UniProtKB/Swiss-Prot P08397: Variant p.Val215Glu

Porphobilinogen deaminase
Gene: HMBS
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Variant information Variant position:

215 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

US 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:

From Valine (V) to Glutamate (E) at position 215 (V215E, p.Val215Glu). 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:

Change from medium size and hydrophobic (V) to medium size and acidic (E) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-2 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:

In AIP; uncertain significance; decreased hydroxymethylbilane synthase activity; results in 30% of wild-type activity; 3-fold decrease of Vmax; normal KM; affects protein conformation. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs1205219549 [ dbSNP | Ensembl ]

Sequence information Variant position:

215 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:

RMGWHNRVGQILHPEECMYA V GQGALGVEVRAKDQDILDLV 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                         RMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLV

Mouse                         RMGWQNRVGQILHPEECMYAVGQGALAVEVRAKDQDILDLV

Rat                           RMGWQNRVGQILHPEECMYAVGQGALAVEVRAKDQDILDLV

Bovine                        RMGWQNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLV

Slime mold                    RMELTDHISEIIPDSISLYAVGQGSLGIECKDGDDFIQSIL

Baker's yeast                 RMGLENRITQRFHSDTMYHAVGQGALGIEIRKGDTKMMKIL

Fission yeast                 RLGLKDRIAQMLTAPFVYYAVGQGALAVEVRADDKEMIEML

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
Chain	2 – 361	Porphobilinogen deaminase
Mutagenesis	195 – 195	R -> A. Loss of hydroxymethylbilane synthase activity.
Turn	215 – 218

Literature citations
Haplotype analysis of Norwegian and Swedish patients with acute intermittent porphyria (AIP): Extreme haplotype heterogeneity for the mutation R116W.
Tjensvoll K.; Bruland O.; Floderus Y.; Skadberg O.; Sandberg S.; Apold J.;
Dis. Markers 19:41-46(2003)
Cited for: VARIANTS AIP GLU-215 AND PRO-238; 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.