Variant position: 20 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 MGRTVVVLGGGISGLAASY HLSRA--------PCPPKVVLVESSERLG
Mouse MGRTVIVLGGGISGLAASY HLIRG--------PSPPKVIL
Bovine MGRTVVVLGGGISGLAASY YLSRA--------PCPPKVVL
Slime mold MIQKVGIIGSGISGLSSYY YLRNGINLTSKFSKNNLKINI
Baker's yeast PRAKVAVVGGGVSGLCFTY FLSKL--------RPDVEITL
Fission yeast --MSIAICGGGIAGLSTAF YLARL--------IPKCTIDL
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
12 – 22
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;
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;
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;
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