Variant position: 26 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 361 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 NAAATAEENSPKMRVIRVGT RKSQLARIQTDSVVATLKASY
Mouse GAATTAEENGSKMRVIRVGT RKSQLARIQTDTVVAMLKALY
Rat GAATTAEENGSMMRVIRVGT RKSQLARIQTDTVVAMLKTLY
Bovine NAAAIAEEDTPKMRVIRVGT RKSQLARIQTDSVVATLKALY
Slime mold ------MSSITKRDKVIIGS RKSQLAMLQTEWVRDRIQELN
Baker's yeast --------MGP--ETLHIGG RKSKLAVIQSNHVLKLIEEKY
Fission yeast ---------MPSCTSFPIGT RKSKLAVIQSEIIREELEKHY
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
2 – 361 Porphobilinogen deaminase
15 – 15 Phosphoserine
20 – 28
Acute intermittent porphyria caused by an arginine to histidine substitution (R26H) in the cofactor-binding cleft of porphobilinogen deaminase.
Llewellyn D.H.; Whatley S.D.; Elder G.H.;
Hum. Mol. Genet. 2:1315-1316(1993)
Cited for: VARIANT AIP HIS-26;
Comparison of complementary and genomic DNA sequencing for the detection of mutations in the HMBS gene in British patients with acute intermittent porphyria: identification of 25 novel mutations.
Whatley S.D.; Woolf J.R.; Elder G.H.;
Hum. Genet. 104:505-510(1999)
Cited for: VARIANTS AIP CYS-22; CYS-26; HIS-26; PRO-31; SER-42; ASN-61; ARG-85; GLY-90; ARG-111; GLN-173; TRP-173; ARG-177; CYS-195; ASP-219; ARG-247 AND ILE-269;
Acute intermittent porphyria in Sweden. Molecular, functional and clinical consequences of some new mutations found in the porphobilinogen deaminase gene.
Floderus Y.; Shoolingin-Jordan P.M.; Harper P.;
Clin. Genet. 62:288-297(2002)
Cited for: VARIANTS AIP CYS-26; HIS-26; VAL-86; PRO-92; GLY-99; ARG-111; THR-113; GLN-173; ASN-178; GLN-225; GLY-225; TYR-256; ASP-260 AND PRO-343;
Molecular study of the hydroxymethylbilane synthase gene (HMBS) among Polish patients with acute intermittent porphyria.
Gregor A.; Schneider-Yin X.; Szlendak U.; Wettstein A.; Lipniacka A.; Ruefenacht U.B.; Minder E.I.;
Hum. Mutat. 19:310-310(2002)
Cited for: VARIANTS AIP HIS-26; TYR-61; VAL-93 DEL; ARG-111; GLN-173 AND ASP-335;
Nine mutations including three novel mutations among Russian patients with acute intermittent porphyria.
Pischik E.; Mehtaelae S.; Kauppinen R.;
Hum. Mutat. 26:496-496(2005)
Cited for: VARIANTS AIP HIS-26; TRP-173; CYS-195; ARG-247 AND ALA-250; CHARACTERIZATION OF VARIANTS AIP HIS-26; TRP-173; CYS-195; ARG-247 AND ALA-250;
Acute intermittent porphyria--impact of mutations found in the hydroxymethylbilane synthase gene on biochemical and enzymatic protein properties.
Ulbrichova D.; Hrdinka M.; Saudek V.; Martasek P.;
FEBS J. 276:2106-2115(2009)
Cited for: VARIANTS AIP CYS-26; HIS-26; GLN-173; LYS-204 AND ASP-250; CHARACTERIZATION OF VARIANTS AIP CYS-26; HIS-26; GLN-173; LYS-204 AND ASP-250;
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