UniProtKB/Swiss-Prot Q9UHD2: Variant p.Val464Ala

Serine/threonine-protein kinase TBK1
Gene: TBK1
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Variant information Variant position:

464 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 Valine (V) to Alanine (A) at position 464 (V464A, p.Val464Ala). 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 small size and hydrophobic (A) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

0 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
Other resources:

Links to websites of interest for the variant.

Variant rs35635889 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

RWLIELIKDDYNETVHKKTE V VITLDFCIRNIEKTVKVYEK 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                         RWLIELIKDDYNETVHKKTEVVITLDFCIRNIEKTVKVYEK

Mouse                         RWLVELVKDDYNETVHKKTEVVITLDFCIRNIEKTVKVYEK

Xenopus laevis                RWLSELMKEEYNENVHRNTEVSLKLNFCNRTTEKDLKIYEQ

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 – 729	Serine/threonine-protein kinase TBK1
Coiled coil	407 – 657
Mutagenesis	448 – 448	E -> R. Decreases phosphorylation and kinase activity. Abolishes dimerization; when associated with R-355.
Mutagenesis	459 – 459	H -> E. Abolishes dimerization and decreases kinase activity but no effect on phosphorylation; when associated with E-466 and E-470.
Mutagenesis	466 – 466	I -> E. Abolishes dimerization and decreases kinase activity but no effect on phosphorylation; when associated with E-459 and E-470.
Mutagenesis	470 – 470	F -> E. Abolishes dimerization and decreases kinase activity but no effect on phosphorylation; when associated with E-459 and E-466.
Helix	408 – 480

Literature citations
Copy number variations on chromosome 12q14 in patients with normal tension glaucoma.
Fingert J.H.; Robin A.L.; Stone J.L.; Roos B.R.; Davis L.K.; Scheetz T.E.; Bennett S.R.; Wassink T.H.; Kwon Y.H.; Alward W.L.; Mullins R.F.; Sheffield V.C.; Stone E.M.;
Hum. Mol. Genet. 20:2482-2494(2011)
Cited for: INVOLVEMENT IN GLC1P; TISSUE SPECIFICITY; VARIANTS PHE-151; ILE-306 AND ALA-464; Patterns of somatic mutation in human cancer genomes.
Greenman C.; Stephens P.; Smith R.; Dalgliesh G.L.; Hunter C.; Bignell G.; Davies H.; Teague J.; Butler A.; Stevens C.; Edkins S.; O'Meara S.; Vastrik I.; Schmidt E.E.; Avis T.; Barthorpe S.; Bhamra G.; Buck G.; Choudhury B.; Clements J.; Cole J.; Dicks E.; Forbes S.; Gray K.; Halliday K.; Harrison R.; Hills K.; Hinton J.; Jenkinson A.; Jones D.; Menzies A.; Mironenko T.; Perry J.; Raine K.; Richardson D.; Shepherd R.; Small A.; Tofts C.; Varian J.; Webb T.; West S.; Widaa S.; Yates A.; Cahill D.P.; Louis D.N.; Goldstraw P.; Nicholson A.G.; Brasseur F.; Looijenga L.; Weber B.L.; Chiew Y.-E.; DeFazio A.; Greaves M.F.; Green A.R.; Campbell P.; Birney E.; Easton D.F.; Chenevix-Trench G.; Tan M.-H.; Khoo S.K.; Teh B.T.; Yuen S.T.; Leung S.Y.; Wooster R.; Futreal P.A.; Stratton M.R.;
Nature 446:153-158(2007)
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-271; GLU-291; HIS-296; ARG-410 AND ALA-464;

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.