Variant position: 401 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 GCVLSQELFQQRAQEAAATQ LGLKEMPSHC---LVHLHKNCIPQ
Mouse GHQLSPELFQQQAQEAAATQ LGLKEPPSHC---LVHLHKNC
Bovine GCVLSQELLQQEAEKAAATQ LGLNEPPSHC---LVHLHKNS
Slime mold ----SKDKLLDIALKHLDKV LDIESSPDFT---NVSIYDNG
Baker's yeast VVP-SREVTINAVKDALNNH LGISNKDLEAGQWEFTIADRC
Fission yeast LIPTNPEEAVNNALKALQHT LKISSKPTLT---NATLQQNC
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
386 – 401
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;
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;
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.