UniProtKB/Swiss-Prot P12838 : Variant p.Arg74Gln
Defensin alpha 4
Gene: DEFA4
Feedback ?
Variant information
Variant position:
74
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:
US
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 Glutamine (Q) at position 74 (R74Q, p.Arg74Gln).
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 (Q)
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
Variant description:
In a colorectal cancer sample; somatic mutation.
Any additional useful information about the variant.
Other resources:
Links to websites of interest for the variant.
Sequence information
Variant position:
74
The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:
97
The length of the canonical sequence.
Location on the sequence:
LQVSGSTRGMVCSCRLVFCR
R TELRVGNCLIGGVSFTYCCT
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
Peptide
64 – 96
Defensin alpha 4
Disulfide bond
65 – 93
Disulfide bond
67 – 82
Disulfide bond
72 – 92
Mutagenesis
65 – 65
C -> A. Impairs bactericidal activity against E.coli and S.aureus; when associated with Ala-67, Ala-72, Ala-82, Ala-92 and Ala-93.
Mutagenesis
67 – 67
C -> A. Impairs bactericidal activity against E.coli and S.aureus; when associated with Ala-65, Ala-72, Ala-82, Ala-92 and Ala-93.
Mutagenesis
69 – 69
L -> A. Slight decrease in antibacterial activity against E.coli.
Mutagenesis
71 – 71
F -> A. Decreased antibacterial activity against S.aureus.
Mutagenesis
72 – 72
C -> A. Impairs bactericidal activity against E.coli and S.aureus; when associated with Ala-65, Ala-67, Ala-82, Ala-92 and Ala-93.
Mutagenesis
73 – 73
R -> A. Decreased antibacterial activity against E.coli. Weakens interaction with B.anthracis lef and with HIV-1 gp120.
Mutagenesis
74 – 74
R -> A. Decreased antibacterial activity against E.coli. Weakens interaction with B.anthracis lef and with HIV-1 gp120.
Mutagenesis
78 – 78
R -> A. Decreased antibacterial activity against E.coli and S.aureus. Weakens interaction with B.anthracis lef and with HIV-1 gp120.
Mutagenesis
82 – 82
C -> A. Impairs bactericidal activity against E.coli and S.aureus; when associated with Ala-65, Ala-67, Ala-72, Ala-92 and Ala-93.
Mutagenesis
89 – 89
F -> A. Impaired homodimerization. Decreased antibacterial activity against S.aureus. Disrupts interaction with B.anthracis lef and with HIV-1 gp120.
Mutagenesis
91 – 91
Y -> A. Slight decrease in antibacterial activity against E.coli and S.aureus.
Mutagenesis
92 – 92
C -> A. Impairs bactericidal activity against E.coli and S.aureus; when associated with Ala-65, Ala-67, Ala-72, Ala-82 and Ala-93.
Mutagenesis
93 – 93
C -> A. Impairs bactericidal activity against E.coli and S.aureus; when associated with Ala-65, Ala-67, Ala-72, Ala-82 and Ala-92.
Literature citations
The consensus coding sequences of human breast and colorectal cancers.
Sjoeblom T.; Jones S.; Wood L.D.; Parsons D.W.; Lin J.; Barber T.D.; Mandelker D.; Leary R.J.; Ptak J.; Silliman N.; Szabo S.; Buckhaults P.; Farrell C.; Meeh P.; Markowitz S.D.; Willis J.; Dawson D.; Willson J.K.V.; Gazdar A.F.; Hartigan J.; Wu L.; Liu C.; Parmigiani G.; Park B.H.; Bachman K.E.; Papadopoulos N.; Vogelstein B.; Kinzler K.W.; Velculescu V.E.;
Science 314:268-274(2006)
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-74;
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.