UniProtKB - P50336 (PPOX_HUMAN)
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>sp|P50336|PPOX_HUMAN Protoporphyrinogen oxidase OS=Homo sapiens OX=9606 GN=PPOX PE=1 SV=1 MGRTVVVLGGGISGLAASYHLSRAPCPPKVVLVESSERLGGWIRSVRGPNGAIFELGPRG IRPAGALGARTLLLVSELGLDSEVLPVRGDHPAAQNRFLYVGGALHALPTGLRGLLRPSP PFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSI RSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERWSQWSLRGGLEMLPQAL ETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAA PLARALSAITAVSVAVVNLQYQGAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPEQDGSP PGLRVTVMLGGSWLQTLEASGCVLSQELFQQRAQEAAATQLGLKEMPSHCLVHLHKNCIP QYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLGTEPNSCommunity curation ()Add a publicationFeedback
Protoporphyrinogen oxidase
PPOX
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>Select a section on the left to see content.
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.1"Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in vivo of a hemG mutant of Escherichia coli."
Nishimura K., Taketani S., Inokuchi H.
J. Biol. Chem. 270:8076-8080(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION. - Ref.9"Structural insight into human variegate porphyria disease."
Qin X., Tan Y., Wang L., Wang Z., Wang B., Wen X., Yang G., Xi Z., Shen Y.
FASEB J. 25:653-664(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FAD AND ACIFLUORFEN, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, CHARACTERIZATION OF VARIANTS VP ASP-11; THR-12; PHE-15; PRO-20; PRO-38; ALA-40; GLU-40; TRP-59; PRO-73; GLY-84; PRO-85; PRO-106; PRO-138; ASP-139; VAL-143; CYS-152; PRO-154; MET-158; HIS-168; VAL-178; VAL-205; CYS-217; GLY-224; ARG-232; ASP-282; ASN-283; PRO-295; ARG-330; ALA-332; GLY-335; CYS-348; ALA-349; PRO-350; ARG-358; ASP-397; PHE-401; PRO-433; PRO-444; ARG-448; PRO-450 AND ARG-453, MUTAGENESIS OF LEU-74; ARG-97; LEU-166; GLY-169; SER-284; VAL-290; PHE-331; LEU-334; VAL-347 AND MET-368. - Ref.10"Quantitative structural insight into human variegate porphyria disease."
Wang B., Wen X., Qin X., Wang Z., Tan Y., Shen Y., Xi Z.
J. Biol. Chem. 288:11731-11740(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF MUTANTS GLY-59 AND GLN-59 IN COMPLEXES WITH FAD AND ACIFLUORFEN, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-59; ARG-97; LEU-166; GLY-169; PHE-331; LEU-334; VAL-347 AND MET-368, CHARACTERIZATION OF VARIANTS VP TRP-59; HIS-168; ARG-330; GLY-335; ALA-349; PHE-401 AND ARG-453.
<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
- 3 O2EC:1.3.3.4
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Manual assertion based on experiment ini
- Ref.9"Structural insight into human variegate porphyria disease."
Qin X., Tan Y., Wang L., Wang Z., Wang B., Wen X., Yang G., Xi Z., Shen Y.
FASEB J. 25:653-664(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FAD AND ACIFLUORFEN, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, CHARACTERIZATION OF VARIANTS VP ASP-11; THR-12; PHE-15; PRO-20; PRO-38; ALA-40; GLU-40; TRP-59; PRO-73; GLY-84; PRO-85; PRO-106; PRO-138; ASP-139; VAL-143; CYS-152; PRO-154; MET-158; HIS-168; VAL-178; VAL-205; CYS-217; GLY-224; ARG-232; ASP-282; ASN-283; PRO-295; ARG-330; ALA-332; GLY-335; CYS-348; ALA-349; PRO-350; ARG-358; ASP-397; PHE-401; PRO-433; PRO-444; ARG-448; PRO-450 AND ARG-453, MUTAGENESIS OF LEU-74; ARG-97; LEU-166; GLY-169; SER-284; VAL-290; PHE-331; LEU-334; VAL-347 AND MET-368. - Ref.10"Quantitative structural insight into human variegate porphyria disease."
Wang B., Wen X., Qin X., Wang Z., Tan Y., Shen Y., Xi Z.
J. Biol. Chem. 288:11731-11740(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF MUTANTS GLY-59 AND GLN-59 IN COMPLEXES WITH FAD AND ACIFLUORFEN, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-59; ARG-97; LEU-166; GLY-169; PHE-331; LEU-334; VAL-347 AND MET-368, CHARACTERIZATION OF VARIANTS VP TRP-59; HIS-168; ARG-330; GLY-335; ALA-349; PHE-401 AND ARG-453.
- Search proteins in UniProtKB for this EC number.
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Manual assertion based on experiment ini
- Ref.9"Structural insight into human variegate porphyria disease."
Qin X., Tan Y., Wang L., Wang Z., Wang B., Wen X., Yang G., Xi Z., Shen Y.
FASEB J. 25:653-664(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FAD AND ACIFLUORFEN, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, CHARACTERIZATION OF VARIANTS VP ASP-11; THR-12; PHE-15; PRO-20; PRO-38; ALA-40; GLU-40; TRP-59; PRO-73; GLY-84; PRO-85; PRO-106; PRO-138; ASP-139; VAL-143; CYS-152; PRO-154; MET-158; HIS-168; VAL-178; VAL-205; CYS-217; GLY-224; ARG-232; ASP-282; ASN-283; PRO-295; ARG-330; ALA-332; GLY-335; CYS-348; ALA-349; PRO-350; ARG-358; ASP-397; PHE-401; PRO-433; PRO-444; ARG-448; PRO-450 AND ARG-453, MUTAGENESIS OF LEU-74; ARG-97; LEU-166; GLY-169; SER-284; VAL-290; PHE-331; LEU-334; VAL-347 AND MET-368. - Ref.10"Quantitative structural insight into human variegate porphyria disease."
Wang B., Wen X., Qin X., Wang Z., Tan Y., Shen Y., Xi Z.
J. Biol. Chem. 288:11731-11740(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF MUTANTS GLY-59 AND GLN-59 IN COMPLEXES WITH FAD AND ACIFLUORFEN, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-59; ARG-97; LEU-166; GLY-169; PHE-331; LEU-334; VAL-347 AND MET-368, CHARACTERIZATION OF VARIANTS VP TRP-59; HIS-168; ARG-330; GLY-335; ALA-349; PHE-401 AND ARG-453.
Source: Rhea- Search for this reaction in UniProtKB.
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3O2- Search proteins in UniProtKB for this molecule.
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+protoporphyrinogen IX- Search proteins in UniProtKB for this molecule.
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+protoporphyrin IX- Search proteins in UniProtKB for this molecule.
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<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
- Search proteins in UniProtKB for this molecule.
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- See the description of this molecule in ChEBI.
<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:
- Protoporphyrinogen oxidase (PPOX), Protoporphyrinogen oxidase (PPOX), Protoporphyrinogen oxidase, Protoporphyrinogen oxidase (PPOX), Protoporphyrinogen oxidase, Protoporphyrinogen oxidase (PPOX)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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 sitei | 42 | FAD; via amide nitrogen1 Publication Manual assertion based on experiment ini
| 1 | |
Binding sitei | 257 | FAD; via amide nitrogen and carbonyl oxygen1 Publication Manual assertion based on experiment ini
| 1 | |
Binding sitei | 449 | FAD; via amide nitrogen1 Publication Manual assertion based on experiment ini
| 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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 bindingi | 9 – 14 | FAD1 Publication Manual assertion based on experiment ini
| 6 | |
Nucleotide bindingi | 34 – 35 | FAD1 Publication Manual assertion based on experiment ini
| 2 | |
Nucleotide bindingi | 57 – 60 | FAD1 Publication Manual assertion based on experiment ini
| 4 | |
Nucleotide bindingi | 454 – 456 | FAD1 Publication Manual assertion based on experiment ini
| 3 |
<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
<p>Traceable Author Statement</p>
<p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p>
Traceable author statementi
- Ref.1"Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in vivo of a hemG mutant of Escherichia coli."
Nishimura K., Taketani S., Inokuchi H.
J. Biol. Chem. 270:8076-8080(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
- oxidoreductase activity Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- oxygen-dependent protoporphyrinogen oxidase activity Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.1"Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in vivo of a hemG mutant of Escherichia coli."
Nishimura K., Taketani S., Inokuchi H.
J. Biol. Chem. 270:8076-8080(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
GO - Biological processi
- heme biosynthetic process Source: UniProtKBInferred from direct assayi
- Ref.1"Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in vivo of a hemG mutant of Escherichia coli."
Nishimura K., Taketani S., Inokuchi H.
J. Biol. Chem. 270:8076-8080(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
- oxidation-reduction process Source: UniProtKBInferred from direct assayi
- Ref.1"Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in vivo of a hemG mutant of Escherichia coli."
Nishimura K., Taketani S., Inokuchi H.
J. Biol. Chem. 270:8076-8080(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
- porphyrin-containing compound biosynthetic process Source: UniProtKBInferred from direct assayi
- Ref.1"Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in vivo of a hemG mutant of Escherichia coli."
Nishimura K., Taketani S., Inokuchi H.
J. Biol. Chem. 270:8076-8080(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
- protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
- response to drug Source: Ensembl
<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 function | Oxidoreductase |
Biological process | Heme biosynthesis, Porphyrin biosynthesis |
Ligand | FAD, 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>Organismi | Homo 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 identifieri | 9606 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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 |
|
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
Mitochondrion
- Mitochondrion inner membrane By similarity; Peripheral membrane protein By similarity; Intermembrane side By similarity
Mitochondrion
- integral component of mitochondrial inner membrane Source: Ensembl
- intrinsic component of mitochondrial inner membrane Source: UniProtKB
- mitochondrial intermembrane space Source: Reactome
- mitochondrial membrane Source: UniProtKB
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- Ref.1"Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in vivo of a hemG mutant of Escherichia coli."
Nishimura K., Taketani S., Inokuchi H.
J. Biol. Chem. 270:8076-8080(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
- mitochondrion Source: GO_CentralInferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
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 PublicationsManual assertion based on experiment ini
- Ref.9"Structural insight into human variegate porphyria disease."
Qin X., Tan Y., Wang L., Wang Z., Wang B., Wen X., Yang G., Xi Z., Shen Y.
FASEB J. 25:653-664(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FAD AND ACIFLUORFEN, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, CHARACTERIZATION OF VARIANTS VP ASP-11; THR-12; PHE-15; PRO-20; PRO-38; ALA-40; GLU-40; TRP-59; PRO-73; GLY-84; PRO-85; PRO-106; PRO-138; ASP-139; VAL-143; CYS-152; PRO-154; MET-158; HIS-168; VAL-178; VAL-205; CYS-217; GLY-224; ARG-232; ASP-282; ASN-283; PRO-295; ARG-330; ALA-332; GLY-335; CYS-348; ALA-349; PRO-350; ARG-358; ASP-397; PHE-401; PRO-433; PRO-444; ARG-448; PRO-450 AND ARG-453, MUTAGENESIS OF LEU-74; ARG-97; LEU-166; GLY-169; SER-284; VAL-290; PHE-331; LEU-334; VAL-347 AND MET-368. - Ref.10"Quantitative structural insight into human variegate porphyria disease."
Wang B., Wen X., Qin X., Wang Z., Tan Y., Shen Y., Xi Z.
J. Biol. Chem. 288:11731-11740(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF MUTANTS GLY-59 AND GLN-59 IN COMPLEXES WITH FAD AND ACIFLUORFEN, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-59; ARG-97; LEU-166; GLY-169; PHE-331; LEU-334; VAL-347 AND MET-368, CHARACTERIZATION OF VARIANTS VP TRP-59; HIS-168; ARG-330; GLY-335; ALA-349; PHE-401 AND ARG-453. - Ref.11"Mutations in the protoporphyrinogen oxidase gene in patients with variegate porphyria."
Deybach J.-C., Puy H., Robreau A.-M., Lamoril J., da Silva V., Grandchamp B., Nordmann Y.
Hum. Mol. Genet. 5:407-410(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VP ARG-232, VARIANT HIS-304. - Ref.12"Identification of three mutations and associated haplotypes in the protoporphyrinogen oxidase gene in South African families with variegate porphyria."
Warnich L., Kotze M.J., Groenewald I.M., Groenewald J.Z., van Brakel M.G., van Heerden C.J., de Villiers J.N., van de Ven W.J., Schoenmakers E.F., Taketani S., Retief A.E.
Hum. Mol. Genet. 5:981-984(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS VP PRO-20; TRP-59 AND CYS-168. - Ref.13"A R59W mutation in human protoporphyrinogen oxidase results in decreased enzyme activity and is prevalent in South Africans with variegate porphyria."
Meissner P.N., Dailey T.A., Hift R.J., Ziman M., Corrigall A.V., Roberts A.G., Meissner D.M., Kirsch R.E., Dailey H.A.
Nat. Genet. 13:95-97(1996) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS VP TRP-59 AND CYS-168. - Ref.14"The genetic basis of 'Scarsdale Gourmet Diet' variegate porphyria: a missense mutation in the protoporphyrinogen oxidase gene."
Frank J., Poh-Fitzpatrick M.B., King L.E. Jr., Christiano A.M.
Arch. Dermatol. Res. 290:441-445(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VP CYS-152. - Ref.15"Molecular basis of variegate porphyria: a missense mutation in the protoporphyrinogen oxidase gene."
Frank J., Lam H., Zaider E., Poh-Fitzpatrick M., Christiano A.M.
J. Med. Genet. 35:244-247(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VP PRO-450. - Ref.16"Molecular characterization of homozygous variegate porphyria."
Roberts A.G., Puy H., Dailey T.A., Morgan R.R., Whatley S.D., Dailey H.A., Martasek P., Nordmann Y., Deybach J.C., Elder G.H.
Hum. Mol. Genet. 7:1921-1925(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS VP GLU-169; ALA-349; ARG-358 AND PRO-433, CHARACTERIZATION OF VARIANTS VP GLU-169; ALA-349; ARG-358 AND PRO-433. - Ref.17"Variegate porphyria in Western Europe: identification of PPOX gene mutations in 104 families, extent of allelic heterogeneity, and absence of correlation between phenotype and type of mutation."
Whatley S.D., Puy H., Morgan R.R., Robreau A.M., Roberts A.G., Nordmann Y., Elder G.H., Deybach J.C.
Am. J. Hum. Genet. 65:984-994(1999) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARG-256 AND HIS-304, VARIANTS VP PRO-38; GLU-40; PRO-73; GLY-84; PRO-85; VAL-143; CYS-152; PRO-154; MET-158; HIS-168; VAL-172; ARG-232; HIS-281 DEL; ASP-282; PRO-295; GLY-335; PRO-350; PRO-444; ARG-453 AND VAL-453. - Ref.18"Three novel mutations in the protoporphyrinogen oxidase gene in Japanese patients with variegate porphyria."
Maeda N., Horie Y., Sasaki Y., Adachi K., Nanba E., Nishida K., Saigo R., Nakagawa M., Kawasaki H., Kudo Y., Kondo M.
Clin. Biochem. 33:495-500(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VP ARG-448. - Ref.19"Two new mutations (H106P and L178V) in the protoporphyrinogen oxidase gene in Argentinean patients with variegate porphyria."
De Siervi A., Parera V.E., del C Batlle A.M., Rossetti M.V.
Hum. Mutat. 16:532-532(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS VP PRO-106 AND VAL-178. - Ref.20"Homozygous variegate porphyria in South Africa: genotypic analysis in two cases."
Corrigall A.V., Hift R.J., Davids L.M., Hancock V., Meissner D., Kirsch R.E., Meissner P.N.
Mol. Genet. Metab. 69:323-330(2000) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS VP TRP-59; PRO-138 AND CYS-348. - Ref.21"Homozygous variegate porphyria: 20 y follow-up and characterization of molecular defect."
Kauppinen R., Timonen K., von und zu Fraunberg M., Laitinen E., Ahola H., Tenhunen R., Taketani S., Mustajoki P.
J. Invest. Dermatol. 116:610-613(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VP THR-12, VARIANT ARG-256, CHARACTERIZATION OF VARIANT VP THR-12, CHARACTERIZATION OF VARIANT ARG-256. - Ref.22"A spectrum of novel mutations in the protoporphyrinogen oxidase gene in 13 families with variegate porphyria."
Frank J., Jugert F.K., Merk H.F., Kalka K., Goerz G., Anderson K., Bickers D.R., Poh-Fitzpatrick M.B., Christiano A.M.
J. Invest. Dermatol. 116:821-823(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VP SER-11. - Ref.23"Identification of the first variegate porphyria mutation in an indigenous black South African and further evidence for heterogeneity in variegate porphyria."
Corrigall A.V., Hift R.J., Davids L.M., Hancock V., Meissner D., Kirsch R.E., Meissner P.N.
Mol. Genet. Metab. 73:91-96(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS VP PHE-15 AND MET-290. - Ref.24"Expression and characterization of six mutations in the protoporphyrinogen oxidase gene among Finnish variegate porphyria patients."
von und zu Fraunberg M., Tenhunen R., Kauppinen R.
Mol. Med. 7:320-328(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS VP CYS-152 AND PHE-401, CHARACTERIZATION OF VARIANT VP CYS-152. - Ref.25"Variegate porphyria in Western Australian Aboriginal patients."
Rossi E., Chin C.Y., Beilby J.P., Waso H.F., Warnich L.
Intern. Med. J. 32:445-450(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS VP TRP-59; CYS-217 AND SER-236. - Ref.26"Kinetic and physical characterisation of recombinant wild-type and mutant human protoporphyrinogen oxidases."
Maneli M.H., Corrigall A.V., Klump H.H., Davids L.M., Kirsch R.E., Meissner P.N.
Biochim. Biophys. Acta 1650:10-21(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS VP PRO-20; TRP-59; CYS-168 AND CYS-348. - Ref.27"Nine novel mutations in the protoporphyrinogen oxidase gene in Swedish families with variegate porphyria."
Wiman A., Harper P., Floderus Y.
Clin. Genet. 64:122-130(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS VP CYS-152; LEU-158; VAL-205 AND ARG-330. - Ref.28"Genetic analysis of variegate porphyria (VP) in Italy: identification of six novel mutations in the protoporphyrinogen oxidase (PPOX) gene."
D'Amato M., Bonuglia M., Barile S., Griso D., Macri A., Biolcati G.
Hum. Mutat. 21:448-448(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VP ASN-283. - Ref.29"Modulation of penetrance by the wild-type allele in dominantly inherited erythropoietic protoporphyria and acute hepatic porphyrias."
Gouya L., Puy H., Robreau A.-M., Lyoumi S., Lamoril J., Da Silva V., Grandchamp B., Deybach J.-C.
Hum. Genet. 114:256-262(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VP ALA-40. - Ref.30"A Chilean boy with severe photosensitivity and finger shortening: the first case of homozygous variegate porphyria in South America."
Poblete-Gutierrez P., Wolff C., Farias R., Frank J.
Br. J. Dermatol. 154:368-371(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VP SER-232. - Ref.31"Mitochondrial targeting of human protoporphyrinogen oxidase."
Davids L.M., Corrigall A.V., Meissner P.N.
Cell Biol. Int. 30:416-426(2006) [PubMed] [Europe PMC] [Abstract]Cited for: CHARACTERIZATION OF VARIANTS VP PRO-20; TRP-59 AND CYS-168. - Ref.32"Genetic studies in variegate porphyria in Spain. Identification of gene mutations and family study for carrier detection."
Lecha M., Badenas C., Puig S., Orfila J., Mila M., To-Figueras J., Munoz C., Mercader P., Herrero C.
J. Eur. Acad. Dermatol. Venereol. 20:974-979(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VP ARG-224. - Ref.33"Swiss patients with variegate porphyria have unique mutations."
Schneider-Yin X., Minder E.I.
Swiss. Med. Wkly. 136:515-519(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VP ASP-11. - Ref.34"Novel human pathological mutations. Gene symbol: PPOX. Disease: porphyria, variegate."
Ausenda S., Di Pierro E., Brancaleoni V., Besana V., Cappellini M.D.
Hum. Genet. 122:417-417(2007) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VP ASP-139. - Ref.35"Genetic and biochemical studies in Argentinean patients with variegate porphyria."
Rossetti M.V., Granata B.X., Giudice J., Parera V.E., Batlle A.
BMC Med. Genet. 9:54-54(2008) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS VP VAL-34; GLY-224 AND ALA-332. - Ref.36"Novel human pathological mutations. Gene symbol: PPOX. Disease: porphyria, variegate."
Ausenda S., Moriondo V., Marchini S., Besana V., Di Pierro E., Brancaleoni V., Ventura P., Rocchi E., Cappellini M.D.
Hum. Genet. 125:344-344(2009) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT VP ASP-397. - Ref.37"Functional characterization of five protoporphyrinogen oxidase missense mutations found in Argentinean variegate porphyria patients."
Mendez M., Granata B.X., Jimenez M.J., Parera V.E., Batlle A., de Salamanca R.E., Rossetti M.V.
JIMD Rep. 4:91-97(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS VP VAL-34; PHE-76; GLY-224; ALA-332 AND CYS-422, CHARACTERIZATION OF VARIANTS VP VAL-34; PHE-76; GLY-224; ALA-332 AND CYS-422. - Ref.38"Homozygous variegate porphyria presenting with developmental and language delay in childhood."
Pinder V.A., Holden S.T., Deshpande C., Siddiqui A., Mellerio J.E., Wraige E., Powell A.M.
Clin. Exp. Dermatol. 38:737-740(2013) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS VP ARG-57 AND ARG-420.
Qin X., Tan Y., Wang L., Wang Z., Wang B., Wen X., Yang G., Xi Z., Shen Y.
FASEB J. 25:653-664(2011) [PubMed] [Europe PMC] [Abstract]
Wang B., Wen X., Qin X., Wang Z., Tan Y., Shen Y., Xi Z.
J. Biol. Chem. 288:11731-11740(2013) [PubMed] [Europe PMC] [Abstract]
Deybach J.-C., Puy H., Robreau A.-M., Lamoril J., da Silva V., Grandchamp B., Nordmann Y.
Hum. Mol. Genet. 5:407-410(1996) [PubMed] [Europe PMC] [Abstract]
Warnich L., Kotze M.J., Groenewald I.M., Groenewald J.Z., van Brakel M.G., van Heerden C.J., de Villiers J.N., van de Ven W.J., Schoenmakers E.F., Taketani S., Retief A.E.
Hum. Mol. Genet. 5:981-984(1996) [PubMed] [Europe PMC] [Abstract]
Meissner P.N., Dailey T.A., Hift R.J., Ziman M., Corrigall A.V., Roberts A.G., Meissner D.M., Kirsch R.E., Dailey H.A.
Nat. Genet. 13:95-97(1996) [PubMed] [Europe PMC] [Abstract]
Frank J., Poh-Fitzpatrick M.B., King L.E. Jr., Christiano A.M.
Arch. Dermatol. Res. 290:441-445(1998) [PubMed] [Europe PMC] [Abstract]
Frank J., Lam H., Zaider E., Poh-Fitzpatrick M., Christiano A.M.
J. Med. Genet. 35:244-247(1998) [PubMed] [Europe PMC] [Abstract]
Roberts A.G., Puy H., Dailey T.A., Morgan R.R., Whatley S.D., Dailey H.A., Martasek P., Nordmann Y., Deybach J.C., Elder G.H.
Hum. Mol. Genet. 7:1921-1925(1998) [PubMed] [Europe PMC] [Abstract]
Whatley S.D., Puy H., Morgan R.R., Robreau A.M., Roberts A.G., Nordmann Y., Elder G.H., Deybach J.C.
Am. J. Hum. Genet. 65:984-994(1999) [PubMed] [Europe PMC] [Abstract]
Maeda N., Horie Y., Sasaki Y., Adachi K., Nanba E., Nishida K., Saigo R., Nakagawa M., Kawasaki H., Kudo Y., Kondo M.
Clin. Biochem. 33:495-500(2000) [PubMed] [Europe PMC] [Abstract]
De Siervi A., Parera V.E., del C Batlle A.M., Rossetti M.V.
Hum. Mutat. 16:532-532(2000) [PubMed] [Europe PMC] [Abstract]
Corrigall A.V., Hift R.J., Davids L.M., Hancock V., Meissner D., Kirsch R.E., Meissner P.N.
Mol. Genet. Metab. 69:323-330(2000) [PubMed] [Europe PMC] [Abstract]
Kauppinen R., Timonen K., von und zu Fraunberg M., Laitinen E., Ahola H., Tenhunen R., Taketani S., Mustajoki P.
J. Invest. Dermatol. 116:610-613(2001) [PubMed] [Europe PMC] [Abstract]
Frank J., Jugert F.K., Merk H.F., Kalka K., Goerz G., Anderson K., Bickers D.R., Poh-Fitzpatrick M.B., Christiano A.M.
J. Invest. Dermatol. 116:821-823(2001) [PubMed] [Europe PMC] [Abstract]
Corrigall A.V., Hift R.J., Davids L.M., Hancock V., Meissner D., Kirsch R.E., Meissner P.N.
Mol. Genet. Metab. 73:91-96(2001) [PubMed] [Europe PMC] [Abstract]
von und zu Fraunberg M., Tenhunen R., Kauppinen R.
Mol. Med. 7:320-328(2001) [PubMed] [Europe PMC] [Abstract]
Rossi E., Chin C.Y., Beilby J.P., Waso H.F., Warnich L.
Intern. Med. J. 32:445-450(2002) [PubMed] [Europe PMC] [Abstract]
Maneli M.H., Corrigall A.V., Klump H.H., Davids L.M., Kirsch R.E., Meissner P.N.
Biochim. Biophys. Acta 1650:10-21(2003) [PubMed] [Europe PMC] [Abstract]
Wiman A., Harper P., Floderus Y.
Clin. Genet. 64:122-130(2003) [PubMed] [Europe PMC] [Abstract]
D'Amato M., Bonuglia M., Barile S., Griso D., Macri A., Biolcati G.
Hum. Mutat. 21:448-448(2003) [PubMed] [Europe PMC] [Abstract]
Gouya L., Puy H., Robreau A.-M., Lyoumi S., Lamoril J., Da Silva V., Grandchamp B., Deybach J.-C.
Hum. Genet. 114:256-262(2004) [PubMed] [Europe PMC] [Abstract]
Poblete-Gutierrez P., Wolff C., Farias R., Frank J.
Br. J. Dermatol. 154:368-371(2006) [PubMed] [Europe PMC] [Abstract]
Davids L.M., Corrigall A.V., Meissner P.N.
Cell Biol. Int. 30:416-426(2006) [PubMed] [Europe PMC] [Abstract]
Lecha M., Badenas C., Puig S., Orfila J., Mila M., To-Figueras J., Munoz C., Mercader P., Herrero C.
J. Eur. Acad. Dermatol. Venereol. 20:974-979(2006) [PubMed] [Europe PMC] [Abstract]
Schneider-Yin X., Minder E.I.
Swiss. Med. Wkly. 136:515-519(2006) [PubMed] [Europe PMC] [Abstract]
Ausenda S., Di Pierro E., Brancaleoni V., Besana V., Cappellini M.D.
Hum. Genet. 122:417-417(2007) [PubMed] [Europe PMC] [Abstract]
Rossetti M.V., Granata B.X., Giudice J., Parera V.E., Batlle A.
BMC Med. Genet. 9:54-54(2008) [PubMed] [Europe PMC] [Abstract]
Ausenda S., Moriondo V., Marchini S., Besana V., Di Pierro E., Brancaleoni V., Ventura P., Rocchi E., Cappellini M.D.
Hum. Genet. 125:344-344(2009) [PubMed] [Europe PMC] [Abstract]
Mendez M., Granata B.X., Jimenez M.J., Parera V.E., Batlle A., de Salamanca R.E., Rossetti M.V.
JIMD Rep. 4:91-97(2012) [PubMed] [Europe PMC] [Abstract]
Pinder V.A., Holden S.T., Deshpande C., Siddiqui A., Mellerio J.E., Wraige E., Powell A.M.
Clin. Exp. Dermatol. 38:737-740(2013) [PubMed] [Europe PMC] [Abstract]
Manual assertion based on experiment ini
- Ref.16"Molecular characterization of homozygous variegate porphyria."
Roberts A.G., Puy H., Dailey T.A., Morgan R.R., Whatley S.D., Dailey H.A., Martasek P., Nordmann Y., Deybach J.C., Elder G.H.
Hum. Mol. Genet. 7:1921-1925(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS VP GLU-169; ALA-349; ARG-358 AND PRO-433, CHARACTERIZATION OF VARIANTS VP GLU-169; ALA-349; ARG-358 AND PRO-433. - Ref.17"Variegate porphyria in Western Europe: identification of PPOX gene mutations in 104 families, extent of allelic heterogeneity, and absence of correlation between phenotype and type of mutation."
Whatley S.D., Puy H., Morgan R.R., Robreau A.M., Roberts A.G., Nordmann Y., Elder G.H., Deybach J.C.
Am. J. Hum. Genet. 65:984-994(1999) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS ARG-256 AND HIS-304, VARIANTS VP PRO-38; GLU-40; PRO-73; GLY-84; PRO-85; VAL-143; CYS-152; PRO-154; MET-158; HIS-168; VAL-172; ARG-232; HIS-281 DEL; ASP-282; PRO-295; GLY-335; PRO-350; PRO-444; ARG-453 AND VAL-453.
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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_070378 | 11 | G → D in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070377 | 11 | G → S in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070379 | 12 | I → T in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070380 | 15 | L → F in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070381 | 20 | H → P in VP; strongly decreases enzyme activity; more resistant to thermal denaturation than wild-type enzyme; abolishes mitochondrial protein targeting and localization. 4 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070382 | 34 | E → V in VP; decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070383 | 38 | R → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070384 | 40 | G → A in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070385 | 40 | G → E in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070386 | 57 | G → R in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_003686 | 59 | R → 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 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070387 | 73 | L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070388 | 76 | S → F in VP; decreases enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070389 | 84 | V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070390 | 85 | L → P in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070391 | 106 | H → P in VP; strongly decreases enzyme activity;. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070392 | 138 | R → P in VP; slightly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070393 | 139 | G → D in VP; strongly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070394 | 143 | D → V in VP; strongly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_003687 | 152 | R → C in VP; strongly decreases enzyme activity. 5 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070395 | 154 | L → P in VP; strongly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070396 | 158 | V → L in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070397 | 158 | V → M in VP; strongly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_003688 | 168 | R → C in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization. 4 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070398 | 168 | R → H in VP; strongly decreases enzyme activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070399 | 169 | G → E in VP; strongly decreases enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070400 | 172 | A → V in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070401 | 178 | L → V in VP; strongly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070402 | 205 | A → V in VP; no effect on enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070403 | 217 | R → C in VP; decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070404 | 224 | W → G in VP; abolishes enzyme activity; impairs protein folding and/or stability. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070405 | 224 | W → R in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_003689 | 232 | G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070406 | 232 | G → S in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070407 | 236 | L → S in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070408 | 281 | Missing in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070409 | 282 | V → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070410 | 283 | I → N in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070411 | 290 | V → M in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070412 | 295 | L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070413 | 330 | G → R in VP; strongly decreases enzyme activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070414 | 332 | G → A in VP; abolishes activity; impairs protein folding and/or stability. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070415 | 335 | V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070416 | 348 | Y → C in VP; results in enzyme activity decrease; impairs protein folding and/or stability; more resistant to thermal denaturation than wild-type enzyme. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070417 | 349 | D → A in VP; decreases enzyme activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070418 | 350 | S → P in VP; abolishes activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070419 | 358 | G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070420 | 397 | A → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070421 | 401 | L → F in VP; strongly decreases enzyme activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070422 | 420 | P → R in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070423 | 422 | Y → C in VP; decreases enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070424 | 433 | A → P in VP; decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070425 | 444 | L → P in VP; strongly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070426 | 448 | G → R in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070427 | 450 | S → P in VP; strongly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070428 | 453 | G → R in VP; strongly decreases enzyme activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070429 | 453 | G → V in VP. 1 Publication Manual assertion based on experiment ini
| 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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>Mutagenesisi | 59 | R → G: Decreases enzyme activity by 75%. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 59 | R → Q: Decreases enzyme activity by 90%. Strongly decreases affinity for protoporphyrinogen-IX. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 74 | L → P: Abolishes enzyme activity. Impairs protein folding and/or stability. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 97 | R → D: Decreases enzyme activity by 89%. Impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 166 | L → N: Decreases enzyme activity by 95%. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 169 | G → A: Decreases enzyme activity by 64%. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 284 | S → I: Decreases enzyme activity by 87%. Impairs protein folding and/or stability. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 290 | V → L: No effect on enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 331 | F → A: Decreases enzyme activity by 50%. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 334 | L → A: Decreases enzyme activity by 86%. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 347 | V → A: Decreases enzyme activity by 45%. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 368 | M → A: Decreases enzyme activity by 52%. 2 Publications Manual assertion based on experiment ini
| 1 |
Keywords - Diseasei
Disease mutationOrganism-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 |
MIMi | 176200, 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<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_0000135270 | 1 – 477 | Protoporphyrinogen oxidaseAdd BLAST | 477 |
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
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 PublicationManual assertion based on experiment ini
- Ref.9"Structural insight into human variegate porphyria disease."
Qin X., Tan Y., Wang L., Wang Z., Wang B., Wen X., Yang G., Xi Z., Shen Y.
FASEB J. 25:653-664(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FAD AND ACIFLUORFEN, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, CHARACTERIZATION OF VARIANTS VP ASP-11; THR-12; PHE-15; PRO-20; PRO-38; ALA-40; GLU-40; TRP-59; PRO-73; GLY-84; PRO-85; PRO-106; PRO-138; ASP-139; VAL-143; CYS-152; PRO-154; MET-158; HIS-168; VAL-178; VAL-205; CYS-217; GLY-224; ARG-232; ASP-282; ASN-283; PRO-295; ARG-330; ALA-332; GLY-335; CYS-348; ALA-349; PRO-350; ARG-358; ASP-397; PHE-401; PRO-433; PRO-444; ARG-448; PRO-450 AND ARG-453, MUTAGENESIS OF LEU-74; ARG-97; LEU-166; GLY-169; SER-284; VAL-290; PHE-331; LEU-334; VAL-347 AND MET-368.
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
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 4 – 8 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 12 – 22 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Beta strandi | 24 – 26 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 29 – 33 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 35 – 40 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Beta strandi | 45 – 47 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 53 – 57 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 59 – 61 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 65 – 77 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
Helixi | 81 – 83 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 84 – 87 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 92 – 95 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 97 – 101 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 104 – 107 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 128 – 131 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 132 – 135 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 146 – 154 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Helixi | 156 – 161 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 163 – 171 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Turni | 175 – 177 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 180 – 183 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 185 – 194 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
Helixi | 197 – 203 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 214 – 221 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 225 – 229 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Helixi | 235 – 246 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
Beta strandi | 250 – 252 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 259 – 262 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 264 – 266 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 268 – 271 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 276 – 284 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Helixi | 288 – 294 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 297 – 299 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 300 – 307 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 311 – 321 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Beta strandi | 330 – 334 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Turni | 337 – 339 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 341 – 347 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 349 – 352 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 354 – 356 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Turni | 358 – 361 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 363 – 369 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
Helixi | 371 – 379 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Helixi | 386 – 401 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 16 | |
Beta strandi | 408 – 420 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
Helixi | 426 – 439 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
Beta strandi | 443 – 446 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Turni | 449 – 451 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 456 – 472 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 17 |
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
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
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
<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 basketEntry | Entry name | Protein names | Gene names | Length | Annotation | ||
---|---|---|---|---|---|---|---|
A0A494C0D4 | A0A494C0D4_HUMAN | Protoporphyrinogen oxidase Protoporphyrinogen oxidase, EC 1.3.3.4 | PPOX | 379 | Annotation 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> | ||
A0A494C146 | A0A494C146_HUMAN | Protoporphyrinogen oxidase Protoporphyrinogen oxidase, EC 1.3.3.4 | PPOX | 435 | Annotation 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> | ||
F5H825 | F5H825_HUMAN | Protoporphyrinogen oxidase Protoporphyrinogen oxidase | PPOX | 156 | Annotation 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> | ||
D3DVG2 | D3DVG2_HUMAN | Protoporphyrinogen oxidase Protoporphyrinogen oxidase (Protoporphyrinogen oxidase, isoform CRA_d) | PPOX hCG_1766487 | 158 | Annotation 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> | ||
F5GZT7 | F5GZT7_HUMAN | Protoporphyrinogen oxidase Protoporphyrinogen oxidase | PPOX | 185 | Annotation 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> | ||
F5H1I5 | F5H1I5_HUMAN | Protoporphyrinogen oxidase Protoporphyrinogen oxidase | PPOX | 113 | Annotation 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> | ||
H0YFE1 | H0YFE1_HUMAN | Protoporphyrinogen oxidase Protoporphyrinogen oxidase | PPOX | 161 | Annotation 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> | ||
H0YFP3 | H0YFP3_HUMAN | Protoporphyrinogen oxidase Protoporphyrinogen oxidase | PPOX | 230 | Annotation 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> | ||
A0A1W2PPA5 | A0A1W2PPA5_HUMAN | Protoporphyrinogen oxidase Protoporphyrinogen oxidase | PPOX | 188 | Annotation 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> | ||
A0A1W2PQM0 | A0A1W2PQM0_HUMAN | Protoporphyrinogen oxidase Protoporphyrinogen oxidase | PPOX | 140 | Annotation 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_070378 | 11 | G → D in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070377 | 11 | G → S in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070379 | 12 | I → T in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070380 | 15 | L → F in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070381 | 20 | H → P in VP; strongly decreases enzyme activity; more resistant to thermal denaturation than wild-type enzyme; abolishes mitochondrial protein targeting and localization. 4 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070382 | 34 | E → V in VP; decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070383 | 38 | R → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070384 | 40 | G → A in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070385 | 40 | G → E in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070386 | 57 | G → R in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_003686 | 59 | R → 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 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070387 | 73 | L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070388 | 76 | S → F in VP; decreases enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070389 | 84 | V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070390 | 85 | L → P in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070391 | 106 | H → P in VP; strongly decreases enzyme activity;. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070392 | 138 | R → P in VP; slightly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070393 | 139 | G → D in VP; strongly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070394 | 143 | D → V in VP; strongly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_003687 | 152 | R → C in VP; strongly decreases enzyme activity. 5 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070395 | 154 | L → P in VP; strongly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070396 | 158 | V → L in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070397 | 158 | V → M in VP; strongly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_003688 | 168 | R → C in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization. 4 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070398 | 168 | R → H in VP; strongly decreases enzyme activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070399 | 169 | G → E in VP; strongly decreases enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070400 | 172 | A → V in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070401 | 178 | L → V in VP; strongly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070402 | 205 | A → V in VP; no effect on enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070403 | 217 | R → C in VP; decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070404 | 224 | W → G in VP; abolishes enzyme activity; impairs protein folding and/or stability. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070405 | 224 | W → R in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_003689 | 232 | G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070406 | 232 | G → S in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070407 | 236 | L → S in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_034395 | 256 | P → 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 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070408 | 281 | Missing in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070409 | 282 | V → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070410 | 283 | I → N in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070411 | 290 | V → M in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070412 | 295 | L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_003690 | 304 | R → H3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070413 | 330 | G → R in VP; strongly decreases enzyme activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070414 | 332 | G → A in VP; abolishes activity; impairs protein folding and/or stability. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070415 | 335 | V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070416 | 348 | Y → C in VP; results in enzyme activity decrease; impairs protein folding and/or stability; more resistant to thermal denaturation than wild-type enzyme. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070417 | 349 | D → A in VP; decreases enzyme activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070418 | 350 | S → P in VP; abolishes activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070419 | 358 | G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070420 | 397 | A → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070421 | 401 | L → F in VP; strongly decreases enzyme activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070422 | 420 | P → R in VP. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070423 | 422 | Y → C in VP; decreases enzyme activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070424 | 433 | A → P in VP; decreases enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070425 | 444 | L → P in VP; strongly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070426 | 448 | G → R in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070427 | 450 | S → P in VP; strongly decreases enzyme activity. 2 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070428 | 453 | G → R in VP; strongly decreases enzyme activity. 3 Publications Manual assertion based on experiment ini
| 1 | |
Natural variantiVAR_070429 | 453 | G → V in VP. 1 Publication Manual assertion based on experiment ini
| 1 |
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P50336 | Protoporphyrinogen oxidase | 477 | UniRef100_P50336 | |||
Protoporphyrinogen oxidase (Fragment) | 148 | |||||
Protoporphyrinogen oxidase | 477 | |||||
+2 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P50336 | Protoporphyrinogen oxidase | 477 | UniRef90_P50336 | |||
Protoporphyrinogen oxidase (Fragment) | 148 | |||||
Protoporphyrinogen oxidase | 441 | |||||
Protoporphyrinogen oxidase | 477 | |||||
+4 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
P50336 | Protoporphyrinogen oxidase | 477 | UniRef50_P50336 | |||
Protoporphyrinogen oxidase | 477 | |||||
Protoporphyrinogen oxidase | 477 | |||||
Protoporphyrinogen oxidase | 477 | |||||
Protoporphyrinogen oxidase (Fragment) | 148 | |||||
+358 |
<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 |
CCDSi | CCDS1221.1 |
PIRi | JC4971, A56449 |
RefSeqi | NP_000300.1, NM_000309.3 NP_001116236.1, NM_001122764.1 |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
3NKS | X-ray | 1.90 | A | 1-477 | [»] | |
4IVM | X-ray | 2.77 | B | 1-477 | [»] | |
4IVO | X-ray | 2.60 | B | 1-477 | [»] | |
SMRi | P50336 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 111492, 40 interactors |
IntActi | P50336, 30 interactors |
STRINGi | 9606.ENSP00000356978 |
Chemistry databases
BindingDBi | P50336 |
ChEMBLi | CHEMBL1926488 |
PTM databases
iPTMneti | P50336 |
PhosphoSitePlusi | P50336 |
SwissPalmi | P50336 |
Polymorphism and mutation databases
BioMutai | PPOX |
DMDMi | 1709742 |
Proteomic databases
EPDi | P50336 |
jPOSTi | P50336 |
MassIVEi | P50336 |
MaxQBi | P50336 |
PaxDbi | P50336 |
PeptideAtlasi | P50336 |
PRIDEi | P50336 |
ProteomicsDBi | 56214 |
Protocols and materials databases
Antibodypedia a portal for validated antibodies More...Antibodypediai | 34299, 252 antibodies |
Genome annotation databases
Ensembli | ENST00000352210; ENSP00000343943; ENSG00000143224 ENST00000367999; ENSP00000356978; ENSG00000143224 |
GeneIDi | 5498 |
KEGGi | hsa:5498 |
UCSCi | uc001fyg.3, human |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 5498 |
DisGeNETi | 5498 |
EuPathDBi | HostDB:ENSG00000143224.17 |
GeneCards: human genes, protein and diseases More...GeneCardsi | PPOX |
GeneReviewsi | PPOX |
HGNCi | HGNC:9280, PPOX |
HPAi | ENSG00000143224, Low tissue specificity |
MalaCardsi | PPOX |
MIMi | 176200, phenotype 600923, gene |
neXtProti | NX_P50336 |
OpenTargetsi | ENSG00000143224 |
Orphaneti | 79473, Porphyria variegata |
PharmGKBi | PA33608 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG1276, Eukaryota |
GeneTreei | ENSGT00390000008744 |
HOGENOMi | CLU_009629_2_1_1 |
InParanoidi | P50336 |
OMAi | IFDSCCF |
OrthoDBi | 1578484at2759 |
PhylomeDBi | P50336 |
TreeFami | TF323479 |
Enzyme and pathway databases
UniPathwayi | UPA00251;UER00324 |
BioCyci | MetaCyc:HS07011-MONOMER |
BRENDAi | 1.3.3.4, 2681 |
PathwayCommonsi | P50336 |
Reactomei | R-HSA-189451, Heme biosynthesis |
SABIO-RKi | P50336 |
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 |
Pharosi | P50336, Tchem |
Protein Ontology More...PROi | PR:P50336 |
RNActi | P50336, protein |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000143224, Expressed in right uterine tube and 219 other tissues |
ExpressionAtlasi | P50336, baseline and differential |
Genevisiblei | P50336, HS |
Family and domain databases
Gene3Di | 3.50.50.60, 1 hit |
InterProi | View protein in InterPro IPR002937, Amino_oxidase IPR036188, FAD/NAD-bd_sf IPR004572, Protoporphyrinogen_oxidase |
Pfami | View protein in Pfam PF01593, Amino_oxidase, 1 hit |
SUPFAMi | SSF51905, SSF51905, 1 hit |
TIGRFAMsi | TIGR00562, 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 namei | PPOX_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>Accessioni | P50336Primary (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 historyi | Integrated 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 statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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 proteomeDocuments
- Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 1
Human chromosome 1: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations