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UniProtKB/Swiss-Prot Q06187: Variant p.Arg28His

Tyrosine-protein kinase BTK
Gene: BTK
Variant information

Variant position:  28
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LP/P [Disclaimer]
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 Histidine (H) at position 28 (R28H, p.Arg28His).
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 large size and basic (R) to medium size and polar (H)
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

Variant description:  In XLA; moderate.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.

Sequence information

Variant position:  28
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  659
The length of the canonical sequence.

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.




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.

Chain 2 – 659 Tyrosine-protein kinase BTK
Domain 3 – 133 PH
Binding site 26 – 26 Inositol-(1,3,4,5)-tetrakisphosphate
Binding site 28 – 28 Inositol-(1,3,4,5)-tetrakisphosphate
Binding site 39 – 39 Inositol-(1,3,4,5)-tetrakisphosphate
Modified residue 21 – 21 Phosphoserine
Modified residue 40 – 40 Phosphotyrosine
Mutagenesis 41 – 41 E -> K. No effect on phosphorylation of GTF2I.
Beta strand 25 – 32

Literature citations

Mutation analysis of the Bruton's tyrosine kinase gene in X-linked agammaglobulinemia: identification of a mutation which affects the same codon as is altered in immunodeficient xid mice.
de Weers M.; Mensink R.G.J.; Kraakman M.E.M.; Schuurman R.K.B.; Hendriks R.W.;
Hum. Mol. Genet. 3:161-166(1994)
Cited for: VARIANTS XLA HIS-28 AND TRP-288;

Unique mutations of Bruton's tyrosine kinase in fourteen unrelated X-linked agammaglobulinemia families.
Zhu Q.; Zhang M.; Winkelstein J.; Chen S.-H.; Ochs H.D.;
Hum. Mol. Genet. 3:1899-1900(1994)
Cited for: VARIANTS XLA HIS-28; PRO-33; PRO-408; GLY-589; ASP-613 AND 260-GLN--GLU-280 DEL;

Mutation screening of the BTK gene in 56 families with X-linked agammaglobulinemia (XLA): 47 unique mutations without correlation to clinical course.
Holinski-Feder E.; Weiss M.; Brandau O.; Jedele K.B.; Nore B.; Baeckesjoe C.-M.; Vihinen M.; Hubbard S.R.; Belohradsky B.H.; Smith C.I.E.; Meindl A.;
Pediatrics 101:276-284(1998)
Cited for: VARIANTS XLA GLU-19; HIS-28; ASN-61; PRO-117; HIS-127; ARG-155; PRO-295; PHE-369; GLY-372; ARG-414; TYR-506; GLY-521; GLN-525; SER-559; TRP-562; GLU-594; THR-619; GLY-626 AND HIS-641;

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.