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UniProtKB - P50336 (PPOX_HUMAN)

Entry version 185 (02 Dec 2020)
Sequence version 1 (01 Oct 1996)
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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%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

FADNote: Binds 1 FAD per subunit.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'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 (PPOX), Protoporphyrinogen oxidase (PPOX), Protoporphyrinogen oxidase, Protoporphyrinogen oxidase (PPOX), Protoporphyrinogen oxidase, 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 <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 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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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
  • oxidoreductase activity Source: GO_Central
  • oxygen-dependent protoporphyrinogen oxidase activity Source: UniProtKB
Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

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

Molecular functionOxidoreductase
Biological processHeme biosynthesis, Porphyrin biosynthesis
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:HS07011-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		1.3.3.4, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P50336

Reactome - a knowledgebase of biological pathways and processes

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

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P50336

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

More...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%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:
Protoporphyrinogen oxidase (EC:1.3.3.4)
Short name:
PPO
<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:PPOX
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...EuPathDBi		HostDB:ENSG00000143224.17

Human Gene Nomenclature Database

More...HGNCi		HGNC:9280, PPOX

Online Mendelian Inheritance in Man (OMIM)

More...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 & Seán O’Donoghue; 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.
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_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 PublicationsCorresponds to variant dbSNP:rs1361576529Ensembl.1
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%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>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.

More...GeneReviewsi		PPOX

MalaCards human disease database

More...MalaCardsi		PPOX
MIMi176200, phenotype

Open Targets

More...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

More...PharmGKBi		PA33608

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P50336, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL1926488

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PPOX

Domain mapping of disease mutations (DMDM)

More...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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001352701 – 477Protoporphyrinogen oxidaseAdd BLAST477

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P50336

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P50336

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P50336

MaxQB - The MaxQuant DataBase

More...MaxQBi		P50336

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

More...PaxDbi		P50336

PeptideAtlas

More...PeptideAtlasi		P50336

PRoteomics IDEntifications database

More...PRIDEi		P50336

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		56214

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P50336

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

More...PhosphoSitePlusi		P50336

SwissPalm database of S-palmitoylation events

More...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 right uterine tube and 219 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P50336, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P50336, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000143224, Low tissue specificity

<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. Homodimer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111492, 40 interactors

Protein interaction database and analysis system

More...IntActi		P50336, 30 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000356978

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P50336

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P50336, 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

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

3D structure databases

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

More...SMRi		P50336

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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/coproporphyrinogen oxidase family. Protoporphyrinogen oxidase subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1276, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00390000008744

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_009629_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P50336

Identification of Orthologs from Complete Genome Data

More...OMAi		IFDSCCF

Database of Orthologous Groups

More...OrthoDBi		1578484at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P50336

TreeFam database of animal gene trees

More...TreeFami		TF323479

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.50.50.60, 1 hit

Integrated resource of protein families, domains and functional sites

More...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

More...SUPFAMi		SSF51905, SSF51905, 1 hit

TIGRFAMs; a protein family database

More...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%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>Sequence (1+)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.

This entry has 1 described isoform and 17 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 17 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A494C0D4A0A494C0D4_HUMAN
Protoporphyrinogen oxidase
PPOX
379Annotation score:

Annotation score:2 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>
A0A494C146A0A494C146_HUMAN
Protoporphyrinogen oxidase
PPOX
435Annotation score:

Annotation score:2 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>
D3DVG2D3DVG2_HUMAN
Protoporphyrinogen oxidase
PPOX hCG_1766487
158Annotation 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>
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>
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>
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>
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>
There are more potential isoformsShow all

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 PublicationsCorresponds to variant dbSNP:rs1361576529Ensembl.1
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

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%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

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

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[»]
SMRiP50336
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111492, 40 interactors
IntActiP50336, 30 interactors
STRINGi9606.ENSP00000356978

Chemistry databases

BindingDBiP50336
ChEMBLiCHEMBL1926488

PTM databases

iPTMnetiP50336
PhosphoSitePlusiP50336
SwissPalmiP50336

Polymorphism and mutation databases

BioMutaiPPOX
DMDMi1709742

Proteomic databases

EPDiP50336
jPOSTiP50336
MassIVEiP50336
MaxQBiP50336
PaxDbiP50336
PeptideAtlasiP50336
PRIDEiP50336
ProteomicsDBi56214

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		34299, 252 antibodies

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
HPAiENSG00000143224, Low tissue specificity
MalaCardsiPPOX
MIMi176200, phenotype
600923, gene
neXtProtiNX_P50336
OpenTargetsiENSG00000143224
Orphaneti79473, Porphyria variegata
PharmGKBiPA33608

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG1276, Eukaryota
GeneTreeiENSGT00390000008744
HOGENOMiCLU_009629_2_1_1
InParanoidiP50336
OMAiIFDSCCF
OrthoDBi1578484at2759
PhylomeDBiP50336
TreeFamiTF323479

Enzyme and pathway databases

UniPathwayiUPA00251;UER00324
BioCyciMetaCyc:HS07011-MONOMER
BRENDAi1.3.3.4, 2681
PathwayCommonsiP50336
ReactomeiR-HSA-189451, Heme biosynthesis
SABIO-RKiP50336

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5498, 11 hits in 845 CRISPR screens

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
PharosiP50336, Tchem

Protein Ontology

More...PROi		PR:P50336
RNActiP50336, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000143224, Expressed in right uterine tube and 219 other tissues
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...

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 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%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: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 2, 2020
This is version 185 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 polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
  6. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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