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UniProtKB/Swiss-Prot Q16637: Variant p.Gln136Glu

Survival motor neuron protein
Gene: SMN2
Variant information

Variant position:  136
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 Glutamine (Q) to Glutamate (E) at position 136 (Q136E, p.Gln136Glu).
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 polar (Q) to medium size and acidic (E)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  2
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.



Sequence information

Variant position:  136
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:   IDFKRETCVVVYTGYGNREE  Q NLSDLLSPICEVANNIEQNA
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                         IDFKRETCVVVYTGYGNREEQNLSDLLSPICEVANNIEQNA

                              IDFKRETCVVVYTGYGNREEQNVSDLLSPACEVANNVEQDT

Mouse                         IDFKRETCVVVYTGYGNREEQNLSDLLSPTCEVANSTEQNT

Rat                           VDLKRETCVVVYTGYGNKEEQNLSDLLSPTCEVANNTEQNT

Bovine                        IDFKRETCVVVYTGYGNREEQNLSDLLSPTSEVAN-IEQNA

Cat                           IDFKRETCVVVYTGYGNREEQNVSDLLSPASAVDNNVEQNA

Drosophila                    INEEKGTCVLRYLGYENEQEVLLVDLLPSWGKRVRREQFLI

Fission yeast                 LDGEKLISAA-------RTEESISKL-EEGEQMINQQTETT

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 2 – 294 Survival motor neuron protein
Domain 91 – 151 Tudor
Region 97 – 209 Required for interaction with RPP20/POP7
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 – 136 EEQ -> SEV. 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 133 – 137


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.