Variant position: 152 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 477 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human RELTKP-----RGKEP--DETVHSFAQ RRLGPE-VASLAMDSLCRGVFA
Mouse RELLKP-----RGKEP--DETVHSFAQ RRLGPE-VASLAMD
Bovine RDLTTP-----RGKDP--DETVHSFAQ RRLGPE-VASLAMD
Slime mold KEPFKKVPSQVKEMDPNWDESVHDFFS RRLGKT-MTKTFIE
Baker's yeast GEWFRK-----KSPHPGQDESVESICD RRFGNNYISNNMIS
Fission yeast LEPFR------KSKRDSTDESVGSFMR RRFGKN-VTDRVMS
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
1 – 477 Protoporphyrinogen oxidase
166 – 166 L -> N. Decreases enzyme activity by 95%.
169 – 169 G -> A. Decreases enzyme activity by 64%.
146 – 154
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)
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;
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)
Cited for: VARIANT VP CYS-152;
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)
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;
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)
Cited for: VARIANTS VP CYS-152 AND PHE-401; CHARACTERIZATION OF VARIANT VP CYS-152;
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)
Cited for: VARIANTS VP CYS-152; LEU-158; VAL-205 AND ARG-330;
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