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P50336

- PPOX_HUMAN

UniProt

P50336 - PPOX_HUMAN

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Protein
Protoporphyrinogen oxidase
Gene
PPOX
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Binds 1 FAD per subunit.

Pathwayi

Sites

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

Regions

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

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
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.
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
Complete GO annotation...

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.
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 (1 Publication). Mutations with intermediate effect on catalytic activity may cause VP, but with a low clinical penetrance (1 Publication).30 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti11 – 111G → D in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications
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. 2 Publications
VAR_070379
Natural varianti15 – 151L → F in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
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. 4 Publications
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. 2 Publications
VAR_070383
Natural varianti40 – 401G → A in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
VAR_070384
Natural varianti40 – 401G → E in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications
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. 8 Publications
VAR_003686
Natural varianti73 – 731L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
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. 2 Publications
VAR_070389
Natural varianti85 – 851L → P in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications
VAR_070390
Natural varianti106 – 1061H → P in VP; strongly decreases enzyme activity;. 2 Publications
VAR_070391
Natural varianti138 – 1381R → P in VP; slightly decreases enzyme activity. 2 Publications
VAR_070392
Natural varianti139 – 1391G → D in VP; strongly decreases enzyme activity. 2 Publications
VAR_070393
Natural varianti143 – 1431D → V in VP; strongly decreases enzyme activity. 2 Publications
VAR_070394
Natural varianti152 – 1521R → C in VP; strongly decreases enzyme activity. 5 Publications
VAR_003687
Natural varianti154 – 1541L → P in VP; strongly decreases enzyme activity. 2 Publications
VAR_070395
Natural varianti158 – 1581V → L in VP. 1 Publication
VAR_070396
Natural varianti158 – 1581V → M in VP; strongly decreases enzyme activity. 2 Publications
VAR_070397
Natural varianti168 – 1681R → C in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization. 4 Publications
VAR_003688
Natural varianti168 – 1681R → H in VP; strongly decreases enzyme activity. 3 Publications
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. 2 Publications
VAR_070401
Natural varianti205 – 2051A → V in VP; no effect on enzyme activity. 2 Publications
VAR_070402
Natural varianti217 – 2171R → C in VP; decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
VAR_070403
Natural varianti224 – 2241W → G in VP; abolishes enzyme activity; impairs protein folding and/or stability. 3 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. 3 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. 2 Publications
VAR_070409
Natural varianti283 – 2831I → N in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
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. 2 Publications
VAR_070412
Natural varianti330 – 3301G → R in VP; strongly decreases enzyme activity. 3 Publications
VAR_070413
Natural varianti332 – 3321G → A in VP; abolishes activity; impairs protein folding and/or stability. 3 Publications
VAR_070414
Natural varianti335 – 3351V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 3 Publications
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. 3 Publications
VAR_070416
Natural varianti349 – 3491D → A in VP; decreases enzyme activity. 3 Publications
VAR_070417
Natural varianti350 – 3501S → P in VP; abolishes activity; impairs protein folding and/or stability. 2 Publications
VAR_070418
Natural varianti358 – 3581G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
VAR_070419
Natural varianti397 – 3971A → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
VAR_070420
Natural varianti401 – 4011L → F in VP; strongly decreases enzyme activity. 3 Publications
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. 2 Publications
VAR_070424
Natural varianti444 – 4441L → P in VP; strongly decreases enzyme activity. 2 Publications
VAR_070425
Natural varianti448 – 4481G → R in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications
VAR_070426
Natural varianti450 – 4501S → P in VP; strongly decreases enzyme activity. 2 Publications
VAR_070427
Natural varianti453 – 4531G → R in VP; strongly decreases enzyme activity. 3 Publications
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 oxidase
PRO_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

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.

Family & Domainsi

Sequence similaritiesi

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. 2 Publications
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. 2 Publications
VAR_070379
Natural varianti15 – 151L → F in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
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. 4 Publications
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. 2 Publications
VAR_070383
Natural varianti40 – 401G → A in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
VAR_070384
Natural varianti40 – 401G → E in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications
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. 8 Publications
VAR_003686
Natural varianti73 – 731L → P in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
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. 2 Publications
VAR_070389
Natural varianti85 – 851L → P in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications
VAR_070390
Natural varianti106 – 1061H → P in VP; strongly decreases enzyme activity;. 2 Publications
VAR_070391
Natural varianti138 – 1381R → P in VP; slightly decreases enzyme activity. 2 Publications
VAR_070392
Natural varianti139 – 1391G → D in VP; strongly decreases enzyme activity. 2 Publications
VAR_070393
Natural varianti143 – 1431D → V in VP; strongly decreases enzyme activity. 2 Publications
VAR_070394
Natural varianti152 – 1521R → C in VP; strongly decreases enzyme activity. 5 Publications
VAR_003687
Natural varianti154 – 1541L → P in VP; strongly decreases enzyme activity. 2 Publications
VAR_070395
Natural varianti158 – 1581V → L in VP. 1 Publication
VAR_070396
Natural varianti158 – 1581V → M in VP; strongly decreases enzyme activity. 2 Publications
VAR_070397
Natural varianti168 – 1681R → C in VP; strongly decreases enzyme activity; does not affect mitochondrial protein targeting and localization. 4 Publications
VAR_003688
Natural varianti168 – 1681R → H in VP; strongly decreases enzyme activity. 3 Publications
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. 2 Publications
VAR_070401
Natural varianti205 – 2051A → V in VP; no effect on enzyme activity. 2 Publications
VAR_070402
Natural varianti217 – 2171R → C in VP; decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
VAR_070403
Natural varianti224 – 2241W → G in VP; abolishes enzyme activity; impairs protein folding and/or stability. 3 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. 3 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. 2 Publications
VAR_070409
Natural varianti283 – 2831I → N in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
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. 2 Publications
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. 3 Publications
VAR_070413
Natural varianti332 – 3321G → A in VP; abolishes activity; impairs protein folding and/or stability. 3 Publications
VAR_070414
Natural varianti335 – 3351V → G in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 3 Publications
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. 3 Publications
VAR_070416
Natural varianti349 – 3491D → A in VP; decreases enzyme activity. 3 Publications
VAR_070417
Natural varianti350 – 3501S → P in VP; abolishes activity; impairs protein folding and/or stability. 2 Publications
VAR_070418
Natural varianti358 – 3581G → R in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
VAR_070419
Natural varianti397 – 3971A → D in VP; strongly decreases enzyme activity; impairs protein folding and/or stability. 2 Publications
VAR_070420
Natural varianti401 – 4011L → F in VP; strongly decreases enzyme activity. 3 Publications
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. 2 Publications
VAR_070424
Natural varianti444 – 4441L → P in VP; strongly decreases enzyme activity. 2 Publications
VAR_070425
Natural varianti448 – 4481G → R in VP; abolishes enzyme activity; impairs protein folding and/or stability. 2 Publications
VAR_070426
Natural varianti450 – 4501S → P in VP; strongly decreases enzyme activity. 2 Publications
VAR_070427
Natural varianti453 – 4531G → R in VP; strongly decreases enzyme activity. 3 Publications
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 136 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

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