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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q16637: Variant p.Tyr272Cys

Survival motor neuron protein
Gene: SMN2
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Variant information Variant position: help 272 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 Tyrosine (Y) to Cysteine (C) at position 272 (Y272C, p.Tyr272Cys). 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 large size and aromatic (Y) to medium size and polar (C) 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 SMA1; abolishes SMN1 binding to RPP20/POP7 and severely impairs binding to SNRPB, GEMIN8 and homooligomerization. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 272 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 DSLDDADALGSMLISWYMSG Y HTGYYMGFRQNQKEGRCSHS 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                         DSLDDADA----LGSMLISWYMSGYHTGYYMGFRQNQKEG-RCSHS

                              DSLDDADA----LGSMLISWYMSGYHTGYYMGFKQNQKEG-

Mouse                         DCLDDTDA----LGSMLISWYMSGYHTGYYMGFRQNKKEG-

Rat                           DCLDDTDA----LGSMLISWYMSGYHTGYYMGFRQNKKEGK

Bovine                        DSLDDADA----LGSMLISWYMSGYHTGYYMGFKQSQKEG-

Cat                           DSLDDADA----LGSMLISWYMSGYHTGYYMGFKQNQKEG-

Drosophila                    MIVGQGDGAEQDFVAMLTAWYMSGYYTGLYQGKKEASTTSG

Fission yeast                 LTYDET------YKKLIMSWYYAGYYTGLAEGLAKSEQR--
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 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.
Helix 263 – 280



Literature citations
Identification and characterization of a spinal muscular atrophy-determining gene.
Lefebvre S.; Buerglen L.; Reboullet S.; Clermont O.; Burlet P.; Viollet L.; Benichou B.; Cruaud C.; Millasseau P.; Zeviani M.; le Paslier D.; Frezal J.; Cohen D.; Weissenbach J.; Munnich A.; Melki J.;
Cell 80:155-165(1995)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]; ALTERNATIVE SPLICING; VARIANT SMA1 CYS-272; 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.;
Structure 20:1929-1939(2012)
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; Molecular diagnosis of non-deletion SMA patients using quantitative PCR of SMN exon 7.
Rochette C.F.; Surh L.C.; Ray P.N.; McAndrew P.E.; Prior T.W.; Burghes A.H.M.; Vanasse M.; Simard L.R.;
Neurogenetics 1:141-147(1997)
Cited for: VARIANT SMA3 LEU-245; VARIANT SMA1 CYS-272; SMN mutants of spinal muscular atrophy patients are defective in binding to snRNP proteins.
Pellizzoni L.; Charroux B.; Dreyfuss G.;
Proc. Natl. Acad. Sci. U.S.A. 96:11167-11172(1999)
Cited for: SUBUNIT; INTERACTION WITH SNRPB; GEMIN2; SNRPD1; SNRPD2; SNRPD3 AND SNRPE; CHARACTERIZATION OF VARIANT SMA1 CYS-272; Molecular and functional analysis of intragenic SMN1 mutations in patients with spinal muscular atrophy.
Sun Y.; Grimmler M.; Schwarzer V.; Schoenen F.; Fischer U.; Wirth B.;
Hum. Mutat. 25:64-71(2005)
Cited for: VARIANTS SMA1/SMA2/SMA3 ASN-30; VAL-44; ARG-95; GLY-111; GLY-262; CYS-272 AND ILE-274; CHARACTERIZATION OF VARIANTS SMA1/SMA2/SMA3 ASN-30; VAL-44; ARG-95 AND GLY-111; Identification and structural analysis of the Schizosaccharomyces pombe SMN complex.
Veepaschit J.; Viswanathan A.; Bordonne R.; Grimm C.; Fischer U.;
Nucleic Acids Res. 49:gkab158-gkab158(2021)
Cited for: INTERACTION WITH GEMIN8; CHARACTERIZATION OF VARIANTS SMA1 CYS-272 AND SMA3 ILE-274; MUTAGENESIS OF MET-263; SER-266 AND HIS-273;
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.