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UniProtKB/Swiss-Prot P27695: Variant p.Gln51His

DNA-(apurinic or apyrimidinic site) lyase
Gene: APEX1
Variant information

Variant position:  51
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Polymorphism
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Glutamine (Q) to Histidine (H) at position 51 (Q51H, p.Gln51His).
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:  Similar physico-chemical property. Both residues are medium size and polar.
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.



Sequence information

Variant position:  51
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  318
The length of the canonical sequence.

Location on the sequence:   KKNDKEAAGEGPALYEDPPD  Q KTSPSGKPATLKICSWNVDG
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                         KKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDG

Gorilla                       KKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDG

Chimpanzee                    KKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDG

Mouse                         KKTEKEAAGEGPVLYEDPPDQKTSPSGKSATLKICSWNVDG

Rat                           KKTEKEAAGEGPVLYEDPPDQKTSASGKSATLKICSWNVDG

Bovine                        KKNEKEAVGEGAVLYEDPPDQKTSPSGKSATLKICSWNVDG

Zebrafish                     KKEKKGKEPEAPILYEDPPEKLTSKDGRAANMKITSWNVDG

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.

TypePositionsDescription
Chain 2 – 318 DNA-(apurinic or apyrimidinic site) lyase
Chain 32 – 318 DNA-(apurinic or apyrimidinic site) lyase, mitochondrial
Metal binding 70 – 70 Magnesium 1
Modified residue 31 – 31 N6-acetyllysine
Modified residue 32 – 32 N6-acetyllysine
Modified residue 35 – 35 N6-acetyllysine
Modified residue 54 – 54 Phosphoserine
Modified residue 65 – 65 S-nitrosocysteine; alternate
Mutagenesis 31 – 31 K -> A. Enhances the interaction with TOMM20. Does not inhibit redox and AP endodeoyribonuclease activities. Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoxyribonuclease activity; when associated with A-24; A-25; A-27 and A-32. Reduces protection from granzyme A-mediated cell death; when associated with A-65 and A-210.
Mutagenesis 32 – 32 K -> A. Inhibits rRNA binding, interaction with NPM1, nuclear localization and modulates its endodeoxyribonuclease activity; when associated with A-24; A-25; A-27 and A-31.
Mutagenesis 65 – 65 C -> A. Abolishes the redox activity. Does not abolish the AP endodeoxyribonuclease and phosphodiesterase activities. Reduces protection from granzyme A-mediated cell death; when associated with A-31 and A-210.
Mutagenesis 65 – 65 C -> S. Does not abolish NO-induced nitrosylation. Enhances NO-induced nuclear export.
Mutagenesis 68 – 68 N -> A. Nearly abolishes AP endodeoxyribonuclease activity.
Mutagenesis 70 – 70 D -> A. Strongly reduces AP endodeoxyribonuclease activity.


Literature citations

Submission
NIEHS SNPs program;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS HIS-51; VAL-64 AND GLU-148;

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.