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Entry version 182 (31 Jul 2019)
Sequence version 1 (01 Mar 2001)
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Protein

Egl nine homolog 1

Gene

EGLN1

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

Cellular oxygen sensor that catalyzes, under normoxic conditions, the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates a specific proline found in each of the oxygen-dependent degradation (ODD) domains (N-terminal, NODD, and C-terminal, CODD) of HIF1A. Also hydroxylates HIF2A. Has a preference for the CODD site for both HIF1A and HIF1B. Hydroxylated HIFs are then targeted for proteasomal degradation via the von Hippel-Lindau ubiquitination complex. Under hypoxic conditions, the hydroxylation reaction is attenuated allowing HIFs to escape degradation resulting in their translocation to the nucleus, heterodimerization with HIF1B, and increased expression of hypoxy-inducible genes. EGLN1 is the most important isozyme under normoxia and, through regulating the stability of HIF1, involved in various hypoxia-influenced processes such as angiogenesis in retinal and cardiac functionality. Target proteins are preferentially recognized via a LXXLAP motif.7 Publications

Caution

It was previously reported that this protein was the ortholog of rat SM-20. However, EGLN3 is now considered the true ortholog of rat SM-20 since it shows substantially greater similarity.Curated

<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 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

Protein has several cofactor binding sites:

<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

Following exposure to hypoxia, activated in HeLa cells but not in cardiovascular cells.2 Publications

<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=70 nM for HIF2A1 Publication
  2. KM=150 µM for O21 Publication
  3. KM=1.3 µM for 2-oxoglutarate1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi313IronCombined sources3 Publications1
    Metal bindingi315IronCombined sources3 Publications1
    Metal bindingi374IronCombined sources3 Publications1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei3832-oxoglutarate1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri21 – 58MYND-typePROSITE-ProRule annotationAdd BLAST38

    <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 functionDioxygenase, Oxidoreductase
    LigandIron, Metal-binding, Vitamin C, Zinc

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    1.14.11.2 2681
    1.14.11.29 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha

    <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:
    Egl nine homolog 1 (EC:1.14.11.291 Publication)
    Alternative name(s):
    Hypoxia-inducible factor prolyl hydroxylase 2
    Short name:
    HIF-PH2
    Short name:
    HIF-prolyl hydroxylase 2
    Short name:
    HPH-2
    Prolyl hydroxylase domain-containing protein 2
    Short name:
    PHD2
    SM-20
    <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:EGLN1Imported
    Synonyms:C1orf12
    ORF Names:PNAS-118, PNAS-137
    <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 1

    Organism-specific databases

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:1232 EGLN1

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    606425 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q9GZT9

    <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

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    <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

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    Erythrocytosis, familial, 3 (ECYT3)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionAn autosomal dominant disorder characterized by elevated serum hemoglobin and hematocrit, and normal serum erythropoietin levels.
    Related information in OMIM
    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_027371317P → R in ECYT3; marked decrease in enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs80358193EnsemblClinVar.1
    Natural variantiVAR_045902371R → H in ECYT3; decreased interaction with HIF1A and EPAS1 and decreased enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs119476044EnsemblClinVar.1

    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>Mutagenesisi201C → A: Little change in enzyme activity. 1 Publication1
    Mutagenesisi208C → A: Little change in enzyme activity. 1 Publication1
    Mutagenesisi252R → A: Reduced C-terminal ODD domain (CODD) hydroxylation of HIF1A. 1
    Mutagenesisi254D → A or K: Reduced C-terminal ODD domain (CODD) hxdroxylation of HIF1A. 1
    Mutagenesisi266C → A: Little change in enzyme activity. 1 Publication1
    Mutagenesisi283C → A: Little change in enzyme activity. 1 Publication1
    Mutagenesisi302C → A: Slight increase in enzyme activity. 1 Publication1
    Mutagenesisi303Y → F: No effect. 1 Publication1
    Mutagenesisi323C → A: Little change in enzyme activity. 1 Publication1
    Mutagenesisi326C → A: Slight increase in enzyme activity. 1 Publication1
    Mutagenesisi383R → A: Reduces enzyme activity by 95%. 1 Publication1

    Keywords - Diseasei

    Congenital erythrocytosis, Disease mutation

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    54583

    MalaCards human disease database

    More...
    MalaCardsi
    EGLN1
    MIMi609820 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000135766

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    247511 Autosomal dominant secondary polycythemia

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA27670

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL5697

    Drug and drug target database

    More...
    DrugBanki
    DB04847 FG-4592
    DB08687 N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE
    DB07112 N-[(4-HYDROXY-8-IODOISOQUINOLIN-3-YL)CARBONYL]GLYCINE
    DB00126 Vitamin C

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    2833

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    EGLN1

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    32129514

    <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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
    <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_00002066612 – 426Egl nine homolog 1Add BLAST425

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <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 residuei2N-acetylalanineCombined sources1
    Modified residuei12PhosphoserineCombined sources1
    Modified residuei125PhosphoserineCombined sources1
    Modified residuei201S-nitrosocysteine1 Publication1
    Modified residuei208S-nitrosocysteine1 Publication1
    Modified residuei302S-nitrosocysteine1 Publication1
    Modified residuei323S-nitrosocysteine1 Publication1
    Modified residuei326S-nitrosocysteine1 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

    S-nitrosylation inhibits the enzyme activity up to 60% under aerobic conditions. Chelation of Fe2+ has no effect on the S-nitrosylation. It is uncertain whether nitrosylation occurs on Cys-323 or Cys-326.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, S-nitrosylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q9GZT9

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q9GZT9

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

    More...
    PaxDbi
    Q9GZT9

    PeptideAtlas

    More...
    PeptideAtlasi
    Q9GZT9

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9GZT9

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    80138 [Q9GZT9-1]
    80139 [Q9GZT9-2]
    80140 [Q9GZT9-3]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9GZT9

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

    More...
    PhosphoSitePlusi
    Q9GZT9

    <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

    According to PubMed:11056053, widely expressed with highest levels in skeletal muscle and heart, moderate levels in pancreas, brain (dopaminergic neurons of adult and fetal substantia nigra) and kidney, and lower levels in lung and liver. According to PubMed:12351678 widely expressed with highest levels in brain, kidney and adrenal gland. Expressed in cardiac myocytes, aortic endothelial cells and coronary artery smooth muscle. According to PubMed:12788921; expressed in adult and fetal heart, brain, liver, lung, skeletal muscle and kidney. Also expressed in placenta. Highest levels in adult heart, brain, lung and liver and fetal brain, heart spleen and skeletal muscle.5 Publications

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000135766 Expressed in 223 organ(s), highest expression level in female gonad

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q9GZT9 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q9GZT9 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    HPA022129

    <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

    Monomer.

    Interacts with ING4; the interaction inhibits the hydroxylation of HIF alpha proteins.

    Interacts with PTGES3 (via PXLE motif); thereby recruiting EGLN1 to the HSP90 pathway to facilitate HIF alpha proteins hydroxylation.

    Interacts with LIMD1.

    Found in a complex composed of LIMD1, VHL, EGLN1/PHD2, ELOB and CUL2.

    Interacts with EPAS1.

    Interacts with CBFA2T3 (PubMed:25974097).

    Interacts with HIF1A (PubMed:25974097).

    8 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
    120060, 42 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    Q9GZT9

    Database of interacting proteins

    More...
    DIPi
    DIP-37495N

    The Eukaryotic Linear Motif resource for Functional Sites in Proteins

    More...
    ELMi
    Q9GZT9

    Protein interaction database and analysis system

    More...
    IntActi
    Q9GZT9, 17 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q9GZT9

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000355601

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    Q9GZT9

    <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

    1426
    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
    Q9GZT9

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    Q9GZT9

    <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>Domaini291 – 392Fe2OG dioxygenasePROSITE-ProRule annotationAdd BLAST102

    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>Regioni6 – 20Required for nuclear exportAdd BLAST15
    Regioni241 – 251Beta(2)beta(3) 'finger-like' loop1 PublicationAdd BLAST11

    <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 beta2beta3 'finger-like' loop domain is important for substrate (HIFs' CODD/NODD) selectivity.1 Publication

    Zinc finger

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Zinc fingeri21 – 58MYND-typePROSITE-ProRule annotationAdd BLAST38

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG3710 Eukaryota
    ENOG410ZHZN LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000155704

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000004818

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9GZT9

    KEGG Orthology (KO)

    More...
    KOi
    K09592

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    KANLYPP

    Database of Orthologous Groups

    More...
    OrthoDBi
    1604981at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9GZT9

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF314595

    Family and domain databases

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR005123 Oxoglu/Fe-dep_dioxygenase
    IPR006620 Pro_4_hyd_alph
    IPR002893 Znf_MYND

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF13640 2OG-FeII_Oxy_3, 1 hit
    PF01753 zf-MYND, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00702 P4Hc, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51471 FE2OG_OXY, 1 hit
    PS01360 ZF_MYND_1, 1 hit
    PS50865 ZF_MYND_2, 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.

    <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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    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
    Isoform 1 (identifier: Q9GZT9-1) [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
    MANDSGGPGG PSPSERDRQY CELCGKMENL LRCSRCRSSF YCCKEHQRQD
    60 70 80 90 100
    WKKHKLVCQG SEGALGHGVG PHQHSGPAPP AAVPPPRAGA REPRKAAARR
    110 120 130 140 150
    DNASGDAAKG KVKAKPPADP AAAASPCRAA AGGQGSAVAA EAEPGKEEPP
    160 170 180 190 200
    ARSSLFQEKA NLYPPSNTPG DALSPGGGLR PNGQTKPLPA LKLALEYIVP
    210 220 230 240 250
    CMNKHGICVV DDFLGKETGQ QIGDEVRALH DTGKFTDGQL VSQKSDSSKD
    260 270 280 290 300
    IRGDKITWIE GKEPGCETIG LLMSSMDDLI RHCNGKLGSY KINGRTKAMV
    310 320 330 340 350
    ACYPGNGTGY VRHVDNPNGD GRCVTCIYYL NKDWDAKVSG GILRIFPEGK
    360 370 380 390 400
    AQFADIEPKF DRLLFFWSDR RNPHEVQPAY ATRYAITVWY FDADERARAK
    410 420
    VKYLTGEKGV RVELNKPSDS VGKDVF
    Length:426
    Mass (Da):46,021
    Last modified:March 1, 2001 - 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:i81A97FF772CAA14C
    GO
    Isoform 2 (identifier: Q9GZT9-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         338-359: Missing.

    Note: Inactive isoform.
    Show »
    Length:404
    Mass (Da):43,666
    Checksum:i32B08D27CD89A8B9
    GO
    Isoform 3 (identifier: Q9GZT9-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         58-175: CQGSEGALGH...SNTPGDALSP → LLGGYRFAFSWNSDERA

    Note: No experimental confirmation available.
    Show »
    Length:325
    Mass (Da):36,486
    Checksum:i116F684A91222E6A
    GO

    <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 AAK07534 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAK07536 differs from that shown. Reason: Frameshift at position 239.Curated

    <p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>Polymorphismi

    Variations in EGLN1 are associated with adaptation to high altitude (PubMed:20838600, PubMed:20466884, PubMed:24711448, PubMed:25129147). High-altitude hypoxia (reduced inspired oxygen tension due to decreased barometric pressure) exerts severe physiological stress on the human body and leads to an elevation of hematocrit levels and an increased number of erythrocytes (polycythemia) in non-adapted individuals. Genetic variations in EGLN1 contribute to adaptation to high altitute by maintaining hematocrit levels comparable to those for populations living at sea level and are present in two high-altitude regions where humans have lived for millennia, the Andean Altiplano and the Tibetan Plateau (PubMed:20838600, PubMed:20466884). Variants Glu-4 and Ser-127, which are frequently associated together and are present in the majority of Tibetan populations, participate in adaptation to high altitude (PubMed:24711448, PubMed:25129147). Molecular mechanisms explaining this adaptation are however unclear. According to a report, variants Glu-4 and Ser-127 lead to decreased interaction with PTGES3 and subsequent decrease of HIF alpha proteins degradation (PubMed:24711448). According to a second report, Glu-4 and Ser-127 haplotype enhances the catalytic activity under hypoxic conditions, promoting increased HIF alpha proteins degradation, thereby abrogating hypoxia-induced and HIF alpha-mediated augmentation of erythropoiesis and protecting Tibetans from polycythemia at high altitude (PubMed:25129147).Curated4 Publications

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_0718584D → E Polymorphism present in the majority of Tibetans; increased protection from polycythemia at high altitude; when associated with S-127. 2 PublicationsCorresponds to variant dbSNP:rs186996510EnsemblClinVar.1
    Natural variantiVAR_071859127C → S Polymorphism present in the majority of Tibetans; increased protection from polycythemia at high altitude; when associated with E-4. 2 PublicationsCorresponds to variant dbSNP:rs12097901EnsemblClinVar.1
    Natural variantiVAR_027371317P → R in ECYT3; marked decrease in enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs80358193EnsemblClinVar.1
    Natural variantiVAR_045902371R → H in ECYT3; decreased interaction with HIF1A and EPAS1 and decreased enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs119476044EnsemblClinVar.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_04219158 – 175CQGSE…DALSP → LLGGYRFAFSWNSDERA in isoform 3. 1 PublicationAdd BLAST118
    Alternative sequenceiVSP_007569338 – 359Missing in isoform 2. 1 PublicationAdd BLAST22

    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
    AF246631, AF246630 Genomic DNA Translation: AAG34568.1
    AF229245 mRNA Translation: AAG33965.1
    AJ310543 mRNA Translation: CAC42509.1
    AL833885 mRNA Translation: CAD38741.2
    AF277174 mRNA Translation: AAK07534.1 Different initiation.
    AF277176 mRNA Translation: AAK07536.1 Frameshift.
    AL117352 Genomic DNA No translation available.
    AL445524 Genomic DNA No translation available.

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS1595.1 [Q9GZT9-1]

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_071334.1, NM_022051.2 [Q9GZT9-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000366641; ENSP00000355601; ENSG00000135766 [Q9GZT9-1]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    54583

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:54583

    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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF246631, AF246630 Genomic DNA Translation: AAG34568.1
    AF229245 mRNA Translation: AAG33965.1
    AJ310543 mRNA Translation: CAC42509.1
    AL833885 mRNA Translation: CAD38741.2
    AF277174 mRNA Translation: AAK07534.1 Different initiation.
    AF277176 mRNA Translation: AAK07536.1 Frameshift.
    AL117352 Genomic DNA No translation available.
    AL445524 Genomic DNA No translation available.
    CCDSiCCDS1595.1 [Q9GZT9-1]
    RefSeqiNP_071334.1, NM_022051.2 [Q9GZT9-1]

    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
    2G19X-ray1.70A181-417[»]
    2G1MX-ray2.20A181-426[»]
    2HBTX-ray1.60A188-426[»]
    2HBUX-ray1.85A188-426[»]
    2Y33X-ray2.00A181-426[»]
    2Y34X-ray2.01A181-426[»]
    3HQRX-ray2.00A181-426[»]
    3HQUX-ray2.30A181-426[»]
    3OUHX-ray2.51A181-416[»]
    3OUIX-ray1.70A181-392[»]
    3OUJX-ray2.30A181-416[»]
    4BQWX-ray1.79A181-426[»]
    4BQXX-ray1.79A181-426[»]
    4BQYX-ray1.53A181-426[»]
    4JZRX-ray2.10A189-399[»]
    4KBZX-ray2.15A184-419[»]
    4UWDX-ray1.72A181-426[»]
    5A3UX-ray3.30A/B/C181-426[»]
    5L9BX-ray1.95A/B181-426[»]
    5L9RX-ray1.81A181-426[»]
    5L9VX-ray1.83A/B181-426[»]
    5LA9X-ray2.81A/B181-426[»]
    5LASX-ray2.10A/B181-426[»]
    5LATX-ray1.90A181-426[»]
    5LB6X-ray1.70A181-426[»]
    5LBBX-ray1.70A181-426[»]
    5LBCX-ray1.82A181-426[»]
    5LBEX-ray1.75A181-426[»]
    5LBFX-ray1.90A181-426[»]
    5OX5X-ray2.25A181-426[»]
    5OX6X-ray1.99A181-426[»]
    5V18X-ray2.15A181-416[»]
    6NMQX-ray1.58A180-392[»]
    SMRiQ9GZT9
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi120060, 42 interactors
    CORUMiQ9GZT9
    DIPiDIP-37495N
    ELMiQ9GZT9
    IntActiQ9GZT9, 17 interactors
    MINTiQ9GZT9
    STRINGi9606.ENSP00000355601

    Chemistry databases

    BindingDBiQ9GZT9
    ChEMBLiCHEMBL5697
    DrugBankiDB04847 FG-4592
    DB08687 N-[(1-CHLORO-4-HYDROXYISOQUINOLIN-3-YL)CARBONYL]GLYCINE
    DB07112 N-[(4-HYDROXY-8-IODOISOQUINOLIN-3-YL)CARBONYL]GLYCINE
    DB00126 Vitamin C
    GuidetoPHARMACOLOGYi2833

    PTM databases

    iPTMnetiQ9GZT9
    PhosphoSitePlusiQ9GZT9

    Polymorphism and mutation databases

    BioMutaiEGLN1
    DMDMi32129514

    Proteomic databases

    EPDiQ9GZT9
    jPOSTiQ9GZT9
    PaxDbiQ9GZT9
    PeptideAtlasiQ9GZT9
    PRIDEiQ9GZT9
    ProteomicsDBi80138 [Q9GZT9-1]
    80139 [Q9GZT9-2]
    80140 [Q9GZT9-3]

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000366641; ENSP00000355601; ENSG00000135766 [Q9GZT9-1]
    GeneIDi54583
    KEGGihsa:54583

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    54583
    DisGeNETi54583

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    EGLN1
    HGNCiHGNC:1232 EGLN1
    HPAiHPA022129
    MalaCardsiEGLN1
    MIMi606425 gene
    609820 phenotype
    neXtProtiNX_Q9GZT9
    OpenTargetsiENSG00000135766
    Orphaneti247511 Autosomal dominant secondary polycythemia
    PharmGKBiPA27670

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG3710 Eukaryota
    ENOG410ZHZN LUCA
    GeneTreeiENSGT00940000155704
    HOGENOMiHOG000004818
    InParanoidiQ9GZT9
    KOiK09592
    OMAiKANLYPP
    OrthoDBi1604981at2759
    PhylomeDBiQ9GZT9
    TreeFamiTF314595

    Enzyme and pathway databases

    BRENDAi1.14.11.2 2681
    1.14.11.29 2681
    ReactomeiR-HSA-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha

    Miscellaneous databases

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

    More...
    ChiTaRSi
    EGLN1 human
    EvolutionaryTraceiQ9GZT9

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    EGLN1

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

    More...
    GenomeRNAii
    54583

    Protein Ontology

    More...
    PROi
    PR:Q9GZT9

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000135766 Expressed in 223 organ(s), highest expression level in female gonad
    ExpressionAtlasiQ9GZT9 baseline and differential
    GenevisibleiQ9GZT9 HS

    Family and domain databases

    InterProiView protein in InterPro
    IPR005123 Oxoglu/Fe-dep_dioxygenase
    IPR006620 Pro_4_hyd_alph
    IPR002893 Znf_MYND
    PfamiView protein in Pfam
    PF13640 2OG-FeII_Oxy_3, 1 hit
    PF01753 zf-MYND, 1 hit
    SMARTiView protein in SMART
    SM00702 P4Hc, 1 hit
    PROSITEiView protein in PROSITE
    PS51471 FE2OG_OXY, 1 hit
    PS01360 ZF_MYND_1, 1 hit
    PS50865 ZF_MYND_2, 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 nameiEGLN1_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: Q9GZT9
    Secondary accession number(s): Q8N3M8, Q9BZS8, Q9BZT0
    <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: June 16, 2003
    Last sequence update: March 1, 2001
    Last modified: July 31, 2019
    This is version 182 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
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