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1:  NP_000850Reports  3-hydroxy-3-methy...[gi:4557643] BLink, Conserved Domains, Links
LOCUS       NP_000850                888 aa            linear   PRI 13-NOV-2008
DEFINITION  3-hydroxy-3-methylglutaryl-Coenzyme A reductase isoform 1 [Homo
            sapiens].
ACCESSION   NP_000850
VERSION     NP_000850.1  GI:4557643
DBSOURCE    REFSEQ: accession NM_000859.2
KEYWORDS    .
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 888)
  AUTHORS   Burkhardt,R., Kenny,E.E., Lowe,J.K., Birkeland,A., Josowitz,R.,
            Noel,M., Salit,J., Maller,J.B., Pe'er,I., Daly,M.J., Altshuler,D.,
            Stoffel,M., Friedman,J.M. and Breslow,J.L.
  TITLE     Common SNPs in HMGCR in micronesians and whites associated with
            LDL-cholesterol levels affect alternative splicing of exon13
  JOURNAL   Arterioscler. Thromb. Vasc. Biol. 28 (11), 2078-2084 (2008)
   PUBMED   18802019
  REMARK    GeneRIF: Genome-wide association study of gene-disease association.
            (HuGE Navigator)
REFERENCE   2  (residues 1 to 888)
  AUTHORS   Hosgood,H.D. III, Menashe,I., Shen,M., Yeager,M., Yuenger,J.,
            Rajaraman,P., He,X., Chatterjee,N., Caporaso,N.E., Zhu,Y.,
            Chanock,S.J., Zheng,T. and Lan,Q.
  TITLE     Pathway-based evaluation of 380 candidate genes and lung cancer
            susceptibility suggests the importance of the cell cycle pathway
  JOURNAL   Carcinogenesis 29 (10), 1938-1943 (2008)
   PUBMED   18676680
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
REFERENCE   3  (residues 1 to 888)
  AUTHORS   Donnelly,L.A., Doney,A.S., Dannfald,J., Whitley,A.L., Lang,C.C.,
            Morris,A.D., Donnan,P.T. and Palmer,C.N.
  TITLE     A paucimorphic variant in the HMG-CoA reductase gene is associated
            with lipid-lowering response to statin treatment in diabetes: a
            GoDARTS study
  JOURNAL   Pharmacogenet. Genomics (2008) In press
   PUBMED   18815589
  REMARK    GeneRIF: Observational study of gene-disease association,
            gene-environment interaction, and pharmacogenomic / toxicogenomic.
            (HuGE Navigator)
            Publication Status: Available-Online prior to print
REFERENCE   4  (residues 1 to 888)
  AUTHORS   Knouff,C.W., Lim,N., Song,K., Yuan,X., Walker,M.C., Townsend,R.,
            Waeber,G., Matthews,P.M., Vollenweider,P., Waterworth,D.M. and
            Mooser,V.
  TITLE     Pharmacological effects of lipid-lowering drugs recapitulate with a
            larger amplitude the phenotypic effects of common variants within
            their target genes
  JOURNAL   Pharmacogenet. Genomics (2008) In press
   PUBMED   18787507
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Available-Online prior to print
REFERENCE   5  (residues 1 to 888)
  AUTHORS   Lu,Y., Dolle,M.E., Imholz,S., Slot,R.V., Verschuren,W.M.,
            Wijmenga,C., Feskens,E.J. and Boer,J.M.
  TITLE     Multiple genetic variants along candidate pathways influence plasma
            high-density lipoprotein cholesterol concentrations
  JOURNAL   J. Lipid Res. (2008) In press
   PUBMED   18660489
  REMARK    GeneRIF: Observational study of gene-disease association. (HuGE
            Navigator)
            Publication Status: Available-Online prior to print
REFERENCE   6  (residues 1 to 888)
  AUTHORS   Hodge,V.J., Gould,S.J., Subramani,S., Moser,H.W. and Krisans,S.K.
  TITLE     Normal cholesterol synthesis in human cells requires functional
            peroxisomes
  JOURNAL   Biochem. Biophys. Res. Commun. 181 (2), 537-541 (1991)
   PUBMED   1755834
REFERENCE   7  (residues 1 to 888)
  AUTHORS   Ramharack,R., Tam,S.P. and Deeley,R.G.
  TITLE     Characterization of three distinct size classes of human
            3-hydroxy-3-methylglutaryl coenzyme A reductase mRNA: expression of
            the transcripts in hepatic and nonhepatic cells
  JOURNAL   DNA Cell Biol. 9 (9), 677-690 (1990)
   PUBMED   1979742
REFERENCE   8  (residues 1 to 888)
  AUTHORS   Clarke,P.R. and Hardie,D.G.
  TITLE     Regulation of HMG-CoA reductase: identification of the site
            phosphorylated by the AMP-activated protein kinase in vitro and in
            intact rat liver
  JOURNAL   EMBO J. 9 (8), 2439-2446 (1990)
   PUBMED   2369897
REFERENCE   9  (sites)
  AUTHORS   Clarke,P.R. and Hardie,D.G.
  TITLE     Regulation of HMG-CoA reductase: identification of the site
            phosphorylated by the AMP-activated protein kinase in vitro and in
            intact rat liver
  JOURNAL   EMBO J. 9 (8), 2439-2446 (1990)
   PUBMED   2369897
REFERENCE   10 (residues 1 to 888)
  AUTHORS   Luskey,K.L. and Stevens,B.
  TITLE     Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. Conserved
            domains responsible for catalytic activity and sterol-regulated
            degradation
  JOURNAL   J. Biol. Chem. 260 (18), 10271-10277 (1985)
   PUBMED   2991281
REFERENCE   11 (residues 1 to 888)
  AUTHORS   Humphries,S.E., Tata,F., Henry,I., Barichard,F., Holm,M., Junien,C.
            and Williamson,R.
  TITLE     The isolation, characterisation, and chromosomal assignment of the
            gene for human 3-hydroxy-3-methylglutaryl coenzyme A reductase,
            (HMG-CoA reductase)
  JOURNAL   Hum. Genet. 71 (3), 254-258 (1985)
   PUBMED   2998972
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from M62627.1, BC033692.1, M11058.1,
            CN278665.1 and AA648735.1.
            
            Summary: HMG-CoA reductase is the rate-limiting enzyme for
            cholesterol synthesis and is regulated via a negative feedback
            mechanism mediated by sterols and non-sterol metabolites derived
            from mevalonate, the product of the reaction catalyzed by
            reductase. Normally in mammalian cells this enzyme is suppressed by
            cholesterol derived from the internalization and degradation of low
            density lipoprotein (LDL) via the LDL receptor. Competitive
            inhibitors of the reductase induce the expression of LDL receptors
            in the liver, which in turn increases the catabolism of plasma LDL
            and lowers the plasma concentration of cholesterol, an important
            determinant of atherosclerosis. Alternatively spliced transcript
            variants encoding different isoforms have been found for this gene.
            [provided by RefSeq].
            
            Transcript Variant: This variant (1) encodes the longer isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the
            Entrez Gene record to access additional publications.
FEATURES             Location/Qualifiers
     source          1..888
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="5"
                     /map="5q13.3-q14"
     Protein         1..888
                     /product="3-hydroxy-3-methylglutaryl-Coenzyme A reductase
                     isoform 1"
                     /EC_number="1.1.1.34"
                     /note="hydroxymethylglutaryl-CoA reductase;
                     3-hydroxy-3-methylglutaryl CoA reductase (NADPH)"
                     /calculated_mol_wt=97345
     Site            872
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /citation=[8]
                     /db_xref="HPRD:03382"
     CDS             1..888
                     /gene="HMGCR"
                     /coded_by="NM_000859.2:157..2823"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="CCDS:CCDS4027.1"
                     /db_xref="GeneID:3156"
                     /db_xref="HGNC:5006"
                     /db_xref="HPRD:00836"
                     /db_xref="MIM:142910"
ORIGIN      
        1 mlsrlfrmhg lfvashpwev ivgtvtltic mmsmnmftgn nkicgwnyec pkfeedvlss
       61 diiiltitrc iailyiyfqf qnlrqlgsky ilgiaglfti fssfvfstvv ihfldkeltg
      121 lnealpffll lidlsrastl akfalssnsq devreniarg mailgptftl dalveclvig
      181 vgtmsgvrql eimccfgcms vlanyfvfmt ffpacvslvl elsresregr piwqlshfar
      241 vleeeenkpn pvtqrvkmim slglvlvhah srwiadpspq nstadtskvs lgldenvskr
      301 iepsvslwqf ylskmismdi eqvitlslal llavkyiffe qtetestlsl knpitspvvt
      361 qkkvpdnccr repmlvrnnq kcdsveeetg inrerkvevi kplvaetdtp nratfvvgns
      421 slldtssvlv tqepeielpr eprpneeclq ilgnaekgak flsdaeiiql vnakhipayk
      481 letlmether gvsirrqlls kklsepsslq ylpyrdynys lvmgaccenv igympipvgv
      541 agplcldeke fqvpmatteg clvastnrgc raiglgggas srvladgmtr gpvvrlprac
      601 dsaevkawle tsegfavike afdstsrfar lqklhtsiag rnlyirfqsr sgdamgmnmi
      661 skgtekalsk lheyfpemqi lavsgnyctd kkpaainwie grgksvvcea vipakvvrev
      721 lkttteamie vninknlvgs amagsiggyn ahaanivtai yiacgqdaaq nvgssncitl
      781 measgptned lyisctmpsi eigtvgggtn llpqqaclqm lgvqgackdn pgenarqlar
      841 ivcgtvmage lslmaalaag hlvkshmihn rskinlqdlq gactkkta
//

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Last update: Wed, 05 Nov 2008 Rev. 145015