UniProtKB/Swiss-Prot P07225: Variant p.Arg233Lys

• Variant information
• Sequence information
• Literature citations
• All

Variant information

Variant position: 233 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 Arginine (R) to Lysine (K) at position 233 (R233K, p.Arg233Lys). 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: Similar physico-chemical property. Both residues are large size and basic. 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: Does not affect protein levels; the mutant is normally secreted. Any additional useful information about the variant.
Other resources: Links to websites of interest for the variant.

• Variant rs41267007 [ dbSNP | Ensembl ]

Sequence information

Variant position: 233 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 676 The length of the canonical sequence.
Location on the sequence: GTAVCKNIPGDFECECPEGY R YNLKSKSCEDIDECSENMCA 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.
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	42 – 676	Vitamin K-dependent protein S
Domain	201 – 242	EGF-like 3; calcium-binding
Disulfide bond	228 – 241
Beta strand	233 – 235

Literature citations

Optimization of a simple and rapid single-strand conformation analysis for detection of mutations in the PROS1 gene: identification of seven novel mutations and three novel, apparently neutral, variants.
Espinosa-Parrilla Y.; Morell M.; Borrell M.; Souto J.C.; Fontcuberta J.; Estivill X.; Sala N.;
Hum. Mutat. 15:463-473(2000)
Cited for: VARIANTS THPH5 HIS-15; THR-640 AND LEU-667; VARIANTS SER-98; LYS-233 AND MET-559; Functional characterization of twelve natural PROS1 mutations associated with anticoagulant protein S deficiency.
Hurtado B.; Munoz X.; Mulero M.C.; Navarro G.; Domenech P.; Garcia de Frutos P.; Perez-Riba M.; Sala N.;
Haematologica 93:574-580(2008)
Cited for: CHARACTERIZATION OF VARIANTS THPH5 HIS-15 AND THR-640; CHARACTERIZATION OF VARIANT LYS-233; Analysis of protein-coding genetic variation in 60,706 humans.
Lek M.; Karczewski K.J.; Minikel E.V.; Samocha K.E.; Banks E.; Fennell T.; O'Donnell-Luria A.H.; Ware J.S.; Hill A.J.; Cummings B.B.; Tukiainen T.; Birnbaum D.P.; Kosmicki J.A.; Duncan L.E.; Estrada K.; Zhao F.; Zou J.; Pierce-Hoffman E.; Berghout J.; Cooper D.N.; Deflaux N.; DePristo M.; Do R.; Flannick J.; Fromer M.; Gauthier L.; Goldstein J.; Gupta N.; Howrigan D.; Kiezun A.; Kurki M.I.; Moonshine A.L.; Natarajan P.; Orozco L.; Peloso G.M.; Poplin R.; Rivas M.A.; Ruano-Rubio V.; Rose S.A.; Ruderfer D.M.; Shakir K.; Stenson P.D.; Stevens C.; Thomas B.P.; Tiao G.; Tusie-Luna M.T.; Weisburd B.; Won H.H.; Yu D.; Altshuler D.M.; Ardissino D.; Boehnke M.; Danesh J.; Donnelly S.; Elosua R.; Florez J.C.; Gabriel S.B.; Getz G.; Glatt S.J.; Hultman C.M.; Kathiresan S.; Laakso M.; McCarroll S.; McCarthy M.I.; McGovern D.; McPherson R.; Neale B.M.; Palotie A.; Purcell S.M.; Saleheen D.; Scharf J.M.; Sklar P.; Sullivan P.F.; Tuomilehto J.; Tsuang M.T.; Watkins H.C.; Wilson J.G.; Daly M.J.; MacArthur D.G.;
Nature 536:285-291(2016)
Cited for: VARIANT LYS-233;