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Entry version 136 (26 Feb 2020)
Sequence version 1 (01 Oct 1996)
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Protein

Squalene monooxygenase

Gene

Sqle

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

Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FAD1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Inhibited by NB-598 ((E)N-ethyl-N-(6,6-dimethyl-2-hepten-4-ynyl)-3-[(3,3'-bi-thiophen-5-yl)methoxy]benzene-methanamine). Contrary to fungal enzymes, the mammalian enzyme is only slightly inhibited by terbinafine.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=9.87 µM for squalene1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: lanosterol biosynthesis

    This protein is involved in step 2 of the subpathway that synthesizes lanosterol from farnesyl diphosphate.1 Publication
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. Squalene synthase (Fdft1)
    2. Squalene monooxygenase (Sqle)
    3. Lanosterol synthase (Lss)
    This subpathway is part of the pathway lanosterol biosynthesis, which is itself part of Terpene metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes lanosterol from farnesyl diphosphate, the pathway lanosterol biosynthesis and in Terpene metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei160FADBy similarity1
    <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei194Important for enzyme activityBy similarity1
    Binding sitei233FADBy similarity1
    Binding sitei249FAD; via amide nitrogen and carbonyl oxygenBy similarity1
    Binding sitei407FADBy similarity1
    Binding sitei420FAD; via amide nitrogenBy similarity1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi132 – 133FADBy similarity2
    Nucleotide bindingi152 – 153FADBy similarity2

    <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

    • FAD binding Source: UniProtKB
    • squalene monooxygenase activity 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
    LigandFAD, Flavoprotein

    Enzyme and pathway databases

    Reactome - a knowledgebase of biological pathways and processes

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

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P52020

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

    More...
    UniPathwayi
    UPA00767;UER00752

    <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%5Fand%5Ftaxonomy%5Fsection">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:
    Squalene monooxygenase (EC:1.14.14.172 Publications)
    Alternative name(s):
    Squalene epoxidase1 Publication
    Short name:
    SE1 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Sqle
    Synonyms:Erg1
    <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 7

    Organism-specific databases

    Rat genome database

    More...
    RGDi
    3755 Sqle

    <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%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 19CytoplasmicBy similarityAdd BLAST19
    <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei20 – 40By similarityAdd BLAST21
    Topological domaini41 – 573CytoplasmicBy similarityAdd BLAST533

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    <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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi194Y → A: Strongly decreased catalytic activity. 1 Publication1
    Mutagenesisi209Y → A: Nearly abolishes catalytic activity. 1 Publication1
    Mutagenesisi223F → A: Increased enzyme activity. 1 Publication1
    Mutagenesisi228F → A: Strongly decreased affinity for squalene. 1 Publication1
    Mutagenesisi287F → A: Decreased enzyme activity. 1 Publication1
    Mutagenesisi305F → A: Decreased enzyme activity. 1 Publication1
    Mutagenesisi334Y → A: Decreased enzyme activity. 1 Publication1
    Mutagenesisi473Y → A: Nearly abolishes enzyme activity. 1 Publication1
    Mutagenesisi476F → A: Decreased enzyme activity. 1 Publication1
    Mutagenesisi491F → A: Decreased enzyme activity. 1 Publication1
    Mutagenesisi522F → A: Decreased enzyme activity. 1 Publication1
    Mutagenesisi523F → A: Decreased enzyme activity. 1 Publication1
    Mutagenesisi528Y → A: Decreased enzyme activity. 1 Publication1

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL4241

    DrugCentral

    More...
    DrugCentrali
    P52020

    <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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002098401 – 573Squalene monooxygenaseAdd BLAST573

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

    Ubiquitinated by MARCHF6 in response to high cholesterol levels in intracellular membranes, leading to proteasomal degradation.By similarity

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P52020

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

    More...
    PaxDbi
    P52020

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P52020

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

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

    Detected in lever (at protein level).1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSRNOG00000009550 Expressed in liver and 9 other tissues

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P52020 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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Interacts (via N-terminal domain) with MARCHF6.

    Interacts with SMIM22; this interaction modulates lipid droplet formation.

    By similarity

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    10116.ENSRNOP00000012883

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P52020

    <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

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

    More...
    SMRi
    P52020

    Database of comparative protein structure models

    More...
    ModBasei
    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

    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>Regioni1 – 99Interaction with MARCHF6By similarityAdd BLAST99
    Regioni61 – 72Required for degradation in response to high membrane cholesterol levelsBy similarityAdd BLAST12
    Regioni100 – 573Sufficient for catalytic activity2 PublicationsAdd BLAST474
    Regioni515 – 573Hydrophobic; mediates interaction with membranesBy similarityAdd BLAST59

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

    The C-terminal hydrophobic region contains two helices that mediate interaction with membranes. Contrary to predictions, this region does not contain transmembrane helices.By similarity
    The N-terminal region mediates interaction with MARCHF6, leading to SQLE ubiquitination and proteasomal degradation when cholosterol levels are high. The first part of the N-terminal region contains a hydrophobic region that inserts into the membrane; contrary to predictions, there are no transmembrane helices. The second part contains a region that can form an amphipathic region that associates with membranes. This region is ejected from the membrane by high cholesterol levels and becomes disordered in an aqueous environment. This is critical for cholesterol-dependent proteasomal degradation. Additional parts of the N-terminal region are predicted to be disordered and contribute to flagging the protein for proteasomal degradation already under basal conditions.By similarity

    <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 squalene monooxygenase family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG1298 Eukaryota
    COG0654 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000011759

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_026390_0_0_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P52020

    KEGG Orthology (KO)

    More...
    KOi
    K00511

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    LILWKAC

    Database of Orthologous Groups

    More...
    OrthoDBi
    583514at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P52020

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF331056

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.50.50.60, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR036188 FAD/NAD-bd_sf
    IPR013698 Squalene_epoxidase
    IPR040125 Squalene_monox

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR10835 PTHR10835, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF08491 SE, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51905 SSF51905, 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%5Flength">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>Sequencei

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

    P52020-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MWTFLGIATF TYFYKKCGDV TLANKELLLC VLVFLSLGLV LSYRCRHRNG
    60 70 80 90 100
    GLLGRHQSGS QFAAFSDILS ALPLIGFFWA KSPPESEKKE QLESKRRRKE
    110 120 130 140 150
    VNLSETTLTG AATSVSTSSV TDPEVIIIGS GVLGSALATV LSRDGRTVTV
    160 170 180 190 200
    IERDLKEPDR ILGECLQPGG YRVLRELGLG DTVESLNAHH IHGYVIHDCE
    210 220 230 240 250
    SRSEVQIPYP VSENNQVQSG VAFHHGKFIM SLRKAAMAEP NVKFIEGVVL
    260 270 280 290 300
    RLLEEDDAVI GVQYKDKETG DTKELHAPLT VVADGLFSKF RKNLISNKVS
    310 320 330 340 350
    VSSHFVGFIM KDAPQFKANF AELVLVDPSP VLIYQISPSE TRVLVDIRGE
    360 370 380 390 400
    LPRNLREYMT EQIYPQIPDH LKESFLEACQ NARLRTMPAS FLPPSSVNKR
    410 420 430 440 450
    GVLLLGDAYN LRHPLTGGGM TVALKDIKIW RQLLKDIPDL YDDAAIFQAK
    460 470 480 490 500
    KSFFWSRKRS HSFVVNVLAQ ALYELFSATD DSLRQLRKAC FLYFKLGGEC
    510 520 530 540 550
    LTGPVGLLSI LSPDPLLLIR HFFSVAVYAT YFCFKSEPWA TKPRALFSSG
    560 570
    AILYKACSII FPLIYSEMKY LVH
    Length:573
    Mass (Da):64,024
    Last modified:October 1, 1996 - 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:i55222C911E2B8777
    GO

    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
    D37920 mRNA Translation: BAA07141.1
    BC097330 mRNA Translation: AAH97330.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A55767

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_058832.1, NM_017136.2

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENSRNOT00000012883; ENSRNOP00000012883; ENSRNOG00000009550

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    29230

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    rno:29230

    UCSC genome browser

    More...
    UCSCi
    RGD:3755 rat

    <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
    D37920 mRNA Translation: BAA07141.1
    BC097330 mRNA Translation: AAH97330.1
    PIRiA55767
    RefSeqiNP_058832.1, NM_017136.2

    3D structure databases

    SMRiP52020
    ModBaseiSearch...

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000012883

    Chemistry databases

    BindingDBiP52020
    ChEMBLiCHEMBL4241
    DrugCentraliP52020

    Proteomic databases

    jPOSTiP52020
    PaxDbiP52020
    PRIDEiP52020

    Genome annotation databases

    EnsembliENSRNOT00000012883; ENSRNOP00000012883; ENSRNOG00000009550
    GeneIDi29230
    KEGGirno:29230
    UCSCiRGD:3755 rat

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    6713
    RGDi3755 Sqle

    Phylogenomic databases

    eggNOGiKOG1298 Eukaryota
    COG0654 LUCA
    GeneTreeiENSGT00390000011759
    HOGENOMiCLU_026390_0_0_1
    InParanoidiP52020
    KOiK00511
    OMAiLILWKAC
    OrthoDBi583514at2759
    PhylomeDBiP52020
    TreeFamiTF331056

    Enzyme and pathway databases

    UniPathwayiUPA00767;UER00752
    ReactomeiR-RNO-191273 Cholesterol biosynthesis
    SABIO-RKiP52020

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P52020

    Gene expression databases

    BgeeiENSRNOG00000009550 Expressed in liver and 9 other tissues
    GenevisibleiP52020 RN

    Family and domain databases

    Gene3Di3.50.50.60, 1 hit
    InterProiView protein in InterPro
    IPR036188 FAD/NAD-bd_sf
    IPR013698 Squalene_epoxidase
    IPR040125 Squalene_monox
    PANTHERiPTHR10835 PTHR10835, 1 hit
    PfamiView protein in Pfam
    PF08491 SE, 1 hit
    SUPFAMiSSF51905 SSF51905, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

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    ProtoNeti
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    MobiDB: a database of protein disorder and mobility annotations

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    MobiDBi
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    <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 nameiERG1_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: P52020
    Secondary accession number(s): Q4V8L3
    <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%5Fand%5Fisoforms">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 1, 1996
    Last modified: February 26, 2020
    This is version 136 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

    <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

    Reference proteome

    Documents

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