UniProtKB/SwissProt variant VAR

Variant information

Variant position:

192

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:

LB/B

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 Glutamine (Q) to Arginine (R) at position 192 (Q192R, p.Gln192Arg).

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 polar (Q) to large size and basic (R)

The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:

1

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

Polymorphism:

The allelic form of the enzyme with Gln-192 (allozyme A) hydrolyzes paraoxon with a low turnover number and the one with Arg-192 (allozyme B) with a high turnover number.

Additional information on the polymorphism described.

Variant description:

In allozyme B; increased arylesterase activity.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs662 [ dbSNP | Ensembl ]

Sequence information

Variant position:

192

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:

355

The length of the canonical sequence.

Location on the sequence:

AVGPEHFYGTNDHYFLDPYL Q SWEMYLGLAWSYVVYYSPSE

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                         AVGPEHFYGTNDHYFLDPYLQSWEMYLGLAWSYVVYYSPSE

Mouse                         AIGPESFYATNDHYFADPYLRSWEMYLGLSWSNVVYYSPDK

Rat                           AVGPESFYATNDHYFADPYLRSWEMYLGLSWSNVVYYSPDK

Rabbit                        AVGPEHFYATNDHYFIDPYLKSWEMHLGLAWSFVTYYSPND

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 – 355	Serum paraoxonase/arylesterase 1
Disulfide bond	42 – 353	In form B
Helix	189 – 197

Literature citations

Characterization of cDNA clones encoding rabbit and human serum paraoxonase: the mature protein retains its signal sequence.
Hassett C.; Richter R.J.; Humbert R.; Chapline C.; Crabb J.W.; Omiecinski C.J.; Furlong C.E.;
Biochemistry 30:10141-10149(1991)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANTS MET-55 AND ARG-192;

Molecular basis for the polymorphic forms of human serum paraoxonase/arylesterase: glutamine or arginine at position 191, for the respective A or B allozymes.
Adkins S.; Gan K.N.; Mody M.; La Du B.N.;
Am. J. Hum. Genet. 52:598-608(1993)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; POLYMORPHISM; VARIANTS MET-55 AND ARG-192;

Studies on human serum paraoxonase/arylesterase.
La Du B.N.; Adkins S.; Kuo C.L.; Lipsig D.;
Chem. Biol. Interact. 87:25-34(1993)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; CATALYTIC ACTIVITY; VARIANTS MET-55 AND ARG-192;

Human and rabbit paraoxonases: purification, cloning, sequencing, mapping and role of polymorphism in organophosphate detoxification.
Furlong C.E.; Costa L.G.; Hassett C.; Richter R.J.; Sundstrom J.A.; Adler D.A.; Disteche C.M.; Omiecinski C.J.; Chapline C.; Crabb J.W.;
Chem. Biol. Interact. 87:35-48(1993)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANTS MET-55 AND ARG-192; CHARACTERIZATION;

Submission
SeattleSNPs variation discovery resource;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANT ARG-192;

The molecular basis of the human serum paraoxonase activity polymorphism.
Humbert R.; Adler D.A.; Disteche C.M.; Hassett C.; Omiecinski C.J.; Furlong C.E.;
Nat. Genet. 3:73-76(1993)
Cited for: POLYMORPHISM; VARIANT ARG-192; CHARACTERIZATION OF VARIANT ARG-192;

DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome.
Ley T.J.; Mardis E.R.; Ding L.; Fulton B.; McLellan M.D.; Chen K.; Dooling D.; Dunford-Shore B.H.; McGrath S.; Hickenbotham M.; Cook L.; Abbott R.; Larson D.E.; Koboldt D.C.; Pohl C.; Smith S.; Hawkins A.; Abbott S.; Locke D.; Hillier L.W.; Miner T.; Fulton L.; Magrini V.; Wylie T.; Glasscock J.; Conyers J.; Sander N.; Shi X.; Osborne J.R.; Minx P.; Gordon D.; Chinwalla A.; Zhao Y.; Ries R.E.; Payton J.E.; Westervelt P.; Tomasson M.H.; Watson M.; Baty J.; Ivanovich J.; Heath S.; Shannon W.D.; Nagarajan R.; Walter M.J.; Link D.C.; Graubert T.A.; DiPersio J.F.; Wilson R.K.;
Nature 456:66-72(2008)
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-192;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P27169: Variant p.Gln192Arg