UniProtKB/Swiss-Prot Q92979: Variant p.Asp86Gly

• Variant information
• Sequence information
• Literature citations
• All

Variant information

Variant position: 86 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: LP/P [Disclaimer: Variants classification is intended for research purposes only, not for clinical and diagnostic use. The label disease variant is assigned according to literature reports on probable disease-association that can be based on theoretical reasons. This label must not be considered as a definitive proof for the pathogenic role of a variant.] 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 Glycine (G) at position 86 (D86G, p.Asp86Gly). 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 glycine (G) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: -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: In BWCNS; studies in fibroblasts show a dramatically reduced level of EMG1 protein in a BWCNS-affected patient compared to normal fibroblasts although patient fibroblasts do not have complete EMG1 deficiency; increased dimerization of EMG1 subunits, suggesting that aggregation of EMG1 leads to reduced levels of the protein; reduced localization to the nucleolus with a large fraction of the protein detected in the nucleoplasm where it accumulates in nuclear foci; reduced methylation efficiency; impaired maturation of the small ribosomal subunit. Any additional useful information about the variant.
Other resources: Links to websites of interest for the variant.

• Variant rs74435397 [ dbSNP | Ensembl ]

Sequence information

Variant position: 86 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 244 The length of the canonical sequence.
Location on the sequence: CDKHKSILLKNGRDPGEARP D ITHQSLLMLMDSPLNRAGLL 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: 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.

Type	Positions	Description
Chain	2 – 244	Ribosomal RNA small subunit methyltransferase NEP1
Site	84 – 84	Interaction with substrate rRNA
Site	86 – 86	Stabilizes Arg-84
Helix	85 – 96

Literature citations

Effects of the Bowen-Conradi syndrome mutation in EMG1 on its nuclear import, stability and nucleolar recruitment.
Warda A.S.; Freytag B.; Haag S.; Sloan K.E.; Goerlich D.; Bohnsack M.T.;
Hum. Mol. Genet. 25:5353-5364(2016)
Cited for: FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANT BWCNS GLY-86;
Mutation of a gene essential for ribosome biogenesis, EMG1, causes Bowen-Conradi syndrome.
Armistead J.; Khatkar S.; Meyer B.; Mark B.L.; Patel N.; Coghlan G.; Lamont R.E.; Liu S.; Wiechert J.; Cattini P.A.; Koetter P.; Wrogemann K.; Greenberg C.R.; Entian K.-D.; Zelinski T.; Triggs-Raine B.;
Am. J. Hum. Genet. 84:728-739(2009)
Cited for: VARIANT BWCNS GLY-86; CHARACTERIZATION OF VARIANT BWCNS GLY-86;