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P98155

- VLDLR_HUMAN

UniProt

P98155 - VLDLR_HUMAN

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Protein

Very low-density lipoprotein receptor

Gene

VLDLR

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

Functioni

Binds VLDL and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits. Binding to Reelin induces tyrosine phosphorylation of Dab1 and modulation of Tau phosphorylation (By similarity).By similarity

GO - Molecular functioni

  1. apolipoprotein binding Source: BHF-UCL
  2. calcium-dependent protein binding Source: BHF-UCL
  3. calcium ion binding Source: InterPro
  4. glycoprotein binding Source: BHF-UCL
  5. glycoprotein transporter activity Source: BHF-UCL
  6. low-density lipoprotein receptor activity Source: ProtInc
  7. reelin receptor activity Source: BHF-UCL
  8. very-low-density lipoprotein particle binding Source: BHF-UCL
  9. very-low-density lipoprotein particle receptor activity Source: BHF-UCL

GO - Biological processi

  1. cholesterol metabolic process Source: UniProtKB-KW
  2. glycoprotein transport Source: BHF-UCL
  3. lipid transport Source: UniProtKB-KW
  4. memory Source: ProtInc
  5. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  6. nervous system development Source: ProtInc
  7. positive regulation of dendrite development Source: BHF-UCL
  8. positive regulation of protein kinase activity Source: Ensembl
  9. receptor-mediated endocytosis Source: BHF-UCL
  10. reelin-mediated signaling pathway Source: BHF-UCL
  11. signal transduction Source: ProtInc
  12. ventral spinal cord development Source: Ensembl
  13. very-low-density lipoprotein particle clearance Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cholesterol metabolism, Endocytosis, Lipid metabolism, Lipid transport, Steroid metabolism, Sterol metabolism, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Very low-density lipoprotein receptor
Short name:
VLDL receptor
Short name:
VLDL-R
Gene namesi
Name:VLDLR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:12698. VLDLR.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini28 – 797770ExtracellularSequence AnalysisAdd
BLAST
Transmembranei798 – 81922HelicalSequence AnalysisAdd
BLAST
Topological domaini820 – 87354CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. coated pit Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: MGI
  4. plasma membrane Source: ProtInc
  5. receptor complex Source: MGI
  6. very-low-density lipoprotein particle Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Coated pit, Membrane, VLDL

Pathology & Biotechi

Involvement in diseasei

Cerebellar ataxia, mental retardation, and dysequilibrium syndrome 1 (CAMRQ1) [MIM:224050]: A congenital, non-progressive cerebellar ataxia associated with disturbed equilibrium, delayed ambulation, mental retardation, cerebellar hypoplasia and mild cerebral gyral simplification. Additional features include short stature, strabismus, pes planus and, rarely, seizures.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi825 – 8251K → R: Insensitive to MYLIP-triggered degradation; when associated with R-828 and R-839. 1 Publication
Mutagenesisi828 – 8281K → R: Insensitive to MYLIP-triggered degradation; when associated with R-825 and R-839. 1 Publication
Mutagenesisi839 – 8391K → R: Insensitive to MYLIP-triggered degradation. Insensitive to MYLIP-triggered degradation; when associated with R-825 and R-828. 1 Publication

Keywords - Diseasei

Mental retardation

Organism-specific databases

MIMi224050. phenotype.
Orphaneti1766. Dysequilibrium syndrome.
PharmGKBiPA37317.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence AnalysisAdd
BLAST
Chaini28 – 873846Very low-density lipoprotein receptorPRO_0000017343Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 45By similarity
Disulfide bondi40 ↔ 58By similarity
Disulfide bondi52 ↔ 67By similarity
Disulfide bondi72 ↔ 84By similarity
Disulfide bondi79 ↔ 97By similarity
Disulfide bondi91 ↔ 108By similarity
Disulfide bondi113 ↔ 127
Disulfide bondi120 ↔ 140
Disulfide bondi134 ↔ 149
Glycosylationi151 – 1511N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi154 ↔ 166By similarity
Disulfide bondi161 ↔ 179By similarity
Disulfide bondi173 ↔ 188By similarity
Disulfide bondi193 ↔ 205By similarity
Disulfide bondi200 ↔ 218By similarity
Disulfide bondi212 ↔ 229By similarity
Disulfide bondi239 ↔ 251By similarity
Disulfide bondi246 ↔ 264By similarity
Disulfide bondi258 ↔ 273By similarity
Disulfide bondi278 ↔ 290By similarity
Disulfide bondi285 ↔ 303By similarity
Disulfide bondi297 ↔ 312By similarity
Disulfide bondi318 ↔ 331By similarity
Disulfide bondi326 ↔ 344By similarity
Disulfide bondi338 ↔ 355By similarity
Disulfide bondi360 ↔ 371By similarity
Disulfide bondi367 ↔ 380By similarity
Disulfide bondi382 ↔ 394By similarity
Disulfide bondi400 ↔ 410By similarity
Disulfide bondi406 ↔ 419By similarity
Disulfide bondi421 ↔ 434By similarity
Disulfide bondi706 ↔ 719By similarity
Disulfide bondi715 ↔ 734By similarity
Disulfide bondi736 ↔ 749By similarity
Glycosylationi765 – 7651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi781 – 7811N-linked (GlcNAc...)Sequence Analysis
Cross-linki839 – 839Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Post-translational modificationi

Ubiquitinated at Lys-839 by MYLIP leading to degradation.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP98155.
PaxDbiP98155.
PRIDEiP98155.

PTM databases

PhosphoSiteiP98155.

Expressioni

Tissue specificityi

Abundant in heart and skeletal muscle; also ovary and kidney; not in liver.

Gene expression databases

BgeeiP98155.
CleanExiHS_VLDLR.
ExpressionAtlasiP98155. baseline and differential.
GenevestigatoriP98155.

Organism-specific databases

HPAiCAB032462.
HPA051312.

Interactioni

Subunit structurei

Binds to the extracellular matrix protein Reelin. Interacts with VLDLR. Interacts with SNX17 (By similarity). Interacts with DAB1. Receptor for the minor-group human rhinoviruses (HRVs); binds protein VP1 through the second and third LDL-receptor class A domains. Interacts with PCSK9.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LRPAP1P305334EBI-9004309,EBI-715927
Lrpap1Q990682EBI-9004309,EBI-919734From a different organism.
RelnQ608414EBI-9004309,EBI-9248666From a different organism.

Protein-protein interaction databases

BioGridi113277. 9 interactions.
DIPiDIP-40925N.
IntActiP98155. 3 interactions.
MINTiMINT-111579.
STRINGi9606.ENSP00000371532.

Structurei

Secondary structure

1
873
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni115 – 1173Combined sources
Beta strandi121 – 1255Combined sources
Beta strandi132 – 1376Combined sources
Turni141 – 1455Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1V9UX-ray3.605111-151[»]
3DPRX-ray3.50E113-151[»]
ProteinModelPortaliP98155.
SMRiP98155. Positions 33-753.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP98155.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 6939LDL-receptor class A 1PROSITE-ProRule annotationAdd
BLAST
Domaini70 – 11041LDL-receptor class A 2PROSITE-ProRule annotationAdd
BLAST
Domaini111 – 15141LDL-receptor class A 3PROSITE-ProRule annotationAdd
BLAST
Domaini152 – 19039LDL-receptor class A 4PROSITE-ProRule annotationAdd
BLAST
Domaini191 – 23141LDL-receptor class A 5PROSITE-ProRule annotationAdd
BLAST
Domaini237 – 27539LDL-receptor class A 6PROSITE-ProRule annotationAdd
BLAST
Domaini276 – 31439LDL-receptor class A 7PROSITE-ProRule annotationAdd
BLAST
Domaini316 – 35540LDL-receptor class A 8PROSITE-ProRule annotationAdd
BLAST
Domaini356 – 39540EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini396 – 43540EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Repeati439 – 48042LDL-receptor class B 1Add
BLAST
Repeati481 – 52444LDL-receptor class B 2Add
BLAST
Repeati525 – 56743LDL-receptor class B 3Add
BLAST
Repeati568 – 61144LDL-receptor class B 4Add
BLAST
Repeati612 – 65443LDL-receptor class B 5Add
BLAST
Repeati655 – 69743LDL-receptor class B 6Add
BLAST
Domaini702 – 75049EGF-like 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni751 – 79040Clustered O-linked oligosaccharidesAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi832 – 8376Endocytosis signalSequence Analysis

Sequence similaritiesi

Contains 3 EGF-like domains.PROSITE-ProRule annotation
Contains 8 LDL-receptor class A domains.PROSITE-ProRule annotation
Contains 6 LDL-receptor class B repeats.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG255913.
GeneTreeiENSGT00760000118968.
HOGENOMiHOG000115656.
HOVERGENiHBG006250.
InParanoidiP98155.
OMAiMGTSARW.
OrthoDBiEOG7NGQ9P.
PhylomeDBiP98155.
TreeFamiTF351700.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
4.10.400.10. 8 hits.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
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.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view]
PfamiPF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 8 hits.
PF00058. Ldl_recept_b. 5 hits.
[Graphical view]
PRINTSiPR00261. LDLRECEPTOR.
SMARTiSM00181. EGF. 1 hit.
SM00179. EGF_CA. 2 hits.
SM00192. LDLa. 8 hits.
SM00135. LY. 5 hits.
[Graphical view]
SUPFAMiSSF57424. SSF57424. 8 hits.
PROSITEiPS00010. ASX_HYDROXYL. 2 hits.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
PS01209. LDLRA_1. 8 hits.
PS50068. LDLRA_2. 8 hits.
PS51120. LDLRB. 5 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: P98155-1) [UniParc]FASTAAdd to Basket

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
MGTSALWALW LLLALCWAPR ESGATGTGRK AKCEPSQFQC TNGRCITLLW
60 70 80 90 100
KCDGDEDCVD GSDEKNCVKK TCAESDFVCN NGQCVPSRWK CDGDPDCEDG
110 120 130 140 150
SDESPEQCHM RTCRIHEISC GAHSTQCIPV SWRCDGENDC DSGEDEENCG
160 170 180 190 200
NITCSPDEFT CSSGRCISRN FVCNGQDDCS DGSDELDCAP PTCGAHEFQC
210 220 230 240 250
STSSCIPISW VCDDDADCSD QSDESLEQCG RQPVIHTKCP ASEIQCGSGE
260 270 280 290 300
CIHKKWRCDG DPDCKDGSDE VNCPSRTCRP DQFECEDGSC IHGSRQCNGI
310 320 330 340 350
RDCVDGSDEV NCKNVNQCLG PGKFKCRSGE CIDISKVCNQ EQDCRDWSDE
360 370 380 390 400
PLKECHINEC LVNNGGCSHI CKDLVIGYEC DCAAGFELID RKTCGDIDEC
410 420 430 440 450
QNPGICSQIC INLKGGYKCE CSRGYQMDLA TGVCKAVGKE PSLIFTNRRD
460 470 480 490 500
IRKIGLERKE YIQLVEQLRN TVALDADIAA QKLFWADLSQ KAIFSASIDD
510 520 530 540 550
KVGRHVKMID NVYNPAAIAV DWVYKTIYWT DAASKTISVA TLDGTKRKFL
560 570 580 590 600
FNSDLREPAS IAVDPLSGFV YWSDWGEPAK IEKAGMNGFD RRPLVTADIQ
610 620 630 640 650
WPNGITLDLI KSRLYWLDSK LHMLSSVDLN GQDRRIVLKS LEFLAHPLAL
660 670 680 690 700
TIFEDRVYWI DGENEAVYGA NKFTGSELAT LVNNLNDAQD IIVYHELVQP
710 720 730 740 750
SGKNWCEEDM ENGGCEYLCL PAPQINDHSP KYTCSCPSGY NVEENGRDCQ
760 770 780 790 800
STATTVTYSE TKDTNTTEIS ATSGLVPGGI NVTTAVSEVS VPPKGTSAAW
810 820 830 840 850
AILPLLLLVM AAVGGYLMWR NWQHKNMKSM NFDNPVYLKT TEEDLSIDIG
860 870
RHSASVGHTY PAISVVSTDD DLA
Length:873
Mass (Da):96,098
Last modified:October 1, 1996 - v1
Checksum:i8BAC29438A78C2B8
GO
Isoform Short (identifier: P98155-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     751-779: STATTVTYSETKDTNTTEISATSGLVPGG → R

Show »
Length:845
Mass (Da):93,383
Checksum:i588311D7C6B2C1FD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91L → V in AAA53684. (PubMed:8128315)Curated
Sequence conflicti13 – 131L → V in AAA61344. (PubMed:8020981)Curated
Sequence conflicti424 – 4241G → A in AAA53684. (PubMed:8128315)Curated
Sequence conflicti678 – 6781L → H in AAA53684. (PubMed:8128315)Curated
Sequence conflicti766 – 7661T → S in AAA61344. (PubMed:8020981)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591V → I.2 Publications
Corresponds to variant rs6149 [ dbSNP | Ensembl ].
VAR_011865
Natural varianti262 – 2621P → H.1 Publication
Corresponds to variant rs34761707 [ dbSNP | Ensembl ].
VAR_025063
Natural varianti379 – 3791E → K.1 Publication
Corresponds to variant rs6146 [ dbSNP | Ensembl ].
VAR_011866
Natural varianti464 – 4641L → I.1 Publication
Corresponds to variant rs34753566 [ dbSNP | Ensembl ].
VAR_025064
Natural varianti561 – 5611I → V.1 Publication
Corresponds to variant rs35724190 [ dbSNP | Ensembl ].
VAR_025065
Natural varianti613 – 6131R → H.1 Publication
Corresponds to variant rs35948251 [ dbSNP | Ensembl ].
VAR_025066
Natural varianti791 – 7911V → I.1 Publication
Corresponds to variant rs35334949 [ dbSNP | Ensembl ].
VAR_025067

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei751 – 77929STATT…LVPGG → R in isoform Short. CuratedVSP_004304Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20470 mRNA. Translation: AAA53684.1.
S73849 mRNA. Translation: AAB31735.1.
D16532 Genomic DNA. Translation: BAA03969.1.
D16493 mRNA. Translation: BAA03945.1.
D16494 mRNA. Translation: BAA03946.1.
L22431 mRNA. Translation: AAA61344.1.
DQ067198 Genomic DNA. Translation: AAY46157.1.
AL450467 Genomic DNA. Translation: CAH72454.1.
CH471071 Genomic DNA. Translation: EAW58805.1.
CH471071 Genomic DNA. Translation: EAW58806.1.
BC136562 mRNA. Translation: AAI36563.1.
CCDSiCCDS34979.1. [P98155-2]
CCDS6446.1. [P98155-1]
PIRiA49729.
RefSeqiNP_001018066.1. NM_001018056.1. [P98155-2]
NP_003374.3. NM_003383.3. [P98155-1]
UniGeneiHs.370422.

Genome annotation databases

EnsembliENST00000382099; ENSP00000371531; ENSG00000147852. [P98155-2]
ENST00000382100; ENSP00000371532; ENSG00000147852. [P98155-1]
GeneIDi7436.
KEGGihsa:7436.
UCSCiuc003zhk.1. human. [P98155-1]

Polymorphism databases

DMDMi1730111.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L20470 mRNA. Translation: AAA53684.1 .
S73849 mRNA. Translation: AAB31735.1 .
D16532 Genomic DNA. Translation: BAA03969.1 .
D16493 mRNA. Translation: BAA03945.1 .
D16494 mRNA. Translation: BAA03946.1 .
L22431 mRNA. Translation: AAA61344.1 .
DQ067198 Genomic DNA. Translation: AAY46157.1 .
AL450467 Genomic DNA. Translation: CAH72454.1 .
CH471071 Genomic DNA. Translation: EAW58805.1 .
CH471071 Genomic DNA. Translation: EAW58806.1 .
BC136562 mRNA. Translation: AAI36563.1 .
CCDSi CCDS34979.1. [P98155-2 ]
CCDS6446.1. [P98155-1 ]
PIRi A49729.
RefSeqi NP_001018066.1. NM_001018056.1. [P98155-2 ]
NP_003374.3. NM_003383.3. [P98155-1 ]
UniGenei Hs.370422.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1V9U X-ray 3.60 5 111-151 [» ]
3DPR X-ray 3.50 E 113-151 [» ]
ProteinModelPortali P98155.
SMRi P98155. Positions 33-753.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113277. 9 interactions.
DIPi DIP-40925N.
IntActi P98155. 3 interactions.
MINTi MINT-111579.
STRINGi 9606.ENSP00000371532.

PTM databases

PhosphoSitei P98155.

Polymorphism databases

DMDMi 1730111.

Proteomic databases

MaxQBi P98155.
PaxDbi P98155.
PRIDEi P98155.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000382099 ; ENSP00000371531 ; ENSG00000147852 . [P98155-2 ]
ENST00000382100 ; ENSP00000371532 ; ENSG00000147852 . [P98155-1 ]
GeneIDi 7436.
KEGGi hsa:7436.
UCSCi uc003zhk.1. human. [P98155-1 ]

Organism-specific databases

CTDi 7436.
GeneCardsi GC09P002611.
GeneReviewsi VLDLR.
HGNCi HGNC:12698. VLDLR.
HPAi CAB032462.
HPA051312.
MIMi 192977. gene.
224050. phenotype.
neXtProti NX_P98155.
Orphaneti 1766. Dysequilibrium syndrome.
PharmGKBi PA37317.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG255913.
GeneTreei ENSGT00760000118968.
HOGENOMi HOG000115656.
HOVERGENi HBG006250.
InParanoidi P98155.
OMAi MGTSARW.
OrthoDBi EOG7NGQ9P.
PhylomeDBi P98155.
TreeFami TF351700.

Miscellaneous databases

EvolutionaryTracei P98155.
GeneWikii VLDL_receptor.
GenomeRNAii 7436.
NextBioi 29124.
PROi P98155.
SOURCEi Search...

Gene expression databases

Bgeei P98155.
CleanExi HS_VLDLR.
ExpressionAtlasi P98155. baseline and differential.
Genevestigatori P98155.

Family and domain databases

Gene3Di 2.120.10.30. 1 hit.
4.10.400.10. 8 hits.
InterProi IPR011042. 6-blade_b-propeller_TolB-like.
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.
IPR023415. LDLR_class-A_CS.
IPR000033. LDLR_classB_rpt.
IPR002172. LDrepeatLR_classA_rpt.
[Graphical view ]
Pfami PF07645. EGF_CA. 1 hit.
PF00057. Ldl_recept_a. 8 hits.
PF00058. Ldl_recept_b. 5 hits.
[Graphical view ]
PRINTSi PR00261. LDLRECEPTOR.
SMARTi SM00181. EGF. 1 hit.
SM00179. EGF_CA. 2 hits.
SM00192. LDLa. 8 hits.
SM00135. LY. 5 hits.
[Graphical view ]
SUPFAMi SSF57424. SSF57424. 8 hits.
PROSITEi PS00010. ASX_HYDROXYL. 2 hits.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 2 hits.
PS01187. EGF_CA. 1 hit.
PS01209. LDLRA_1. 8 hits.
PS50068. LDLRA_2. 8 hits.
PS51120. LDLRB. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a cDNA encoding a putative human very low density lipoprotein/apolipoprotein E receptor and assignment of the gene to chromosome 9pter-p23."
    Gafvels M.E., Caird M., Britt D., Jackson C.L., Patterson D., Strauss J.F.
    Somat. Cell Mol. Genet. 19:557-569(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  2. "Characterization and tissue-specific expression of the human 'very low density lipoprotein (VLDL) receptor' mRNA."
    Webb J.C., Patel D.D., Jones M.D., Knight B.L., Soutar A.K.
    Hum. Mol. Genet. 3:531-537(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  3. "Structure, chromosome location, and expression of the human very low density lipoprotein receptor gene."
    Sakai J., Hoshino A., Takahashi S., Miura Y., Ishii H., Suzuki H., Kawarabayasi Y., Yamamoto T.
    J. Biol. Chem. 269:2173-2182(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  4. "Human very-low-density lipoprotein receptor complementary DNA and deduced amino acid sequence and localization of its gene (VLDLR) to chromosome band 9p24 by fluorescence in situ hybridization."
    Oka K., Tzung K.W., Sullivan M., Lindsay E., Baldini A., Chan L.
    Genomics 20:298-300(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Heart.
  5. SeattleSNPs variation discovery resource
    Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-59; HIS-262; ILE-464; VAL-561; HIS-613 AND ILE-791.
  6. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
  9. "A cellular receptor of human rhinovirus type 2, the very-low-density lipoprotein receptor, binds to two neighboring proteins of the viral capsid."
    Neumann E., Moser R., Snyers L., Blaas D., Hewat E.A.
    J. Virol. 77:8504-8511(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HRV VP1.
  10. "The proprotein convertase PCSK9 induces the degradation of low density lipoprotein receptor (LDLR) and its closest family members VLDLR and ApoER2."
    Poirier S., Mayer G., Benjannet S., Bergeron E., Marcinkiewicz J., Nassoury N., Mayer H., Nimpf J., Prat A., Seidah N.G.
    J. Biol. Chem. 283:2363-2372(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PCSK9.
  11. "The E3 ubiquitin ligase IDOL induces the degradation of the low density lipoprotein receptor family members VLDLR and ApoER2."
    Hong C., Duit S., Jalonen P., Out R., Scheer L., Sorrentino V., Boyadjian R., Rodenburg K.W., Foley E., Korhonen L., Lindholm D., Nimpf J., van Berkel T.J., Tontonoz P., Zelcer N.
    J. Biol. Chem. 285:19720-19726(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-839 BY MYLIP, GLYCOSYLATION, MUTAGENESIS OF LYS-825; LYS-828 AND LYS-839.
  12. "X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein."
    Verdaguer N., Fita I., Reithmayer M., Moser R., Blaas D.
    Nat. Struct. Mol. Biol. 11:429-434(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS) OF 111-151 IN COMPLEX WITH HRV2.
  13. Cited for: VARIANTS ILE-59 AND LYS-379.
  14. "Homozygous deletion of the very low density lipoprotein receptor gene causes autosomal recessive cerebellar hypoplasia with cerebral gyral simplification."
    Boycott K.M., Flavelle S., Bureau A., Glass H.C., Fujiwara T.M., Wirrell E., Davey K., Chudley A.E., Scott J.N., McLeod D.R., Parboosingh J.S.
    Am. J. Hum. Genet. 77:477-483(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CAMRQ1.

Entry informationi

Entry nameiVLDLR_HUMAN
AccessioniPrimary (citable) accession number: P98155
Secondary accession number(s): B2RMZ7, D3DRH6, Q5VVF6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 26, 2014
This is version 158 of the entry and version 1 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 9
    Human chromosome 9: 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