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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P12838: Variant p.Arg74Gln

Defensin alpha 4
Gene: DEFA4
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Variant information Variant position: help 74 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help 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: help 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: help 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: help In a colorectal cancer sample; somatic mutation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 74 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 97 The length of the canonical sequence.
Location on the sequence: help 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: help 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.
TypePositionsDescription
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.