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UniProtKB/Swiss-Prot Q11203: Variant p.Asp370Tyr

CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase
Gene: ST3GAL3
Variant information

Variant position:  370
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Aspartate (D) to Tyrosine (Y) at position 370 (D370Y, p.Asp370Tyr).
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 acidic (D) to large size and aromatic (Y)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -3
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 MRT12; the mutant protein is improperly localized to the endoplasmic reticulum preventing the protein from interacting with its substrates in the Golgi and resulting in a loss-of-function; shows a complete lack of enzyme activity; secretion of the mutant protein is dramatically reduced compared to wild-type.
Any additional useful information about the variant.

Sequence information

Variant position:  370
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  375
The length of the canonical sequence.

Location on the sequence:   HNIQREKEFLRKLVKARVIT  D LSSGI
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                         HNIQREKEFLRKLVKARVITDLSSGI

Chimpanzee                    HNIQREKEFLRKLVKARVITDLSSGI

Mouse                         HNIQREKEFLRKLVKARVITDLSSGI

Rat                           HNIQREKEFLRKLVKARVITDLSSGI

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.

Chain 1 – 375 CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase
Topological domain 29 – 375 Lumenal
Alternative sequence 44 – 375 Missing. In isoform E1.
Alternative sequence 74 – 375 Missing. In isoform E3+32.
Alternative sequence 116 – 375 Missing. In isoform B4+173.
Alternative sequence 118 – 375 Missing. In isoform C12.
Alternative sequence 122 – 375 Missing. In isoform B5+173.
Alternative sequence 152 – 375 Missing. In isoform B10.
Alternative sequence 156 – 375 Missing. In isoform A7, isoform B7 and isoform C7.
Alternative sequence 187 – 375 Missing. In isoform B5+26 and isoform D2+26.
Alternative sequence 190 – 375 Missing. In isoform B1+32.
Alternative sequence 203 – 375 Missing. In isoform C5 and isoform D5.
Alternative sequence 245 – 375 Missing. In isoform C9.

Literature citations

ST3GAL3 mutations impair the development of higher cognitive functions.
Hu H.; Eggers K.; Chen W.; Garshasbi M.; Motazacker M.M.; Wrogemann K.; Kahrizi K.; Tzschach A.; Hosseini M.; Bahman I.; Hucho T.; Muhlenhoff M.; Gerardy-Schahn R.; Najmabadi H.; Ropers H.H.; Kuss A.W.;
Am. J. Hum. Genet. 89:407-414(2011)

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.