Variant ID: 1-55524222-C-T


This variant was identified in 14 publications


A transient amphipathic helix in the prodomain of PCSK9 facilitates binding to low-density lipoprotein particles.

The Journal Of Biological Chemistry
SK Sarkar, ACY Foo, A Matyas, I Asikhia, T Kosenko, NK Goto, A Vergara-Jaque, TA Lagace
Publication Date: 2020-01-16

Variant appearance in text: PCSK9: R469W
PMID: 31949048
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Effects of Genetic Variants Associated with Familial Hypercholesterolemia on Low-Density Lipoprotein-Cholesterol Levels and Cardiovascular Outcomes in the Million Veteran Program.

Circulation. Genomic And Precision Medicine
YV Sun, SM Damrauer, Q Hui, TL Assimes, YL Ho, P Natarajan, D Klarin, J Huang, J Lynch, SL DuVall, S Pyarajan, JP Honerlaw, JM Gaziano, K Cho, DJ Rader, CJ O'Donnell, PS Tsao, PWF Wilson
Publication Date: 2018-12

Variant appearance in text: PCSK9: Arg469Trp; rs141502002
PMID: 31106297
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Identifying individual risk rare variants using protein structure guided local tests (POINT).

Plos Computational Biology
R Marceau West, W Lu, DM Rotroff, MA Kuenemann, SM Chang, MC Wu, MJ Wagner, JB Buse, AA Motsinger-Reif, D Fourches, JY Tzeng
Publication Date: 2019-02

Variant appearance in text: rs141502002
PMID: 30779729
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Identification and in vitro characterization of two new PCSK9 Gain of Function variants found in patients with Familial Hypercholesterolemia.

Scientific Reports
MD Di Taranto, A Benito-Vicente, C Giacobbe, KB Uribe, P Rubba, A Etxebarria, O Guardamagna, M Gentile, C Martín, G Fortunato
Publication Date: 2017-11-10

Variant appearance in text: PCSK9: 1405C>T; Arg469Trp; rs141502002
PMID: 29127338
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Development of a Targeted Multi-Disorder High-Throughput Sequencing Assay for the Effective Identification of Disease-Causing Variants.

Plos One
M Delio, K Patel, A Maslov, RW Marion, TV McDonald, EM Cadoff, A Golden, JM Greally, J Vijg, B Morrow, C Montagna
Publication Date: 2015

Variant appearance in text: PCSK9: R469W; rs141502002
PMID: 26214305
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Plasma Membrane Tetraspanin CD81 Complexes with Proprotein Convertase Subtilisin/Kexin Type 9 (PCSK9) and Low Density Lipoprotein Receptor (LDLR), and Its Levels Are Reduced by PCSK9.

The Journal Of Biological Chemistry
QT Le, M Blanchet, NG Seidah, P Labonté
Publication Date: 2015-09-18

Variant appearance in text: PCSK9: R469W
PMID: 26195630
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PCSK9 variation and association with blood pressure in African Americans: preliminary findings from the HyperGEN and REGARDS studies.

Frontiers In Genetics
NT Tran, S Aslibekyan, HK Tiwari, D Zhi, YJ Sung, SC Hunt, DC Rao, U Broeckel, SE Judd, P Muntner, ST Kent, DK Arnett, MR Irvin
Publication Date: 2015

Variant appearance in text: PCSK9: 1405C>T; R469W; rs141502002
PMID: 25904937
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Annexin A2 reduces PCSK9 protein levels via a translational mechanism and interacts with the M1 and M2 domains of PCSK9.

The Journal Of Biological Chemistry
K Ly, YG Saavedra, M Canuel, S Routhier, R Desjardins, J Hamelin, J Mayne, C Lazure, NG Seidah, R Day
Publication Date: 2014-06-20

Variant appearance in text: PCSK9: R469W
PMID: 24808179
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Differential effects of PCSK9 loss of function variants on serum lipid and PCSK9 levels in Caucasian and African Canadian populations.

Lipids In Health And Disease
J Mayne, TC Ooi, A Raymond, M Cousins, L Bernier, T Dewpura, F Sirois, M Mbikay, J Davignon, M Chrétien
Publication Date: 2013-05-10

Variant appearance in text: PCSK9: R469W
PMID: 23663650
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The M2 module of the Cys-His-rich domain (CHRD) of PCSK9 protein is needed for the extracellular low-density lipoprotein receptor (LDLR) degradation pathway.

The Journal Of Biological Chemistry
YG Saavedra, R Day, NG Seidah
Publication Date: 2012-12-21

Variant appearance in text: PCSK9: R469W
PMID: 23105118
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Mechanisms and genetic determinants regulating sterol absorption, circulating LDL levels, and sterol elimination: implications for classification and disease risk.

Journal Of Lipid Research
S Calandra, P Tarugi, HE Speedy, AF Dean, S Bertolini, CC Shoulders
Publication Date: 2011-11

Variant appearance in text: PCSK9: R469W
PMID: 21862702
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Evidence for positive selection in the C-terminal domain of the cholesterol metabolism gene PCSK9 based on phylogenetic analysis in 14 primate species.

Plos One
K Ding, SJ McDonough, IJ Kullo
Publication Date: 2007-10-31

Variant appearance in text: PCSK9: R469W
PMID: 17971861
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The self-inhibited structure of full-length PCSK9 at 1.9 A reveals structural homology with resistin within the C-terminal domain.

Proceedings Of The National Academy Of Sciences Of The United States Of America
EN Hampton, MW Knuth, J Li, JL Harris, SA Lesley, G Spraggon
Publication Date: 2007-09-11

Variant appearance in text: PCSK9: R469W
PMID: 17804797
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A spectrum of PCSK9 alleles contributes to plasma levels of low-density lipoprotein cholesterol.

American Journal Of Human Genetics
IK Kotowski, A Pertsemlidis, A Luke, RS Cooper, GL Vega, JC Cohen, HH Hobbs
Publication Date: 2006-03

Variant appearance in text: PCSK9: 1405C>T; R469W
PMID: 16465619
View BVdb publication page

Alternative transcript annotations:

Transcript cDNA Protein Consequence Exon Intron
ENST00000302118.5 c.1405C>T p.Arg469Trp missense_variant 9/12 -
ENST00000490692.1 n.2129C>T - non_coding_transcript_exon_variant 6/8 -
ENST00000543384.1 c.753C>T p.His251= synonymous_variant 7/10 -
NM_174936.4 c.1405C>T p.Arg469Trp missense_variant 9/12 -
NR_110451.1 n.1012C>T - non_coding_transcript_exon_variant 7/10 -