Variant position: 34 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 GLAASYHLSRA--------PCPPKVVLV ESSERLGGWIRSVR------GPNGAIF
Mouse GLAASYHLIRG--------PSPPKVILV EGSKRLGGWIRSI
Bovine GLAASYYLSRA--------PCPPKVVLV EGSERLGGWIRSV
Slime mold GLSSYYYLRNGINLTSKFSKNNLKINIF EKSNKVGGNIQT-
Baker's yeast GLCFTYFLSKL--------RPDVEITLF ESQNRTGGWIYSC
Fission yeast GLSTAFYLARL--------IPKCTIDLY EKGPRLGGWLQSV
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
34 – 35 FAD
42 – 42 FAD; via amide nitrogen
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;
Quantitative structural insight into human variegate porphyria disease.
Wang B.; Wen X.; Qin X.; Wang Z.; Tan Y.; Shen Y.; Xi Z.;
J. Biol. Chem. 288:11731-11740(2013)
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF MUTANTS GLY-59 AND GLN-59 IN COMPLEXES WITH FAD AND ACIFLUORFEN; FUNCTION; CATALYTIC ACTIVITY; MUTAGENESIS OF ARG-59; ARG-97; LEU-166; GLY-169; PHE-331; LEU-334; VAL-347 AND MET-368; CHARACTERIZATION OF VARIANTS VP TRP-59; HIS-168; ARG-330; GLY-335; ALA-349; PHE-401 AND ARG-453;
Genetic and biochemical studies in Argentinean patients with variegate porphyria.
Rossetti M.V.; Granata B.X.; Giudice J.; Parera V.E.; Batlle A.;
BMC Med. Genet. 9:54-54(2008)
Cited for: VARIANTS VP VAL-34; GLY-224 AND ALA-332;
Functional characterization of five protoporphyrinogen oxidase missense mutations found in Argentinean variegate porphyria patients.
Mendez M.; Granata B.X.; Jimenez M.J.; Parera V.E.; Batlle A.; de Salamanca R.E.; Rossetti M.V.;
JIMD Rep. 4:91-97(2012)
Cited for: VARIANTS VP VAL-34; PHE-76; GLY-224; ALA-332 AND CYS-422; CHARACTERIZATION OF VARIANTS VP VAL-34; PHE-76; GLY-224; ALA-332 AND CYS-422;
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