Variant position: 279 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 A----LGSMLISWYMSGYHTGYYM GFRQNQKE-GRCSHSLN
Mouse A----LGSMLISWYMSGYHTGYYM GFRQNKKE-GKC
Rat A----LGSMLISWYMSGYHTGYYM GFRQNKKEGKKC
Bovine A----LGSMLISWYMSGYHTGYYM GFKQSQKE-GRY
Cat A----LGSMLISWYMSGYHTGYYM GFKQNQKE-GRC
Drosophila GAEQDFVAMLTAWYMSGYYTGLYQ GKKEASTTSGKK
Fission yeast -----YKKLIMSWYYAGYYTGLAE GLAKSEQR----
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
252 – 280 Involved in homooligomerization
279 – 294 Required for interaction with SYNCRIP
279 – 282 GFRQ -> EMLA. In isoform SMN-delta7 and isoform SMN-delta57.
260 – 260 L -> S. Impairs homooligomerization.
263 – 263 M -> RTA. Impairs homooligomerization and GEMIN8 binding.
264 – 264 L -> A. Impairs homooligomerization.
266 – 266 S -> P. Impairs homooligomerization and GEMIN8 binding.
267 – 267 W -> A. Impairs homooligomerization.
268 – 268 Y -> A. Impairs homooligomerization.
271 – 271 G -> A. Impairs homooligomerization.
272 – 272 Y -> A. Impairs homooligomerization.
273 – 273 H -> R. Impairs GEMIN8 binding.
274 – 274 T -> A. Impairs homooligomerization.
275 – 275 G -> A. Impairs homooligomerization.
279 – 279 G -> E. Impairs homooligomerization.
263 – 280
Rpp20 interacts with SMN and is re-distributed into SMN granules in response to stress.
Hua Y.; Zhou J.;
Biochem. Biophys. Res. Commun. 314:268-276(2004)
Cited for: SUBUNIT; INTERACTION WITH RPP20/POP7; SUBCELLULAR LOCATION; MUTAGENESIS OF GLU-134; CHARACTERIZATION OF VARIANTS SMA1 CYS-272 AND VAL-279; CHARACTERIZATION OF VARIANT SMA2 AND SMA3 ILE-274; CHARACTERIZATION OF VARIANT SMA3 ILE-262;
The survival motor neuron protein forms soluble glycine zipper oligomers.
Martin R.; Gupta K.; Ninan N.S.; Perry K.; Van Duyne G.D.;
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 263-294; SUBUNIT; INTERACTION WITH GEMIN2; CHARACTERIZATION OF VARIANTS SMA1 CYS-272; SMA2/SMA3 ILE-274; SMA3 SER-275 AND SMA1 VAL-279; MUTAGENESIS OF LEU-260; MET-263; LEU-264; SER-266; TRP-267; TYR-268; GLY-271; TYR-272; THR-274; GLY-275 AND GLY-279;
Missense mutation clustering in the survival motor neuron gene: a role for a conserved tyrosine and glycine rich region of the protein in RNA metabolism?
Talbot K.; Ponting C.P.; Theodosiou A.M.; Rodriques N.R.; Surtees R.; Mountford R.; Davies K.E.;
Hum. Mol. Genet. 6:497-500(1997)
Cited for: VARIANT SMA1 VAL-279;
The survival of motor neuron (SMN) protein interacts with the mRNA-binding protein HuD and regulates localization of poly(A) mRNA in primary motor neuron axons.
Fallini C.; Zhang H.; Su Y.; Silani V.; Singer R.H.; Rossoll W.; Bassell G.J.;
J. Neurosci. 31:3914-3925(2011)
Cited for: INTERACTION WITH ELAVL4; VARIANT SMA1 VAL-279; MUTAGENESIS OF GLU-134;
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