Variant position: 134 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 367 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 EEQDLER-LRDPEVVASELGY VFQAITLTRQRLAGRVPLIGF
Mouse EERDLER-LRDPAAAASELGY VFQAITLTRQRLAGRVPLIG
Sheep EERDLER-LRDPATVASELGY VFQAITLTRQQLAGRVPLIG
Zebrafish EPEDLQR-LKTQVDVYSELDY VFKAITLTRHKIEGKVPLIG
Drosophila VPEDLKR-L-TPDGALSRLSY VGDAITMMRHKLEGRVPLIG
Slime mold TIEDLSR-VQFPVDVNKELGY VFDALTLTRKRLEGRVPLIG
Baker's yeast NPEDLQTVLDYKVDVLKELDW AFKAITMTRIKLDGEVPLFG
Fission yeast VPEDIDL-LEKTPNISAKLGY VMDAISLTREKLDGQVPLMG
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 – 367 Uroporphyrinogen decarboxylase
132 – 145
Functional consequences of naturally occurring mutations in human uroporphyrinogen decarboxylase.
Phillips J.D.; Parker T.L.; Schubert H.L.; Whitby F.G.; Hill C.P.; Kushner J.P.;
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF VARIANTS FPCT ASP-156; LEU-232 AND THR-260; VARIANTS FPCT GLU-25; SER-80; GLN-134; ASP-156; ARG-165; LYS-167; PRO-193; LEU-232; GLN-253 AND THR-260; CHARACTERIZATION OF VARIANTS FPCT GLU-25; SER-80; GLN-134; ASP-156; ARG-165; LYS-167; PRO-193; LEU-232; GLN-253 AND THR-260;
Molecular defects of uroporphyrinogen decarboxylase in a patient with mild hepatoerythropoietic porphyria.
Meguro K.; Fujita H.; Ishida N.; Akagi R.; Kurihara T.; Galbraith R.A.; Kappas A.; Zabriskie J.B.; Toback A.C.; Harber L.C.; Sassa S.;
J. Invest. Dermatol. 102:681-685(1994)
Cited for: VARIANTS HEP GLN-134 AND PRO-220;
Three new mutations in the uroporphyrinogen decarboxylase gene in familial porphyria cutanea tarda.
McManus J.F.; Begley C.G.; Sassa S.; Ratnaike S.;
Hum. Mutat. 13:412-412(1999)
Cited for: VARIANT FPCT GLN-134;
Co-inheritance of mutations in the uroporphyrinogen decarboxylase and hemochromatosis genes accelerates the onset of porphyria cutanea tarda.
Brady J.J.; Jackson H.A.; Roberts A.G.; Morgan R.R.; Whatley S.D.; Rowlands G.L.; Darby C.; Shudell E.; Watson R.; Paiker J.; Worwood M.W.; Elder G.H.;
J. Invest. Dermatol. 115:868-874(2000)
Cited for: VARIANTS FPCT SER-80; GLN-134; PRO-144; GLN-216; LYS-218; VAL-281; ARG-282; SER-303 AND ARG-318; CHARACTERIZATION OF VARIANTS FPCT PRO-144 AND LYS-218;
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