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Q80W65

- PCSK9_MOUSE

UniProt

Q80W65 - PCSK9_MOUSE

Protein

Proprotein convertase subtilisin/kexin type 9

Gene

Pcsk9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (07 Nov 2003)
      Previous versions | rss
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    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. 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. 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. 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.2 Publications

    Cofactori

    Calcium.Curated

    Enzyme 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)LengthDescriptionGraphical viewFeature identifierActions
    Sitei155 – 1562Cleavage; by autolysisBy similarity
    Active sitei189 – 1891Charge relay systemBy similarity
    Sitei221 – 2222Cleavage; by furin and PCSK5By similarity
    Active sitei229 – 2291Charge relay systemBy similarity
    Active sitei389 – 3891Charge relay systemBy similarity

    GO - Molecular functioni

    1. apolipoprotein binding Source: UniProtKB
    2. low-density lipoprotein particle binding Source: UniProtKB
    3. low-density lipoprotein particle receptor binding Source: HGNC
    4. protein self-association Source: UniProtKB
    5. serine-type endopeptidase activity Source: HGNC
    6. sodium channel inhibitor activity Source: Ensembl
    7. very-low-density lipoprotein particle binding Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cellular response to insulin stimulus Source: HGNC
    3. cellular response to starvation Source: HGNC
    4. cholesterol homeostasis Source: HGNC
    5. cholesterol metabolic process Source: MGI
    6. kidney development Source: HGNC
    7. lipoprotein metabolic process Source: MGI
    8. liver development Source: HGNC
    9. low-density lipoprotein particle receptor catabolic process Source: UniProtKB
    10. low-density lipoprotein receptor particle metabolic process Source: MGI
    11. lysosomal transport Source: Ensembl
    12. negative regulation of low-density lipoprotein particle clearance Source: Ensembl
    13. negative regulation of receptor recycling Source: Ensembl
    14. neurogenesis Source: HGNC
    15. neuron differentiation Source: HGNC
    16. phospholipid metabolic process Source: MGI
    17. positive regulation of neuron apoptotic process Source: HGNC
    18. positive regulation of receptor internalization Source: Ensembl
    19. protein autoprocessing Source: HGNC
    20. proteolysis Source: RefGenome
    21. regulation of low-density lipoprotein particle receptor catabolic process Source: MGI
    22. regulation of neuron apoptotic process Source: UniProtKB
    23. regulation of receptor activity Source: Ensembl
    24. triglyceride metabolic process Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Apoptosis, Cholesterol metabolism, Lipid metabolism, Steroid metabolism, Sterol metabolism

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_206713. NGF processing.

    Protein family/group databases

    MEROPSiS08.039.

    Names & Taxonomyi

    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
    Gene namesi
    Name:Pcsk9
    Synonyms:Narc1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:2140260. Pcsk9.

    Subcellular locationi

    Cytoplasm By similarity. Secreted. Endosome By similarity. Lysosome By similarity. Cell surface By similarity. Endoplasmic reticulum By similarity. Golgi apparatus By similarity
    Note: Autocatalytic cleavage is required to transport it from the endoplasmic reticulum to the Golgi apparatus and for the secretion of the mature protein. Localizes to the endoplasmic reticulum in the absence of LDLR and co-localizes to the cell surface and to the endosomes/lysosomes in the presence of LDLR. The sorting to the cell surface and endosomes is required in order to fully promote LDLR degradation By similarity.By similarity

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. early endosome Source: UniProtKB
    4. endoplasmic reticulum Source: UniProtKB
    5. endoplasmic reticulum lumen Source: Reactome
    6. ER to Golgi transport vesicle Source: MGI
    7. extracellular region Source: MGI
    8. extracellular space Source: HGNC
    9. Golgi apparatus Source: UniProtKB
    10. late endosome Source: UniProtKB
    11. lysosome Source: UniProtKB
    12. perinuclear region of cytoplasm Source: Ensembl
    13. rough endoplasmic reticulum Source: Ensembl

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3434Sequence AnalysisAdd
    BLAST
    Propeptidei35 – 155121PRO_0000027122Add
    BLAST
    Chaini156 – 694539Proprotein convertase subtilisin/kexin type 9PRO_0000027123Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei41 – 411SulfotyrosineBy similarity
    Modified residuei50 – 501Phosphoserine1 Publication
    Disulfide bondi226 ↔ 258Sequence Analysis
    Disulfide bondi326 ↔ 361Sequence Analysis
    Disulfide bondi460 ↔ 530Sequence Analysis
    Disulfide bondi480 ↔ 529Sequence Analysis
    Disulfide bondi489 ↔ 512Sequence Analysis
    Glycosylationi536 – 5361N-linked (GlcNAc...)By similarity
    Disulfide bondi537 ↔ 604Sequence Analysis
    Disulfide bondi555 ↔ 603Sequence Analysis
    Disulfide bondi565 ↔ 591Sequence Analysis
    Disulfide bondi611 ↔ 682Sequence Analysis
    Disulfide bondi629 ↔ 681Sequence Analysis
    Disulfide bondi638 ↔ 657Sequence Analysis
    Modified residuei691 – 6911PhosphoserineBy similarity

    Post-translational modificationi

    Cleavage by furin and PCSK5 generates a truncated inactive protein that is unable to induce LDLR degradation.By similarity
    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 By similarity.By similarity
    Phosphorylation protects the propeptide against proteolysis.By similarity

    Keywords - PTMi

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

    Proteomic databases

    PaxDbiQ80W65.
    PRIDEiQ80W65.

    PTM databases

    PhosphoSiteiQ80W65.

    Expressioni

    Tissue specificityi

    Hepatocytes, kidney mesenchymal cells, intestinal ileum, colon epithelia and embryonic brain telencephalon neurons.

    Developmental stagei

    In the embryo, expressed in the liver at day E9, in the skin and transiently in the telencephalon at day E12, and in the kidney, small intestine and cerebellum at E15.

    Inductioni

    Down-regulated following a high-cholesterol diet.1 Publication

    Gene expression databases

    BgeeiQ80W65.
    CleanExiMM_PCSK9.
    GenevestigatoriQ80W65.

    Interactioni

    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 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000055757.

    Structurei

    3D structure databases

    ProteinModelPortaliQ80W65.
    SMRiQ80W65. Positions 64-685.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini185 – 423239Peptidase S8Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni453 – 694242C-terminal domainBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi499 – 5013Cell attachment siteSequence Analysis

    Domaini

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

    Sequence similaritiesi

    Belongs to the peptidase S8 family.Curated
    Contains 1 peptidase S8 domain.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG1404.
    GeneTreeiENSGT00490000043472.
    HOGENOMiHOG000049267.
    HOVERGENiHBG053530.
    InParanoidiB1AZI4.
    KOiK13050.
    OMAiHVLTGCS.
    OrthoDBiEOG79PJNT.
    PhylomeDBiQ80W65.
    TreeFamiTF106271.

    Family and domain databases

    Gene3Di3.40.50.200. 1 hit.
    InterProiIPR010259. Inhibitor_I9.
    IPR000209. Peptidase_S8/S53_dom.
    IPR015500. Peptidase_S8_subtilisin-rel.
    IPR009020. Prot_inh_propept.
    [Graphical view]
    PANTHERiPTHR10795. PTHR10795. 1 hit.
    PfamiPF05922. Inhibitor_I9. 1 hit.
    PF00082. Peptidase_S8. 1 hit.
    [Graphical view]
    PRINTSiPR00723. SUBTILISIN.
    SUPFAMiSSF52743. SSF52743. 1 hit.
    SSF54897. SSF54897. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q80W65-1 [UniParc]FASTAAdd to Basket

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    MGTHCSAWLR WPLLPLLPPL LLLLLLLCPT GAGAQDEDGD YEELMLALPS    50
    QEDGLADEAA HVATATFRRC SKEAWRLPGT YIVVLMEETQ RLQIEQTAHR 100
    LQTRAARRGY VIKVLHIFYD LFPGFLVKMS SDLLGLALKL PHVEYIEEDS 150
    FVFAQSIPWN LERIIPAWHQ TEEDRSPDGS SQVEVYLLDT SIQGAHREIE 200
    GRVTITDFNS VPEEDGTRFH RQASKCDSHG THLAGVVSGR DAGVAKGTSL 250
    HSLRVLNCQG KGTVSGTLIG LEFIRKSQLI QPSGPLVVLL PLAGGYSRIL 300
    NAACRHLART GVVLVAAAGN FRDDACLYSP ASAPEVITVG ATNAQDQPVT 350
    LGTLGTNFGR CVDLFAPGKD IIGASSDCST CFMSQSGTSQ AAAHVAGIVA 400
    RMLSREPTLT LAELRQRLIH FSTKDVINMA WFPEDQQVLT PNLVATLPPS 450
    THETGGQLLC RTVWSAHSGP TRTATATARC APEEELLSCS SFSRSGRRRG 500
    DWIEAIGGQQ VCKALNAFGG EGVYAVARCC LVPRANCSIH NTPAARAGLE 550
    THVHCHQKDH VLTGCSFHWE VEDLSVRRQP ALRSRRQPGQ CVGHQAASVY 600
    ASCCHAPGLE CKIKEHGISG PSEQVTVACE AGWTLTGCNV LPGASLTLGA 650
    YSVDNLCVAR VHDTARADRT SGEATVAAAI CCRSRPSAKA SWVQ 694
    Length:694
    Mass (Da):74,823
    Last modified:November 7, 2003 - v2
    Checksum:i977BD4BD1FAF98C0
    GO

    Sequence cautioni

    The sequence AAP31672.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE28934.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAC60362.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti17 – 193Missing in CAC60362. 1 PublicationCurated
    Sequence conflicti34 – 341A → T in CAC60362. 1 PublicationCurated
    Sequence conflicti189 – 1891D → G in CAC60362. 1 PublicationCurated
    Sequence conflicti196 – 1961H → Y in CAC60362. 1 PublicationCurated
    Sequence conflicti200 – 2001E → A in CAC60362. 1 PublicationCurated
    Sequence conflicti305 – 3051R → Q in CAC60362. 1 PublicationCurated
    Sequence conflicti534 – 5341R → H in CAC60362. 1 PublicationCurated
    Sequence conflicti626 – 6261T → A in CAC60362. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AX207688 Unassigned DNA. Translation: CAC60362.1. Different initiation.
    AY273821 mRNA. Translation: AAP31672.1. Different initiation.
    AK149520 mRNA. Translation: BAE28934.1. Different initiation.
    AL954352 Genomic DNA. Translation: CAM15751.1.
    BC038085 mRNA. Translation: AAH38085.1.
    CCDSiCCDS18418.1.
    RefSeqiNP_705793.1. NM_153565.2.
    UniGeneiMm.133268.

    Genome annotation databases

    EnsembliENSMUST00000049507; ENSMUSP00000055757; ENSMUSG00000044254.
    GeneIDi100102.
    KEGGimmu:100102.
    UCSCiuc008tyi.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AX207688 Unassigned DNA. Translation: CAC60362.1 . Different initiation.
    AY273821 mRNA. Translation: AAP31672.1 . Different initiation.
    AK149520 mRNA. Translation: BAE28934.1 . Different initiation.
    AL954352 Genomic DNA. Translation: CAM15751.1 .
    BC038085 mRNA. Translation: AAH38085.1 .
    CCDSi CCDS18418.1.
    RefSeqi NP_705793.1. NM_153565.2.
    UniGenei Mm.133268.

    3D structure databases

    ProteinModelPortali Q80W65.
    SMRi Q80W65. Positions 64-685.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000055757.

    Protein family/group databases

    MEROPSi S08.039.

    PTM databases

    PhosphoSitei Q80W65.

    Proteomic databases

    PaxDbi Q80W65.
    PRIDEi Q80W65.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000049507 ; ENSMUSP00000055757 ; ENSMUSG00000044254 .
    GeneIDi 100102.
    KEGGi mmu:100102.
    UCSCi uc008tyi.2. mouse.

    Organism-specific databases

    CTDi 255738.
    MGIi MGI:2140260. Pcsk9.

    Phylogenomic databases

    eggNOGi COG1404.
    GeneTreei ENSGT00490000043472.
    HOGENOMi HOG000049267.
    HOVERGENi HBG053530.
    InParanoidi B1AZI4.
    KOi K13050.
    OMAi HVLTGCS.
    OrthoDBi EOG79PJNT.
    PhylomeDBi Q80W65.
    TreeFami TF106271.

    Enzyme and pathway databases

    Reactomei REACT_206713. NGF processing.

    Miscellaneous databases

    NextBioi 354261.
    PROi Q80W65.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q80W65.
    CleanExi MM_PCSK9.
    Genevestigatori Q80W65.

    Family and domain databases

    Gene3Di 3.40.50.200. 1 hit.
    InterProi IPR010259. Inhibitor_I9.
    IPR000209. Peptidase_S8/S53_dom.
    IPR015500. Peptidase_S8_subtilisin-rel.
    IPR009020. Prot_inh_propept.
    [Graphical view ]
    PANTHERi PTHR10795. PTHR10795. 1 hit.
    Pfami PF05922. Inhibitor_I9. 1 hit.
    PF00082. Peptidase_S8. 1 hit.
    [Graphical view ]
    PRINTSi PR00723. SUBTILISIN.
    SUPFAMi SSF52743. SSF52743. 1 hit.
    SSF54897. SSF54897. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Narc-1, novel subtilase-like homologs."
      Chiang L.W.
      Patent number WO0157081, 09-AUG-2001
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "Novel putative SREBP and LXR target genes identified by microarray analysis in liver of cholesterol-fed mice."
      Maxwell K.N., Soccio R.E., Duncan E.M., Sehayek E., Breslow J.L.
      J. Lipid Res. 44:2109-2119(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
      Strain: C57BL/6.
      Tissue: Liver.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Liver.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "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].
      Strain: C57BL/6.
      Tissue: Eye.
    6. "The secretory proprotein convertase neural apoptosis-regulated convertase 1 (NARC-1): liver regeneration and neuronal differentiation."
      Seidah N.G., Benjannet S., Wickham L., Marcinkiewicz J., Jasmin S.B., Stifani S., Basak A., Prat A., Chretien M.
      Proc. Natl. Acad. Sci. U.S.A. 100:928-933(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF PROPEPTIDE CLEAVAGE SITE, CHARACTERIZATION.
    7. Cited for: AUTOCATALYTIC CLEAVAGE SITE.
    8. "PCSK9 is phosphorylated by a Golgi casein kinase-like kinase ex vivo and circulates as a phosphoprotein in humans."
      Dewpura T., Raymond A., Hamelin J., Seidah N.G., Mbikay M., Chretien M., Mayne J.
      FEBS J. 275:3480-3493(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-50, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Proprotein convertase subtilisin/kexin type 9 interacts with apolipoprotein B and prevents its intracellular degradation, irrespective of the low-density lipoprotein receptor."
      Sun H., Samarghandi A., Zhang N., Yao Z., Xiong M., Teng B.B.
      Arterioscler. Thromb. Vasc. Biol. 32:1585-1595(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "PCSK9 regulates neuronal apoptosis by adjusting ApoER2 levels and signaling."
      Kysenius K., Muggalla P., Maetlik K., Arumaee U., Huttunen H.J.
      Cell. Mol. Life Sci. 69:1903-1916(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiPCSK9_MOUSE
    AccessioniPrimary (citable) accession number: Q80W65
    Secondary accession number(s): B1AZI4
    , Q3UEH7, Q8BXW9, Q8CFT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 7, 2003
    Last sequence update: November 7, 2003
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3