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Entry version 169 (13 Feb 2019)
Sequence version 2 (31 Oct 2006)
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Protein

3-hydroxy-3-methylglutaryl-coenzyme A reductase

Gene

Hmgcr

Organism
Rattus norvegicus (Rat)
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

Transmembrane glycoprotein that is the rate-limiting enzyme in cholesterol biosynthesis as well as in the biosynthesis of nonsterol isoprenoids that are essential for normal cell function including ubiquinone and geranylgeranyl proteins.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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

Regulated by a negative feedback mechanism through sterols and non-sterol metabolites derived from mevalonate.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: (R)-mevalonate biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes (R)-mevalonate from acetyl-CoA.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. 3-hydroxy-3-methylglutaryl coenzyme A synthase (Hmgcs2), Hydroxymethylglutaryl-CoA synthase, cytoplasmic (Hmgcs1), Hydroxymethylglutaryl-CoA synthase, mitochondrial (Hmgcs2)
  3. 3-hydroxy-3-methylglutaryl-coenzyme A reductase (Hmgcr)
This subpathway is part of the pathway (R)-mevalonate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-mevalonate from acetyl-CoA, the pathway (R)-mevalonate biosynthesis and in Metabolic intermediate biosynthesis.

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 sitei558Charge relay systemBy similarity1
Active sitei690Charge relay systemBy similarity1
Active sitei766Charge relay systemBy similarity1
Active sitei865Proton donorPROSITE-ProRule annotation1

<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

  • hydroxymethylglutaryl-CoA reductase (NADPH) activity Source: GO_Central
  • hydroxymethylglutaryl-CoA reductase activity Source: RGD
  • NADPH binding Source: Ensembl
  • protein homodimerization activity Source: RGD
  • protein phosphatase 2A binding Source: RGD

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 functionOxidoreductase
Biological processCholesterol biosynthesis, Cholesterol metabolism, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
LigandNADP

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.34 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-191273 Cholesterol biosynthesis

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00058;UER00103

<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:
3-hydroxy-3-methylglutaryl-coenzyme A reductase (EC:1.1.1.34)
Short name:
HMG-CoA reductase
<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:Hmgcr
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 2

Organism-specific databases

Rat genome database

More...
RGDi
2803 Hmgcr

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei10 – 39HelicalSequence analysisAdd BLAST30
Transmembranei57 – 78HelicalSequence analysisAdd BLAST22
Transmembranei90 – 114HelicalSequence analysisAdd BLAST25
Transmembranei124 – 149HelicalSequence analysisAdd BLAST26
Transmembranei160 – 187HelicalSequence analysisAdd BLAST28
Transmembranei192 – 220HelicalSequence analysisAdd BLAST29
Transmembranei315 – 339HelicalSequence analysisAdd BLAST25

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3247

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
639

<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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001144241 – 8873-hydroxy-3-methylglutaryl-coenzyme A reductaseAdd BLAST887

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki248Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
<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>Glycosylationi281N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi517N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi869N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei871Phosphoserine; by AMPK1 Publication1

<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

Undergoes sterol-mediated ubiquitination and ER-associated degradation (ERAD). Accumulation of sterols in the endoplasmic reticulum (ER) membrane, triggers binding of the reductase to the ER membrane protein INSIG1. This INSIG1 binding leads to the recruitment of the ubiquitin ligase, AMFR/gp78 or RNF145, initiating ubiquitination of the reductase. The ubiquitinated reductase is then extracted from the ER membrane and delivered to cytosolic 26S proteosomes by a mechanism probably mediated by the ATPase Valosin-containing protein VCP/p97. Lys-248 is the main site of ubiquitination. Ubiquitination is enhanced by the presence of a geranylgeranylated protein.By similarity
N-glycosylated. Deglycosylated by NGLY1 on release from the endoplasmic reticulum (ER) in a sterol-mediated manner.By similarity

Keywords - PTMi

Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P51639

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

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PaxDbi
P51639

PRoteomics IDEntifications database

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PRIDEi
P51639

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P51639

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

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PhosphoSitePlusi
P51639

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000016122 Expressed in 10 organ(s), highest expression level in liver

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P51639 RN

<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

Homodimer. Interacts with INSIG1 (via its SSD); the interaction, accelerated by sterols, leads to the recruitment of HMGCR to AMFR/gp78 for its ubiquitination by the sterol-mediated ERAD pathway. Interacts with UBIAD1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
247704, 1 interactor

Molecular INTeraction database

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MINTi
P51639

STRING: functional protein association networks

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STRINGi
10116.ENSRNOP00000022055

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P51639

<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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P51639

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

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SMRi
P51639

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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>Domaini61 – 218SSDPROSITE-ProRule annotationAdd BLAST158

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>Regioni340 – 449LinkerAdd BLAST110
Regioni450 – 887CatalyticAdd BLAST438

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi75 – 78INSIG-binding motifBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi243 – 246Poly-Glu4

<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 HMG-CoA reductase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2480 Eukaryota
COG1257 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000155305

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000183489

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000453

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P51639

KEGG Orthology (KO)

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KOi
K00021

Identification of Orthologs from Complete Genome Data

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OMAi
CASHPWE

Database of Orthologous Groups

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OrthoDBi
498994at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P51639

TreeFam database of animal gene trees

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TreeFami
TF105362

Family and domain databases

Conserved Domains Database

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CDDi
cd00643 HMG-CoA_reductase_classI, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.3270.10, 1 hit
3.30.70.420, 1 hit
3.90.770.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002202 HMG_CoA_Rdtase
IPR023074 HMG_CoA_Rdtase_cat_sf
IPR023076 HMG_CoA_Rdtase_CS
IPR004554 HMG_CoA_Rdtase_eu_arc
IPR004816 HMG_CoA_Rdtase_metazoan
IPR023282 HMG_CoA_Rdtase_N
IPR009023 HMG_CoA_Rdtase_NAD(P)-bd_sf
IPR009029 HMG_CoA_Rdtase_sub-bd_dom_sf
IPR000731 SSD

The PANTHER Classification System

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PANTHERi
PTHR10572 PTHR10572, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00368 HMG-CoA_red, 1 hit
PF12349 Sterol-sensing, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00071 HMGCOARDTASE

Superfamily database of structural and functional annotation

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SUPFAMi
SSF55035 SSF55035, 1 hit
SSF56542 SSF56542, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00920 2A060605, 1 hit
TIGR00533 HMG_CoA_R_NADP, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00066 HMG_COA_REDUCTASE_1, 1 hit
PS00318 HMG_COA_REDUCTASE_2, 1 hit
PS01192 HMG_COA_REDUCTASE_3, 1 hit
PS50065 HMG_COA_REDUCTASE_4, 1 hit
PS50156 SSD, 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>Sequencei

<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.

P51639-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLSRLFRMHG LFVASHPWEV IVGTVTLTIC MMSMNMFTGN NKICGWNYEC
60 70 80 90 100
PKFEEDVLSS DIIILTITRC IAILYIYFQF QNLRQLGSKY ILGIAGLFTI
110 120 130 140 150
FSSFVFSTVV IHFLDKELTG LNEALPFFLL LIDLSRASAL AKFALSSNSQ
160 170 180 190 200
DEVRENIARG MAILGPTFTL DALVECLVIG VGTMSGVRQL EIMCCFGCMS
210 220 230 240 250
VLANYFVFMT FFPACVSLVL ELSRESREGR PIWQLSHFAR VLEEEENKPN
260 270 280 290 300
PVTQRVKMIM SLGLVLVHAH SRWIADPSPQ NSTAEQSKVS LGLAEDVSKR
310 320 330 340 350
IEPSVSLWQF YLSKMISMDI EQVITLSLAL LLAVKYIFFE QAETESTLSL
360 370 380 390 400
KNPITSPVVT PKKAQDNCCR REPLLVRRNQ KLSSVEEDPG VNQDRKVEVI
410 420 430 440 450
KPLVAEAETS GRATFVLGAS AASPPLALGA QEPGIELPSE PRPNEECLQI
460 470 480 490 500
LESAEKGAKF LSDAEIIQLV NAKHIPAYKL ETLMETHERG VSIRRQLLSA
510 520 530 540 550
KLAEPSSLQY LPYRDYNYSL VMGACCENVI GYMPIPVGVA GPLCLDGKEY
560 570 580 590 600
QVPMATTEGC LVASTNRGCR AISLGGGASS RVLADGMSRG PVVRLPRACD
610 620 630 640 650
SAEVKSWLET PEGFAVVKEA FDSTSRFARL QKLHVTLAGR NLYIRLQSKT
660 670 680 690 700
GDAMGMNMIS KGTEKALLKL QEFFPELQIL AVSGNYCTDK KPAAINWIEG
710 720 730 740 750
RGKTVVCEAV IPAKVVREVL KTTTEAMVDV NINKNLVGSA MAGSIGGYNA
760 770 780 790 800
HAANIVTAIY IACGQDAAQN VGSSNCITLM EASGPTNEDL YISCTMPSIE
810 820 830 840 850
IGTVGGGTNL LPQQACLQML GVQGACKDNP GENARQLARI VCGTVMAGEL
860 870 880
SLMAALAAGH LVRSHMVHNR SKINLQDLQG TCTKKAA
Length:887
Mass (Da):96,688
Last modified:October 31, 2006 - v2
<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:i856D99A9D5FA965C
GO

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 conflicti423S → T AA sequence (PubMed:2369897).Curated1
Sequence conflicti428L → V AA sequence (PubMed:2369897).Curated1
Sequence conflicti443P → N AA sequence (PubMed:2369897).Curated1
Sequence conflicti644 – 653IRLQSKTGDA → PIRSPKRGTS in CAA39001 (Ref. 3) Curated10
Sequence conflicti673 – 674FF → GV in AAA40608 (Ref. 1) Curated2
Sequence conflicti722T → S in CAA39001 (Ref. 3) Curated1
Sequence conflicti750A → L in AAA40608 (Ref. 1) Curated1
Sequence conflicti764G → A in CAA39001 (Ref. 3) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M29249 Genomic DNA Translation: AAA40608.1
BC064654 mRNA Translation: AAH64654.1
X55286 mRNA Translation: CAA39001.1

Protein sequence database of the Protein Information Resource

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PIRi
S33175

NCBI Reference Sequences

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RefSeqi
NP_037266.2, NM_013134.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Rn.9437

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000022055; ENSRNOP00000022055; ENSRNOG00000016122

Database of genes from NCBI RefSeq genomes

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GeneIDi
25675

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:25675

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29249 Genomic DNA Translation: AAA40608.1
BC064654 mRNA Translation: AAH64654.1
X55286 mRNA Translation: CAA39001.1
PIRiS33175
RefSeqiNP_037266.2, NM_013134.2
UniGeneiRn.9437

3D structure databases

ProteinModelPortaliP51639
SMRiP51639
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247704, 1 interactor
MINTiP51639
STRINGi10116.ENSRNOP00000022055

Chemistry databases

BindingDBiP51639
ChEMBLiCHEMBL3247
GuidetoPHARMACOLOGYi639

PTM databases

iPTMnetiP51639
PhosphoSitePlusiP51639

Proteomic databases

jPOSTiP51639
PaxDbiP51639
PRIDEiP51639

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022055; ENSRNOP00000022055; ENSRNOG00000016122
GeneIDi25675
KEGGirno:25675

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3156
RGDi2803 Hmgcr

Phylogenomic databases

eggNOGiKOG2480 Eukaryota
COG1257 LUCA
GeneTreeiENSGT00940000155305
HOGENOMiHOG000183489
HOVERGENiHBG000453
InParanoidiP51639
KOiK00021
OMAiCASHPWE
OrthoDBi498994at2759
PhylomeDBiP51639
TreeFamiTF105362

Enzyme and pathway databases

UniPathwayi
UPA00058;UER00103

BRENDAi1.1.1.34 5301
ReactomeiR-RNO-191273 Cholesterol biosynthesis

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P51639

Gene expression databases

BgeeiENSRNOG00000016122 Expressed in 10 organ(s), highest expression level in liver
GenevisibleiP51639 RN

Family and domain databases

CDDicd00643 HMG-CoA_reductase_classI, 1 hit
Gene3Di1.10.3270.10, 1 hit
3.30.70.420, 1 hit
3.90.770.10, 1 hit
InterProiView protein in InterPro
IPR002202 HMG_CoA_Rdtase
IPR023074 HMG_CoA_Rdtase_cat_sf
IPR023076 HMG_CoA_Rdtase_CS
IPR004554 HMG_CoA_Rdtase_eu_arc
IPR004816 HMG_CoA_Rdtase_metazoan
IPR023282 HMG_CoA_Rdtase_N
IPR009023 HMG_CoA_Rdtase_NAD(P)-bd_sf
IPR009029 HMG_CoA_Rdtase_sub-bd_dom_sf
IPR000731 SSD
PANTHERiPTHR10572 PTHR10572, 1 hit
PfamiView protein in Pfam
PF00368 HMG-CoA_red, 1 hit
PF12349 Sterol-sensing, 1 hit
PRINTSiPR00071 HMGCOARDTASE
SUPFAMiSSF55035 SSF55035, 1 hit
SSF56542 SSF56542, 1 hit
TIGRFAMsiTIGR00920 2A060605, 1 hit
TIGR00533 HMG_CoA_R_NADP, 1 hit
PROSITEiView protein in PROSITE
PS00066 HMG_COA_REDUCTASE_1, 1 hit
PS00318 HMG_COA_REDUCTASE_2, 1 hit
PS01192 HMG_COA_REDUCTASE_3, 1 hit
PS50065 HMG_COA_REDUCTASE_4, 1 hit
PS50156 SSD, 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 nameiHMDH_RAT
<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: P51639
Secondary accession number(s): Q64601, Q6P2A6
<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: October 1, 1996
Last sequence update: October 31, 2006
Last modified: February 13, 2019
This is version 169 of the entry and version 2 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

<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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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