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Entry version 189 (08 May 2019)
Sequence version 2 (01 Feb 1996)
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Protein

Eosinophil peroxidase

Gene

EPX

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

Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. Shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

Protein has several cofactor binding sites:
  • Ca2+PROSITE-ProRule annotationNote: Binds 1 Ca2+ ion per heterodimer.PROSITE-ProRule annotation
  • heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) covalently through ester linkages to hydroxylated methyl groups formed auto-catalytically with hydrogen peroxide at the heme C-1 and C-5 positions. The ester linkage to Asp-232 was observed in 30% of the chains.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei232Heme (covalent; via 2 links); partial1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei233Proton acceptorPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi234CalciumPROSITE-ProRule annotation1
Metal bindingi306CalciumPROSITE-ProRule annotation1
Metal bindingi308Calcium; via carbonyl oxygenPROSITE-ProRule annotation1
Metal bindingi310CalciumPROSITE-ProRule annotation1
Metal bindingi312CalciumPROSITE-ProRule annotation1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei377Transition state stabilizerPROSITE-ProRule annotation1
Binding sitei380Heme (covalent; via 2 links)1
Metal bindingi474Iron (heme axial ligand)PROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase, Peroxidase
Biological processHydrogen peroxide
LigandCalcium, Heme, Iron, Metal-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-6798695 Neutrophil degranulation

Protein family/group databases

PeroxiBase, a peroxidase database

More...
PeroxiBasei
3317 HsEPO

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Eosinophil peroxidase (EC:1.11.1.7)
Short name:
EPO
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:EPX
Synonyms:EPER, EPO, EPP
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3423 EPX

Online Mendelian Inheritance in Man (OMIM)

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MIMi
131399 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P11678

<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

<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

Eosinophil peroxidase deficiency (EPXD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare abnormality without clinical symptoms characterized by decreased or absent peroxidase activity and decreased volume of the granule matrix in eosinophils.
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_015376286R → H in EPXD. 1 PublicationCorresponds to variant dbSNP:rs121434566EnsemblClinVar.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
8288

MalaCards human disease database

More...
MalaCardsi
EPX
MIMi261500 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000121053

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA27841

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2438

Drug and drug target database

More...
DrugBanki
DB01065 Melatonin

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
EPX

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1352738

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 17Sequence analysisAdd BLAST17
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000002363918 – 1391 PublicationAdd BLAST122
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000023640140 – 250Eosinophil peroxidase light chainAdd BLAST111
ChainiPRO_0000023641251 – 715Eosinophil peroxidase heavy chainAdd BLAST465

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi52N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi113N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi141 ↔ 152PROSITE-ProRule annotation
Disulfide bondi253 ↔ 263PROSITE-ProRule annotation
Disulfide bondi257 ↔ 281PROSITE-ProRule annotation
Glycosylationi327N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi359 ↔ 370PROSITE-ProRule annotation
Glycosylationi363N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei488Nitrated tyrosine1 Publication1
Disulfide bondi578 ↔ 635PROSITE-ProRule annotation
Disulfide bondi676 ↔ 701PROSITE-ProRule annotation
Glycosylationi700N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi708N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Nitration

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P11678

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P11678

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

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PaxDbi
P11678

PeptideAtlas

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PeptideAtlasi
P11678

PRoteomics IDEntifications database

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PRIDEi
P11678

ProteomicsDB human proteome resource

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ProteomicsDBi
52797

Consortium for Top Down Proteomics

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TopDownProteomicsi
P11678

PTM databases

GlyConnect protein glycosylation platform

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GlyConnecti
1208

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P11678

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

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PhosphoSitePlusi
P11678

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000121053 Expressed in 49 organ(s), highest expression level in trabecular bone tissue

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P11678 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA050507

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Tetramer of two light chains and two heavy chains.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
113893, 2 interactors

Protein interaction database and analysis system

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IntActi
P11678, 3 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000225371

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

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

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SMRi
P11678

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peroxidase family. XPO subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2408 Eukaryota
ENOG410XPZ3 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000156009

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000016084

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P11678

KEGG Orthology (KO)

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KOi
K10788

Identification of Orthologs from Complete Genome Data

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OMAi
QLPPCFP

Database of Orthologous Groups

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OrthoDBi
276568at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P11678

TreeFam database of animal gene trees

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TreeFami
TF314316

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.640.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR029599 EPX/EPO
IPR019791 Haem_peroxidase_animal
IPR010255 Haem_peroxidase_sf
IPR037120 Haem_peroxidase_sf_animal

The PANTHER Classification System

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PANTHERi
PTHR11475:SF63 PTHR11475:SF63, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF03098 An_peroxidase, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00457 ANPEROXIDASE

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48113 SSF48113, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00435 PEROXIDASE_1, 1 hit
PS50292 PEROXIDASE_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P11678-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MHLLPALAGV LATLVLAQPC EGTDPASPGA VETSVLRDCI AEAKLLVDAA
60 70 80 90 100
YNWTQKSIKQ RLRSGSASPM DLLSYFKQPV AATRTVVRAA DYMHVALGLL
110 120 130 140 150
EEKLQPQRSG PFNVTDVLTE PQLRLLSQAS GCALRDQAER CSDKYRTITG
160 170 180 190 200
RCNNKRRPLL GASNQALARW LPAEYEDGLS LPFGWTPSRR RNGFLLPLVR
210 220 230 240 250
AVSNQIVRFP NERLTSDRGR ALMFMQWGQF IDHDLDFSPE SPARVAFTAG
260 270 280 290 300
VDCERTCAQL PPCFPIKIPP NDPRIKNQRD CIPFFRSAPS CPQNKNRVRN
310 320 330 340 350
QINALTSFVD ASMVYGSEVS LSLRLRNRTN YLGLLAINQR FQDNGRALLP
360 370 380 390 400
FDNLHDDPCL LTNRSARIPC FLAGDTRSTE TPKLAAMHTL FMREHNRLAT
410 420 430 440 450
ELRRLNPRWN GDKLYNEARK IMGAMVQIIT YRDFLPLVLG KARARRTLGH
460 470 480 490 500
YRGYCSNVDP RVANVFTLAF RFGHTMLQPF MFRLDSQYRA SAPNSHVPLS
510 520 530 540 550
SAFFASWRIV YEGGIDPILR GLMATPAKLN RQDAMLVDEL RDRLFRQVRR
560 570 580 590 600
IGLDLAALNM QRSRDHGLPG YNAWRRFCGL SQPRNLAQLS RVLKNQDLAR
610 620 630 640 650
KFLNLYGTPD NIDIWIGAIA EPLLPGARVG PLLACLFENQ FRRARDGDRF
660 670 680 690 700
WWQKRGVFTK RQRKALSRIS LSRIICDNTG ITTVSRDIFR ANIYPRGFVN
710
CSRIPRLNLS AWRGT
Length:715
Mass (Da):81,040
Last modified:February 1, 1996 - v2
<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:iCEB4E689A6C46374
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti13 – 18TLVLAQ → EFRGQD AA sequence (PubMed:2541222).Curated6
Sequence conflicti21E → Q AA sequence (PubMed:2541222).Curated1
Sequence conflicti113N → I in CAA32530 (PubMed:2541222).Curated1
Sequence conflicti163S → C AA sequence (PubMed:2541222).Curated1
Sequence conflicti645 – 660RDGDR…GVFTK → ETETGSGGRTRCFHQ AA sequence (PubMed:2541222).CuratedAdd BLAST16

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

Allelic variant in EPX is associated with Japanese cedar pollinosis which is a type I allergic disease with ocular and nasal symptoms that develop paroxysmally on contact with Japanese cedar pollen. These symptoms, which occur seasonally each year, are typical features of allergic rhinitis, such as sneezing, excessive nasal secretion, nasal congestion, and conjunctival itching.

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05048535V → I. Corresponds to variant dbSNP:rs34553736Ensembl.1
Natural variantiVAR_02513840I → M1 PublicationCorresponds to variant dbSNP:rs11079339Ensembl.1
Natural variantiVAR_025139122Q → H1 PublicationCorresponds to variant dbSNP:rs11652709Ensembl.1
Natural variantiVAR_025140249A → E1 PublicationCorresponds to variant dbSNP:rs35896669Ensembl.1
Natural variantiVAR_025141276K → R1 PublicationCorresponds to variant dbSNP:rs35074452Ensembl.1
Natural variantiVAR_015376286R → H in EPXD. 1 PublicationCorresponds to variant dbSNP:rs121434566EnsemblClinVar.1
Natural variantiVAR_025142292P → L1 PublicationCorresponds to variant dbSNP:rs33971258Ensembl.1
Natural variantiVAR_060197326R → H1 PublicationCorresponds to variant dbSNP:rs35832094Ensembl.1
Natural variantiVAR_060198326R → L1 Publication1
Natural variantiVAR_025143326R → P1 PublicationCorresponds to variant dbSNP:rs35832094Ensembl.1
Natural variantiVAR_025144358P → L Associated with Japanese cedar pollinosis. 2 PublicationsCorresponds to variant dbSNP:rs35135976Ensembl.1
Natural variantiVAR_025145364R → H1 PublicationCorresponds to variant dbSNP:rs35232062Ensembl.1
Natural variantiVAR_025146441K → T1 PublicationCorresponds to variant dbSNP:rs35750729Ensembl.1
Natural variantiVAR_050486458V → M. Corresponds to variant dbSNP:rs34817773Ensembl.1
Natural variantiVAR_025147496H → Q1 PublicationCorresponds to variant dbSNP:rs33955150Ensembl.1
Natural variantiVAR_020031572N → Y1 PublicationCorresponds to variant dbSNP:rs2302311Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M29913
, M29904, M29905, M29906, M29907, M29908, M29909, M29910, M29911, M29912 Genomic DNA Translation: AAA58458.1
DQ054598 Genomic DNA Translation: AAY43126.1
X14346 mRNA Translation: CAA32530.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS11602.1

Protein sequence database of the Protein Information Resource

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PIRi
A34408

NCBI Reference Sequences

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RefSeqi
NP_000493.1, NM_000502.5

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000225371; ENSP00000225371; ENSG00000121053

Database of genes from NCBI RefSeq genomes

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GeneIDi
8288

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:8288

UCSC genome browser

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UCSCi
uc002ivq.4 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29913
, M29904, M29905, M29906, M29907, M29908, M29909, M29910, M29911, M29912 Genomic DNA Translation: AAA58458.1
DQ054598 Genomic DNA Translation: AAY43126.1
X14346 mRNA Translation: CAA32530.1
CCDSiCCDS11602.1
PIRiA34408
RefSeqiNP_000493.1, NM_000502.5

3D structure databases

SMRiP11678
ModBaseiSearch...

Protein-protein interaction databases

BioGridi113893, 2 interactors
IntActiP11678, 3 interactors
STRINGi9606.ENSP00000225371

Chemistry databases

ChEMBLiCHEMBL2438
DrugBankiDB01065 Melatonin

Protein family/group databases

PeroxiBasei3317 HsEPO

PTM databases

GlyConnecti1208
iPTMnetiP11678
PhosphoSitePlusiP11678

Polymorphism and mutation databases

BioMutaiEPX
DMDMi1352738

Proteomic databases

EPDiP11678
jPOSTiP11678
PaxDbiP11678
PeptideAtlasiP11678
PRIDEiP11678
ProteomicsDBi52797
TopDownProteomicsiP11678

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
8288
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000225371; ENSP00000225371; ENSG00000121053
GeneIDi8288
KEGGihsa:8288
UCSCiuc002ivq.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
8288
DisGeNETi8288

GeneCards: human genes, protein and diseases

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GeneCardsi
EPX

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0202542
HGNCiHGNC:3423 EPX
HPAiHPA050507
MalaCardsiEPX
MIMi131399 gene
261500 phenotype
neXtProtiNX_P11678
OpenTargetsiENSG00000121053
PharmGKBiPA27841

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG2408 Eukaryota
ENOG410XPZ3 LUCA
GeneTreeiENSGT00940000156009
HOGENOMiHOG000016084
InParanoidiP11678
KOiK10788
OMAiQLPPCFP
OrthoDBi276568at2759
PhylomeDBiP11678
TreeFamiTF314316

Enzyme and pathway databases

ReactomeiR-HSA-6798695 Neutrophil degranulation

Miscellaneous databases

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

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ChiTaRSi
EPX human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Eosinophil_peroxidase

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

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GenomeRNAii
8288

Protein Ontology

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PROi
PR:P11678

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000121053 Expressed in 49 organ(s), highest expression level in trabecular bone tissue
GenevisibleiP11678 HS

Family and domain databases

Gene3Di1.10.640.10, 1 hit
InterProiView protein in InterPro
IPR029599 EPX/EPO
IPR019791 Haem_peroxidase_animal
IPR010255 Haem_peroxidase_sf
IPR037120 Haem_peroxidase_sf_animal
PANTHERiPTHR11475:SF63 PTHR11475:SF63, 1 hit
PfamiView protein in Pfam
PF03098 An_peroxidase, 1 hit
PRINTSiPR00457 ANPEROXIDASE
SUPFAMiSSF48113 SSF48113, 1 hit
PROSITEiView protein in PROSITE
PS00435 PEROXIDASE_1, 1 hit
PS50292 PEROXIDASE_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPERE_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: P11678
Secondary accession number(s): Q4TVP3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: February 1, 1996
Last modified: May 8, 2019
This is version 189 of the entry and version 2 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  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. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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