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:
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 IDFKRETCVVVYTGYGNREE QNLSDLLSPICEVANNIEQNA
Mouse IDFKRETCVVVYTGYGNREE QNLSDLLSPTCEVANSTEQNT
Rat VDLKRETCVVVYTGYGNKEE QNLSDLLSPTCEVANNTEQNT
Bovine IDFKRETCVVVYTGYGNREE QNLSDLLSPTSEVAN-IEQNA
Cat IDFKRETCVVVYTGYGNREE QNVSDLLSPASAVDNNVEQNA
Drosophila INEEKGTCVLRYLGYENEQE VLLVDLLPSWGKRVRREQFLI
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
2 – 294 Survival motor neuron protein
91 – 151 Tudor
97 – 209 Required for interaction with RPP20/POP7
134 – 134 E -> K. Reduces SMN binding to RPP20/POP7. Abolishes the interaction with ELAVL4.
133 – 137
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.;
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;
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.