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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q16637: Variant p.Ser262Ile

Survival motor neuron protein
Gene: SMN2
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Variant information Variant position: help 262 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 Serine (S) to Isoleucine (I) at position 262 (S262I, p.Ser262Ile). 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 polar (S) to medium size and hydrophobic (I) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In SMA3; slightly reduces SMN binding to RPP20/POP7. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 262 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 IIPPPPPICPDSLDDADALG S MLISWYMSGYHTGYYMGFRQ 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                         IIPPPPPICPDSLDDADA----LGSMLISWYMSGYHTGYYMGFRQ

                              IIPPPPPICPDSLDDADA----LGSMLISWYMSGYHTGYYM

Mouse                         IIPPPPPISPDCLDDTDA----LGSMLISWYMSGYHTGYYM

Rat                           IIPPPPPISPDCLDDTDA----LGSMLISWYMSGYHTGYYM

Bovine                        MIPPPPPICPDSLDDADA----LGSMLISWYMSGYHTGYYM

Cat                           IIPPPPPICPDSLDDADA----LGSMLISWYMSGYHTGYYM

Drosophila                    VMPPMPPVPPMIVGQGDGAEQDFVAMLTAWYMSGYYTGLYQ

Fission yeast                 FMEVPPPIRGLTYDET------YKKLIMSWYYAGYYTGLAE
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
Region 240 – 267 P2 (binding site for SNRPB)
Region 252 – 280 Involved in homooligomerization
Mutagenesis 260 – 260 L -> S. Impairs homooligomerization.
Mutagenesis 263 – 263 M -> RTA. Impairs homooligomerization and GEMIN8 binding.
Mutagenesis 264 – 264 L -> A. Impairs homooligomerization.
Mutagenesis 266 – 266 S -> P. Impairs homooligomerization and GEMIN8 binding.
Mutagenesis 267 – 267 W -> A. Impairs homooligomerization.
Mutagenesis 268 – 268 Y -> A. Impairs homooligomerization.
Mutagenesis 271 – 271 G -> A. Impairs homooligomerization.
Mutagenesis 272 – 272 Y -> A. Impairs homooligomerization.
Mutagenesis 273 – 273 H -> R. Impairs GEMIN8 binding.
Mutagenesis 274 – 274 T -> A. Impairs homooligomerization.
Mutagenesis 275 – 275 G -> A. Impairs homooligomerization.
Mutagenesis 279 – 279 G -> E. Impairs homooligomerization.



Literature citations
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; Missense mutations in exon 6 of the survival motor neuron gene in patients with spinal muscular atrophy (SMA).
Hahnen E.; Schoenling J.; Rudnik-Schoeneborn S.; Raschke H.; Zerres K.; Wirth B.;
Hum. Mol. Genet. 6:821-825(1997)
Cited for: VARIANT SMA3 ILE-262; VARIANT SMA2/SMA3 ILE-274;
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.