UniProtKB/Swiss-Prot Q86W24: Variant p.Asp86Val

NACHT, LRR and PYD domains-containing protein 14
Gene: NLRP14
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Variant information Variant position:

86 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 Aspartate (D) to Valine (V) at position 86 (D86V, p.Asp86Val). 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 acidic (D) to medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-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:

Increased tendency to form aggregates. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs199735773 [ dbSNP | Ensembl ]

Sequence information Variant position:

86 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

1093 The length of the canonical sequence.
Location on the sequence:

YPGEKAWSVSLKIFGKMNLK D LCERAKEEINWSAQTIGPDD 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                         YPGEKAWSVSLKIFGKMNLKDLCERAKEEINWSAQTIGPDD

Mouse                         ----------------------MKTEDDEMEYEA-------

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	1 – 1093	NACHT, LRR and PYD domains-containing protein 14
Domain	1 – 97	Pyrin
Mutagenesis	84 – 84	L -> R. Increased thermal stability of the Pyrin domain.
Helix	85 – 100

Literature citations
Mutations in the testis-specific NALP14 gene in men suffering from spermatogenic failure.
Westerveld G.H.; Korver C.M.; van Pelt A.M.M.; Leschot N.J.; van der Veen F.; Repping S.; Lombardi M.P.;
Hum. Reprod. 21:3178-3184(2006)
Cited for: TISSUE SPECIFICITY; DEVELOPMENTAL STAGE; VARIANTS THR-48; GLN-55; VAL-86; ARG-92; LEU-98; THR-375; ILE-397; MET-441; GLY-522; LYS-808; THR-951; SER-954; PHE-1010 AND ILE-1019; Structures of the NLRP14 pyrin domain reveal a conformational switch mechanism regulating its molecular interactions.
Eibl C.; Hessenberger M.; Wenger J.; Brandstetter H.;
Acta Crystallogr. D 70:2007-2018(2014)
Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 1-100 OF WILD-TYPE AND VARIANT VAL-86; DOMAIN; CHARACTERIZATION OF VARIANT VAL-86; MUTAGENESIS OF LEU-84; 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 VAL-86;

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.