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Protein

Protoporphyrinogen oxidase

Gene

PPOX

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

Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.3 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

FADNote: Binds 1 FAD per subunit.

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

This protein is involved in step 1 of the subpathway that synthesizes protoporphyrin-IX from protoporphyrinogen-IX.
Proteins known to be involved in this subpathway in this organism are:
  1. Protoporphyrinogen oxidase, Protoporphyrinogen oxidase, Protoporphyrinogen oxidase (PPOX), Protoporphyrinogen oxidase (PPOX)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes protoporphyrin-IX from protoporphyrinogen-IX, the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei42FAD; via amide nitrogen1 Publication1
Binding sitei257FAD; via amide nitrogen and carbonyl oxygen1 Publication1
Binding sitei449FAD; via amide nitrogen1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi9 – 14FAD1 Publication6
Nucleotide bindingi34 – 35FAD1 Publication2
Nucleotide bindingi57 – 60FAD1 Publication4
Nucleotide bindingi454 – 456FAD1 Publication3

<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

  • flavin adenine dinucleotide binding Source: UniProtKB
  • oxygen-dependent protoporphyrinogen oxidase activity Source: UniProtKB

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
Biological processHeme biosynthesis, Porphyrin biosynthesis
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS07011-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.3.3.4 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-189451 Heme biosynthesis

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P50336

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

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UniPathwayi
UPA00251;UER00324

<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:
Protoporphyrinogen oxidase (EC:1.3.3.4)
Short name:
PPO
<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:PPOX
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000143224.17

Human Gene Nomenclature Database

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HGNCi
HGNC:9280 PPOX

Online Mendelian Inheritance in Man (OMIM)

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MIMi
600923 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P50336

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

<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

Variegate porphyria (VP)30 Publications
The disease is caused by mutations affecting the gene represented in this entry. Mutations leading to severe PPOX deficiency cause the rare homozygous variant form of VP. Missense mutations that preserve 10%-25% of wild-type activity may not cause clinically overt VP in heterozygotes (PubMed:9811936). Mutations with intermediate effect on catalytic activity may cause VP, but with a low clinical penetrance (PubMed:10486317).2 Publications
Disease descriptionA form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. Variegate porphyria is the most common form of porphyria in South Africa. It is characterized by skin hyperpigmentation and hypertrichosis, abdominal pain, tachycardia, hypertension and neuromuscular disturbances. High fecal levels of protoporphyrin and coproporphyrin, increased urine uroporphyrins and iron overload are typical markers of the disease.
See also OMIM:176200
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_07037811G → D in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07037711G → S in VP. 1 Publication1
Natural variantiVAR_07037912I → T in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs28936677EnsemblClinVar.1
Natural variantiVAR_07038015L → F in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs769452432Ensembl.1
Natural variantiVAR_07038120H → P in VP; strongly decreases enzyme activity; more resistant to thermal denaturation than wild-type enzyme; abolishes mitochondrial protein targeting and localization. 4 PublicationsCorresponds to variant dbSNP:rs121918326EnsemblClinVar.1
Natural variantiVAR_07038234E → V in VP; decreases enzyme activity. 2 Publications1
Natural variantiVAR_07038338R → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07038440G → A in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07038540G → E in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs1317835140Ensembl.1
Natural variantiVAR_07038657G → R in VP. 1 PublicationCorresponds to variant dbSNP:rs764352037Ensembl.1
Natural variantiVAR_00368659R → W in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization; more resistant to thermal denaturation than wild-type enzyme. 8 PublicationsCorresponds to variant dbSNP:rs121918324EnsemblClinVar.1
Natural variantiVAR_07038773L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07038876S → F in VP; decreases enzyme activity. 1 Publication1
Natural variantiVAR_07038984V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07039085L → P in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070391106H → P in VP; strongly decreases enzyme activity;. 2 Publications1
Natural variantiVAR_070392138R → P in VP; slightly decreases enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs767419411Ensembl.1
Natural variantiVAR_070393139G → D in VP; strongly decreases enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs369381477Ensembl.1
Natural variantiVAR_070394143D → V in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_003687152R → C in VP; strongly decreases enzyme activity. 5 Publications1
Natural variantiVAR_070395154L → P in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_070396158V → L in VP. 1 Publication1
Natural variantiVAR_070397158V → M in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_003688168R → C in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization. 4 PublicationsCorresponds to variant dbSNP:rs121918325EnsemblClinVar.1
Natural variantiVAR_070398168R → H in VP; strongly decreases enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs41270025EnsemblClinVar.1
Natural variantiVAR_070399169G → E in VP; strongly decreases enzyme activity. 1 Publication1
Natural variantiVAR_070400172A → V in VP. 1 Publication1
Natural variantiVAR_070401178L → V in VP; strongly decreases enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs757473753Ensembl.1
Natural variantiVAR_070402205A → V in VP; no effect on enzyme activity. 2 Publications1
Natural variantiVAR_070403217R → C in VP; decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs751599052Ensembl.1
Natural variantiVAR_070404224W → G in VP; abolishes enzyme activity; impairs protein folding and/or stability. 3 Publications1
Natural variantiVAR_070405224W → R in VP. 1 Publication1
Natural variantiVAR_003689232G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 3 PublicationsCorresponds to variant dbSNP:rs121918323EnsemblClinVar.1
Natural variantiVAR_070406232G → S in VP. 1 Publication1
Natural variantiVAR_070407236L → S in VP. 1 Publication1
Natural variantiVAR_070408281Missing in VP. 1 Publication1
Natural variantiVAR_070409282V → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070410283I → N in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070411290V → M in VP. 1 Publication1
Natural variantiVAR_070412295L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070413330G → R in VP; strongly decreases enzyme activity. 3 Publications1
Natural variantiVAR_070414332G → A in VP; abolishes activity; impairs protein folding and/or stability. 3 Publications1
Natural variantiVAR_070415335V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 3 Publications1
Natural variantiVAR_070416348Y → C in VP; results in enzyme activity decrease; impairs protein folding and/or stability; more resistant to thermal denaturation than wild-type enzyme. 3 PublicationsCorresponds to variant dbSNP:rs900431442Ensembl.1
Natural variantiVAR_070417349D → A in VP; decreases enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs28936676EnsemblClinVar.1
Natural variantiVAR_070418350S → P in VP; abolishes activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070419358G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs374936130Ensembl.1
Natural variantiVAR_070420397A → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs141274934Ensembl.1
Natural variantiVAR_070421401L → F in VP; strongly decreases enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs776530007Ensembl.1
Natural variantiVAR_070422420P → R in VP. 1 Publication1
Natural variantiVAR_070423422Y → C in VP; decreases enzyme activity. 1 Publication1
Natural variantiVAR_070424433A → P in VP; decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070425444L → P in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_070426448G → R in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070427450S → P in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_070428453G → R in VP; strongly decreases enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs928944841Ensembl.1
Natural variantiVAR_070429453G → V in VP. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi59R → G: Decreases enzyme activity by 75%. 1 Publication1
Mutagenesisi59R → Q: Decreases enzyme activity by 90%. Strongly decreases affinity for protoporphyrinogen-IX. 1 Publication1
Mutagenesisi74L → P: Abolishes enzyme activity. Impairs protein folding and/or stability. 1 Publication1
Mutagenesisi97R → D: Decreases enzyme activity by 89%. Impairs protein folding and/or stability. 2 Publications1
Mutagenesisi166L → N: Decreases enzyme activity by 95%. 2 Publications1
Mutagenesisi169G → A: Decreases enzyme activity by 64%. 2 Publications1
Mutagenesisi284S → I: Decreases enzyme activity by 87%. Impairs protein folding and/or stability. 1 Publication1
Mutagenesisi290V → L: No effect on enzyme activity. 1 Publication1
Mutagenesisi331F → A: Decreases enzyme activity by 50%. 2 Publications1
Mutagenesisi334L → A: Decreases enzyme activity by 86%. 2 Publications1
Mutagenesisi347V → A: Decreases enzyme activity by 45%. 2 Publications1
Mutagenesisi368M → A: Decreases enzyme activity by 52%. 2 Publications1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
5498

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
PPOX

MalaCards human disease database

More...
MalaCardsi
PPOX
MIMi176200 phenotype

Open Targets

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OpenTargetsi
ENSG00000143224

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

More...
Orphaneti
79473 Porphyria variegata

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33608

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1926488

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PPOX

Domain mapping of disease mutations (DMDM)

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DMDMi
1709742

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001352701 – 477Protoporphyrinogen oxidaseAdd BLAST477

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P50336

MaxQB - The MaxQuant DataBase

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MaxQBi
P50336

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

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PaxDbi
P50336

PeptideAtlas

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PeptideAtlasi
P50336

PRoteomics IDEntifications database

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PRIDEi
P50336

ProteomicsDB human proteome resource

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ProteomicsDBi
56214

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P50336

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

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PhosphoSitePlusi
P50336

SwissPalm database of S-palmitoylation events

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SwissPalmi
P50336

<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

Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000143224 Expressed in 208 organ(s), highest expression level in right uterine tube

CleanEx database of gene expression profiles

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CleanExi
HS_PPOX

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P50336 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P50336 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA030123

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

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

Monomer. Homodimer.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111492, 21 interactors

Protein interaction database and analysis system

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IntActi
P50336, 21 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000343943

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P50336

<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

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P50336

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

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SMRi
P50336

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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 protoporphyrinogen oxidase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1276 Eukaryota
COG1232 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000008744

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000269479

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG001709

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P50336

KEGG Orthology (KO)

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KOi
K00231

Identification of Orthologs from Complete Genome Data

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OMAi
PMICGIC

Database of Orthologous Groups

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OrthoDBi
EOG091G08PW

Database for complete collections of gene phylogenies

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PhylomeDBi
P50336

TreeFam database of animal gene trees

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TreeFami
TF323479

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.50.50.60, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002937 Amino_oxidase
IPR036188 FAD/NAD-bd_sf
IPR004572 Protoporphyrinogen_oxidase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01593 Amino_oxidase, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51905 SSF51905, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR00562 proto_IX_ox, 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

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

This entry has 1 described isoform and 9 potential isoforms that are computationally mapped.Show allAlign All

P50336-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGRTVVVLGG GISGLAASYH LSRAPCPPKV VLVESSERLG GWIRSVRGPN
60 70 80 90 100
GAIFELGPRG IRPAGALGAR TLLLVSELGL DSEVLPVRGD HPAAQNRFLY
110 120 130 140 150
VGGALHALPT GLRGLLRPSP PFSKPLFWAG LRELTKPRGK EPDETVHSFA
160 170 180 190 200
QRRLGPEVAS LAMDSLCRGV FAGNSRELSI RSCFPSLFQA EQTHRSILLG
210 220 230 240 250
LLLGAGRTPQ PDSALIRQAL AERWSQWSLR GGLEMLPQAL ETHLTSRGVS
260 270 280 290 300
VLRGQPVCGL SLQAEGRWKV SLRDSSLEAD HVISAIPASV LSELLPAEAA
310 320 330 340 350
PLARALSAIT AVSVAVVNLQ YQGAHLPVQG FGHLVPSSED PGVLGIVYDS
360 370 380 390 400
VAFPEQDGSP PGLRVTVMLG GSWLQTLEAS GCVLSQELFQ QRAQEAAATQ
410 420 430 440 450
LGLKEMPSHC LVHLHKNCIP QYTLGHWQKL ESARQFLTAH RLPLTLAGAS
460 470
YEGVAVNDCI ESGRQAAVSV LGTEPNS
Length:477
Mass (Da):50,765
Last modified:October 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2444DEAC2E6C33EE
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 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5H1I5F5H1I5_HUMAN
Protoporphyrinogen oxidase
PPOX
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>
F5GZT7F5GZT7_HUMAN
Protoporphyrinogen oxidase
PPOX
185Annotation 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>
H0YFP3H0YFP3_HUMAN
Protoporphyrinogen oxidase
PPOX
230Annotation 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>
H0YFE1H0YFE1_HUMAN
Protoporphyrinogen oxidase
PPOX
161Annotation 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>
A0A1W2PRF9A0A1W2PRF9_HUMAN
Protoporphyrinogen oxidase
PPOX
184Annotation 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>
A0A1W2PNH4A0A1W2PNH4_HUMAN
Protoporphyrinogen oxidase
PPOX
78Annotation 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>
A0A1W2PPA5A0A1W2PPA5_HUMAN
Protoporphyrinogen oxidase
PPOX
188Annotation 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>
A0A1W2PQM0A0A1W2PQM0_HUMAN
Protoporphyrinogen oxidase
PPOX
140Annotation 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>
F5H825F5H825_HUMAN
Protoporphyrinogen oxidase
PPOX
156Annotation 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07037811G → D in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07037711G → S in VP. 1 Publication1
Natural variantiVAR_07037912I → T in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs28936677EnsemblClinVar.1
Natural variantiVAR_07038015L → F in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs769452432Ensembl.1
Natural variantiVAR_07038120H → P in VP; strongly decreases enzyme activity; more resistant to thermal denaturation than wild-type enzyme; abolishes mitochondrial protein targeting and localization. 4 PublicationsCorresponds to variant dbSNP:rs121918326EnsemblClinVar.1
Natural variantiVAR_07038234E → V in VP; decreases enzyme activity. 2 Publications1
Natural variantiVAR_07038338R → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07038440G → A in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07038540G → E in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs1317835140Ensembl.1
Natural variantiVAR_07038657G → R in VP. 1 PublicationCorresponds to variant dbSNP:rs764352037Ensembl.1
Natural variantiVAR_00368659R → W in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization; more resistant to thermal denaturation than wild-type enzyme. 8 PublicationsCorresponds to variant dbSNP:rs121918324EnsemblClinVar.1
Natural variantiVAR_07038773L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07038876S → F in VP; decreases enzyme activity. 1 Publication1
Natural variantiVAR_07038984V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07039085L → P in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070391106H → P in VP; strongly decreases enzyme activity;. 2 Publications1
Natural variantiVAR_070392138R → P in VP; slightly decreases enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs767419411Ensembl.1
Natural variantiVAR_070393139G → D in VP; strongly decreases enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs369381477Ensembl.1
Natural variantiVAR_070394143D → V in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_003687152R → C in VP; strongly decreases enzyme activity. 5 Publications1
Natural variantiVAR_070395154L → P in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_070396158V → L in VP. 1 Publication1
Natural variantiVAR_070397158V → M in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_003688168R → C in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization. 4 PublicationsCorresponds to variant dbSNP:rs121918325EnsemblClinVar.1
Natural variantiVAR_070398168R → H in VP; strongly decreases enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs41270025EnsemblClinVar.1
Natural variantiVAR_070399169G → E in VP; strongly decreases enzyme activity. 1 Publication1
Natural variantiVAR_070400172A → V in VP. 1 Publication1
Natural variantiVAR_070401178L → V in VP; strongly decreases enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs757473753Ensembl.1
Natural variantiVAR_070402205A → V in VP; no effect on enzyme activity. 2 Publications1
Natural variantiVAR_070403217R → C in VP; decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs751599052Ensembl.1
Natural variantiVAR_070404224W → G in VP; abolishes enzyme activity; impairs protein folding and/or stability. 3 Publications1
Natural variantiVAR_070405224W → R in VP. 1 Publication1
Natural variantiVAR_003689232G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 3 PublicationsCorresponds to variant dbSNP:rs121918323EnsemblClinVar.1
Natural variantiVAR_070406232G → S in VP. 1 Publication1
Natural variantiVAR_070407236L → S in VP. 1 Publication1
Natural variantiVAR_034395256P → R Found in patients with the homozygous variant of variegate porphyria; unknown pathological significance; reported as a polymorphism in some Western European populations; the variant results in reduction of activity in a prokariotyc expression system but has normal activity when expressed in an eukaryotic system. 2 PublicationsCorresponds to variant dbSNP:rs12735723EnsemblClinVar.1
Natural variantiVAR_070408281Missing in VP. 1 Publication1
Natural variantiVAR_070409282V → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070410283I → N in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070411290V → M in VP. 1 Publication1
Natural variantiVAR_070412295L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_003690304R → H3 PublicationsCorresponds to variant dbSNP:rs36013429EnsemblClinVar.1
Natural variantiVAR_070413330G → R in VP; strongly decreases enzyme activity. 3 Publications1
Natural variantiVAR_070414332G → A in VP; abolishes activity; impairs protein folding and/or stability. 3 Publications1
Natural variantiVAR_070415335V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 3 Publications1
Natural variantiVAR_070416348Y → C in VP; results in enzyme activity decrease; impairs protein folding and/or stability; more resistant to thermal denaturation than wild-type enzyme. 3 PublicationsCorresponds to variant dbSNP:rs900431442Ensembl.1
Natural variantiVAR_070417349D → A in VP; decreases enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs28936676EnsemblClinVar.1
Natural variantiVAR_070418350S → P in VP; abolishes activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070419358G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs374936130Ensembl.1
Natural variantiVAR_070420397A → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs141274934Ensembl.1
Natural variantiVAR_070421401L → F in VP; strongly decreases enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs776530007Ensembl.1
Natural variantiVAR_070422420P → R in VP. 1 Publication1
Natural variantiVAR_070423422Y → C in VP; decreases enzyme activity. 1 Publication1
Natural variantiVAR_070424433A → P in VP; decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070425444L → P in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_070426448G → R in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070427450S → P in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_070428453G → R in VP; strongly decreases enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs928944841Ensembl.1
Natural variantiVAR_070429453G → V in VP. 1 Publication1

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
D38537 mRNA Translation: BAA07538.1
U26446 mRNA Translation: AAA67690.1
X99450 Genomic DNA No translation available.
AL590714 Genomic DNA No translation available.
CH471121 Genomic DNA Translation: EAW52636.1
CH471121 Genomic DNA Translation: EAW52639.1
CH471121 Genomic DNA Translation: EAW52641.1
BC002357 mRNA Translation: AAH02357.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS1221.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC4971 A56449

NCBI Reference Sequences

More...
RefSeqi
NP_000300.1, NM_000309.3
NP_001116236.1, NM_001122764.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.517373

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000352210; ENSP00000343943; ENSG00000143224
ENST00000367999; ENSP00000356978; ENSG00000143224

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5498

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5498

UCSC genome browser

More...
UCSCi
uc001fyg.3 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

Wikipedia

Protoporphyrinogen oxidase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38537 mRNA Translation: BAA07538.1
U26446 mRNA Translation: AAA67690.1
X99450 Genomic DNA No translation available.
AL590714 Genomic DNA No translation available.
CH471121 Genomic DNA Translation: EAW52636.1
CH471121 Genomic DNA Translation: EAW52639.1
CH471121 Genomic DNA Translation: EAW52641.1
BC002357 mRNA Translation: AAH02357.1
CCDSiCCDS1221.1
PIRiJC4971 A56449
RefSeqiNP_000300.1, NM_000309.3
NP_001116236.1, NM_001122764.1
UniGeneiHs.517373

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
3NKSX-ray1.90A1-477[»]
4IVMX-ray2.77B1-477[»]
4IVOX-ray2.60B1-477[»]
ProteinModelPortaliP50336
SMRiP50336
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111492, 21 interactors
IntActiP50336, 21 interactors
STRINGi9606.ENSP00000343943

Chemistry databases

BindingDBiP50336
ChEMBLiCHEMBL1926488

PTM databases

iPTMnetiP50336
PhosphoSitePlusiP50336
SwissPalmiP50336

Polymorphism and mutation databases

BioMutaiPPOX
DMDMi1709742

Proteomic databases

EPDiP50336
MaxQBiP50336
PaxDbiP50336
PeptideAtlasiP50336
PRIDEiP50336
ProteomicsDBi56214

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000352210; ENSP00000343943; ENSG00000143224
ENST00000367999; ENSP00000356978; ENSG00000143224
GeneIDi5498
KEGGihsa:5498
UCSCiuc001fyg.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5498
DisGeNETi5498
EuPathDBiHostDB:ENSG00000143224.17

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PPOX
GeneReviewsiPPOX
HGNCiHGNC:9280 PPOX
HPAiHPA030123
MalaCardsiPPOX
MIMi176200 phenotype
600923 gene
neXtProtiNX_P50336
OpenTargetsiENSG00000143224
Orphaneti79473 Porphyria variegata
PharmGKBiPA33608

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1276 Eukaryota
COG1232 LUCA
GeneTreeiENSGT00390000008744
HOGENOMiHOG000269479
HOVERGENiHBG001709
InParanoidiP50336
KOiK00231
OMAiPMICGIC
OrthoDBiEOG091G08PW
PhylomeDBiP50336
TreeFamiTF323479

Enzyme and pathway databases

UniPathwayi
UPA00251;UER00324

BioCyciMetaCyc:HS07011-MONOMER
BRENDAi1.3.3.4 2681
ReactomeiR-HSA-189451 Heme biosynthesis
SABIO-RKiP50336

Miscellaneous databases

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

More...
ChiTaRSi
PPOX human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PPOX

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

More...
GenomeRNAii
5498

Protein Ontology

More...
PROi
PR:P50336

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000143224 Expressed in 208 organ(s), highest expression level in right uterine tube
CleanExiHS_PPOX
ExpressionAtlasiP50336 baseline and differential
GenevisibleiP50336 HS

Family and domain databases

Gene3Di3.50.50.60, 1 hit
InterProiView protein in InterPro
IPR002937 Amino_oxidase
IPR036188 FAD/NAD-bd_sf
IPR004572 Protoporphyrinogen_oxidase
PfamiView protein in Pfam
PF01593 Amino_oxidase, 1 hit
SUPFAMiSSF51905 SSF51905, 1 hit
TIGRFAMsiTIGR00562 proto_IX_ox, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiPPOX_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: P50336
Secondary accession number(s): D3DVG0, Q5VTW8
<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, 1996
Last sequence update: October 1, 1996
Last modified: December 5, 2018
This is version 173 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  7. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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