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Protein

Low-density lipoprotein receptor-related protein 8

Gene

LRP8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation. May also function as an endocytic receptor. Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2 (By similarity).By similarity3 Publications

Miscellaneous

Natural isoforms of apoE (E2, E3, E4) have similar affinities for LRP8.

GO - Molecular functioni

  • apolipoprotein binding Source: BHF-UCL
  • calcium ion binding Source: InterPro
  • high-density lipoprotein particle binding Source: Ensembl
  • low-density lipoprotein particle receptor activity Source: ARUK-UCL
  • reelin receptor activity Source: BHF-UCL
  • transmembrane signaling receptor activity Source: ProtInc
  • very-low-density lipoprotein particle receptor activity Source: BHF-UCL

GO - Biological processi

Keywordsi

Molecular functionReceptor
Biological processEndocytosis
LigandCalcium

Enzyme and pathway databases

ReactomeiR-HSA-432142 Platelet sensitization by LDL
R-HSA-975634 Retinoid metabolism and transport
SIGNORiQ14114

Names & Taxonomyi

Protein namesi
Recommended name:
Low-density lipoprotein receptor-related protein 8
Short name:
LRP-8
Alternative name(s):
Apolipoprotein E receptor 2
Gene namesi
Name:LRP8
Synonyms:APOER2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000157193.14
HGNCiHGNC:6700 LRP8
MIMi602600 gene
neXtProtiNX_Q14114

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini42 – 826ExtracellularSequence analysisAdd BLAST785
Transmembranei827 – 847HelicalSequence analysisAdd BLAST21
Topological domaini848 – 963CytoplasmicSequence analysisAdd BLAST116

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Myocardial infarction 1 (MCI1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition defined by the irreversible necrosis of heart muscle secondary to prolonged ischemia.
See also OMIM:608446

Organism-specific databases

DisGeNETi7804
MalaCardsiLRP8
MIMi608446 phenotype
OpenTargetsiENSG00000157193
PharmGKBiPA30457

Polymorphism and mutation databases

BioMutaiLRP8
DMDMi259016389

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32Sequence analysisAdd BLAST32
ChainiPRO_000001733233 – 963Low-density lipoprotein receptor-related protein 8Add BLAST931

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi47 ↔ 59By similarity
Disulfide bondi54 ↔ 72By similarity
Disulfide bondi66 ↔ 81By similarity
Disulfide bondi86 ↔ 98By similarity
Disulfide bondi93 ↔ 111By similarity
Disulfide bondi105 ↔ 122By similarity
Disulfide bondi127 ↔ 141By similarity
Disulfide bondi134 ↔ 154By similarity
Disulfide bondi148 ↔ 163By similarity
Disulfide bondi167 ↔ 179By similarity
Disulfide bondi174 ↔ 192By similarity
Glycosylationi176N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi186 ↔ 201By similarity
Disulfide bondi206 ↔ 221By similarity
Disulfide bondi213 ↔ 234By similarity
Disulfide bondi228 ↔ 245By similarity
Disulfide bondi259 ↔ 272By similarity
Disulfide bondi267 ↔ 285By similarity
Disulfide bondi279 ↔ 294By similarity
Disulfide bondi299 ↔ 311By similarity
Disulfide bondi306 ↔ 324By similarity
Disulfide bondi318 ↔ 333By similarity
Disulfide bondi340 ↔ 351By similarity
Disulfide bondi347 ↔ 360By similarity
Disulfide bondi362 ↔ 374By similarity
Disulfide bondi380 ↔ 390By similarity
Disulfide bondi386 ↔ 399By similarity
Disulfide bondi401 ↔ 414By similarity
Glycosylationi441N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi518N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi538N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi772N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi807N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

O-glycosylated. Some alternatively spliced isoforms lack the O-linked sugar domain (By similarity).By similarity
Undergoes sequential, furin and gamma-secretase dependent, proteolytic processing, resulting in the extracellular release of the entire ligand-binding domain as a soluble polypeptide and in the intracellular domain (ICD) release into the cytoplasm. The gamma-secretase-dependent proteolytical processing occurs after the bulk of the extracellular domain has been shed, in a furin-dependent manner, in alternatively spliced isoforms carrying the furin cleavage site. Hypoglycosylation (mainly hypo-O-glycosylation) leads to increased extracellular cleavage, which in turn results in accelerating release of the intracellular domain (ICD) by the gamma-secretase. The resulting receptor fragment is able to inhibit Reelin signaling and in particular the Reelin-induced DAB1 phosphorylation (By similarity).By similarity
Tyrosine phosphorylated upon apoE binding.1 Publication
Ubiquitinated by MYLIP leading to degradation.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ14114
PaxDbiQ14114
PeptideAtlasiQ14114
PRIDEiQ14114

PTM databases

iPTMnetiQ14114
PhosphoSitePlusiQ14114
SwissPalmiQ14114

Miscellaneous databases

PMAP-CutDBiB1AMT8

Expressioni

Tissue specificityi

Expressed mainly in brain and placenta. Also expressed in platelets and megakaryocytic cells. Not expressed in the liver.2 Publications

Gene expression databases

BgeeiENSG00000157193
CleanExiHS_LRP8
ExpressionAtlasiQ14114 baseline and differential
GenevisibleiQ14114 HS

Interactioni

Subunit structurei

Reelin associates with two or more receptor molecules. Interacts with DAB1 and JNK-interacting proteins. Interacts with SNX17 (By similarity). Interacts with PCSK9.By similarity1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • apolipoprotein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi113579, 37 interactors
DIPiDIP-48670N
ELMiQ14114
IntActiQ14114, 22 interactors
STRINGi9606.ENSP00000303634

Structurei

Secondary structure

1963
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi51 – 53Combined sources3
Beta strandi59 – 61Combined sources3
Helixi62 – 64Combined sources3
Beta strandi67 – 69Combined sources3
Beta strandi72 – 75Combined sources4
Helixi76 – 78Combined sources3
Beta strandi88 – 92Combined sources5
Beta strandi98 – 100Combined sources3
Helixi101 – 103Combined sources3
Beta strandi106 – 108Combined sources3
Helixi115 – 117Combined sources3
Turni119 – 121Combined sources3
Turni339 – 341Combined sources3
Helixi342 – 344Combined sources3
Beta strandi348 – 352Combined sources5
Beta strandi355 – 357Combined sources3
Beta strandi359 – 361Combined sources3
Beta strandi368 – 372Combined sources5
Helixi379 – 381Combined sources3
Beta strandi385 – 393Combined sources9
Beta strandi396 – 400Combined sources5
Beta strandi405 – 407Combined sources3
Beta strandi409 – 412Combined sources4
Beta strandi414 – 416Combined sources3
Beta strandi418 – 420Combined sources3
Beta strandi423 – 427Combined sources5
Beta strandi429 – 439Combined sources11
Beta strandi442 – 458Combined sources17
Turni459 – 462Combined sources4
Beta strandi463 – 468Combined sources6
Turni469 – 472Combined sources4
Beta strandi473 – 478Combined sources6
Helixi479 – 481Combined sources3
Helixi485 – 487Combined sources3
Beta strandi489 – 492Combined sources4
Beta strandi501 – 505Combined sources5
Turni506 – 509Combined sources4
Beta strandi510 – 515Combined sources6
Turni516 – 519Combined sources4
Beta strandi520 – 525Combined sources6
Beta strandi530 – 535Combined sources6
Beta strandi540 – 548Combined sources9
Turni549 – 552Combined sources4
Beta strandi553 – 558Combined sources6
Beta strandi560 – 562Combined sources3
Beta strandi564 – 569Combined sources6
Beta strandi576 – 579Combined sources4
Beta strandi586 – 592Combined sources7
Turni593 – 596Combined sources4
Beta strandi597 – 602Combined sources6
Turni603 – 606Combined sources4
Beta strandi607 – 612Combined sources6
Beta strandi619 – 622Combined sources4
Turni625 – 627Combined sources3
Beta strandi629 – 637Combined sources9
Beta strandi640 – 645Combined sources6
Turni646 – 649Combined sources4
Beta strandi650 – 655Combined sources6
Turni656 – 658Combined sources3
Beta strandi663 – 666Combined sources4
Beta strandi675 – 678Combined sources4
Helixi680 – 682Combined sources3
Turni689 – 691Combined sources3
Beta strandi692 – 695Combined sources4
Helixi696 – 699Combined sources4
Beta strandi701 – 706Combined sources6
Beta strandi710 – 714Combined sources5
Beta strandi716 – 720Combined sources5
Beta strandi731 – 735Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3A7QX-ray2.60B42-83[»]
5B4XX-ray3.20B/D42-736[»]
5B4YX-ray1.90B42-124[»]
ProteinModelPortaliQ14114
SMRiQ14114
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14114

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 82LDL-receptor class A 1PROSITE-ProRule annotationAdd BLAST37
Domaini85 – 123LDL-receptor class A 2PROSITE-ProRule annotationAdd BLAST39
Domaini126 – 164LDL-receptor class A 3PROSITE-ProRule annotationAdd BLAST39
Domaini166 – 202LDL-receptor class A 4PROSITE-ProRule annotationAdd BLAST37
Domaini205 – 246LDL-receptor class A 5PROSITE-ProRule annotationAdd BLAST42
Domaini258 – 295LDL-receptor class A 6PROSITE-ProRule annotationAdd BLAST38
Domaini298 – 334LDL-receptor class A 7PROSITE-ProRule annotationAdd BLAST37
Domaini336 – 375EGF-like 1PROSITE-ProRule annotationAdd BLAST40
Domaini376 – 415EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd BLAST40
Repeati462 – 508LDL-receptor class B 1Add BLAST47
Repeati509 – 551LDL-receptor class B 2Add BLAST43
Repeati552 – 595LDL-receptor class B 3Add BLAST44
Repeati596 – 639LDL-receptor class B 4Add BLAST44
Repeati640 – 681LDL-receptor class B 5Add BLAST42

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni740 – 798Clustered O-linked oligosaccharidesAdd BLAST59

Domaini

The cytoplasmic domain is involved in the binding of DAB1 and in the recruitment of JNK-interacting proteins. Isoforms, which lack part of the cytoplasmic domain, are unable to recruit members of the family of JNK interacting proteins (JIP) to the cytoplasmic tail (By similarity).By similarity

Sequence similaritiesi

Belongs to the LDLR family.Curated

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410IPT5 Eukaryota
ENOG410YQ6J LUCA
GeneTreeiENSGT00760000118968
HOVERGENiHBG006250
InParanoidiQ14114
KOiK20052
OMAiAQFACRS
OrthoDBiEOG091G01MX
PhylomeDBiQ14114
TreeFamiTF351700

Family and domain databases

CDDicd00112 LDLa, 6 hits
Gene3Di2.120.10.30, 1 hit
InterProiView protein in InterPro
IPR011042 6-blade_b-propeller_TolB-like
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000152 EGF-type_Asp/Asn_hydroxyl_site
IPR018097 EGF_Ca-bd_CS
IPR036055 LDL_receptor-like_sf
IPR023415 LDLR_class-A_CS
IPR000033 LDLR_classB_rpt
IPR002172 LDrepeatLR_classA_rpt
PfamiView protein in Pfam
PF00057 Ldl_recept_a, 7 hits
PF00058 Ldl_recept_b, 5 hits
PRINTSiPR00261 LDLRECEPTOR
SMARTiView protein in SMART
SM00181 EGF, 4 hits
SM00179 EGF_CA, 2 hits
SM00192 LDLa, 7 hits
SM00135 LY, 5 hits
SUPFAMiSSF57424 SSF57424, 7 hits
PROSITEiView protein in PROSITE
PS00010 ASX_HYDROXYL, 2 hits
PS01186 EGF_2, 2 hits
PS50026 EGF_3, 2 hits
PS01187 EGF_CA, 1 hit
PS01209 LDLRA_1, 7 hits
PS50068 LDLRA_2, 7 hits
PS51120 LDLRB, 5 hits

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist. No differences were observed in the pattern splicing between control and Alzheimer brains.
Isoform 1 (identifier: Q14114-1) [UniParc]FASTAAdd to basket
Also known as: ApoER2 922

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGLPEPGPLR LLALLLLLLL LLLLQLQHLA AAAADPLLGG QGPAKDCEKD
60 70 80 90 100
QFQCRNERCI PSVWRCDEDD DCLDHSDEDD CPKKTCADSD FTCDNGHCIH
110 120 130 140 150
ERWKCDGEEE CPDGSDESEA TCTKQVCPAE KLSCGPTSHK CVPASWRCDG
160 170 180 190 200
EKDCEGGADE AGCATLCAPH EFQCGNRSCL AAVFVCDGDD DCGDGSDERG
210 220 230 240 250
CADPACGPRE FRCGGDGGGA CIPERWVCDR QFDCEDRSDE AAELCGRPGP
260 270 280 290 300
GATSAPAACA TASQFACRSG ECVHLGWRCD GDRDCKDKSD EADCPLGTCR
310 320 330 340 350
GDEFQCGDGT CVLAIKHCNQ EQDCPDGSDE AGCLQGLNEC LHNNGGCSHI
360 370 380 390 400
CTDLKIGFEC TCPAGFQLLD QKTCGDIDEC KDPDACSQIC VNYKGYFKCE
410 420 430 440 450
CYPGYEMDLL TKNCKAAAGK SPSLIFTNRH EVRRIDLVKR NYSRLIPMLK
460 470 480 490 500
NVVALDVEVA TNRIYWCDLS YRKIYSAYMD KASDPKEQEV LIDEQLHSPE
510 520 530 540 550
GLAVDWVHKH IYWTDSGNKT ISVATVDGGR RRTLFSRNLS EPRAIAVDPL
560 570 580 590 600
RGFMYWSDWG DQAKIEKSGL NGVDRQTLVS DNIEWPNGIT LDLLSQRLYW
610 620 630 640 650
VDSKLHQLSS IDFSGGNRKT LISSTDFLSH PFGIAVFEDK VFWTDLENEA
660 670 680 690 700
IFSANRLNGL EISILAENLN NPHDIVIFHE LKQPRAPDAC ELSVQPNGGC
710 720 730 740 750
EYLCLPAPQI SSHSPKYTCA CPDTMWLGPD MKRCYRAPQS TSTTTLASTM
760 770 780 790 800
TRTVPATTRA PGTTVHRSTY QNHSTETPSL TAAVPSSVSV PRAPSISPST
810 820 830 840 850
LSPATSNHSQ HYANEDSKMG STVTAAVIGI IVPIVVIALL CMSGYLIWRN
860 870 880 890 900
WKRKNTKSMN FDNPVYRKTT EEEDEDELHI GRTAQIGHVY PAAISSFDRP
910 920 930 940 950
LWAEPCLGET REPEDPAPAL KELFVLPGEP RSQLHQLPKN PLSELPVVKS
960
KRVALSLEDD GLP
Length:963
Mass (Da):105,634
Last modified:September 22, 2009 - v4
Checksum:iB10DCF72F62DE71C
GO
Isoform 2 (identifier: Q14114-2) [UniParc]FASTAAdd to basket
Also known as: ApoER2 906

The sequence of this isoform differs from the canonical sequence as follows:
     166-295: LCAPHEFQCG...KDKSDEADCP → S
     737-812: APQSTSTTTL...PATSNHSQHY → D
     893-951: Missing.

Show »
Length:700
Mass (Da):77,845
Checksum:iB996C9CAEC69C1E9
GO
Isoform 3 (identifier: Q14114-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     893-951: Missing.

Show »
Length:904
Mass (Da):99,092
Checksum:i043E708314261E3C
GO
Isoform 4 (identifier: Q14114-4) [UniParc]FASTAAdd to basket
Also known as: ApoER2delta4-7

The sequence of this isoform differs from the canonical sequence as follows:
     166-166: L → W
     167-336: Missing.

Show »
Length:793
Mass (Da):87,959
Checksum:i1A414B09D40BA1BC
GO
Isoform 5 (identifier: Q14114-5)
Sequence is not available
Note: Contains an insert in the extracellular part which carries a furin cleavage site.
Length:
Mass (Da):

Sequence cautioni

The sequence CAA99509 differs from that shown. Reason: Frameshift at positions 430, 432 and 438.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti262A → V in BAA09328 (PubMed:8626535).Curated1
Sequence conflicti262A → V in BAA21824 (PubMed:9079678).Curated1
Sequence conflicti405Y → C in CAA99509 (PubMed:11152697).Curated1
Sequence conflicti418A → G in BAA09328 (PubMed:8626535).Curated1
Sequence conflicti418A → G in BAA21824 (PubMed:9079678).Curated1
Sequence conflicti418A → G in BAA21825 (PubMed:9079678).Curated1
Sequence conflicti430H → Y in BAA09328 (PubMed:8626535).Curated1
Sequence conflicti430H → Y in BAA21824 (PubMed:9079678).Curated1
Sequence conflicti430H → Y in BAA21825 (PubMed:9079678).Curated1
Sequence conflicti430H → Y in CAA99509 (PubMed:11152697).Curated1
Sequence conflicti488Q → R in CAA99509 (PubMed:11152697).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04697425Q → R4 PublicationsCorresponds to variant dbSNP:rs4926972Ensembl.1
Natural variantiVAR_01846846D → E5 PublicationsCorresponds to variant dbSNP:rs3820198Ensembl.1
Natural variantiVAR_037624453V → M. Corresponds to variant dbSNP:rs5180Ensembl.1
Natural variantiVAR_037625466W → C. Corresponds to variant dbSNP:rs5181Ensembl.1
Natural variantiVAR_037626607Q → R. Corresponds to variant dbSNP:rs5172Ensembl.1
Natural variantiVAR_037627611I → L. Corresponds to variant dbSNP:rs5170Ensembl.1
Natural variantiVAR_037628653S → T. Corresponds to variant dbSNP:rs5171Ensembl.1
Natural variantiVAR_059079736R → Q. Corresponds to variant dbSNP:rs5172Ensembl.1
Natural variantiVAR_018469952R → Q Associated with susceptibility to myocardial infarction type 1; increases activation of MAPK14 by oxidized low density lipoprotein. 2 PublicationsCorresponds to variant dbSNP:rs5174EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_010305166 – 295LCAPH…EADCP → S in isoform 2. 1 PublicationAdd BLAST130
Alternative sequenceiVSP_038181166L → W in isoform 4. Curated1
Alternative sequenceiVSP_010306167 – 336Missing in isoform 4. CuratedAdd BLAST170
Alternative sequenceiVSP_010307737 – 812APQST…HSQHY → D in isoform 2. 1 PublicationAdd BLAST76
Alternative sequenceiVSP_010308893 – 951Missing in isoform 2 and isoform 3. 2 PublicationsAdd BLAST59

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50678 mRNA Translation: BAA09328.1
D86407 Genomic DNA Translation: BAA21824.1
D86407 Genomic DNA Translation: BAA21825.1
Z75190 mRNA Translation: CAA99509.1 Frameshift.
AL355483 Genomic DNA No translation available.
AL606760 Genomic DNA No translation available.
BC006443 mRNA Translation: AAH06443.1
BC051836 mRNA Translation: AAH51836.2
CCDSiCCDS30720.1 [Q14114-3]
CCDS578.1 [Q14114-1]
CCDS579.1 [Q14114-2]
CCDS580.1 [Q14114-4]
RefSeqiNP_001018064.1, NM_001018054.2 [Q14114-3]
NP_004622.2, NM_004631.4 [Q14114-1]
NP_059992.3, NM_017522.4 [Q14114-2]
NP_150643.2, NM_033300.3 [Q14114-4]
UniGeneiHs.280387

Genome annotation databases

EnsembliENST00000306052; ENSP00000303634; ENSG00000157193 [Q14114-1]
ENST00000347547; ENSP00000334522; ENSG00000157193 [Q14114-4]
ENST00000354412; ENSP00000346391; ENSG00000157193 [Q14114-2]
ENST00000371454; ENSP00000360509; ENSG00000157193 [Q14114-3]
GeneIDi7804
KEGGihsa:7804
UCSCiuc001cvi.4 human [Q14114-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiLRP8_HUMAN
AccessioniPrimary (citable) accession number: Q14114
Secondary accession number(s): B1AMT6
, B1AMT7, B1AMT8, O14968, Q86V27, Q99876, Q9BR78
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: September 22, 2009
Last modified: May 23, 2018
This is version 177 of the entry and version 4 of the sequence. See 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 1
    Human chromosome 1: 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

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