Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P50336

- PPOX_HUMAN

UniProt

P50336 - PPOX_HUMAN

Protein

Protoporphyrinogen oxidase

Gene

PPOX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    Binds 1 FAD per subunit.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei42 – 421FAD; via amide nitrogen1 Publication
    Binding sitei257 – 2571FAD; via amide nitrogen and carbonyl oxygen1 Publication
    Binding sitei449 – 4491FAD; via amide nitrogen1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi9 – 146FAD1 Publication
    Nucleotide bindingi34 – 352FAD1 Publication
    Nucleotide bindingi57 – 604FAD1 Publication
    Nucleotide bindingi454 – 4563FAD1 Publication

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: UniProtKB
    2. oxygen-dependent protoporphyrinogen oxidase activity Source: UniProtKB

    GO - Biological processi

    1. heme biosynthetic process Source: UniProtKB
    2. oxidation-reduction process Source: UniProtKB
    3. porphyrin-containing compound biosynthetic process Source: UniProtKB
    4. porphyrin-containing compound metabolic process Source: Reactome
    5. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
    6. response to drug Source: Ensembl
    7. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Heme biosynthesis, Porphyrin biosynthesis

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07011-MONOMER.
    ReactomeiREACT_9465. 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
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:9280. PPOX.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of mitochondrial inner membrane Source: Ensembl
    2. intrinsic component of mitochondrial inner membrane Source: UniProtKB
    3. mitochondrial intermembrane space Source: Reactome
    4. mitochondrial membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Involvement in diseasei

    Variegate porphyria (VP) [MIM:176200]: A 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.26 Publications
    Note: 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
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111G → D in VP; abolishes enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070378
    Natural varianti11 – 111G → S in VP. 1 Publication
    VAR_070377
    Natural varianti12 – 121I → T in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070379
    Natural varianti15 – 151L → F in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070380
    Natural varianti20 – 201H → P in VP; strongly decreases enzyme activity; more resistant to thermal denaturation than wild-type enzyme; abolishes mitochondrial protein targeting and localization. 1 Publication
    VAR_070381
    Natural varianti34 – 341E → V in VP; decreases enzyme activity. 2 Publications
    VAR_070382
    Natural varianti38 – 381R → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070383
    Natural varianti40 – 401G → A in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070384
    Natural varianti40 – 401G → E in VP; abolishes enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070385
    Natural varianti57 – 571G → R in VP. 1 Publication
    VAR_070386
    Natural varianti59 – 591R → W in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization; more resistant to thermal denaturation than wild-type enzyme. 4 Publications
    VAR_003686
    Natural varianti73 – 731L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070387
    Natural varianti76 – 761S → F in VP; decreases enzyme activity. 1 Publication
    VAR_070388
    Natural varianti84 – 841V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070389
    Natural varianti85 – 851L → P in VP; abolishes enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070390
    Natural varianti106 – 1061H → P in VP; strongly decreases enzyme activity;. 1 Publication
    VAR_070391
    Natural varianti138 – 1381R → P in VP; slightly decreases enzyme activity. 1 Publication
    VAR_070392
    Natural varianti139 – 1391G → D in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070393
    Natural varianti143 – 1431D → V in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070394
    Natural varianti152 – 1521R → C in VP; strongly decreases enzyme activity. 4 Publications
    VAR_003687
    Natural varianti154 – 1541L → P in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070395
    Natural varianti158 – 1581V → L in VP. 1 Publication
    VAR_070396
    Natural varianti158 – 1581V → M in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070397
    Natural varianti168 – 1681R → C in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization. 2 Publications
    VAR_003688
    Natural varianti168 – 1681R → H in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070398
    Natural varianti169 – 1691G → E in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070399
    Natural varianti172 – 1721A → V in VP. 1 Publication
    VAR_070400
    Natural varianti178 – 1781L → V in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070401
    Natural varianti205 – 2051A → V in VP; no effect on enzyme activity. 1 Publication
    VAR_070402
    Natural varianti217 – 2171R → C in VP; decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070403
    Natural varianti224 – 2241W → G in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications
    VAR_070404
    Natural varianti224 – 2241W → R in VP. 1 Publication
    VAR_070405
    Natural varianti232 – 2321G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
    VAR_003689
    Natural varianti232 – 2321G → S in VP. 1 Publication
    VAR_070406
    Natural varianti236 – 2361L → S in VP. 1 Publication
    VAR_070407
    Natural varianti281 – 2811Missing in VP. 1 Publication
    VAR_070408
    Natural varianti282 – 2821V → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070409
    Natural varianti283 – 2831I → N in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070410
    Natural varianti290 – 2901V → M in VP. 1 Publication
    VAR_070411
    Natural varianti295 – 2951L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070412
    Natural varianti330 – 3301G → R in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070413
    Natural varianti332 – 3321G → A in VP; abolishes activity; impairs protein folding and/or stability. 2 Publications
    VAR_070414
    Natural varianti335 – 3351V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070415
    Natural varianti348 – 3481Y → C in VP; results in enzyme activity decrease; impairs protein folding and/or stability; more resistant to thermal denaturation than wild-type enzyme. 1 Publication
    VAR_070416
    Natural varianti349 – 3491D → A in VP; decreases enzyme activity. 1 Publication
    VAR_070417
    Natural varianti350 – 3501S → P in VP; abolishes activity; impairs protein folding and/or stability. 1 Publication
    VAR_070418
    Natural varianti358 – 3581G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070419
    Natural varianti397 – 3971A → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070420
    Natural varianti401 – 4011L → F in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070421
    Natural varianti420 – 4201P → R in VP. 1 Publication
    VAR_070422
    Natural varianti422 – 4221Y → C in VP; decreases enzyme activity. 1 Publication
    VAR_070423
    Natural varianti433 – 4331A → P in VP; decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070424
    Natural varianti444 – 4441L → P in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070425
    Natural varianti448 – 4481G → R in VP; abolishes enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070426
    Natural varianti450 – 4501S → P in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070427
    Natural varianti453 – 4531G → R in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070428
    Natural varianti453 – 4531G → V in VP. 1 Publication
    VAR_070429

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi59 – 591R → G: Decreases enzyme activity by 75%. 1 Publication
    Mutagenesisi59 – 591R → Q: Decreases enzyme activity by 90%. Strongly decreases affinity for protoporphyrinogen-IX. 1 Publication
    Mutagenesisi74 – 741L → P: Abolishes enzyme activity. Impairs protein folding and/or stability. 1 Publication
    Mutagenesisi97 – 971R → D: Decreases enzyme activity by 89%. Impairs protein folding and/or stability. 2 Publications
    Mutagenesisi166 – 1661L → N: Decreases enzyme activity by 95%. 2 Publications
    Mutagenesisi169 – 1691G → A: Decreases enzyme activity by 64%. 2 Publications
    Mutagenesisi284 – 2841S → I: Decreases enzyme activity by 87%. Impairs protein folding and/or stability. 1 Publication
    Mutagenesisi290 – 2901V → L: No effect on enzyme activity. 1 Publication
    Mutagenesisi331 – 3311F → A: Decreases enzyme activity by 50%. 2 Publications
    Mutagenesisi334 – 3341L → A: Decreases enzyme activity by 86%. 2 Publications
    Mutagenesisi347 – 3471V → A: Decreases enzyme activity by 45%. 2 Publications
    Mutagenesisi368 – 3681M → A: Decreases enzyme activity by 52%. 2 Publications

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi176200. phenotype.
    Orphaneti79473. Porphyria variegata.
    PharmGKBiPA33608.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 477477Protoporphyrinogen oxidasePRO_0000135270Add
    BLAST

    Proteomic databases

    MaxQBiP50336.
    PaxDbiP50336.
    PeptideAtlasiP50336.
    PRIDEiP50336.

    PTM databases

    PhosphoSiteiP50336.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP50336.
    BgeeiP50336.
    CleanExiHS_PPOX.
    GenevestigatoriP50336.

    Organism-specific databases

    HPAiHPA030123.

    Interactioni

    Subunit structurei

    Monomer. Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi111492. 5 interactions.
    IntActiP50336. 3 interactions.
    MINTiMINT-1402949.
    STRINGi9606.ENSP00000343943.

    Structurei

    Secondary structure

    1
    477
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Helixi12 – 2211
    Beta strandi24 – 263
    Beta strandi29 – 335
    Beta strandi35 – 406
    Beta strandi45 – 473
    Beta strandi53 – 575
    Beta strandi59 – 613
    Helixi65 – 7713
    Helixi81 – 833
    Beta strandi84 – 874
    Helixi92 – 954
    Beta strandi97 – 1015
    Beta strandi104 – 1074
    Helixi128 – 1314
    Turni132 – 1354
    Helixi146 – 1549
    Helixi156 – 1616
    Helixi163 – 1719
    Turni175 – 1773
    Helixi180 – 1834
    Helixi185 – 19410
    Helixi197 – 2037
    Helixi214 – 2218
    Beta strandi225 – 2295
    Helixi235 – 24612
    Beta strandi250 – 2523
    Beta strandi259 – 2624
    Helixi264 – 2663
    Beta strandi268 – 2714
    Beta strandi276 – 2849
    Helixi288 – 2947
    Helixi297 – 2993
    Helixi300 – 3078
    Beta strandi311 – 32111
    Beta strandi330 – 3345
    Turni337 – 3393
    Beta strandi341 – 3477
    Helixi349 – 3524
    Helixi354 – 3563
    Turni358 – 3614
    Beta strandi363 – 3697
    Helixi371 – 3799
    Helixi386 – 40116
    Beta strandi408 – 42013
    Helixi426 – 43914
    Beta strandi443 – 4464
    Turni449 – 4513
    Helixi456 – 47217

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3NKSX-ray1.90A1-477[»]
    4IVMX-ray2.77B1-477[»]
    4IVOX-ray2.60B1-477[»]
    ProteinModelPortaliP50336.
    SMRiP50336. Positions 2-474.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the protoporphyrinogen oxidase family.Curated

    Phylogenomic databases

    eggNOGiCOG1232.
    HOGENOMiHOG000269479.
    HOVERGENiHBG001709.
    InParanoidiP50336.
    KOiK00231.
    OMAiWIRSIRG.
    OrthoDBiEOG7DJSMB.
    PhylomeDBiP50336.
    TreeFamiTF323479.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.660.20. 1 hit.
    InterProiIPR002937. Amino_oxidase.
    IPR016040. NAD(P)-bd_dom.
    IPR027418. PPOX_C.
    IPR004572. Protoporphyrinogen_oxidase.
    [Graphical view]
    PfamiPF01593. Amino_oxidase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00562. proto_IX_ox. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P50336-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGRTVVVLGG GISGLAASYH LSRAPCPPKV VLVESSERLG GWIRSVRGPN    50
    GAIFELGPRG IRPAGALGAR TLLLVSELGL DSEVLPVRGD HPAAQNRFLY 100
    VGGALHALPT GLRGLLRPSP PFSKPLFWAG LRELTKPRGK EPDETVHSFA 150
    QRRLGPEVAS LAMDSLCRGV FAGNSRELSI RSCFPSLFQA EQTHRSILLG 200
    LLLGAGRTPQ PDSALIRQAL AERWSQWSLR GGLEMLPQAL ETHLTSRGVS 250
    VLRGQPVCGL SLQAEGRWKV SLRDSSLEAD HVISAIPASV LSELLPAEAA 300
    PLARALSAIT AVSVAVVNLQ YQGAHLPVQG FGHLVPSSED PGVLGIVYDS 350
    VAFPEQDGSP PGLRVTVMLG GSWLQTLEAS GCVLSQELFQ QRAQEAAATQ 400
    LGLKEMPSHC LVHLHKNCIP QYTLGHWQKL ESARQFLTAH RLPLTLAGAS 450
    YEGVAVNDCI ESGRQAAVSV LGTEPNS 477
    Length:477
    Mass (Da):50,765
    Last modified:October 1, 1996 - v1
    Checksum:i2444DEAC2E6C33EE
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111G → D in VP; abolishes enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070378
    Natural varianti11 – 111G → S in VP. 1 Publication
    VAR_070377
    Natural varianti12 – 121I → T in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070379
    Natural varianti15 – 151L → F in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070380
    Natural varianti20 – 201H → P in VP; strongly decreases enzyme activity; more resistant to thermal denaturation than wild-type enzyme; abolishes mitochondrial protein targeting and localization. 1 Publication
    VAR_070381
    Natural varianti34 – 341E → V in VP; decreases enzyme activity. 2 Publications
    VAR_070382
    Natural varianti38 – 381R → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070383
    Natural varianti40 – 401G → A in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070384
    Natural varianti40 – 401G → E in VP; abolishes enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070385
    Natural varianti57 – 571G → R in VP. 1 Publication
    VAR_070386
    Natural varianti59 – 591R → W in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization; more resistant to thermal denaturation than wild-type enzyme. 4 Publications
    VAR_003686
    Natural varianti73 – 731L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070387
    Natural varianti76 – 761S → F in VP; decreases enzyme activity. 1 Publication
    VAR_070388
    Natural varianti84 – 841V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070389
    Natural varianti85 – 851L → P in VP; abolishes enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070390
    Natural varianti106 – 1061H → P in VP; strongly decreases enzyme activity;. 1 Publication
    VAR_070391
    Natural varianti138 – 1381R → P in VP; slightly decreases enzyme activity. 1 Publication
    VAR_070392
    Natural varianti139 – 1391G → D in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070393
    Natural varianti143 – 1431D → V in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070394
    Natural varianti152 – 1521R → C in VP; strongly decreases enzyme activity. 4 Publications
    VAR_003687
    Natural varianti154 – 1541L → P in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070395
    Natural varianti158 – 1581V → L in VP. 1 Publication
    VAR_070396
    Natural varianti158 – 1581V → M in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070397
    Natural varianti168 – 1681R → C in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization. 2 Publications
    VAR_003688
    Natural varianti168 – 1681R → H in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070398
    Natural varianti169 – 1691G → E in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070399
    Natural varianti172 – 1721A → V in VP. 1 Publication
    VAR_070400
    Natural varianti178 – 1781L → V in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070401
    Natural varianti205 – 2051A → V in VP; no effect on enzyme activity. 1 Publication
    VAR_070402
    Natural varianti217 – 2171R → C in VP; decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070403
    Natural varianti224 – 2241W → G in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications
    VAR_070404
    Natural varianti224 – 2241W → R in VP. 1 Publication
    VAR_070405
    Natural varianti232 – 2321G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
    VAR_003689
    Natural varianti232 – 2321G → S in VP. 1 Publication
    VAR_070406
    Natural varianti236 – 2361L → S in VP. 1 Publication
    VAR_070407
    Natural varianti256 – 2561P → 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
    Corresponds to variant rs12735723 [ dbSNP | Ensembl ].
    VAR_034395
    Natural varianti281 – 2811Missing in VP. 1 Publication
    VAR_070408
    Natural varianti282 – 2821V → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070409
    Natural varianti283 – 2831I → N in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070410
    Natural varianti290 – 2901V → M in VP. 1 Publication
    VAR_070411
    Natural varianti295 – 2951L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070412
    Natural varianti304 – 3041R → H.3 Publications
    Corresponds to variant rs36013429 [ dbSNP | Ensembl ].
    VAR_003690
    Natural varianti330 – 3301G → R in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070413
    Natural varianti332 – 3321G → A in VP; abolishes activity; impairs protein folding and/or stability. 2 Publications
    VAR_070414
    Natural varianti335 – 3351V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070415
    Natural varianti348 – 3481Y → C in VP; results in enzyme activity decrease; impairs protein folding and/or stability; more resistant to thermal denaturation than wild-type enzyme. 1 Publication
    VAR_070416
    Natural varianti349 – 3491D → A in VP; decreases enzyme activity. 1 Publication
    VAR_070417
    Natural varianti350 – 3501S → P in VP; abolishes activity; impairs protein folding and/or stability. 1 Publication
    VAR_070418
    Natural varianti358 – 3581G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070419
    Natural varianti397 – 3971A → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070420
    Natural varianti401 – 4011L → F in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070421
    Natural varianti420 – 4201P → R in VP. 1 Publication
    VAR_070422
    Natural varianti422 – 4221Y → C in VP; decreases enzyme activity. 1 Publication
    VAR_070423
    Natural varianti433 – 4331A → P in VP; decreases enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070424
    Natural varianti444 – 4441L → P in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070425
    Natural varianti448 – 4481G → R in VP; abolishes enzyme activity; impairs protein folding and/or stability. 1 Publication
    VAR_070426
    Natural varianti450 – 4501S → P in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070427
    Natural varianti453 – 4531G → R in VP; strongly decreases enzyme activity. 1 Publication
    VAR_070428
    Natural varianti453 – 4531G → V in VP. 1 Publication
    VAR_070429

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.2. human.

    Polymorphism databases

    DMDMi1709742.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Protoporphyrinogen oxidase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1221.1.
    PIRi JC4971. A56449.
    RefSeqi NP_000300.1. NM_000309.3.
    NP_001116236.1. NM_001122764.1.
    UniGenei Hs.517373.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P50336.
    SMRi P50336. Positions 2-474.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111492. 5 interactions.
    IntActi P50336. 3 interactions.
    MINTi MINT-1402949.
    STRINGi 9606.ENSP00000343943.

    Chemistry

    BindingDBi P50336.
    ChEMBLi CHEMBL1926488.

    PTM databases

    PhosphoSitei P50336.

    Polymorphism databases

    DMDMi 1709742.

    Proteomic databases

    MaxQBi P50336.
    PaxDbi P50336.
    PeptideAtlasi P50336.
    PRIDEi P50336.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000352210 ; ENSP00000343943 ; ENSG00000143224 .
    ENST00000367999 ; ENSP00000356978 ; ENSG00000143224 .
    GeneIDi 5498.
    KEGGi hsa:5498.
    UCSCi uc001fyg.2. human.

    Organism-specific databases

    CTDi 5498.
    GeneCardsi GC01P161136.
    GeneReviewsi PPOX.
    HGNCi HGNC:9280. PPOX.
    HPAi HPA030123.
    MIMi 176200. phenotype.
    600923. gene.
    neXtProti NX_P50336.
    Orphaneti 79473. Porphyria variegata.
    PharmGKBi PA33608.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1232.
    HOGENOMi HOG000269479.
    HOVERGENi HBG001709.
    InParanoidi P50336.
    KOi K00231.
    OMAi WIRSIRG.
    OrthoDBi EOG7DJSMB.
    PhylomeDBi P50336.
    TreeFami TF323479.

    Enzyme and pathway databases

    UniPathwayi UPA00251 ; UER00324 .
    BioCyci MetaCyc:HS07011-MONOMER.
    Reactomei REACT_9465. Heme biosynthesis.
    SABIO-RK P50336.

    Miscellaneous databases

    ChiTaRSi PPOX. human.
    GeneWikii PPOX.
    GenomeRNAii 5498.
    NextBioi 21268.
    PROi P50336.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50336.
    Bgeei P50336.
    CleanExi HS_PPOX.
    Genevestigatori P50336.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.660.20. 1 hit.
    InterProi IPR002937. Amino_oxidase.
    IPR016040. NAD(P)-bd_dom.
    IPR027418. PPOX_C.
    IPR004572. Protoporphyrinogen_oxidase.
    [Graphical view ]
    Pfami PF01593. Amino_oxidase. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00562. proto_IX_ox. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      Tissue: Placenta.
    2. "Human protoporphyrinogen oxidase: expression, purification, and characterization of the cloned enzyme."
      Dailey T.A., Dailey H.A.
      Protein Sci. 5:98-105(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Placenta.
    3. "Protoporphyrinogen oxidase: complete genomic sequence and polymorphisms in the human gene."
      Puy H., Robreau A.-M., Rosipal R., Nordmann Y., Deybach J.-C.
      Biochem. Biophys. Res. Commun. 226:226-230(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-304.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Lung.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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.
    9. "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.
    10. "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.
    11. "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.
    12. "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.
    13. "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.
    14. "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.
    15. 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.
    16. "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.
    17. "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.
    18. "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.
    19. "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.
    20. "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.
    21. "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.
    22. "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.
    23. "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.
    24. "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.
    25. "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.
    26. "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.
    27. "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.
    28. "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.
    29. "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.
    30. "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.
    31. "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.
    32. "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.
    33. "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.
    34. "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.
    35. "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.
    36. "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.
    37. "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.

    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: October 1, 2014
    This is version 137 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

    External Data

    Dasty 3