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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P50336: Variant p.Tyr348Cys

Protoporphyrinogen oxidase
Gene: PPOX
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Variant information Variant position: help 348 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 Tyrosine (Y) to Cysteine (C) at position 348 (Y348C, p.Tyr348Cys). 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 aromatic (Y) to medium size and polar (C) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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; results in enzyme activity decrease; impairs protein folding and/or stability; more resistant to thermal denaturation than wild-type enzyme. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 348 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 VQGFGHLVPSSEDPGVLGIV Y DSVAFPEQDGSPPGLRVTVM 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                         VQGFGHLVPSS--EDPG-VLGIVYDSVAFPE-------QDGSPPGLR------VTVM

Mouse                         VQGFGHLVPSS--EDPT-VLGIVYDSVAFPE-------QDG

Bovine                        VQGFGHLVPSS--EDPV-ILGIVYDSVAFPE-------QDG

Slime mold                    DKGFGYLVPSK--ENQS-VIGVCFDSNTFPEFVNNNNNNNN

Baker's yeast                 LQGFGYLVPKSN-KNPGKLLGVIFDSVIERNFKPLFDKLST

Fission yeast                 IRGFGLLIPSCTPNNPNHVLGIVFDS------------EQN

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 331 – 331 F -> A. Decreases enzyme activity by 50%.
Mutagenesis 334 – 334 L -> A. Decreases enzyme activity by 86%.
Mutagenesis 347 – 347 V -> A. Decreases enzyme activity by 45%.
Mutagenesis 368 – 368 M -> A. Decreases enzyme activity by 52%.



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; 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)
Cited for: VARIANTS VP TRP-59; PRO-138 AND CYS-348; 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;
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.