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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9UIF7: Variant p.Tyr125His

Adenine DNA glycosylase
Gene: MUTYH
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Variant information Variant position: help 125 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Tyrosine (Y) to Histidine (H) at position 125 (Y125H, p.Tyr125His). 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 aromatic (Y) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 2 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 FAP2; decreased function in DNA repair. Any additional useful information about the variant.


Sequence information Variant position: help 125 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 546 The length of the canonical sequence.
Location on the sequence: help KRDLPWRRRAEDEMDLDRRA Y AVWVSEVMLQQTQVATVINY 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         KRDLPWRRRAEDEMDLDRRAYAVWVSEVMLQQTQVATVINY

Mouse                         KRDLPWRNLAKEEANSDRRAYAVWVSEVMLQQTQVATVIDY

Rat                           KRDLPWRKRVKEETNLDRRAYAVWVSEVMLQQTQVATVIDY
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
Chain 1 – 546 Adenine DNA glycosylase
Active site 131 – 131 Proton donor/acceptor
Mutagenesis 121 – 121 D -> G. Does not affect DNA glycosylase activity. Does not affect function in DNA repair.
Helix 120 – 135



Literature citations
Germline MUTYH (MYH) mutations in Portuguese individuals with multiple colorectal adenomas.
Isidro G.; Laranjeira F.; Pires A.; Leite J.; Regateiro F.; Castro e Sousa F.; Soares J.; Castro C.; Giria J.; Brito M.J.; Medeira A.; Teixeira R.; Morna H.; Gaspar I.; Marinho C.; Jorge R.; Brehm A.; Ramos J.S.; Boavida M.G.;
Hum. Mutat. 24:353-354(2004)
Cited for: VARIANTS FAP2 HIS-125; HIS-179 AND TRP-238; Functional complementation assay for 47 MUTYH variants in a MutY-disrupted Escherichia coli strain.
Komine K.; Shimodaira H.; Takao M.; Soeda H.; Zhang X.; Takahashi M.; Ishioka C.;
Hum. Mutat. 36:704-711(2015)
Cited for: CHARACTERIZATION OF VARIANTS FAP2 LEU-18; HIS-125; ARG-128; LEU-154; CYS-176; CYS-179; HIS-179; GLN-182; GLU-186; VAL-220; TRP-238; HIS-242; TRP-271; GLU-283; LEU-292; CYS-306; THR-377; PRO-385; ASP-393; LEU-402; MET-417; CYS-423; ASP-470; THR-470; GLU-477 DEL; THR-486 AND PHE-490; CHARACTERIZATION OF VARIANTS GASC SER-402 AND ARG-411; CHARACTERIZATION OF VARIANTS MET-22; ASP-25; ARG-100; ASN-102; VAL-224; MET-231; CYS-242; PHE-243; TRP-287; HIS-335; ARG-335; GLN-434; PRO-434; GLU-500; PHE-512; LEU-513; MET-526 AND GLN-531; FUNCTION; SUBCELLULAR LOCATION;
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.