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UniProtKB - Q9GZT9 (EGLN1_HUMAN)

Entry version 190 (12 Aug 2020)
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%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

Protein has several cofactor binding sites:

<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

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%5Fsection">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%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 sitei3832-oxoglutarate1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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

    Pathway Commons web resource for biological pathway data

    More...    PathwayCommonsi    		Q9GZT9

    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%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:
    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%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:EGLN1Imported
    Synonyms:C1orf12
    ORF Names:PNAS-118, PNAS-137
    <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>OrganismiHomo sapiens (Human)
    <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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <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
    • UP000005640 <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 1

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...    EuPathDBi    		HostDB:ENSG00000135766.8

    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%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>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

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...    Pharosi    		Q9GZT9, Tchem

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL5697

    Drug and drug target database

    More...    DrugBanki    		DB00126, Ascorbic acid
    DB14490, Ferrous ascorbate
    DB14491, Ferrous fumarate
    DB14488, Ferrous gluconate
    DB14501, Ferrous glycine sulfate
    DB14489, Ferrous succinate
    DB08687, FG-2216
    DB01592, Iron
    DB07112, N-[(4-HYDROXY-8-IODOISOQUINOLIN-3-YL)CARBONYL]GLYCINE
    DB04847, Roxadustat

    DrugCentral

    More...    DrugCentrali    		Q9GZT9

    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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<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%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

    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

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...    MassIVEi    		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: a multi-organism 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 female gonad and 238 other tissues

    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    		ENSG00000135766, Group enriched (blood, skeletal muscle)

    <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

    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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Hide details

    GO - Molecular functioni

    Complete GO annotation on QuickGO ...

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...    BioGRIDi    		120060, 45 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, 19 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

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...    RNActi    		Q9GZT9, protein

    <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...

    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    		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%5Fand%5Fdomains%5Fsection">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

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00940000155704

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		CLU_022206_2_2_1

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		Q9GZT9

    KEGG Orthology (KO)

    More...    KOi    		K09592

    Identification of Orthologs from Complete Genome Data

    More...    OMAi    		YQEKANL

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		Q9GZT9

    TreeFam database of animal gene trees

    More...    TreeFami    		TF314595

    Family and domain databases

    Intrinsically Disordered proteins with Extensive Annotations and Literature

    More...    IDEALi    		IID00345

    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%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>Sequences (3+)i

    <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.

    <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 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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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: 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.Curated
    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

    Show »
    Length:325
    Mass (Da):36,486
    Checksum:i116F684A91222E6A
    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
    A0A590UJ78A0A590UJ78_HUMAN
    Egl nine homolog 1
    EGLN1
    		175Annotation 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>
    A0A590UJT7A0A590UJT7_HUMAN
    Egl nine homolog 1
    EGLN1
    		159Annotation 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>
    A0A590UJD6A0A590UJD6_HUMAN
    Egl nine homolog 1
    EGLN1
    		81Annotation 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>
    A0A590UJZ0A0A590UJZ0_HUMAN
    Egl nine homolog 1
    EGLN1
    		113Annotation 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 AAK07534 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
    The sequence AAK07536 differs from that shown. Reason: Frameshift.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%5Fin%5Fdisease">'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%5Freferences%5Fsection">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[»]
    6QGVX-ray1.40A181-407[»]
    6ST3X-ray2.43A/B181-407[»]
    6YVTX-ray2.85A/B/C/D/E/F181-426[»]
    SMRiQ9GZT9
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi120060, 45 interactors
    CORUMiQ9GZT9
    DIPiDIP-37495N
    ELMiQ9GZT9
    IntActiQ9GZT9, 19 interactors
    MINTiQ9GZT9
    STRINGi9606.ENSP00000355601

    Chemistry databases

    BindingDBiQ9GZT9
    ChEMBLiCHEMBL5697
    DrugBankiDB00126, Ascorbic acid
    DB14490, Ferrous ascorbate
    DB14491, Ferrous fumarate
    DB14488, Ferrous gluconate
    DB14501, Ferrous glycine sulfate
    DB14489, Ferrous succinate
    DB08687, FG-2216
    DB01592, Iron
    DB07112, N-[(4-HYDROXY-8-IODOISOQUINOLIN-3-YL)CARBONYL]GLYCINE
    DB04847, Roxadustat
    DrugCentraliQ9GZT9
    GuidetoPHARMACOLOGYi2833

    PTM databases

    iPTMnetiQ9GZT9
    PhosphoSitePlusiQ9GZT9

    Polymorphism and mutation databases

    BioMutaiEGLN1
    DMDMi32129514

    Proteomic databases

    EPDiQ9GZT9
    jPOSTiQ9GZT9
    MassIVEiQ9GZT9
    PaxDbiQ9GZT9
    PeptideAtlasiQ9GZT9
    PRIDEiQ9GZT9
    ProteomicsDBi80138 [Q9GZT9-1]
    80139 [Q9GZT9-2]
    80140 [Q9GZT9-3]

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

    More...    Antibodypediai    		20799, 635 antibodies

    Genome annotation databases

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

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		54583
    DisGeNETi54583
    EuPathDBiHostDB:ENSG00000135766.8

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		EGLN1
    HGNCiHGNC:1232, EGLN1
    HPAiENSG00000135766, Group enriched (blood, skeletal muscle)
    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
    GeneTreeiENSGT00940000155704
    HOGENOMiCLU_022206_2_2_1
    InParanoidiQ9GZT9
    KOiK09592
    OMAiYQEKANL
    PhylomeDBiQ9GZT9
    TreeFamiTF314595

    Enzyme and pathway databases

    BRENDAi1.14.11.2, 2681
    1.14.11.29, 2681
    PathwayCommonsiQ9GZT9
    ReactomeiR-HSA-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...    BioGRID-ORCSi    		54583, 83 hits in 879 CRISPR screens

    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
    PharosiQ9GZT9, Tchem

    Protein Ontology

    More...    PROi    		PR:Q9GZT9
    RNActiQ9GZT9, protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000135766, Expressed in female gonad and 238 other tissues
    ExpressionAtlasiQ9GZT9, baseline and differential
    GenevisibleiQ9GZT9, HS

    Family and domain databases

    IDEALiIID00345
    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%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: June 16, 2003
    Last sequence update: March 1, 2001
    Last modified: August 12, 2020
    This is version 190 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, Reference proteome

    Documents

    1. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    2. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
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