi | 2701 ↔ 2716 | By similarity | ||
Disulfide bondi | 2720 ↔ 2732 | By similarity | ||
Disulfide bondi | 2727 ↔ 2745 | By similarity | ||
Disulfide bondi | 2739 ↔ 2756 | By similarity | ||
Disulfide bondi | 2761 ↔ 2774 | By similarity | ||
Disulfide bondi | 2768 ↔ 2787 | By similarity | ||
Disulfide bondi | 2781 ↔ 2799 | By similarity | ||
Glycosylationi | 2802 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2805 ↔ 2817 | By similarity | ||
Disulfide bondi | 2812 ↔ 2830 | By similarity | ||
Disulfide bondi | 2824 ↔ 2840 | By similarity | ||
Disulfide bondi | 2845 ↔ 2857 | By similarity | ||
Disulfide bondi | 2852 ↔ 2871 | By similarity | ||
Disulfide bondi | 2865 ↔ 2884 | By similarity | ||
Disulfide bondi | 2891 ↔ 2903 | By similarity | ||
Glycosylationi | 2892 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 2898 ↔ 2916 | By similarity | ||
Disulfide bondi | 2910 ↔ 2925 | By similarity | ||
Disulfide bondi | 2930 ↔ 2942 | By similarity | ||
Disulfide bondi | 2938 ↔ 2951 | By similarity | ||
Disulfide bondi | 2953 ↔ 2966 | By similarity | ||
Disulfide bondi | 2972 ↔ 2982 | By similarity | ||
Disulfide bondi | 2978 ↔ 2991 | By similarity | ||
Disulfide bondi | 2993 ↔ 3007 | By similarity | ||
Glycosylationi | 3034 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3066 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3076 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3164 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3310 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3316 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3317 ↔ 3329 | By similarity | ||
Disulfide bondi | 3324 ↔ 3342 | By similarity | ||
Disulfide bondi | 3336 ↔ 3352 | By similarity | ||
Disulfide bondi | 3357 ↔ 3369 | By similarity | ||
Disulfide bondi | 3364 ↔ 3382 | By similarity | ||
Disulfide bondi | 3376 ↔ 3391 | By similarity | ||
Disulfide bondi | 3396 ↔ 3409 | By similarity | ||
Disulfide bondi | 3403 ↔ 3422 | By similarity | ||
Disulfide bondi | 3416 ↔ 3431 | By similarity | ||
Disulfide bondi | 3436 ↔ 3449 | By similarity | ||
Disulfide bondi | 3443 ↔ 3462 | By similarity | ||
Disulfide bondi | 3456 ↔ 3471 | By similarity | ||
Disulfide bondi | 3476 ↔ 3488 | By similarity | ||
Disulfide bondi | 3483 ↔ 3501 | By similarity | ||
Disulfide bondi | 3495 ↔ 3510 | By similarity | ||
Disulfide bondi | 3515 ↔ 3527 | By similarity | ||
Disulfide bondi | 3522 ↔ 3540 | By similarity | ||
Disulfide bondi | 3534 ↔ 3549 | By similarity | ||
Disulfide bondi | 3553 ↔ 3565 | By similarity | ||
Disulfide bondi | 3560 ↔ 3578 | By similarity | ||
Disulfide bondi | 3572 ↔ 3587 | By similarity | ||
Disulfide bondi | 3594 ↔ 3606 | By similarity | ||
Disulfide bondi | 3601 ↔ 3619 | By similarity | ||
Disulfide bondi | 3613 ↔ 3628 | By similarity | ||
Disulfide bondi | 3632 ↔ 3645 | By similarity | ||
Disulfide bondi | 3639 ↔ 3658 | By similarity | ||
Disulfide bondi | 3652 ↔ 3667 | By similarity | ||
Disulfide bondi | 3674 ↔ 3686 | By similarity | ||
Disulfide bondi | 3681 ↔ 3699 | By similarity | ||
Glycosylationi | 3682 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 3693 ↔ 3710 | By similarity | ||
Disulfide bondi | 3715 ↔ 3729 | By similarity | ||
Disulfide bondi | 3723 ↔ 3742 | By similarity | ||
Disulfide bondi | 3736 ↔ 3751 | By similarity | ||
Disulfide bondi | 3762 ↔ 3774 | By similarity | ||
Disulfide bondi | 3769 ↔ 3787 | By similarity | ||
Disulfide bondi | 3781 ↔ 3796 | By similarity | ||
Disulfide bondi | 3805 ↔ 3818 | By similarity | ||
Disulfide bondi | 3812 ↔ 3827 | By similarity | ||
Disulfide bondi | 3829 ↔ 3842 | By similarity | ||
Disulfide bondi | 3848 ↔ 3858 | By similarity | ||
Disulfide bondi | 3854 ↔ 3867 | By similarity | ||
Disulfide bondi | 3869 ↔ 3880 | By similarity | ||
Glycosylationi | 3877 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3894 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 3906 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 4017 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 4204 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 4217 ↔ 4227 | By similarity | ||
Disulfide bondi | 4221 ↔ 4237 | By similarity | ||
Disulfide bondi | 4253 ↔ 4263 | By similarity | ||
Disulfide bondi | 4257 ↔ 4273 | By similarity | ||
Disulfide bondi | 4275 ↔ 4284 | By similarity | ||
Disulfide bondi | 4289 ↔ 4299 | By similarity | ||
Disulfide bondi | 4293 ↔ 4309 | By similarity | ||
Disulfide bondi | 4311 ↔ 4320 | By similarity | ||
Disulfide bondi | 4325 ↔ 4335 | By similarity | ||
Disulfide bondi | 4329 ↔ 4345 | By similarity | ||
Disulfide bondi | 4347 ↔ 4356 | By similarity | ||
Glycosylationi | 4381 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 4394 ↔ 4404 | By similarity | ||
Disulfide bondi | 4398 ↔ 4415 | By similarity | ||
Disulfide bondi | 4417 ↔ 4426 | By similarity | ||
Glycosylationi | 4420 | N-linked (GlcNAc...) asparagineSequence analysis | 1 |
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
EPDi | Q9NZR2 |
jPOSTi | Q9NZR2 |
MassIVEi | Q9NZR2 |
MaxQBi | Q9NZR2 |
PaxDbi | Q9NZR2 |
PeptideAtlasi | Q9NZR2 |
PRIDEi | Q9NZR2 |
ProteomicsDBi | 83492 |
PTM databases
GlyConnecti | 1466, 4 N-Linked glycans (1 site) |
GlyGeni | Q9NZR2, 46 sites, 4 N-linked glycans (1 site) |
iPTMneti | Q9NZR2 |
PhosphoSitePlusi | Q9NZR2 |
Expressioni
Tissue specificityi
Expressed in thyroid gland and in salivary gland, as well as in adult and fetal brain.1 Publication
Gene expression databases
Bgeei | ENSG00000168702, Expressed in corpus callosum and 150 other tissues |
ExpressionAtlasi | Q9NZR2, baseline and differential |
Genevisiblei | Q9NZR2, HS |
Organism-specific databases
HPAi | ENSG00000168702, Tissue enriched (brain) |
Interactioni
Subunit structurei
Binds LRPAP1, PLAU, PLAT and SERPINE1; binding is followed by internalization and degradation of the ligands.
Binary interactionsi
Q9NZR2
With | #Exp. | IntAct |
---|---|---|
APP [P05067] | 3 | EBI-1642131,EBI-77613 |
CHRNA4 [P43681] | 3 | EBI-1642131,EBI-7132379 |
PPP2R2A [P63151] | 3 | EBI-1642131,EBI-1048931 |
Protein-protein interaction databases
BioGRIDi | 119750, 64 interactors |
IntActi | Q9NZR2, 28 interactors |
STRINGi | 9606.ENSP00000374135 |
Miscellaneous databases
RNActi | Q9NZR2, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 31 – 70 | LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 76 – 114 | LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 116 – 154 | EGF-like 1PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 155 – 194 | EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 40 | |
Repeati | 295 – 337 | LDL-receptor class B 1Add BLAST | 43 | |
Repeati | 338 – 381 | LDL-receptor class B 2Add BLAST | 44 | |
Repeati | 382 – 425 | LDL-receptor class B 3Add BLAST | 44 | |
Domaini | 471 – 517 | EGF-like 3PROSITE-ProRule annotationAdd BLAST | 47 | |
Repeati | 568 – 610 | LDL-receptor class B 4Add BLAST | 43 | |
Repeati | 611 – 656 | LDL-receptor class B 5Add BLAST | 46 | |
Repeati | 657 – 706 | LDL-receptor class B 6Add BLAST | 50 | |
Repeati | 707 – 750 | LDL-receptor class B 7Add BLAST | 44 | |
Domaini | 794 – 834 | EGF-like 4PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 844 – 882 | LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 885 – 923 | LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 926 – 963 | LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 966 – 1003 | LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 1005 – 1043 | LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 1052 – 1089 | LDL-receptor class A 8PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 1094 – 1132 | LDL-receptor class A 9PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 1135 – 1174 | LDL-receptor class A 10PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 1174 – 1213 | EGF-like 5PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 1214 – 1253 | EGF-like 6PROSITE-ProRule annotationAdd BLAST | 40 | |
Repeati | 1300 – 1346 | LDL-receptor class B 8Add BLAST | 47 | |
Repeati | 1347 – 1389 | LDL-receptor class B 9Add BLAST | 43 | |
Repeati | 1390 – 1436 | LDL-receptor class B 10Add BLAST | 47 | |
Repeati | 1437 – 1480 | LDL-receptor class B 11Add BLAST | 44 | |
Repeati | 1481 – 1522 | LDL-receptor class B 12Add BLAST | 42 | |
Domaini | 1527 – 1570 | EGF-like 7PROSITE-ProRule annotationAdd BLAST | 44 | |
Repeati | 1618 – 1660 | LDL-receptor class B 13Add BLAST | 43 | |
Repeati | 1661 – 1704 | LDL-receptor class B 14Add BLAST | 44 | |
Repeati | 1705 – 1744 | LDL-receptor class B 15Add BLAST | 40 | |
Repeati | 1745 – 1787 | LDL-receptor class B 16Add BLAST | 43 | |
Domaini | 1834 – 1875 | EGF-like 8PROSITE-ProRule annotationAdd BLAST | 42 | |
Repeati | 1922 – 1964 | LDL-receptor class B 17Add BLAST | 43 | |
Repeati | 1965 – 2007 | LDL-receptor class B 28Add BLAST | 43 | |
Repeati | 2008 – 2051 | LDL-receptor class B 19Add BLAST | 44 | |
Repeati | 2052 – 2095 | LDL-receptor class B 20Add BLAST | 44 | |
Domaini | 2143 – 2183 | EGF-like 9PROSITE-ProRule annotationAdd BLAST | 41 | |
Repeati | 2239 – 2280 | LDL-receptor class B 21Add BLAST | 42 | |
Repeati | 2281 – 2329 | LDL-receptor class B 22Add BLAST | 49 | |
Repeati | 2330 – 2374 | LDL-receptor class B 23Add BLAST | 45 | |
Repeati | 2375 – 2416 | LDL-receptor class B 24Add BLAST | 42 | |
Repeati | 2417 – 2459 | LDL-receptor class B 25Add BLAST | 43 | |
Domaini | 2464 – 2504 | EGF-like 10PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 2509 – 2548 | LDL-receptor class A 11PROSITE-ProRule annotationAdd BLAST | 40 | |
Domaini | 2551 – 2587 | LDL-receptor class A 12PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 2590 – 2626 | LDL-receptor class A 13PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 2629 – 2675 | LDL-receptor class A 14PROSITE-ProRule annotationAdd BLAST | 47 | |
Domaini | 2681 – 2717 | LDL-receptor class A 15PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 2719 – 2757 | LDL-receptor class A 16PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 2760 – 2800 | LDL-receptor class A 17PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 2804 – 2841 | LDL-receptor class A 18PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 2844 – 2885 | LDL-receptor class A 19PROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 2890 – 2926 | LDL-receptor class A 20PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 2927 – 2967 | EGF-like 11PROSITE-ProRule annotationAdd BLAST | 41 | |
Domaini | 2968 – 3008 | EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST | 41 | |
Repeati | 3055 – 3098 | LDL-receptor class B 26Add BLAST | 44 | |
Repeati | 3099 – 3141 | LDL-receptor class B 27Add BLAST | 43 | |
Repeati | 3142 – 3185 | LDL-receptor class B 28Add BLAST | 44 | |
Repeati | 3186 – 3224 | LDL-receptor class B 29Add BLAST | 39 | |
Repeati | 3225 – 3268 | LDL-receptor class B 30Add BLAST | 44 | |
Domaini | 3273 – 3314 | EGF-like 13PROSITE-ProRule annotationAdd BLAST | 42 | |
Domaini | 3316 – 3353 | LDL-receptor class A 21PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 3356 – 3392 | LDL-receptor class A 22PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 3395 – 3432 | LDL-receptor class A 23PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 3435 – 3472 | LDL-receptor class A 24PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 3475 – 3511 | LDL-receptor class A 25PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 3514 – 3550 | LDL-receptor class A 26PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 3552 – 3588 | LDL-receptor class A 27PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 3593 – 3629 | LDL-receptor class A 28PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 3631 – 3668 | LDL-receptor class A 29PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 3673 – 3711 | LDL-receptor class A 30PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 3714 – 3752 | LDL-receptor class A 31PROSITE-ProRule annotationAdd BLAST | 39 | |
Domaini | 3761 – 3797 | LDL-receptor class A 32PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 3801 – 3843 | EGF-like 14PROSITE-ProRule annotationAdd BLAST | 43 | |
Domaini | 3844 – 3881 | EGF-like 15PROSITE-ProRule annotationAdd BLAST | 38 | |
Repeati | 3933 – 3980 | LDL-receptor class B 31Add BLAST | 48 | |
Repeati | 3981 – 4038 | LDL-receptor class B 32Add BLAST | 58 | |
Repeati | 4039 – 4082 | LDL-receptor class B 33Add BLAST | 44 | |
Repeati | 4083 – 4127 | LDL-receptor class B 34Add BLAST | 45 | |
Domaini | 4171 – 4208 | EGF-like 16PROSITE-ProRule annotationAdd BLAST | 38 | |
Domaini | 4213 – 4249 | EGF-like 17PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 4249 – 4285 | EGF-like 18PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 4285 – 4321 | EGF-like 19PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 4321 – 4357 | EGF-like 20PROSITE-ProRule annotationAdd BLAST | 37 | |
Domaini | 4357 – 4392 | EGF-like 21PROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 4390 – 4427 | EGF-like 22PROSITE-ProRule annotationAdd BLAST | 38 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 4492 – 4495 | Endocytosis signalSequence analysis | 4 | |
Motifi | 4559 – 4562 | Endocytosis signalSequence analysis | 4 |
Sequence similaritiesi
Belongs to the LDLR family.Curated
Keywords - Domaini
EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helixPhylogenomic databases
eggNOGi | KOG1215, Eukaryota |
GeneTreei | ENSGT00940000157521 |
HOGENOMi | CLU_000085_2_1_1 |
InParanoidi | Q9NZR2 |
OMAi | QCIPAKW |
OrthoDBi | 1606at2759 |
PhylomeDBi | Q9NZR2 |
TreeFami | TF315253 |
Family and domain databases
CDDi | cd00112, LDLa, 28 hits |
Gene3Di | 2.120.10.30, 8 hits 4.10.400.10, 32 hits |
InterProi | View protein in InterPro IPR011042, 6-blade_b-propeller_TolB-like IPR026823, cEGF IPR032485, DUF5050 IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR000152, EGF-type_Asp/Asn_hydroxyl_site IPR018097, EGF_Ca-bd_CS IPR009030, Growth_fac_rcpt_cys_sf IPR036055, LDL_receptor-like_sf IPR023415, LDLR_class-A_CS IPR000033, LDLR_classB_rpt IPR002172, LDrepeatLR_classA_rpt |
Pfami | View protein in Pfam PF12662, cEGF, 1 hit PF16472, DUF5050, 1 hit PF00008, EGF, 1 hit PF07645, EGF_CA, 2 hits PF00057, Ldl_recept_a, 30 hits PF00058, Ldl_recept_b, 11 hits |
PRINTSi | PR00261, LDLRECEPTOR |
SMARTi | View protein in SMART SM00181, EGF, 25 hits SM00179, EGF_CA, 6 hits SM00192, LDLa, 32 hits SM00135, LY, 37 hits |
SUPFAMi | SSF57184, SSF57184, 3 hits SSF57424, SSF57424, 32 hits |
PROSITEi | View protein in PROSITE PS00010, ASX_HYDROXYL, 4 hits PS00022, EGF_1, 5 hits PS01186, EGF_2, 9 hits PS50026, EGF_3, 9 hits PS01187, EGF_CA, 3 hits PS01209, LDLRA_1, 27 hits PS50068, LDLRA_2, 32 hits PS51120, LDLRB, 37 hits |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 3 potential isoforms that are computationally mapped.Show allAlign All
Q9NZR2-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSEFLLALLT LSGLLPIARV LTVGADRDQQ LCDPGEFLCH DHVTCVSQSW
60 70 80 90 100
LCDGDPDCPD DSDESLDTCP EEVEIKCPLN HIACLGTNKC VHLSQLCNGV
110 120 130 140 150
LDCPDGYDEG VHCQELLSNC QQLNCQYKCT MVRNSTRCYC EDGFEITEDG
160 170 180 190 200
RSCKDQDECA VYGTCSQTCR NTHGSYTCSC VEGYLMQPDN RSCKAKIEPT
210 220 230 240 250
DRPPILLIAN FETIEVFYLN GSKMATLSSV NGNEIHTLDF IYNEDMICWI
260 270 280 290 300
ESRESSNQLK CIQITKAGGL TDEWTINILQ SFHNVQQMAI DWLTRNLYFV
310 320 330 340 350
DHVGDRIFVC NSNGSVCVTL IDLELHNPKA IAVDPIAGKL FFTDYGNVAK
360 370 380 390 400
VERCDMDGMN RTRIIDSKTE QPAALALDLV NKLVYWVDLY LDYVGVVDYQ
410 420 430 440 450
GKNRHTVIQG RQVRHLYGIT VFEDYLYATN SDNYNIVRIN RFNGTDIHSL
460 470 480 490 500
IKIENAWGIR IYQKRTQPTV RSHACEVDPY GMPGGCSHIC LLSSSYKTRT
510 520 530 540 550
CRCRTGFNLG SDGRSCKRPK NELFLFYGKG RPGIVRGMDL NTKIADEYMI
560 570 580 590 600
PIENLVNPRA LDFHAETNYI YFADTTSFLI GRQKIDGTER ETILKDDLDN
610 620 630 640 650
VEGIAVDWIG NNLYWTNDGH RKTINVARLE KASQSRKTLL EGEMSHPRGI
660 670 680 690 700
VVDPVNGWMY WTDWEEDEID DSVGRIEKAW MDGFNRQIFV TSKMLWPNGL
710 720 730 740 750
TLDFHTNTLY WCDAYYDHIE KVFLNGTHRK IVYSGRELNH PFGLSHHGNY
760 770 780 790 800
VFWTDYMNGS IFQLDLITSE VTLLRHERPP LFGLQIYDPR KQQGDNMCRV
810 820 830 840 850
NNGGCSTLCL AIPGGRVCAC ADNQLLDENG TTCTFNPGEA LPHICKAGEF
860 870 880 890 900
RCKNRHCIQA RWKCDGDDDC LDGSDEDSVN CFNHSCPDDQ FKCQNNRCIP
910 920 930 940 950
KRWLCDGAND CGSNEDESNQ TCTARTCQVD QFSCGNGRCI PRAWLCDRED
960 970 980 990 1000
DCGDQTDEMA SCEFPTCEPL TQFVCKSGRC ISSKWHCDSD DDCGDGSDEV
1010 1020 1030 1040 1050
GCVHSCFDNQ FRCSSGRCIP GHWACDGDND CGDFSDEAQI NCTKEEIHSP
1060 1070 1080 1090 1100
AGCNGNEFQC HPDGNCVPDL WRCDGEKDCE DGSDEKGCNG TIRLCDHKTK
1110 1120 1130 1140 1150
FSCWSTGRCI NKAWVCDGDI DCEDQSDEDD CDSFLCGPPK HPCANDTSVC
1160 1170 1180 1190 1200
LQPEKLCNGK KDCPDGSDEG YLCDECSLNN GGCSNHCSVV PGRGIVCSCP
1210 1220 1230 1240 1250
EGLQLNKDNK TCEIVDYCSN HLKCSQVCEQ HKHTVKCSCY EGWKLDVDGE
1260 1270 1280 1290 1300
SCTSVDPFEA FIIFSIRHEI RRIDLHKRDY SLLVPGLRNT IALDFHFNQS
1310 1320 1330 1340 1350
LLYWTDVVED RIYRGKLSES GGVSAIEVVV EHGLATPEGL TVDWIAGNIY
1360 1370 1380 1390 1400
WIDSNLDQIE VAKLDGSLRT TLIAGAMEHP RAIALDPRYG ILFWTDWDAN
1410 1420 1430 1440 1450
FPRIESASMS GAGRKTIYKD MKTGAWPNGL TVDHFEKRIV WTDARSDAIY
1460 1470 1480 1490 1500
SALYDGTNMI EIIRGHEYLS HPFAVSLYGS EVYWTDWRTN TLSKANKWTG
1510 1520 1530 1540 1550
QNVSVIQKTS AQPFDLQIYH PSRQPQAPNP CAANDGKGPC SHMCLINHNR
1560 1570 1580 1590 1600
SAACACPHLM KLSSDKKTCY EMKKFLLYAR RSEIRGVDID NPYFNFITAF
1610 1620 1630 1640 1650
TVPDIDDVTV IDFDASEERL YWTDIKTQTI KRAFINGTGL ETVISRDIQS
1660 1670 1680 1690 1700
IRGLAVDWVS RNLYWISSEF DETQINVARL DGSLKTSIIH GIDKPQCLAA
1710 1720 1730 1740 1750
HPVRGKLYWT DGNTINMANM DGSNSKILFQ NQKEPVGLSI DYVENKLYWI
1760 1770 1780 1790 1800
SSGNGTINRC NLDGGNLEVI ESMKEELTKA TALTIMDKKL WWADQNLAQL
1810 1820 1830 1840 1850
GTCSKRDGRN PTILRNKTSG VVHMKVYDKE AQQGSNSCQL NNGGCSQLCL
1860 1870 1880 1890 1900
PTSETTRTCM CTVGYYLQKN RMSCQGIESF LMYSVHEGIR GIPLEPSDKM
1910 1920 1930 1940 1950
DALMPISGTS FAVGIDFHAE NDTIYWTDMG FNKISRAKRD QTWKEDIITN
1960 1970 1980 1990 2000
GLGRVEGIAV DWIAGNIYWT DHGFNLIEVA RLNGSFRYVI ISQGLDQPRS
2010 2020 2030 2040 2050
IAVHPEKGLL FWTEWGQMPC IGKARLDGSE KVVLVSMGIA WPNGISIDYE
2060 2070 2080 2090 2100
ENKLYWCDAR TDKIERIDLE TGGNREMVLS GSNVDMFSVA VFGAYIYWSD
2110 2120 2130 2140 2150
RAHANGSVRR GHKNDATETI TMRTGLGVNL KEVKIFNRVR EKGTNVCARD
2160 2170 2180 2190 2200
NGGCKQLCLY RGNSRRTCAC AHGYLAEDGV TCLRHEGYLL YSGRTILKSI
2210 2220 2230 2240 2250
HLSDETNLNS PIRPYENPRY FKNVIALAFD YNQRRKGTNR IFYSDAHFGN
2260 2270 2280 2290 2300
IQLIKDNWED RQVIVENVGS VEGLAYHRAW DTLYWTSSTT SSITRHTVDQ
2310 2320 2330 2340 2350
TRPGAFDREA VITMSEDDHP HVLALDECQN LMFWTNWNEQ HPSIMRSTLT
2360 2370 2380 2390 2400
GKNAQVVVST DILTPNGLTI DYRAEKLYFS DGSLGKIERC EYDGSQRHVI
2410 2420 2430 2440 2450
VKSGPGTFLS LAVYDNYIFW SDWGRRAILR SNKYTGGDTK ILRSDIPHQP
2460 2470 2480 2490 2500
MGIIAVANDT NSCELSPCAL LNGGCHDLCL LTPNGRVNCS CRGDRILLED
2510 2520 2530 2540 2550
NRCVTKNSSC NAYSEFECGN GECIDYQLTC DGIPHCKDKS DEKLLYCENR
2560 2570 2580 2590 2600
SCRRGFKPCY NRRCIPHGKL CDGENDCGDN SDELDCKVST CATVEFRCAD
2610 2620 2630 2640 2650
GTCIPRSARC NQNIDCADAS DEKNCNNTDC THFYKLGVKT TGFIRCNSTS
2660 2670 2680 2690 2700
LCVLPTWICD GSNDCGDYSD ELKCPVQNKH KCEENYFSCP SGRCILNTWI
2710 2720 2730 2740 2750
CDGQKDCEDG RDEFHCDSSC SWNQFACSAQ KCISKHWICD GEDDCGDGLD
2760 2770 2780 2790 2800
ESDSICGAIT CAADMFSCQG SRACVPRHWL CDGERDCPDG SDELSTAGCA
2810 2820 2830 2840 2850
PNNTCDENAF MCHNKVCIPK QFVCDHDDDC GDGSDESPQC GYRQCGTEEF
2860 2870 2880 2890 2900
SCADGRCLLN TQWQCDGDFD CPDHSDEAPL NPKCKSAEQS CNSSFFMCKN
2910 2920 2930 2940 2950
GRCIPSGGLC DNKDDCGDGS DERNCHINEC LSKKVSGCSQ DCQDLPVSYK
2960 2970 2980 2990 3000
CKCWPGFQLK DDGKTCVDID ECSSGFPCSQ QCINTYGTYK CLCTDGYEIQ
3010 3020 3030 3040 3050
PDNPNGCKSL SDEEPFLILA DHHEIRKIST DGSNYTLLKQ GLNNVIAIDF
3060 3070 3080 3090 3100
DYREEFIYWI DSSRPNGSRI NRMCLNGSDI KVVHNTAVPN ALAVDWIGKN
3110 3120 3130 3140 3150
LYWSDTEKRI IEVSKLNGLY PTILVSKRLK FPRDLSLDPQ AGYLYWIDCC
3160 3170 3180 3190 3200
EYPHIGRVGM DGTNQSVVIE TKISRPMALT IDYVNRRLYW ADENHIEFSN
3210 3220 3230 3240 3250
MDGSHRHKVP NQDIPGVIAL TLFEDYIYWT DGKTKSLSRA HKTSGADRLS
3260 3270 3280 3290 3300
LIYSWHAITD IQVYHSYRQP DVSKHLCMIN NGGCSHLCLL APGKTHTCAC
3310 3320 3330 3340 3350
PTNFYLAADN RTCLSNCTAS QFRCKTDKCI PFWWKCDTVD DCGDGSDEPD
3360 3370 3380 3390 3400
DCPEFRCQPG RFQCGTGLCA LPAFICDGEN DCGDNSDELN CDTHVCLSGQ
3410 3420 3430 3440 3450
FKCTKNQKCI PVNLRCNGQD DCGDEEDERD CPENSCSPDY FQCKTTKHCI
3460 3470 3480 3490 3500
SKLWVCDEDP DCADASDEAN CDKKTCGPHE FQCKNNNCIP DHWRCDSQND
3510 3520 3530 3540 3550
CSDNSDEENC KPQTCTLKDF LCANGDCVSS RFWCDGDFDC ADGSDERNCE
3560 3570 3580 3590 3600
TSCSKDQFRC SNGQCIPAKW KCDGHEDCKY GEDEKSCEPA SPTCSSREYI
3610 3620 3630 3640 3650
CASDGCISAS LKCNGEYDCA DGSDEMDCVT ECKEDQFRCK NKAHCIPIRW
3660 3670 3680 3690 3700
LCDGIHDCVD GSDEENCERG GNICRADEFL CNNSLCKLHF WVCDGEDDCG
3710 3720 3730 3740 3750
DNSDEAPDMC VKFLCPSTRP HRCRNNRICL QSEQMCNGID ECGDNSDEDH
3760 3770 3780 3790 3800
CGGKLTYKAR PCKKDEFACS NKKCIPMDLQ CDRLDDCGDG SDEQGCRIAP
3810 3820 3830 3840 3850
TEYTCEDNVN PCGDDAYCNQ IKTSVFCRCK PGFQRNMKNR QCEDLNECLV
3860 3870 3880 3890 3900
FGTCSHQCIN VEGSYKCVCD QNFQERNNTC IAEGSEDQVL YIANDTDILG
3910 3920 3930 3940 3950
FIYPFNYSGD HQQISHIEHN SRITGMDVYY QRDMIIWSTQ FNPGGIFYKR
3960 3970 3980 3990 4000
IHGREKRQAN SGLICPEFKR PRDIAVDWVA GNIYWTDHSR MHWFSYYTTH
4010 4020 4030 4040 4050
WTSLRYSINV GQLNGPNCTR LLTNMAGEPY AIAVNPKRGM MYWTVVGDHS
4060 4070 4080 4090 4100
HIEEAAMDGT LRRILVQKNL QRPTGLAVDY FSERIYWADF ELSIIGSVLY
4110 4120 4130 4140 4150
DGSNSVVSVS SKQGLLHPHR IDIFEDYIYG AGPKNGVFRV QKFGHGSVEY
4160 4170 4180 4190 4200
LALNIDKTKG VLISHRYKQL DLPNPCLDLA CEFLCLLNPS GATCVCPEGK
4210 4220 4230 4240 4250
YLINGTCNDD SLLDDSCKLT CENGGRCILN EKGDLRCHCW PSYSGERCEV
4260 4270 4280 4290 4300
NHCSNYCQNG GTCVPSVLGR PTCSCALGFT GPNCGKTVCE DFCQNGGTCI
4310 4320 4330 4340 4350
VTAGNQPYCH CQPEYTGDRC QYYVCHHYCV NSESCTIGDD GSVECVCPTR
4360 4370 4380 4390 4400
YEGPKCEVDK CVRCHGGHCI INKDSEDIFC NCTNGKIASS CQLCDGYCYN
4410 4420 4430 4440 4450
GGTCQLDPET NVPVCLCSTN WSGTQCERPA PKSSKSDHIS TRSIAIIVPL
4460 4470 4480 4490 4500
VLLVTLITTL VIGLVLCKRK RRTKTIRRQP IINGGINVEI GNPSYNMYEV
4510 4520 4530 4540 4550
DHDHNDGGLL DPGFMIDPTK ARYIGGGPSA FKLPHTAPPI YLNSDLKGPL
4560 4570 4580 4590
TAGPTNYSNP VYAKLYMDGQ NCRNSLGSVD ERKELLPKKI EIGIRETVA
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketH0Y7T7 | H0Y7T7_HUMAN | Low-density lipoprotein receptor-re... | LRP1B | 798 | Annotation score: | ||
E7ERG8 | E7ERG8_HUMAN | Low-density lipoprotein receptor-re... | LRP1B | 781 | Annotation score: | ||
H7C0A8 | H7C0A8_HUMAN | Low-density lipoprotein receptor-re... | LRP1B | 280 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 516 | C → Y in AAL38107 (PubMed:11031110).Curated | 1 | |
Sequence conflicti | 1257 | P → S in AAL38108 (PubMed:11031110).Curated | 1 | |
Sequence conflicti | 1571 | E → G in AAL38108 (PubMed:11031110).Curated | 1 | |
Sequence conflicti | 2654 – 2655 | LP → CQ in AAL38108 (PubMed:11031110).Curated | 2 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_049759 | 48 | Q → R. Corresponds to variant dbSNP:rs12990449Ensembl. | 1 | |
Natural variantiVAR_049760 | 3140 | Q → R. Corresponds to variant dbSNP:rs34488772Ensembl. | 1 | |
Natural variantiVAR_018328 | 3157 | R → C in NSCLC cells. 1 PublicationCorresponds to variant dbSNP:rs371536401Ensembl. | 1 | |
Natural variantiVAR_049761 | 3458 | E → K. Corresponds to variant dbSNP:rs1878740Ensembl. | 1 | |
Natural variantiVAR_049762 | 3734 | Q → K. Corresponds to variant dbSNP:rs35546150Ensembl. | 1 | |
Natural variantiVAR_049763 | 4264 | V → L. Corresponds to variant dbSNP:rs17386226Ensembl. | 1 |
Sequence databases
Genome annotation databases
Ensembli | ENST00000389484; ENSP00000374135; ENSG00000168702 |
GeneIDi | 53353 |
KEGGi | hsa:53353 |
MANE-Selecti | ENST00000389484.8; ENSP00000374135.3; NM_018557.3; NP_061027.2 |
UCSCi | uc002tvj.2, human |
Similar proteinsi
Cross-referencesi
Sequence databases
3D structure databases
SMRi | Q9NZR2 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 119750, 64 interactors |
IntActi | Q9NZR2, 28 interactors |
STRINGi | 9606.ENSP00000374135 |
PTM databases
GlyConnecti | 1466, 4 N-Linked glycans (1 site) |
GlyGeni | Q9NZR2, 46 sites, 4 N-linked glycans (1 site) |
iPTMneti | Q9NZR2 |
PhosphoSitePlusi | Q9NZR2 |
Genetic variation databases
BioMutai | LRP1B |
DMDMi | 57015418 |
Proteomic databases
EPDi | Q9NZR2 |
jPOSTi | Q9NZR2 |
MassIVEi | Q9NZR2 |
MaxQBi | Q9NZR2 |
PaxDbi | Q9NZR2 |
PeptideAtlasi | Q9NZR2 |
PRIDEi | Q9NZR2 |
ProteomicsDBi | 83492 |
Protocols and materials databases
Antibodypediai | 33599, 57 antibodies from 18 providers |
DNASUi | 53353 |
Genome annotation databases
Ensembli | ENST00000389484; ENSP00000374135; ENSG00000168702 |
GeneIDi | 53353 |
KEGGi | hsa:53353 |
MANE-Selecti | ENST00000389484.8; ENSP00000374135.3; NM_018557.3; NP_061027.2 |
UCSCi | uc002tvj.2, human |
Organism-specific databases
CTDi | 53353 |
DisGeNETi | 53353 |
GeneCardsi | LRP1B |
HGNCi | HGNC:6693, LRP1B |
HPAi | ENSG00000168702, Tissue enriched (brain) |
MIMi | 608766, gene |
neXtProti | NX_Q9NZR2 |
OpenTargetsi | ENSG00000168702 |
PharmGKBi | PA30451 |
VEuPathDBi | HostDB:ENSG00000168702 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1215, Eukaryota |
GeneTreei | ENSGT00940000157521 |
HOGENOMi | CLU_000085_2_1_1 |
InParanoidi | Q9NZR2 |
OMAi | QCIPAKW |
OrthoDBi | 1606at2759 |
PhylomeDBi | Q9NZR2 |
TreeFami | TF315253 |
Enzyme and pathway databases
PathwayCommonsi | Q9NZR2 |
SignaLinki | Q9NZR2 |
SIGNORi | Q9NZR2 |
Miscellaneous databases
BioGRID-ORCSi | 53353, 14 hits in 1037 CRISPR screens |
ChiTaRSi | LRP1B, human |
GeneWikii | LRP1B |
GenomeRNAii | 53353 |
Pharosi | Q9NZR2, Tbio |
PROi | PR:Q9NZR2 |
RNActi | Q9NZR2, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000168702, Expressed in corpus callosum and 150 other tissues |
ExpressionAtlasi | Q9NZR2, baseline and differential |
Genevisiblei | Q9NZR2, HS |
Family and domain databases
CDDi | cd00112, LDLa, 28 hits |
Gene3Di | 2.120.10.30, 8 hits 4.10.400.10, 32 hits |
InterProi | View protein in InterPro IPR011042, 6-blade_b-propeller_TolB-like IPR026823, cEGF IPR032485, DUF5050 IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR000152, EGF-type_Asp/Asn_hydroxyl_site IPR018097, EGF_Ca-bd_CS IPR009030, Growth_fac_rcpt_cys_sf IPR036055, LDL_receptor-like_sf IPR023415, LDLR_class-A_CS IPR000033, LDLR_classB_rpt IPR002172, LDrepeatLR_classA_rpt |
Pfami | View protein in Pfam PF12662, cEGF, 1 hit PF16472, DUF5050, 1 hit PF00008, EGF, 1 hit PF07645, EGF_CA, 2 hits PF00057, Ldl_recept_a, 30 hits PF00058, Ldl_recept_b, 11 hits |
PRINTSi | PR00261, LDLRECEPTOR |
SMARTi | View protein in SMART SM00181, EGF, 25 hits SM00179, EGF_CA, 6 hits SM00192, LDLa, 32 hits SM00135, LY, 37 hits |
SUPFAMi | SSF57184, SSF57184, 3 hits SSF57424, SSF57424, 32 hits |
PROSITEi | View protein in PROSITE PS00010, ASX_HYDROXYL, 4 hits PS00022, EGF_1, 5 hits PS01186, EGF_2, 9 hits PS50026, EGF_3, 9 hits PS01187, EGF_CA, 3 hits PS01209, LDLRA_1, 27 hits PS50068, LDLRA_2, 32 hits PS51120, LDLRB, 37 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | LRP1B_HUMAN | |
Accessioni | Q9NZR2Primary (citable) accession number: Q9NZR2 Secondary accession number(s): Q8WY29, Q8WY30, Q8WY31 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 26, 2004 |
Last sequence update: | January 4, 2005 | |
Last modified: | February 23, 2022 | |
This is version 175 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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
Reference proteomeDocuments
- Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families