Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Proprotein convertase subtilisin/kexin type 9

Gene

PCSK9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their degradation in intracellular acidic compartments (PubMed:18039658). Acts via a non-proteolytic mechanism to enhance the degradation of the hepatic LDLR through a clathrin LDLRAP1/ARH-mediated pathway. May prevent the recycling of LDLR from endosomes to the cell surface or direct it to lysosomes for degradation. Can induce ubiquitination of LDLR leading to its subsequent degradation (PubMed:18799458, PubMed:17461796, PubMed:18197702, PubMed:22074827). Inhibits intracellular degradation of APOB via the autophagosome/lysosome pathway in a LDLR-independent manner. Involved in the disposal of non-acetylated intermediates of BACE1 in the early secretory pathway (PubMed:18660751). Inhibits epithelial Na+ channel (ENaC)-mediated Na+ absorption by reducing ENaC surface expression primarily by increasing its proteasomal degradation. Regulates neuronal apoptosis via modulation of LRP8/APOER2 levels and related anti-apoptotic signaling pathways.8 Publications

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+Curated

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Its proteolytic activity is autoinhibited by the non-covalent binding of the propeptide to the catalytic domain. Inhibited by EGTA.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei186Charge relay systemBy similarity1
Active sitei226Charge relay systemBy similarity1
Active sitei386Charge relay systemBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processApoptosis, Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism
LigandCalcium

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.4.21.61 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-8866427 VLDLR internalisation and degradation
R-HSA-8957275 Post-translational protein phosphorylation
R-HSA-8964038 LDL clearance

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q8NBP7

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q8NBP7

Protein family/group databases

MEROPS protease database

More...
MEROPSi
S08.039

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Proprotein convertase subtilisin/kexin type 9 (EC:3.4.21.-)
Alternative name(s):
Neural apoptosis-regulated convertase 1
Short name:
NARC-1
Proprotein convertase 9
Short name:
PC9
Subtilisin/kexin-like protease PC9
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PCSK9
Synonyms:NARC1
ORF Names:PSEC0052
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000169174.10

Human Gene Nomenclature Database

More...
HGNCi
HGNC:20001 PCSK9

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
607786 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q8NBP7

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Endosome, Golgi apparatus, Lysosome, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Hypercholesterolemia, autosomal dominant, 3 (HCHOLA3)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA familial condition characterized by elevated circulating cholesterol contained in either low-density lipoproteins alone or also in very-low-density lipoproteins.
See also OMIM:603776
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_017199127S → R in HCHOLA3. 1 PublicationCorresponds to variant dbSNP:rs28942111EnsemblClinVar.1
Natural variantiVAR_058524129D → G in HCHOLA3. 1
Natural variantiVAR_058526215R → H in HCHOLA3. Corresponds to variant dbSNP:rs794728683EnsemblClinVar.1
Natural variantiVAR_017200216F → L in HCHOLA3; partial loss of cleavage by furin and PCSK5. 1 PublicationCorresponds to variant dbSNP:rs28942112EnsemblClinVar.1
Natural variantiVAR_058527218R → S in HCHOLA3; complete loss of cleavage by furin and PCSK5; reduces glycosylation levels; no effect on protein sulfation and phosphorylation; no effect on protein sulfation but inhibits phosphorylation when associated with Y-374; highly reduces LDL uptake when associated with Y-374. 2 PublicationsCorresponds to variant dbSNP:rs970575319EnsemblClinVar.1
Natural variantiVAR_058530357R → H in HCHOLA3. Corresponds to variant dbSNP:rs370507566EnsemblClinVar.1
Natural variantiVAR_058531374D → H in HCHOLA3. Corresponds to variant dbSNP:rs137852912EnsemblClinVar.1
Natural variantiVAR_058532374D → Y in HCHOLA3; partial loss of cleavage by furin and PCSK5; no effect on protein sulfation but inhibits phosphorylation when associated with S-218; highly increases LDL uptake when associated with S-218. 2 PublicationsCorresponds to variant dbSNP:rs137852912EnsemblClinVar.1
Natural variantiVAR_058534496R → W in HCHOLA3. Corresponds to variant dbSNP:rs374603772EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi67C → A: Does not affect multimerization or zymogen processing. 1 Publication1
Mutagenesisi226H → A: Remains in the endoplasmic reticulum and is not secreted. 1 Publication1
Mutagenesisi533N → A: 1.5 kDa decrease of the apparent molecular mass of pro-PCSK9 and PCSK9 and no effect on processing and secretion. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
255738

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...
GeneReviewsi
PCSK9

MalaCards human disease database

More...
MalaCardsi
PCSK9
MIMi603776 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000169174

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
391665 Homozygous familial hypercholesterolemia
426 NON RARE IN EUROPE: Familial hypobetalipoproteinemia
406 NON RARE IN EUROPE: Heterozygous familial hypercholesterolemia

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA38617

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2929

Drug and drug target database

More...
DrugBanki
DB09302 Alirocumab
DB09303 Evolocumab

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
2388

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PCSK9

Domain mapping of disease mutations (DMDM)

More...
DMDMi
317373487

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 301 PublicationAdd BLAST30
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002712031 – 1521 PublicationAdd BLAST122
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000027121153 – 692Proprotein convertase subtilisin/kexin type 9Add BLAST540

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei38Sulfotyrosine1 Publication1
Modified residuei47Phosphoserine; by FAM20C2 Publications1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi223 ↔ 255Sequence analysis
Disulfide bondi323 ↔ 358Sequence analysis
Disulfide bondi457 ↔ 527Sequence analysis
Disulfide bondi477 ↔ 526Sequence analysis
Disulfide bondi486 ↔ 509Sequence analysis
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi533N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi534 ↔ 601Sequence analysis
Disulfide bondi552 ↔ 600Sequence analysis
Disulfide bondi562 ↔ 588Sequence analysis
Disulfide bondi608 ↔ 679Sequence analysis
Disulfide bondi626 ↔ 678Sequence analysis
Disulfide bondi635 ↔ 654Sequence analysis
Modified residuei688Phosphoserine; by FAM20CCombined sources2 Publications1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation.1 Publication
Undergoes autocatalytic cleavage in the endoplasmic reticulum to release the propeptide from the N-terminus and the cleavage of the propeptide is strictly required for its maturation and activation. The cleaved propeptide however remains associated with the catalytic domain through non-covalent interactions, preventing potential substrates from accessing its active site. As a result, it is secreted from cells as a propeptide-containing, enzymatically inactive protein.1 Publication
Phosphorylation protects the propeptide against proteolysis.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei152 – 153Cleavage; by autolysis1 Publication2
Sitei218 – 219Cleavage; by furin and PCSK51 Publication2

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation, Zymogen

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q8NBP7

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q8NBP7

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q8NBP7

PeptideAtlas

More...
PeptideAtlasi
Q8NBP7

PRoteomics IDEntifications database

More...
PRIDEi
Q8NBP7

ProteomicsDB human proteome resource

More...
ProteomicsDBi
72807
72808 [Q8NBP7-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q8NBP7

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q8NBP7

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in neuro-epithelioma, colon carcinoma, hepatic and pancreatic cell lines, and in Schwann cells.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000169174 Expressed in 85 organ(s), highest expression level in right lobe of liver

CleanEx database of gene expression profiles

More...
CleanExi
HS_PCSK9

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q8NBP7 HS

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer. Can self-associate to form dimers and higher multimers which may have increased LDLR degrading activity. The precursor protein but not the mature protein may form multimers. Interacts with APOB, VLDLR, LRP8/APOER2 and BACE1. The full-length immature form (pro-PCSK9) interacts with SCNN1A, SCNN1B and SCNN1G. The pro-PCSK9 form (via C-terminal domain) interacts with LDLR. Interacts (via the C-terminal domain) with ANXA2 (via repeat Annexin 1); the interaction inhibits the degradation of LDLR (PubMed:18799458).9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
129116, 27 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-128 LDLR-PCSK9 complex
CPX-130 ANXA2-PCSK9 complex

Database of interacting proteins

More...
DIPi
DIP-29694N

Protein interaction database and analysis system

More...
IntActi
Q8NBP7, 5 interactors

Molecular INTeraction database

More...
MINTi
Q8NBP7

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000303208

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q8NBP7

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1692
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q8NBP7

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q8NBP7

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q8NBP7

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini182 – 424Peptidase S8Add BLAST243

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni450 – 692C-terminal domainAdd BLAST243

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal domain (CRD) is essential for the LDLR-binding and degrading activities.1 Publication
The catalytic domain is responsible for mediating its self-association.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase S8 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1153 Eukaryota
COG1404 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00490000043472

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000049267

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG053530

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q8NBP7

KEGG Orthology (KO)

More...
KOi
K13050

Identification of Orthologs from Complete Genome Data

More...
OMAi
KCDSHGT

Database of Orthologous Groups

More...
OrthoDBi
EOG091G067E

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8NBP7

TreeFam database of animal gene trees

More...
TreeFami
TF106271

Family and domain databases

Conserved Domains Database

More...
CDDi
cd04077 Peptidases_S8_PCSK9_Proteinase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.70.80, 1 hit
3.40.50.200, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR034193 PCSK9_ProteinaseK-like
IPR000209 Peptidase_S8/S53_dom
IPR036852 Peptidase_S8/S53_dom_sf
IPR015500 Peptidase_S8_subtilisin-rel
IPR010259 S8pro/Inhibitor_I9
IPR037045 S8pro/Inhibitor_I9_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF05922 Inhibitor_I9, 1 hit
PF00082 Peptidase_S8, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00723 SUBTILISIN

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52743 SSF52743, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q8NBP7-1) [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
MGTVSSRRSW WPLPLLLLLL LLLGPAGARA QEDEDGDYEE LVLALRSEED
60 70 80 90 100
GLAEAPEHGT TATFHRCAKD PWRLPGTYVV VLKEETHLSQ SERTARRLQA
110 120 130 140 150
QAARRGYLTK ILHVFHGLLP GFLVKMSGDL LELALKLPHV DYIEEDSSVF
160 170 180 190 200
AQSIPWNLER ITPPRYRADE YQPPDGGSLV EVYLLDTSIQ SDHREIEGRV
210 220 230 240 250
MVTDFENVPE EDGTRFHRQA SKCDSHGTHL AGVVSGRDAG VAKGASMRSL
260 270 280 290 300
RVLNCQGKGT VSGTLIGLEF IRKSQLVQPV GPLVVLLPLA GGYSRVLNAA
310 320 330 340 350
CQRLARAGVV LVTAAGNFRD DACLYSPASA PEVITVGATN AQDQPVTLGT
360 370 380 390 400
LGTNFGRCVD LFAPGEDIIG ASSDCSTCFV SQSGTSQAAA HVAGIAAMML
410 420 430 440 450
SAEPELTLAE LRQRLIHFSA KDVINEAWFP EDQRVLTPNL VAALPPSTHG
460 470 480 490 500
AGWQLFCRTV WSAHSGPTRM ATAVARCAPD EELLSCSSFS RSGKRRGERM
510 520 530 540 550
EAQGGKLVCR AHNAFGGEGV YAIARCCLLP QANCSVHTAP PAEASMGTRV
560 570 580 590 600
HCHQQGHVLT GCSSHWEVED LGTHKPPVLR PRGQPNQCVG HREASIHASC
610 620 630 640 650
CHAPGLECKV KEHGIPAPQE QVTVACEEGW TLTGCSALPG TSHVLGAYAV
660 670 680 690
DNTCVVRSRD VSTTGSTSEG AVTAVAICCR SRHLAQASQE LQ
Length:692
Mass (Da):74,286
Last modified:January 11, 2011 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9BCB9418B90AEE23
GO
Isoform 2 (identifier: Q8NBP7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-174: MGTVSSRRSW...RYRADEYQPP → MSPWK
     333-365: VITVGATNAQDQPVTLGTLGTNFGRCVDLFAPG → GRTSLVPPATAAPALCHRVGHHRLLPTWLALQP
     366-692: Missing.

Note: No experimental confirmation available.
Show »
Length:196
Mass (Da):20,827
Checksum:i6073DFE87E84FA15
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAC11572 differs from that shown. Reason: Frameshift at position 494.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti423V → A in BAC11572 (PubMed:14702039).Curated1

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

Variant Leu-23 ins polymorphism in PCSK9 might have a modifier effect on LDLR mutation and familial hypercholesterolemia.
Genetic variations in PCSK9 define the low density lipoprotein cholesterol level quantitative trait locus 1 (LDLCQ1) [MIMi:603776].3 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02133623L → LL This polymoprhism seems to have a modifier effect on LDLR mutation and familial hypercholesterolemia. 4 Publications1
Natural variantiVAR_01719746R → L Polymorphism; associated with lower plasma levels of low-density lipoprotein cholesterol; reduced phosphorylation at Ser-47. 4 PublicationsCorresponds to variant dbSNP:rs11591147EnsemblClinVar.1
Natural variantiVAR_01719853A → V Polymorphism; associated with reduced phosphorylation at Ser-47. 4 PublicationsCorresponds to variant dbSNP:rs11583680EnsemblClinVar.1
Natural variantiVAR_02545157E → K1 PublicationCorresponds to variant dbSNP:rs145886902EnsemblClinVar.1
Natural variantiVAR_05852077T → I. Corresponds to variant dbSNP:rs756060557Ensembl.1
Natural variantiVAR_05852193R → C. Corresponds to variant dbSNP:rs151193009EnsemblClinVar.1
Natural variantiVAR_058522106G → R. 1
Natural variantiVAR_058523114V → A. Corresponds to variant dbSNP:rs775988212Ensembl.1
Natural variantiVAR_017199127S → R in HCHOLA3. 1 PublicationCorresponds to variant dbSNP:rs28942111EnsemblClinVar.1
Natural variantiVAR_058524129D → G in HCHOLA3. 1
Natural variantiVAR_058525157N → K. Corresponds to variant dbSNP:rs143117125Ensembl.1
Natural variantiVAR_067351174P → S Found in patients with familial hypercholesterolemia carrying a homozygous LDLR mutation; acts as a disease modifier resulting in a mild phenotype. 1 PublicationCorresponds to variant dbSNP:rs533273863EnsemblClinVar.1
Natural variantiVAR_058526215R → H in HCHOLA3. Corresponds to variant dbSNP:rs794728683EnsemblClinVar.1
Natural variantiVAR_017200216F → L in HCHOLA3; partial loss of cleavage by furin and PCSK5. 1 PublicationCorresponds to variant dbSNP:rs28942112EnsemblClinVar.1
Natural variantiVAR_058527218R → S in HCHOLA3; complete loss of cleavage by furin and PCSK5; reduces glycosylation levels; no effect on protein sulfation and phosphorylation; no effect on protein sulfation but inhibits phosphorylation when associated with Y-374; highly reduces LDL uptake when associated with Y-374. 2 PublicationsCorresponds to variant dbSNP:rs970575319EnsemblClinVar.1
Natural variantiVAR_058528219Q → E. Corresponds to variant dbSNP:rs778617372EnsemblClinVar.1
Natural variantiVAR_025452237R → W1 PublicationCorresponds to variant dbSNP:rs148195424EnsemblClinVar.1
Natural variantiVAR_058529239A → D. 1
Natural variantiVAR_025453253L → F Polymorphism; associated with lower plasma levels of low-density lipoprotein cholesterol. 1 PublicationCorresponds to variant dbSNP:rs72646508EnsemblClinVar.1
Natural variantiVAR_058530357R → H in HCHOLA3. Corresponds to variant dbSNP:rs370507566EnsemblClinVar.1
Natural variantiVAR_058531374D → H in HCHOLA3. Corresponds to variant dbSNP:rs137852912EnsemblClinVar.1
Natural variantiVAR_058532374D → Y in HCHOLA3; partial loss of cleavage by furin and PCSK5; no effect on protein sulfation but inhibits phosphorylation when associated with S-218; highly increases LDL uptake when associated with S-218. 2 PublicationsCorresponds to variant dbSNP:rs137852912EnsemblClinVar.1
Natural variantiVAR_025454391H → N1 PublicationCorresponds to variant dbSNP:rs146471967EnsemblClinVar.1
Natural variantiVAR_067282394G → S Found in a patient associated with autosomal dominant hypercholesterolemia; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs368257906EnsemblClinVar.1
Natural variantiVAR_025455417H → Q1 PublicationCorresponds to variant dbSNP:rs143275858EnsemblClinVar.1
Natural variantiVAR_021337425N → S2 PublicationsCorresponds to variant dbSNP:rs28362261EnsemblClinVar.1
Natural variantiVAR_021338443A → T Polymorphism; associated with lower plasma levels of low-density lipoprotein cholesterol; more extensive cleavage by furin and PCSK5. 2 PublicationsCorresponds to variant dbSNP:rs28362263EnsemblClinVar.1
Natural variantiVAR_058533452G → D. 1
Natural variantiVAR_025456469R → W1 PublicationCorresponds to variant dbSNP:rs141502002EnsemblClinVar.1
Natural variantiVAR_021339474V → I8 PublicationsCorresponds to variant dbSNP:rs562556EnsemblClinVar.1
Natural variantiVAR_025457482E → G1 PublicationCorresponds to variant dbSNP:rs141995194Ensembl.1
Natural variantiVAR_073657482E → Q No effect on interaction with ANXA2. 1 Publication1
Natural variantiVAR_058534496R → W in HCHOLA3. Corresponds to variant dbSNP:rs374603772EnsemblClinVar.1
Natural variantiVAR_025458515F → L1 PublicationCorresponds to variant dbSNP:rs1356131564Ensembl.1
Natural variantiVAR_058535522A → T. Corresponds to variant dbSNP:rs777300852Ensembl.1
Natural variantiVAR_021340553H → R2 PublicationsCorresponds to variant dbSNP:rs28362270EnsemblClinVar.1
Natural variantiVAR_025459554Q → E Increases interaction with ANXA2. 2 PublicationsCorresponds to variant dbSNP:rs149311926EnsemblClinVar.1
Natural variantiVAR_058536616P → L. Corresponds to variant dbSNP:rs755750316Ensembl.1
Natural variantiVAR_021341619Q → P2 PublicationsCorresponds to variant dbSNP:rs28362277EnsemblClinVar.1
Natural variantiVAR_058537668S → R. Corresponds to variant dbSNP:rs762298323EnsemblClinVar.1
Natural variantiVAR_017201670G → E8 PublicationsCorresponds to variant dbSNP:rs505151EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0088441 – 174MGTVS…EYQPP → MSPWK in isoform 2. 1 PublicationAdd BLAST174
Alternative sequenceiVSP_008845333 – 365VITVG…LFAPG → GRTSLVPPATAAPALCHRVG HHRLLPTWLALQP in isoform 2. 1 PublicationAdd BLAST33
Alternative sequenceiVSP_008846366 – 692Missing in isoform 2. 1 PublicationAdd BLAST327

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AX127530 mRNA Translation: CAC38896.1
EF692496 mRNA Translation: ABV59216.1
AK075365 mRNA Translation: BAC11572.1 Frameshift.
AK124635 mRNA Translation: BAC85910.1
AY829011 Genomic DNA Translation: AAV67948.1
FJ525880 Genomic DNA Translation: ACN81318.1
AC091609 Genomic DNA No translation available.
AL589790 Genomic DNA No translation available.
CH471059 Genomic DNA Translation: EAX06660.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS603.1 [Q8NBP7-1]

NCBI Reference Sequences

More...
RefSeqi
NP_777596.2, NM_174936.3 [Q8NBP7-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.18844

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000302118; ENSP00000303208; ENSG00000169174 [Q8NBP7-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
255738

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:255738

UCSC genome browser

More...
UCSCi
uc001cyf.3 human [Q8NBP7-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AX127530 mRNA Translation: CAC38896.1
EF692496 mRNA Translation: ABV59216.1
AK075365 mRNA Translation: BAC11572.1 Frameshift.
AK124635 mRNA Translation: BAC85910.1
AY829011 Genomic DNA Translation: AAV67948.1
FJ525880 Genomic DNA Translation: ACN81318.1
AC091609 Genomic DNA No translation available.
AL589790 Genomic DNA No translation available.
CH471059 Genomic DNA Translation: EAX06660.1
CCDSiCCDS603.1 [Q8NBP7-1]
RefSeqiNP_777596.2, NM_174936.3 [Q8NBP7-1]
UniGeneiHs.18844

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2P4EX-ray1.98A/P1-692[»]
2PMWX-ray2.30A31-152[»]
B153-692[»]
2QTWX-ray1.90A29-152[»]
B153-692[»]
2W2MX-ray2.40A153-451[»]
P53-152[»]
2W2NX-ray2.30A153-451[»]
P53-152[»]
2W2OX-ray2.62A153-451[»]
P53-152[»]
2W2PX-ray2.62A153-451[»]
P53-152[»]
2W2QX-ray2.33A153-451[»]
P53-152[»]
2XTJX-ray2.70A153-451[»]
P53-152[»]
3BPSX-ray2.41A153-692[»]
P53-152[»]
3GCWX-ray2.70A153-692[»]
P53-152[»]
3GCXX-ray2.70A153-692[»]
P53-152[»]
3H42X-ray2.30A31-152[»]
B153-692[»]
3M0CX-ray7.01A29-152[»]
B153-692[»]
3P5BX-ray3.30A153-692[»]
P61-152[»]
3P5CX-ray4.20A153-692[»]
P61-152[»]
3SQOX-ray2.70A153-692[»]
P31-152[»]
4K8RX-ray3.22A61-152[»]
B153-692[»]
4NE9X-ray2.60A/B153-692[»]
C/P1-152[»]
4NMXX-ray1.85A31-152[»]
B153-452[»]
4OV6X-ray2.69A/D60-152[»]
B/E153-446[»]
5OCAX-ray2.30A31-152[»]
B153-692[»]
5VL7X-ray3.50A31-152[»]
B153-692[»]
5VLAX-ray2.40A1-452[»]
5VLHX-ray2.86A1-452[»]
5VLKX-ray2.20A1-452[»]
5VLLX-ray2.37A1-452[»]
5VLPX-ray2.90A1-692[»]
ProteinModelPortaliQ8NBP7
SMRiQ8NBP7
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129116, 27 interactors
ComplexPortaliCPX-128 LDLR-PCSK9 complex
CPX-130 ANXA2-PCSK9 complex
DIPiDIP-29694N
IntActiQ8NBP7, 5 interactors
MINTiQ8NBP7
STRINGi9606.ENSP00000303208

Chemistry databases

BindingDBiQ8NBP7
ChEMBLiCHEMBL2929
DrugBankiDB09302 Alirocumab
DB09303 Evolocumab
GuidetoPHARMACOLOGYi2388

Protein family/group databases

MEROPSiS08.039

PTM databases

iPTMnetiQ8NBP7
PhosphoSitePlusiQ8NBP7

Polymorphism and mutation databases

BioMutaiPCSK9
DMDMi317373487

Proteomic databases

EPDiQ8NBP7
MaxQBiQ8NBP7
PaxDbiQ8NBP7
PeptideAtlasiQ8NBP7
PRIDEiQ8NBP7
ProteomicsDBi72807
72808 [Q8NBP7-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
255738
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302118; ENSP00000303208; ENSG00000169174 [Q8NBP7-1]
GeneIDi255738
KEGGihsa:255738
UCSCiuc001cyf.3 human [Q8NBP7-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
255738
DisGeNETi255738
EuPathDBiHostDB:ENSG00000169174.10

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PCSK9
GeneReviewsiPCSK9

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0023558
HGNCiHGNC:20001 PCSK9
MalaCardsiPCSK9
MIMi603776 phenotype
607786 gene
neXtProtiNX_Q8NBP7
OpenTargetsiENSG00000169174
Orphaneti391665 Homozygous familial hypercholesterolemia
426 NON RARE IN EUROPE: Familial hypobetalipoproteinemia
406 NON RARE IN EUROPE: Heterozygous familial hypercholesterolemia
PharmGKBiPA38617

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1153 Eukaryota
COG1404 LUCA
GeneTreeiENSGT00490000043472
HOGENOMiHOG000049267
HOVERGENiHBG053530
InParanoidiQ8NBP7
KOiK13050
OMAiKCDSHGT
OrthoDBiEOG091G067E
PhylomeDBiQ8NBP7
TreeFamiTF106271

Enzyme and pathway databases

BRENDAi3.4.21.61 2681
ReactomeiR-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-8866427 VLDLR internalisation and degradation
R-HSA-8957275 Post-translational protein phosphorylation
R-HSA-8964038 LDL clearance
SignaLinkiQ8NBP7
SIGNORiQ8NBP7

Miscellaneous databases

EvolutionaryTraceiQ8NBP7

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PCSK9

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
255738

Protein Ontology

More...
PROi
PR:Q8NBP7

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000169174 Expressed in 85 organ(s), highest expression level in right lobe of liver
CleanExiHS_PCSK9
GenevisibleiQ8NBP7 HS

Family and domain databases

CDDicd04077 Peptidases_S8_PCSK9_Proteinase, 1 hit
Gene3Di3.30.70.80, 1 hit
3.40.50.200, 1 hit
InterProiView protein in InterPro
IPR034193 PCSK9_ProteinaseK-like
IPR000209 Peptidase_S8/S53_dom
IPR036852 Peptidase_S8/S53_dom_sf
IPR015500 Peptidase_S8_subtilisin-rel
IPR010259 S8pro/Inhibitor_I9
IPR037045 S8pro/Inhibitor_I9_sf
PfamiView protein in Pfam
PF05922 Inhibitor_I9, 1 hit
PF00082 Peptidase_S8, 1 hit
PRINTSiPR00723 SUBTILISIN
SUPFAMiSSF52743 SSF52743, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPCSK9_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q8NBP7
Secondary accession number(s): A8T640
, C0JYY9, Q5PSM5, Q5SZQ2
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: January 11, 2011
Last modified: November 7, 2018
This is version 176 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again