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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P08397: Variant p.Arg167Trp

Porphobilinogen deaminase
Gene: HMBS
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Variant information Variant position: help 167 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Arginine (R) to Tryptophan (W) at position 167 (R167W, p.Arg167Trp). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from large size and basic (R) to large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In AIP and ENCEP; severely decreased hydroxymethylbilane synthase activity; results in less than 5% of wild-type activity; 2-fold decrease of Vmax; 33-fold increase of KM. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 167 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 361 The length of the canonical sequence.
Location on the sequence: help SLRRAAQLQRKFPHLEFRSI R GNLNTRLRKLDEQQEFSAII 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         SLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDE-QQEFSAII

Mouse                         SLRRVAQLQRKFPHLEFKSIRGNLNTRLRKLDE-LQEFSAI

Rat                           SLRRVAQLQRKFPHLEFKSIRGNLNTRLRKLDE-QLEFSAI

Bovine                        SLRRAAQLQRKFPHLEFKSIRGNLNTRLRKLDE-LQEFSAI

Slime mold                    SLRRVAQLKKAYPHLQFKDIRGNLNTRFKKLEDDSNGYDGM

Baker's yeast                 SVRRSAQLKRKYPHLKFESVRGNIQTRLQKLDDPKSPYQCI

Fission yeast                 SIRRRALLARNFPHLRFVDIRGNVGTRLAKLDAPDSQFDCL
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 2 – 361 Porphobilinogen deaminase
Modified residue 147 – 147 Phosphoserine



Literature citations
High frequency of mutations in exon 10 of the porphobilinogen deaminase gene in patients with a CRIM-positive subtype of acute intermittent porphyria.
Gu X.-F.; de Rooij F.W.M.; Voortman G.; Te Velde K.; Nordmann Y.; Grandchamp B.;
Am. J. Hum. Genet. 51:660-665(1992)
Cited for: VARIANT AIP TRP-167; Homozygous acute intermittent porphyria: compound heterozygosity for adjacent base transitions in the same codon of the porphobilinogen deaminase gene.
Llewellyn D.H.; Smyth S.J.; Elder G.H.; Hutchesson A.C.; Rattenbury J.M.; Smith M.F.;
Hum. Genet. 89:97-98(1992)
Cited for: VARIANTS ENCEP TRP-167 AND GLN-167; INVOLVEMENT IN ENCEP; CRIM-positive mutations of acute intermittent porphyria in Finland.
Kauppinen R.; Peltonen L.; Pihlaja H.; Mustajoki P.;
Hum. Mutat. 1:392-396(1992)
Cited for: VARIANTS AIP TRP-167 AND GLN-173; Acute intermittent porphyria in Finland: 19 mutations in the porphobilinogen deaminase gene.
Kauppinen R.; Mustajoki S.; Pihlaja H.; Peltonen L.; Mustajoki P.;
Hum. Mol. Genet. 4:215-222(1995)
Cited for: VARIANTS AIP CYS-26; ARG-98; TRP-116; TRP-167; GLN-173; TRP-173; CYS-195; GLY-225; ARG-238; PHE-247 AND ARG-280; Genetic investigation of the porphobilinogen deaminase gene in Swedish acute intermittent porphyria families.
Lundin G.; Lee J.-S.; Thunell S.; Anvret M.;
Hum. Genet. 100:63-66(1997)
Cited for: VARIANTS AIP TRP-116; LEU-119; GLN-167; TRP-167; TRP-173; TRP-201 AND ASP-216; Identification and expression of mutations in the hydroxymethylbilane synthase gene causing acute intermittent porphyria (AIP).
Solis C.; Lopez-Echaniz I.; Sefarty-Graneda D.; Astrin K.H.; Desnick R.J.;
Mol. Med. 5:664-671(1999)
Cited for: VARIANTS AIP ARG-111; TRP-116; TRP-167; TRP-173 AND VAL-212; CHARACTERIZATION OF VARIANT AIP VAL-212; Conformational stability and activity analysis of two hydroxymethylbilane synthase mutants, K132N and V215E, with different phenotypic association with acute intermittent porphyria.
Bustad H.J.; Vorland M.; Ronneseth E.; Sandberg S.; Martinez A.; Toska K.;
Biosci. Rep. 33:0-0(2013)
Cited for: VARIANT ASN-132; CHARACTERIZATION OF VARIANTS AIP TRP-116; TRP-167; TRP-173 AND GLU-215; CHARACTERIZATION OF VARIANT ASN-132; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES;
Disclaimer: 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.