UniProtKB/SwissProt variant VAR

Survival motor neuron protein
Gene: SMN2
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Variant information Variant position:

116 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 Isoleucine (I) to Phenylalanine (F) at position 116 (I116F, p.Ile116Phe). 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 (I) to large size and aromatic (F) 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
Variant description:

In SMA1; abolishes the interaction with ELAVL4. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs104893933 [ dbSNP | Ensembl ]

Sequence information Variant position:

116 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

294 The length of the canonical sequence.
Location on the sequence:

DKCSAIWSEDGCIYPATIAS I DFKRETCVVVYTGYGNREEQ 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                         DKCSAIWSEDGCIYPATIASIDFKRETCVVVYTGYGNREEQ

                              DKCSAVWSEDGCIYPATIASIDFKRETCVVVYTGYGNREEQ

Mouse                         DKCSAVWSEDGCIYPATITSIDFKRETCVVVYTGYGNREEQ

Rat                           DKCSAVWSEDGCVYPATITSVDLKRETCVVVYTGYGNKEEQ

Bovine                        DNCCAIWSEDGCIYPATIASIDFKRETCVVVYTGYGNREEQ

Cat                           DKCSAIWSEDGCVYPATIASIDFKRETCVVVYTGYGNREEQ

Drosophila                    DYARATYV-DGVDYEGAVVSINEEKGTCVLRYLGYENEQEV

Fission yeast                 -------------------------------------RTEE

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 – 294	Survival motor neuron protein
Domain	91 – 151	Tudor
Region	97 – 209	Required for interaction with RPP20/POP7
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.
Mutagenesis	132 – 132	N -> DS. Impairs binding to substrate containing dimethylated arginine.
Mutagenesis	134 – 134	E -> K. Impairs SMN binding to RPP20/POP7. Abolishes the interaction with ELAVL4. Abolishes interaction with SNRPD1 and SNRPD3. Impairs binding to substrate containing dimethylated arginine.
Mutagenesis	136 – 136	Q -> E. Impairs binding to substrate containing dimethylated arginine.
Beta strand	107 – 117

Literature citations
Detection of novel mutations in the SMN Tudor domain in type I SMA patients.
Cusco I.; Barcelo M.J.; del Rio E.; Baiget M.; Tizzano E.F.;
Neurology 63:146-149(2004)
Cited for: VARIANTS SMA1 PHE-116 AND GLU-136; HuD interacts with survival motor neuron protein and can rescue spinal muscular atrophy-like neuronal defects.
Hubers L.; Valderrama-Carvajal H.; Laframboise J.; Timbers J.; Sanchez G.; Cote J.;
Hum. Mol. Genet. 20:553-579(2011)
Cited for: INTERACTION WITH ELAVL4; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS SMA2 GLU-111; SMA1 PHE-116 AND SMA1 GLU-136; MUTAGENESIS OF GLU-134;

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.

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q16637: Variant p.Ile116Phe