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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P50336: Variant p.Arg152Cys

Protoporphyrinogen oxidase
Gene: PPOX
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Variant information Variant position: help 152 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Arginine (R) to Cysteine (C) at position 152 (R152C, p.Arg152Cys). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from large size and basic (R) to medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In VP; strongly decreases enzyme activity. Any additional useful information about the variant.


Sequence information Variant position: help 152 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 477 The length of the canonical sequence.
Location on the sequence: help RELTKPRGKEPDETVHSFAQ R RLGPEVASLAMDSLCRGVFA 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         RELTKP-----RGKEP--DETVHSFAQRRLGPE-VASLAMDSLCRGVFA

Mouse                         RELLKP-----RGKEP--DETVHSFAQRRLGPE-VASLAMD

Bovine                        RDLTTP-----RGKDP--DETVHSFAQRRLGPE-VASLAMD

Slime mold                    KEPFKKVPSQVKEMDPNWDESVHDFFSRRLGKT-MTKTFIE

Baker's yeast                 GEWFRK-----KSPHPGQDESVESICDRRFGNNYISNNMIS

Fission yeast                 LEPFRK----SKRDST--DESVGSFMRRRFGKN-VTDRVMS
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 1 – 477 Protoporphyrinogen oxidase
Mutagenesis 166 – 166 L -> N. Decreases enzyme activity by 95%.
Mutagenesis 169 – 169 G -> A. Decreases enzyme activity by 64%.
Helix 146 – 154



Literature citations
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;
Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.