Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 224 (16 Oct 2019)
Sequence version 1 (01 Nov 1986)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

3-hydroxy-3-methylglutaryl-coenzyme A reductase

Gene

HMGCR

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

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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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. Inhibited by statins, a class of hypolipidemic agents used as pharmaceuticals to lower cholesterol levels in individuals at risk from cardiovascular disease due to hypercholesterolemia. Inhibition of HMGCR in the liver stimulates the LDL-receptors, which results in an increased clearance of LDL from the bloodstream and a decrease in blood cholesterol levels. The first results can be seen after one week of statin use and the effect is maximal after four to six weeks.1 Publication

<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, 3-hydroxy-3-methylglutaryl coenzyme A synthase (HMGCS1), Hydroxymethylglutaryl-CoA synthase, cytoplasmic (HMGCS1), 3-hydroxy-3-methylglutaryl coenzyme A synthase, Hydroxymethylglutaryl-CoA synthase, mitochondrial (HMGCS2), 3-hydroxy-3-methylglutaryl coenzyme A synthase, 3-hydroxy-3-methylglutaryl coenzyme A synthase
  3. 3-hydroxy-3-methylglutaryl coenzyme A reductase, 3-hydroxy-3-methylglutaryl coenzyme A reductase (HMGCR), 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR), 3-hydroxy-3-methylglutaryl coenzyme A reductase
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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei559Charge relay system2 Publications1
Active sitei691Charge relay system2 Publications1
Active sitei767Charge relay system2 Publications1
Active sitei866Proton 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

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

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:HS03652-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.34 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-191273 Cholesterol biosynthesis
R-HSA-1989781 PPARA activates gene expression [P04035-1]
R-HSA-2426168 Activation of gene expression by SREBF (SREBP) [P04035-1]

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P04035

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P04035

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

More...
UniPathwayi
UPA00058;UER00103

Protein family/group databases

Transport Classification Database

More...
TCDBi
2.A.6.6.5 the resistance-nodulation-cell division (rnd) superfamily

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001246

<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:HMGCRImported
<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 5

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:5006 HMGCR

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
142910 gene+phenotype

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P04035

<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>Transmembranei11 – 31HelicalSequence analysisAdd BLAST21
Transmembranei58 – 78HelicalSequence analysisAdd BLAST21
Transmembranei91 – 111HelicalSequence analysisAdd BLAST21
Transmembranei125 – 145HelicalSequence analysisAdd BLAST21
Transmembranei161 – 181HelicalSequence analysisAdd BLAST21
Transmembranei192 – 212HelicalSequence analysisAdd BLAST21
Transmembranei320 – 340HelicalSequence analysisAdd BLAST21

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

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>Mutagenesisi75 – 77YIY → AIA: Reduced sterol-mediated release from the ER. Not deglycosylated in response to sterols. 1 Publication3
Mutagenesisi89K → R: Abolishes sterol-mediated ubiquitination and degradation; when associated with R-248. 1 Publication1
Mutagenesisi248K → R: Abolishes sterol-mediated ubiquitination and degradation; when associated with R-89. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
3156
MIMi142910 gene+phenotype

Open Targets

More...
OpenTargetsi
ENSG00000113161

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA189

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P04035

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL402

Drug and drug target database

More...
DrugBanki
DB03169 (S)-Hmg-Coa
DB04447 1,4-Dithiothreitol
DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
DB01076 Atorvastatin
DB09061 Cannabidiol
DB00439 Cerivastatin
DB01992 Coenzyme A
DB01095 Fluvastatin
DB00227 Lovastatin
DB14009 Medical Cannabis
DB04377 Meglutol
DB06693 Mevastatin
DB14011 Nabiximols
DB00157 NADH
DB08860 Pitavastatin
DB00175 Pravastatin
DB01098 Rosuvastatin
DB00641 Simvastatin
DB05317 TAK-475
DB09270 Ubidecarenone

DrugCentral

More...
DrugCentrali
P04035

IUPHAR/BPS Guide to PHARMACOLOGY

More...
GuidetoPHARMACOLOGYi
639

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
HMGCR

Domain mapping of disease mutations (DMDM)

More...
DMDMi
123343

<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_00001144191 – 8883-hydroxy-3-methylglutaryl-coenzyme A reductaseAdd BLAST888

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)1 Publication
Cross-linki248Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
<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...) asparaginePROSITE-ProRule annotation1
Glycosylationi296N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi419N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
<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 residuei504PhosphoserineCombined sources1
Glycosylationi518N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Glycosylationi870N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Modified residuei872PhosphoserineCombined sources1

<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

N-glycosylated. Deglycosylated by NGLY1 on release from the endoplasmic reticulum (ER) in a sterol-mediated manner.1 Publication
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 similarity3 Publications

Keywords - PTMi

Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P04035

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P04035

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
P04035

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P04035

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

More...
PaxDbi
P04035

PeptideAtlas

More...
PeptideAtlasi
P04035

PRoteomics IDEntifications database

More...
PRIDEi
P04035

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
51634 [P04035-1]
51635 [P04035-2]

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
983

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P04035

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

More...
PhosphoSitePlusi
P04035

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P04035

<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
ENSG00000113161 Expressed in 227 organ(s), highest expression level in adrenal tissue

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P04035 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P04035 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB016797
HPA008338

<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 (via its SSD) with INSIG1; 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.

5 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
109399, 72 interactors

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P04035

Protein interaction database and analysis system

More...
IntActi
P04035, 15 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000287936

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P04035

<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

1888
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P04035

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P04035

<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 – 888CatalyticAdd BLAST439

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 motif4

<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

More...
eggNOGi
KOG2480 Eukaryota
COG1257 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155305

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000183489

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P04035

KEGG Orthology (KO)

More...
KOi
K00021

Identification of Orthologs from Complete Genome Data

More...
OMAi
CENVLGY

Database of Orthologous Groups

More...
OrthoDBi
1318335at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P04035

TreeFam database of animal gene trees

More...
TreeFami
TF105362

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00643 HMG-CoA_reductase_classI, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
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

More...
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

More...
PANTHERi
PTHR10572 PTHR10572, 1 hit

Pfam protein domain database

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

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00071 HMGCOARDTASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55035 SSF55035, 1 hit
SSF56542 SSF56542, 1 hit

TIGRFAMs; a protein family database

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

PROSITE; a protein domain and family database

More...
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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)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.

This entry describes 3 <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

This entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P04035-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MLSRLFRMHG LFVASHPWEV IVGTVTLTIC MMSMNMFTGN NKICGWNYEC
60 70 80 90 100
PKFEEDVLSS DIIILTITRC IAILYIYFQF QNLRQLGSKY ILGIAGLFTI
110 120 130 140 150
FSSFVFSTVV IHFLDKELTG LNEALPFFLL LIDLSRASTL 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 NSTADTSKVS LGLDENVSKR
310 320 330 340 350
IEPSVSLWQF YLSKMISMDI EQVITLSLAL LLAVKYIFFE QTETESTLSL
360 370 380 390 400
KNPITSPVVT QKKVPDNCCR REPMLVRNNQ KCDSVEEETG INRERKVEVI
410 420 430 440 450
KPLVAETDTP NRATFVVGNS SLLDTSSVLV TQEPEIELPR EPRPNEECLQ
460 470 480 490 500
ILGNAEKGAK FLSDAEIIQL VNAKHIPAYK LETLMETHER GVSIRRQLLS
510 520 530 540 550
KKLSEPSSLQ YLPYRDYNYS LVMGACCENV IGYMPIPVGV AGPLCLDEKE
560 570 580 590 600
FQVPMATTEG CLVASTNRGC RAIGLGGGAS SRVLADGMTR GPVVRLPRAC
610 620 630 640 650
DSAEVKAWLE TSEGFAVIKE AFDSTSRFAR LQKLHTSIAG RNLYIRFQSR
660 670 680 690 700
SGDAMGMNMI SKGTEKALSK LHEYFPEMQI LAVSGNYCTD KKPAAINWIE
710 720 730 740 750
GRGKSVVCEA VIPAKVVREV LKTTTEAMIE VNINKNLVGS AMAGSIGGYN
760 770 780 790 800
AHAANIVTAI YIACGQDAAQ NVGSSNCITL MEASGPTNED LYISCTMPSI
810 820 830 840 850
EIGTVGGGTN LLPQQACLQM LGVQGACKDN PGENARQLAR IVCGTVMAGE
860 870 880
LSLMAALAAG HLVKSHMIHN RSKINLQDLQ GACTKKTA
Length:888
Mass (Da):97,476
Last modified:November 1, 1986 - v1
<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:i49B610DCCCFA26B6
GO
Isoform 2 (identifier: P04035-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     522-574: Missing.

Note: No experimental confirmation available.
Show »
Length:835
Mass (Da):92,021
Checksum:i20BBFC6C1FB46ADA
GO
Isoform 3 (identifier: P04035-3) [UniParc]FASTAAdd to basket
Also known as: HMGCR-1b

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MQWMSHTRERDAGSKDSVATM

Note: Most highly expressed transcript in skin, esophagus, and uterine cervix.
Show »
Length:908
Mass (Da):99,752
Checksum:iA5CAD1217E9C40B9
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D6RIW0D6RIW0_HUMAN
3-hydroxy-3-methylglutaryl-coenzyme...
HMGCR
111Annotation score:

Annotation score:1 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>
H0Y8F6H0Y8F6_HUMAN
3-hydroxy-3-methylglutaryl-coenzyme...
HMGCR
115Annotation score:

Annotation score:1 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>
H0Y8K6H0Y8K6_HUMAN
3-hydroxy-3-methylglutaryl-coenzyme...
HMGCR
165Annotation score:

Annotation score:1 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>
C9JKX7C9JKX7_HUMAN
3-hydroxy-3-methylglutaryl-coenzyme...
HMGCR
18Annotation score:

Annotation score:1 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>

<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 BAH12375 differs from that shown. Reason: Frameshift.Curated

Natural variant

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_011954638I → V1 PublicationCorresponds to variant dbSNP:rs5908Ensembl.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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0464921M → MQWMSHTRERDAGSKDSVAT M in isoform 3. 1 Publication1
Alternative sequenceiVSP_002207522 – 574Missing in isoform 2. 1 PublicationAdd BLAST53

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
M11058 mRNA Translation: AAA52679.1
AF273765
, AF273754, AF273755, AF273756, AF273757, AF273758, AF273759, AF273760, AF273761, AF273762, AF273763, AF273764 Genomic DNA Translation: AAG21343.1
AY321356 Genomic DNA Translation: AAP72015.1
AK296499 mRNA Translation: BAH12375.1 Frameshift.
AC008897 Genomic DNA No translation available.
BC033692 mRNA Translation: AAH33692.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS4027.1 [P04035-1]
CCDS47234.1 [P04035-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
A00356 RDHUE

NCBI Reference Sequences

More...
RefSeqi
NP_000850.1, NM_000859.2 [P04035-1]
NP_001124468.1, NM_001130996.1 [P04035-2]
XP_011541659.1, XM_011543357.1 [P04035-3]
XP_011541660.1, XM_011543358.1 [P04035-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000287936; ENSP00000287936; ENSG00000113161 [P04035-1]
ENST00000343975; ENSP00000340816; ENSG00000113161 [P04035-2]
ENST00000511206; ENSP00000426745; ENSG00000113161 [P04035-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3156

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:3156

UCSC genome browser

More...
UCSCi
uc003kdp.4 human [P04035-1]

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11058 mRNA Translation: AAA52679.1
AF273765
, AF273754, AF273755, AF273756, AF273757, AF273758, AF273759, AF273760, AF273761, AF273762, AF273763, AF273764 Genomic DNA Translation: AAG21343.1
AY321356 Genomic DNA Translation: AAP72015.1
AK296499 mRNA Translation: BAH12375.1 Frameshift.
AC008897 Genomic DNA No translation available.
BC033692 mRNA Translation: AAH33692.1
CCDSiCCDS4027.1 [P04035-1]
CCDS47234.1 [P04035-2]
PIRiA00356 RDHUE
RefSeqiNP_000850.1, NM_000859.2 [P04035-1]
NP_001124468.1, NM_001130996.1 [P04035-2]
XP_011541659.1, XM_011543357.1 [P04035-3]
XP_011541660.1, XM_011543358.1 [P04035-1]

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
1DQ8X-ray2.10A/B/C/D426-888[»]
1DQ9X-ray2.80A/B/C/D426-888[»]
1DQAX-ray2.00A/B/C/D426-888[»]
1HW8X-ray2.10A/B/C/D426-888[»]
1HW9X-ray2.33A/B/C/D426-888[»]
1HWIX-ray2.30A/B/C/D426-888[»]
1HWJX-ray2.26A/B/C/D426-888[»]
1HWKX-ray2.22A/B/C/D426-888[»]
1HWLX-ray2.10A/B/C/D426-888[»]
2Q1LX-ray2.05A/B/C/D441-875[»]
2Q6BX-ray2.00A/B/C/D441-875[»]
2Q6CX-ray2.00A/B/C/D441-875[»]
2R4FX-ray1.70A/B/C/D441-875[»]
3BGLX-ray2.23A/B/C/D441-875[»]
3CCTX-ray2.12A/B/C/D441-875[»]
3CCWX-ray2.10A/B/C/D441-875[»]
3CCZX-ray1.70A/B/C/D441-875[»]
3CD0X-ray2.40A/B/C/D441-875[»]
3CD5X-ray2.39A/B/C/D441-875[»]
3CD7X-ray2.05A/B/C/D441-875[»]
3CDAX-ray2.07A/B/C/D441-875[»]
3CDBX-ray2.30A/B/C/D441-875[»]
SMRiP04035
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi109399, 72 interactors
ELMiP04035
IntActiP04035, 15 interactors
STRINGi9606.ENSP00000287936

Chemistry databases

BindingDBiP04035
ChEMBLiCHEMBL402
DrugBankiDB03169 (S)-Hmg-Coa
DB04447 1,4-Dithiothreitol
DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
DB01076 Atorvastatin
DB09061 Cannabidiol
DB00439 Cerivastatin
DB01992 Coenzyme A
DB01095 Fluvastatin
DB00227 Lovastatin
DB14009 Medical Cannabis
DB04377 Meglutol
DB06693 Mevastatin
DB14011 Nabiximols
DB00157 NADH
DB08860 Pitavastatin
DB00175 Pravastatin
DB01098 Rosuvastatin
DB00641 Simvastatin
DB05317 TAK-475
DB09270 Ubidecarenone
DrugCentraliP04035
GuidetoPHARMACOLOGYi639
SwissLipidsiSLP:000001246

Protein family/group databases

TCDBi2.A.6.6.5 the resistance-nodulation-cell division (rnd) superfamily

PTM databases

GlyConnecti983
iPTMnetiP04035
PhosphoSitePlusiP04035
SwissPalmiP04035

Polymorphism and mutation databases

BioMutaiHMGCR
DMDMi123343

Proteomic databases

EPDiP04035
jPOSTiP04035
MassIVEiP04035
MaxQBiP04035
PaxDbiP04035
PeptideAtlasiP04035
PRIDEiP04035
ProteomicsDBi51634 [P04035-1]
51635 [P04035-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
3156

Genome annotation databases

EnsembliENST00000287936; ENSP00000287936; ENSG00000113161 [P04035-1]
ENST00000343975; ENSP00000340816; ENSG00000113161 [P04035-2]
ENST00000511206; ENSP00000426745; ENSG00000113161 [P04035-1]
GeneIDi3156
KEGGihsa:3156
UCSCiuc003kdp.4 human [P04035-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3156
DisGeNETi3156

GeneCards: human genes, protein and diseases

More...
GeneCardsi
HMGCR
HGNCiHGNC:5006 HMGCR
HPAiCAB016797
HPA008338
MIMi142910 gene+phenotype
neXtProtiNX_P04035
OpenTargetsiENSG00000113161
PharmGKBiPA189

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2480 Eukaryota
COG1257 LUCA
GeneTreeiENSGT00940000155305
HOGENOMiHOG000183489
InParanoidiP04035
KOiK00021
OMAiCENVLGY
OrthoDBi1318335at2759
PhylomeDBiP04035
TreeFamiTF105362

Enzyme and pathway databases

UniPathwayiUPA00058;UER00103
BioCyciMetaCyc:HS03652-MONOMER
BRENDAi1.1.1.34 2681
ReactomeiR-HSA-191273 Cholesterol biosynthesis
R-HSA-1989781 PPARA activates gene expression [P04035-1]
R-HSA-2426168 Activation of gene expression by SREBF (SREBP) [P04035-1]
SABIO-RKiP04035
SIGNORiP04035

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
HMGCR human
EvolutionaryTraceiP04035

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
HMG-CoA_reductase

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

More...
GenomeRNAii
3156
PharosiP04035

Protein Ontology

More...
PROi
PR:P04035

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000113161 Expressed in 227 organ(s), highest expression level in adrenal tissue
ExpressionAtlasiP04035 baseline and differential
GenevisibleiP04035 HS

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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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_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: P04035
Secondary accession number(s): B7Z3Y9, Q8N190
<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 1, 1986
Last sequence update: November 1, 1986
Last modified: October 16, 2019
This is version 224 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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