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UniProtKB/Swiss-Prot O95863: Variant p.Val118Ala

Zinc finger protein SNAI1
Gene: SNAI1
Variant information

Variant position:  118
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LB/B
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 Valine (V) to Alanine (A) at position 118 (V118A, p.Val118Ala).
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 medium size and hydrophobic (V) to small size and hydrophobic (A)
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:  118
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  264
The length of the canonical sequence.

Location on the sequence:   KGSQPPSPPSPAPSSFSSTS  V SSLEAEAYAAFPGLGQVPKQ
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                         KGSQPPSPPSPAPSSFSSTSVSSLEAEAYAAFPGLGQVPKQ

Mouse                         KSSQPPSPPSPAPSSFSSTSASSLEAEAFIAFPGLGQLPKQ

Xenopus laevis                KTSDPPSPASSATEA--EKFQCNLCSKSYSTFAGLSKHKQL

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 1 – 264 Zinc finger protein SNAI1
Modified residue 100 – 100 Phosphoserine
Modified residue 104 – 104 Phosphoserine
Modified residue 107 – 107 Phosphoserine
Modified residue 111 – 111 Phosphoserine
Modified residue 115 – 115 Phosphoserine
Modified residue 119 – 119 Phosphoserine
Glycosylation 112 – 112 O-linked (GlcNAc) serine
Cross 98 – 98 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross 137 – 137 Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Mutagenesis 98 – 98 K -> R. No change. Complete loss of sensitivity to FBXL14- and BTRC-triggered degradation and loss of ability to repress E-cadherin/CDH1; when associated with R-137 and R-146.
Mutagenesis 100 – 100 S -> A. Lower sensitivity to BTRC-triggered degradation and impaired phosphorylation by GSK3B; when associated with A-96. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-107; A-111; A-115 and A-119. Does not affect NOTCH1-induced degradation; when associated with A-96. Abolishes phosphorylation at S-96.
Mutagenesis 104 – 104 S -> A. Increases protein stability, does not affect repressor activity on E-cadherin/CDH1 promoter, preferentially localizes to the nucleus, induces a more aggressive tissue invasion program and impairs phosphorylation by GSK3B, binding to BTRC and ubiquitination; when associated with A-107. Impairs phosphorylation in the serine-rich domain/region; when associated with A-92 and A-107. Abolishes phosphorylation at S-96.
Mutagenesis 107 – 107 S -> A. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-111; A-115 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-111; A-115 and A-119. Increases protein stability, does not affect repressor activity on E-cadherin promoter, preferentially localizes to the nucleus, induces a more aggressive tissue invasion program and impairs phosphorylation by GSK3B, binding to BTRC and ubiquitination; when associated with A-104. Impairs phosphorylation in the serine-rich region; when associated with A-92 and A-104. Abolishes phosphorylation at S-96.
Mutagenesis 107 – 107 S -> E. Predominantly localized to the cytoplasm; when associated with E-111; E-115 and E-119.
Mutagenesis 111 – 111 S -> A. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-107; A-115 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-107; A-115 and A-119.
Mutagenesis 111 – 111 S -> E. Predominantly localized to the cytoplasm; when associated with E-107; E-115 and E-119.
Mutagenesis 115 – 115 S -> A. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-107; A-111 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-107; A-111 and A-119.
Mutagenesis 115 – 115 S -> E. Predominantly localized to the cytoplasm; when associated with E-107; E-111 and E-119.
Mutagenesis 119 – 119 S -> A. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-107; A-111 and A-119. Lower sensitivity to BTRC-triggered degradation, impaired phosphorylation by GSK3B and loss of cytoplasmic localization; when associated with A-96; A-100; A-107; A-111 and A-115.
Mutagenesis 119 – 119 S -> E. Predominantly localized to the cytoplasm; when associated with E-107; E-111 and E-115.
Mutagenesis 137 – 137 K -> R. Lower sensitivity to FBXL14-triggered degradation. Lower sensitivity to FBXL14-triggered degradation; when associated with R-146. Complete loss of sensitivity to FBXL14- and BTRC-triggered degradation and loss of ability to repress E-cadherin; when associated with R-98 and R-146.


Literature citations

Down-regulation of promoter 1.3 activity of the human aromatase gene in breast tissue by zinc-finger protein, snail (SnaH).
Okubo T.; Truong T.K.; Yu B.; Itoh T.; Zhao J.; Grube B.; Zhou D.; Chen S.;
Cancer Res. 61:1338-1346(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANT ALA-118;

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.