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Entry version 197 (23 Feb 2022)
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 bindingi21Zinc 1PROSITE-ProRule annotation1
Metal bindingi24Zinc 1PROSITE-ProRule annotation1
Metal bindingi33Zinc 2PROSITE-ProRule annotation1
Metal bindingi36Zinc 2PROSITE-ProRule annotation1
Metal bindingi42Zinc 1PROSITE-ProRule annotation1
Metal bindingi46Zinc 1PROSITE-ProRule annotation1
Metal bindingi54Zinc 2PROSITE-ProRule annotation1
Metal bindingi58Zinc 2PROSITE-ProRule annotation1
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-type; atypicalPROSITE-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

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
Q9GZT9

Reactome - a knowledgebase of biological pathways and processes

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

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q9GZT9

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q9GZT9

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q9GZT9

<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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

Human Gene Nomenclature Database

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HGNCi
HGNC:1232, EGLN1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
606425, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q9GZT9

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000135766

<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

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 variants 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 variant

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

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PharmGKBi
PA27670

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q9GZT9, Tclin

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

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GuidetoPHARMACOLOGYi
2833

Genetic variation 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

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jPOSTi
Q9GZT9

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9GZT9

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9GZT9

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

More...
PaxDbi
Q9GZT9

PeptideAtlas

More...
PeptideAtlasi
Q9GZT9

PRoteomics IDEntifications database

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PRIDEi
Q9GZT9

ProteomicsDB: a multi-organism proteome resource

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

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
Q9GZT9, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

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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 239 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, Tissue enhanced (skeletal)

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
120060, 62 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9GZT9

Database of interacting proteins

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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

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MINTi
Q9GZT9

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000355601

Chemistry databases

BindingDB database of measured binding affinities

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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

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SMRi
Q9GZT9

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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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
Regioni65 – 129DisorderedSequence analysisAdd BLAST65
Regioni160 – 184DisorderedSequence analysisAdd BLAST25
Regioni241 – 251Beta(2)beta(3) 'finger-like' loop1 PublicationAdd BLAST11

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi92 – 108Basic and acidic residuesSequence analysisAdd BLAST17

<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-type; atypicalPROSITE-ProRule annotationAdd BLAST38

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3710, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000155704

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_022206_2_2_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9GZT9

Identification of Orthologs from Complete Genome Data

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OMAi
YQEKANL

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9GZT9

TreeFam database of animal gene trees

More...
TreeFami
TF314595

Family and domain databases

Intrinsically Disordered proteins with Extensive Annotations and Literature

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IDEALi
IID00345

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR005123, Oxoglu/Fe-dep_dioxygenase
IPR006620, Pro_4_hyd_alph
IPR044862, Pro_4_hyd_alph_FE2OG_OXY
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.<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 <p><strong>What is the canonical sequence?</strong><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>
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>
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>

<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 Increased protection from polycythemia at high altitude; when associated with S-127. 2 PublicationsCorresponds to variant dbSNP:rs186996510EnsemblClinVar.1
Natural variantiVAR_071859127C → S 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

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
54583

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:54583

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...
MANE-Selecti
ENST00000366641.4; ENSP00000355601.3; NM_022051.3; NP_071334.1

Keywords - Coding sequence diversityi

Alternative splicing

<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[»]
6YVWX-ray1.97A181-426[»]
6YVXX-ray1.80A181-426[»]
6YVZX-ray1.91A181-426[»]
6YW0X-ray2.20A181-426[»]
6YW1X-ray1.46A181-407[»]
6YW2X-ray2.14A181-407[»]
6YW3X-ray2.28A181-407[»]
6YW4X-ray1.53A181-407[»]
6ZBNX-ray2.01A/B/C/D/E/F181-407[»]
6ZBOX-ray1.79A/B/C/D/E/F181-407[»]
SMRiQ9GZT9
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi120060, 62 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

GlyGeniQ9GZT9, 1 site, 1 O-linked glycan (1 site)
iPTMnetiQ9GZT9
PhosphoSitePlusiQ9GZT9

Genetic variation databases

BioMutaiEGLN1
DMDMi32129514

Proteomic databases

EPDiQ9GZT9
jPOSTiQ9GZT9
MassIVEiQ9GZT9
MaxQBiQ9GZT9
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, 656 antibodies from 37 providers

The DNASU plasmid repository

More...
DNASUi
54583

Genome annotation databases

EnsembliENST00000366641; ENSP00000355601; ENSG00000135766
GeneIDi54583
KEGGihsa:54583
MANE-SelectiENST00000366641.4; ENSP00000355601.3; NM_022051.3; NP_071334.1

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
54583
DisGeNETi54583

GeneCards: human genes, protein and diseases

More...
GeneCardsi
EGLN1
HGNCiHGNC:1232, EGLN1
HPAiENSG00000135766, Tissue enhanced (skeletal)
MalaCardsiEGLN1
MIMi606425, gene
609820, phenotype
neXtProtiNX_Q9GZT9
OpenTargetsiENSG00000135766
Orphaneti247511, Autosomal dominant secondary polycythemia
PharmGKBiPA27670
VEuPathDBiHostDB:ENSG00000135766

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3710, Eukaryota
GeneTreeiENSGT00940000155704
HOGENOMiCLU_022206_2_2_1
InParanoidiQ9GZT9
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
SABIO-RKiQ9GZT9
SignaLinkiQ9GZT9
SIGNORiQ9GZT9

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
54583, 94 hits in 1054 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, Tclin

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 239 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
IPR044862, Pro_4_hyd_alph_FE2OG_OXY
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

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: February 23, 2022
This is version 197 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 chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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