Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Protoporphyrinogen oxidase

Gene

PPOX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Protoporphyrinogen-IX + 3 O2 = protoporphyrin-IX + 3 H2O2.2 Publications

Cofactori

FADNote: Binds 1 FAD per subunit.

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, Protoporphyrinogen oxidase (PPOX), Protoporphyrinogen oxidase
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
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
Nucleotide bindingi9 – 14FAD1 Publication6
Nucleotide bindingi34 – 35FAD1 Publication2
Nucleotide bindingi57 – 60FAD1 Publication4
Nucleotide bindingi454 – 456FAD1 Publication3

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processHeme biosynthesis, Porphyrin biosynthesis
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:HS07011-MONOMER
BRENDAi1.3.3.4 2681
ReactomeiR-HSA-189451 Heme biosynthesis
SABIO-RKiP50336
UniPathwayi
UPA00251;UER00324

Names & Taxonomyi

Protein namesi
Recommended name:
Protoporphyrinogen oxidase (EC:1.3.3.4)
Short name:
PPO
Gene namesi
Name:PPOX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000143224.17
HGNCiHGNC:9280 PPOX
MIMi600923 gene
neXtProtiNX_P50336

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Variegate porphyria (VP)30 Publications
The disease is caused by mutations affecting the gene represented in this entry. Mutations leading to severe PPOX deficiency cause the rare homozygous variant form of VP. Missense mutations that preserve 10%-25% of wild-type activity may not cause clinically overt VP in heterozygotes (PubMed:9811936). Mutations with intermediate effect on catalytic activity may cause VP, but with a low clinical penetrance (PubMed:10486317).2 Publications
Disease descriptionA form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. Variegate porphyria is the most common form of porphyria in South Africa. It is characterized by skin hyperpigmentation and hypertrichosis, abdominal pain, tachycardia, hypertension and neuromuscular disturbances. High fecal levels of protoporphyrin and coproporphyrin, increased urine uroporphyrins and iron overload are typical markers of the disease.
See also OMIM:176200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07037811G → D in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07037711G → S in VP. 1 Publication1
Natural variantiVAR_07037912I → T in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs28936677EnsemblClinVar.1
Natural variantiVAR_07038015L → F in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs769452432Ensembl.1
Natural variantiVAR_07038120H → P in VP; strongly decreases enzyme activity; more resistant to thermal denaturation than wild-type enzyme; abolishes mitochondrial protein targeting and localization. 4 PublicationsCorresponds to variant dbSNP:rs121918326EnsemblClinVar.1
Natural variantiVAR_07038234E → V in VP; decreases enzyme activity. 2 Publications1
Natural variantiVAR_07038338R → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07038440G → A in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07038540G → E in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs1317835140Ensembl.1
Natural variantiVAR_07038657G → R in VP. 1 PublicationCorresponds to variant dbSNP:rs764352037Ensembl.1
Natural variantiVAR_00368659R → W in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization; more resistant to thermal denaturation than wild-type enzyme. 8 PublicationsCorresponds to variant dbSNP:rs121918324EnsemblClinVar.1
Natural variantiVAR_07038773L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07038876S → F in VP; decreases enzyme activity. 1 Publication1
Natural variantiVAR_07038984V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_07039085L → P in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070391106H → P in VP; strongly decreases enzyme activity;. 2 Publications1
Natural variantiVAR_070392138R → P in VP; slightly decreases enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs767419411Ensembl.1
Natural variantiVAR_070393139G → D in VP; strongly decreases enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs369381477Ensembl.1
Natural variantiVAR_070394143D → V in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_003687152R → C in VP; strongly decreases enzyme activity. 5 Publications1
Natural variantiVAR_070395154L → P in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_070396158V → L in VP. 1 Publication1
Natural variantiVAR_070397158V → M in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_003688168R → C in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization. 4 PublicationsCorresponds to variant dbSNP:rs121918325EnsemblClinVar.1
Natural variantiVAR_070398168R → H in VP; strongly decreases enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs41270025EnsemblClinVar.1
Natural variantiVAR_070399169G → E in VP; strongly decreases enzyme activity. 1 Publication1
Natural variantiVAR_070400172A → V in VP. 1 Publication1
Natural variantiVAR_070401178L → V in VP; strongly decreases enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs757473753Ensembl.1
Natural variantiVAR_070402205A → V in VP; no effect on enzyme activity. 2 Publications1
Natural variantiVAR_070403217R → C in VP; decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs751599052Ensembl.1
Natural variantiVAR_070404224W → G in VP; abolishes enzyme activity; impairs protein folding and/or stability. 3 Publications1
Natural variantiVAR_070405224W → R in VP. 1 Publication1
Natural variantiVAR_003689232G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 3 PublicationsCorresponds to variant dbSNP:rs121918323EnsemblClinVar.1
Natural variantiVAR_070406232G → S in VP. 1 Publication1
Natural variantiVAR_070407236L → S in VP. 1 Publication1
Natural variantiVAR_070408281Missing in VP. 1 Publication1
Natural variantiVAR_070409282V → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070410283I → N in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070411290V → M in VP. 1 Publication1
Natural variantiVAR_070412295L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070413330G → R in VP; strongly decreases enzyme activity. 3 Publications1
Natural variantiVAR_070414332G → A in VP; abolishes activity; impairs protein folding and/or stability. 3 Publications1
Natural variantiVAR_070415335V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 3 Publications1
Natural variantiVAR_070416348Y → C in VP; results in enzyme activity decrease; impairs protein folding and/or stability; more resistant to thermal denaturation than wild-type enzyme. 3 PublicationsCorresponds to variant dbSNP:rs900431442Ensembl.1
Natural variantiVAR_070417349D → A in VP; decreases enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs28936676EnsemblClinVar.1
Natural variantiVAR_070418350S → P in VP; abolishes activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070419358G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs374936130Ensembl.1
Natural variantiVAR_070420397A → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant dbSNP:rs141274934Ensembl.1
Natural variantiVAR_070421401L → F in VP; strongly decreases enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs776530007Ensembl.1
Natural variantiVAR_070422420P → R in VP. 1 Publication1
Natural variantiVAR_070423422Y → C in VP; decreases enzyme activity. 1 Publication1
Natural variantiVAR_070424433A → P in VP; decreases enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070425444L → P in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_070426448G → R in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications1
Natural variantiVAR_070427450S → P in VP; strongly decreases enzyme activity. 2 Publications1
Natural variantiVAR_070428453G → R in VP; strongly decreases enzyme activity. 3 PublicationsCorresponds to variant dbSNP:rs928944841Ensembl.1
Natural variantiVAR_070429453G → V in VP. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

DisGeNETi5498
GeneReviewsiPPOX
MalaCardsiPPOX
MIMi176200 phenotype
OpenTargetsiENSG00000143224
Orphaneti79473 Porphyria variegata
PharmGKBiPA33608

Chemistry databases

ChEMBLiCHEMBL1926488

Polymorphism and mutation databases

BioMutaiPPOX
DMDMi1709742

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001352701 – 477Protoporphyrinogen oxidaseAdd BLAST477

Proteomic databases

EPDiP50336
MaxQBiP50336
PaxDbiP50336
PeptideAtlasiP50336
PRIDEiP50336
ProteomicsDBi56214

PTM databases

iPTMnetiP50336
PhosphoSitePlusiP50336
SwissPalmiP50336

Expressioni

Tissue specificityi

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

Gene expression databases

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

Organism-specific databases

HPAiHPA030123

Interactioni

Subunit structurei

Monomer. Homodimer.1 Publication

Protein-protein interaction databases

BioGridi111492, 21 interactors
IntActiP50336, 21 interactors
STRINGi9606.ENSP00000343943

Chemistry databases

BindingDBiP50336

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliP50336
SMRiP50336
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the protoporphyrinogen oxidase family.Curated

Phylogenomic databases

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

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

Sequence (1+)i

Sequence statusi: Complete.

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

P50336-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGRTVVVLGG GISGLAASYH LSRAPCPPKV VLVESSERLG GWIRSVRGPN
60 70 80 90 100
GAIFELGPRG IRPAGALGAR TLLLVSELGL DSEVLPVRGD HPAAQNRFLY
110 120 130 140 150
VGGALHALPT GLRGLLRPSP PFSKPLFWAG LRELTKPRGK EPDETVHSFA
160 170 180 190 200
QRRLGPEVAS LAMDSLCRGV FAGNSRELSI RSCFPSLFQA EQTHRSILLG
210 220 230 240 250
LLLGAGRTPQ PDSALIRQAL AERWSQWSLR GGLEMLPQAL ETHLTSRGVS
260 270 280 290 300
VLRGQPVCGL SLQAEGRWKV SLRDSSLEAD HVISAIPASV LSELLPAEAA
310 320 330 340 350
PLARALSAIT AVSVAVVNLQ YQGAHLPVQG FGHLVPSSED PGVLGIVYDS
360 370 380 390 400
VAFPEQDGSP PGLRVTVMLG GSWLQTLEAS GCVLSQELFQ QRAQEAAATQ
410 420 430 440 450
LGLKEMPSHC LVHLHKNCIP QYTLGHWQKL ESARQFLTAH RLPLTLAGAS
460 470
YEGVAVNDCI ESGRQAAVSV LGTEPNS
Length:477
Mass (Da):50,765
Last modified:October 1, 1996 - v1
Checksum:i2444DEAC2E6C33EE
GO

Computationally mapped potential isoform sequencesi

There are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5H1I5F5H1I5_HUMAN
Protoporphyrinogen oxidase
PPOX
113Annotation score:
F5GZT7F5GZT7_HUMAN
Protoporphyrinogen oxidase
PPOX
185Annotation score:
H0YFE1H0YFE1_HUMAN
Protoporphyrinogen oxidase
PPOX
161Annotation score:
H0YFP3H0YFP3_HUMAN
Protoporphyrinogen oxidase
PPOX
230Annotation score:
A0A1W2PRF9A0A1W2PRF9_HUMAN
Protoporphyrinogen oxidase
PPOX
184Annotation score:
A0A1W2PPA5A0A1W2PPA5_HUMAN
Protoporphyrinogen oxidase
PPOX
188Annotation score:
A0A1W2PQM0A0A1W2PQM0_HUMAN
Protoporphyrinogen oxidase
PPOX
140Annotation score:
A0A1W2PNH4A0A1W2PNH4_HUMAN
Protoporphyrinogen oxidase
PPOX
78Annotation score:
F5H825F5H825_HUMAN
Protoporphyrinogen oxidase
PPOX
156Annotation score:

Natural variant

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

Sequence databases

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

Wikipedia

Protoporphyrinogen oxidase entry

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NKSX-ray1.90A1-477[»]
4IVMX-ray2.77B1-477[»]
4IVOX-ray2.60B1-477[»]
ProteinModelPortaliP50336
SMRiP50336
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111492, 21 interactors
IntActiP50336, 21 interactors
STRINGi9606.ENSP00000343943

Chemistry databases

BindingDBiP50336
ChEMBLiCHEMBL1926488

PTM databases

iPTMnetiP50336
PhosphoSitePlusiP50336
SwissPalmiP50336

Polymorphism and mutation databases

BioMutaiPPOX
DMDMi1709742

Proteomic databases

EPDiP50336
MaxQBiP50336
PaxDbiP50336
PeptideAtlasiP50336
PRIDEiP50336
ProteomicsDBi56214

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5498
DisGeNETi5498
EuPathDBiHostDB:ENSG00000143224.17
GeneCardsiPPOX
GeneReviewsiPPOX
HGNCiHGNC:9280 PPOX
HPAiHPA030123
MalaCardsiPPOX
MIMi176200 phenotype
600923 gene
neXtProtiNX_P50336
OpenTargetsiENSG00000143224
Orphaneti79473 Porphyria variegata
PharmGKBiPA33608
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayi
UPA00251;UER00324

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

Miscellaneous databases

ChiTaRSiPPOX human
GeneWikiiPPOX
GenomeRNAii5498
PROiPR:P50336
SOURCEiSearch...

Gene expression databases

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

Family and domain databases

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

Entry informationi

Entry nameiPPOX_HUMAN
AccessioniPrimary (citable) accession number: P50336
Secondary accession number(s): D3DVG0, Q5VTW8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 7, 2018
This is version 172 of the entry and version 1 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again