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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q16637: Variant p.Ala111Gly

Survival motor neuron protein
Gene: SMN2
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Variant information Variant position: help 111 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 Alanine (A) to Glycine (G) at position 111 (A111G, p.Ala111Gly). 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 small size and hydrophobic (A) to glycine (G) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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
Variant description: help In SMA2; reduces SMN binding to Sm proteins; abolishes the interaction with ELAVL4. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 111 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 294 The length of the canonical sequence.
Location on the sequence: help QWKVGDKCSAIWSEDGCIYP A TIASIDFKRETCVVVYTGYG 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                         QWKVGDKCSAIWSEDGCIYPATIASIDFKRETCVVVYTGYG

                              QWKVGDKCSAVWSEDGCIYPATIASIDFKRETCVVVYTGYG

Mouse                         QWKVGDKCSAVWSEDGCIYPATITSIDFKRETCVVVYTGYG

Rat                           QWKAGDKCSAVWSEDGCVYPATITSVDLKRETCVVVYTGYG

Bovine                        QWKVGDNCCAIWSEDGCIYPATIASIDFKRETCVVVYTGYG

Cat                           QWKVGDKCSAIWSEDGCVYPATIASIDFKRETCVVVYTGYG

Drosophila                    SFKVGDYARATYV-DGVDYEGAVVSINEEKGTCVLRYLGYE

Fission yeast                 -----------------------------------------
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 2 – 294 Survival motor neuron protein
Domain 91 – 151 Tudor
Region 97 – 209 Required for interaction with RPP20/POP7
Mutagenesis 92 – 92 W -> S. Impairs binding to substrate containing dimethylated arginine.
Mutagenesis 102 – 102 W -> LV. Impairs binding to substrate containing dimethylated arginine.
Mutagenesis 109 – 109 Y -> H. Impairs binding to substrate containing dimethylated arginine.
Mutagenesis 127 – 127 Y -> LF. Impairs binding to substrate containing dimethylated arginine.
Mutagenesis 130 – 130 Y -> D. Impairs binding to substrate containing dimethylated arginine.
Beta strand 107 – 117



Literature citations
Molecular and functional analysis of intragenic SMN1 mutations in patients with spinal muscular atrophy.
Sun Y.; Grimmler M.; Schwarzer V.; Schoenen F.; Fischer U.; Wirth B.;
Hum. Mutat. 25:64-71(2005)
Cited for: VARIANTS SMA1/SMA2/SMA3 ASN-30; VAL-44; ARG-95; GLY-111; GLY-262; CYS-272 AND ILE-274; CHARACTERIZATION OF VARIANTS SMA1/SMA2/SMA3 ASN-30; VAL-44; ARG-95 AND GLY-111;
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.