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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P50336: Variant p.Arg168Cys

Protoporphyrinogen oxidase
Gene: PPOX
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Variant information Variant position: help 168 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 168 (R168C, p.Arg168Cys). 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; does not affect mitochondrial protein targeting and localization. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 168 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 SFAQRRLGPEVASLAMDSLC R GVFAGNSRELSIRSCFPSLF 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                         SFAQRRLGPE-VASLAMDSLCRGVFAGNSRELSIRSC-FPSLF

Mouse                         SFAQRRLGPE-VASLAMDSLCRGVFAGNSRELSIRSC-FPS

Bovine                        SFAQRRLGPE-VASLAMDSLCRGVFAGNSRELSIRSC-FPS

Slime mold                    DFFSRRLGKT-MTKTFIEPTILGIYGGDYTNLSIKST-FKR

Baker's yeast                 SICDRRFGNNYISNNMISALLRGIYGDDVSLLSAKRT-FKK

Fission yeast                 SFMRRRFGKN-VTDRVMSAMINGIYAGDLNDLSMHSSMFGF

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 163 – 171



Literature citations
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)
Cited for: VARIANTS VP PRO-20; TRP-59 AND CYS-168; 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)
Cited for: VARIANTS VP TRP-59 AND CYS-168; 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)
Cited for: CHARACTERIZATION OF VARIANTS VP PRO-20; TRP-59; CYS-168 AND CYS-348; Mitochondrial targeting of human protoporphyrinogen oxidase.
Davids L.M.; Corrigall A.V.; Meissner P.N.;
Cell Biol. Int. 30:416-426(2006)
Cited for: CHARACTERIZATION OF VARIANTS VP PRO-20; TRP-59 AND CYS-168;
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.