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Protein

Protoporphyrinogen oxidase

Gene

PPOX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)
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

  • heme biosynthetic process Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • porphyrin-containing compound biosynthetic process Source: UniProtKB
  • protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
  • response to drug Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Heme biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

BioCyciMetaCyc:HS07011-MONOMER.
ZFISH:HS07011-MONOMER.
BRENDAi1.3.3.4. 2681.
ReactomeiR-HSA-189451. Heme biosynthesis.
SABIO-RKP50336.
UniPathwayiUPA00251; 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

HGNCiHGNC:9280. PPOX.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Variegate porphyria (VP)26 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 rs28936677dbSNPEnsembl.1
Natural variantiVAR_07038015L → F in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant rs769452432dbSNPEnsembl.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 rs121918326dbSNPEnsembl.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 Publications1
Natural variantiVAR_07038657G → R in VP. 1 PublicationCorresponds to variant rs764352037dbSNPEnsembl.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 rs121918324dbSNPEnsembl.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 rs767419411dbSNPEnsembl.1
Natural variantiVAR_070393139G → D in VP; strongly decreases enzyme activity. 2 PublicationsCorresponds to variant rs369381477dbSNPEnsembl.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 rs121918325dbSNPEnsembl.1
Natural variantiVAR_070398168R → H in VP; strongly decreases enzyme activity. 3 PublicationsCorresponds to variant rs41270025dbSNPEnsembl.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 rs757473753dbSNPEnsembl.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 rs751599052dbSNPEnsembl.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 rs121918323dbSNPEnsembl.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 Publications1
Natural variantiVAR_070417349D → A in VP; decreases enzyme activity. 3 PublicationsCorresponds to variant rs28936676dbSNPEnsembl.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 rs374936130dbSNPEnsembl.1
Natural variantiVAR_070420397A → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant rs141274934dbSNPEnsembl.1
Natural variantiVAR_070421401L → F in VP; strongly decreases enzyme activity. 3 PublicationsCorresponds to variant rs776530007dbSNPEnsembl.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 Publications1
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.
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.

PTM databases

iPTMnetiP50336.
PhosphoSitePlusiP50336.
SwissPalmiP50336.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000143224.
CleanExiHS_PPOX.
ExpressionAtlasiP50336. baseline and differential.
GenevisibleiP50336. HS.

Organism-specific databases

HPAiHPA030123.

Interactioni

Subunit structurei

Monomer. Homodimer.1 Publication

Protein-protein interaction databases

BioGridi111492. 20 interactors.
IntActiP50336. 19 interactors.
MINTiMINT-1402949.
STRINGi9606.ENSP00000343943.

Chemistry databases

BindingDBiP50336.

Structurei

Secondary structure

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Helixi12 – 22Combined sources11
Beta strandi24 – 26Combined sources3
Beta strandi29 – 33Combined sources5
Beta strandi35 – 40Combined sources6
Beta strandi45 – 47Combined sources3
Beta strandi53 – 57Combined sources5
Beta strandi59 – 61Combined sources3
Helixi65 – 77Combined sources13
Helixi81 – 83Combined sources3
Beta strandi84 – 87Combined sources4
Helixi92 – 95Combined sources4
Beta strandi97 – 101Combined sources5
Beta strandi104 – 107Combined sources4
Helixi128 – 131Combined sources4
Turni132 – 135Combined sources4
Helixi146 – 154Combined sources9
Helixi156 – 161Combined sources6
Helixi163 – 171Combined sources9
Turni175 – 177Combined sources3
Helixi180 – 183Combined sources4
Helixi185 – 194Combined sources10
Helixi197 – 203Combined sources7
Helixi214 – 221Combined sources8
Beta strandi225 – 229Combined sources5
Helixi235 – 246Combined sources12
Beta strandi250 – 252Combined sources3
Beta strandi259 – 262Combined sources4
Helixi264 – 266Combined sources3
Beta strandi268 – 271Combined sources4
Beta strandi276 – 284Combined sources9
Helixi288 – 294Combined sources7
Helixi297 – 299Combined sources3
Helixi300 – 307Combined sources8
Beta strandi311 – 321Combined sources11
Beta strandi330 – 334Combined sources5
Turni337 – 339Combined sources3
Beta strandi341 – 347Combined sources7
Helixi349 – 352Combined sources4
Helixi354 – 356Combined sources3
Turni358 – 361Combined sources4
Beta strandi363 – 369Combined sources7
Helixi371 – 379Combined sources9
Helixi386 – 401Combined sources16
Beta strandi408 – 420Combined sources13
Helixi426 – 439Combined sources14
Beta strandi443 – 446Combined sources4
Turni449 – 451Combined sources3
Helixi456 – 472Combined sources17

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...

Family & Domainsi

Sequence similaritiesi

Belongs to the protoporphyrinogen oxidase family.Curated

Phylogenomic databases

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

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.660.20. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
IPR016040. NAD(P)-bd_dom.
IPR027418. PPOX_C.
IPR004572. Protoporphyrinogen_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR00562. proto_IX_ox. 1 hit.

Sequencei

Sequence statusi: Complete.

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

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 rs28936677dbSNPEnsembl.1
Natural variantiVAR_07038015L → F in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant rs769452432dbSNPEnsembl.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 rs121918326dbSNPEnsembl.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 Publications1
Natural variantiVAR_07038657G → R in VP. 1 PublicationCorresponds to variant rs764352037dbSNPEnsembl.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 rs121918324dbSNPEnsembl.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 rs767419411dbSNPEnsembl.1
Natural variantiVAR_070393139G → D in VP; strongly decreases enzyme activity. 2 PublicationsCorresponds to variant rs369381477dbSNPEnsembl.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 rs121918325dbSNPEnsembl.1
Natural variantiVAR_070398168R → H in VP; strongly decreases enzyme activity. 3 PublicationsCorresponds to variant rs41270025dbSNPEnsembl.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 rs757473753dbSNPEnsembl.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 rs751599052dbSNPEnsembl.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 rs121918323dbSNPEnsembl.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 rs12735723dbSNPEnsembl.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 → H.3 PublicationsCorresponds to variant rs36013429dbSNPEnsembl.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 Publications1
Natural variantiVAR_070417349D → A in VP; decreases enzyme activity. 3 PublicationsCorresponds to variant rs28936676dbSNPEnsembl.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 rs374936130dbSNPEnsembl.1
Natural variantiVAR_070420397A → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 PublicationsCorresponds to variant rs141274934dbSNPEnsembl.1
Natural variantiVAR_070421401L → F in VP; strongly decreases enzyme activity. 3 PublicationsCorresponds to variant rs776530007dbSNPEnsembl.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 Publications1
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. Translation: CAH72144.1.
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

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. Translation: CAH72144.1.
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. 20 interactors.
IntActiP50336. 19 interactors.
MINTiMINT-1402949.
STRINGi9606.ENSP00000343943.

Chemistry databases

BindingDBiP50336.
ChEMBLiCHEMBL1926488.

PTM databases

iPTMnetiP50336.
PhosphoSitePlusiP50336.
SwissPalmiP50336.

Polymorphism and mutation databases

BioMutaiPPOX.
DMDMi1709742.

Proteomic databases

EPDiP50336.
MaxQBiP50336.
PaxDbiP50336.
PeptideAtlasiP50336.
PRIDEiP50336.

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.
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.
OMAiDSCCFDM.
OrthoDBiEOG091G08PW.
PhylomeDBiP50336.
TreeFamiTF323479.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00324.
BioCyciMetaCyc:HS07011-MONOMER.
ZFISH:HS07011-MONOMER.
BRENDAi1.3.3.4. 2681.
ReactomeiR-HSA-189451. Heme biosynthesis.
SABIO-RKP50336.

Miscellaneous databases

ChiTaRSiPPOX. human.
GeneWikiiPPOX.
GenomeRNAii5498.
PROiP50336.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143224.
CleanExiHS_PPOX.
ExpressionAtlasiP50336. baseline and differential.
GenevisibleiP50336. HS.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.660.20. 1 hit.
InterProiIPR002937. Amino_oxidase.
IPR023753. FAD/NAD-binding_dom.
IPR016040. NAD(P)-bd_dom.
IPR027418. PPOX_C.
IPR004572. Protoporphyrinogen_oxidase.
[Graphical view]
PfamiPF01593. Amino_oxidase. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR00562. proto_IX_ox. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiPPOX_HUMAN
AccessioniPrimary (citable) accession number: P50336
Secondary accession number(s): D3DVG0, Q5VTW8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 157 of the entry and version 1 of the sequence. [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. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.