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UniProtKB/Swiss-Prot O95425: Variant p.Pro1235Ala

Supervillin
Gene: SVIL
Variant information

Variant position:  1235
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LB/B
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 Proline (P) to Alanine (A) at position 1235 (P1235A, p.Pro1235Ala).
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 hydrophobic (P) to small size and hydrophobic (A)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -1
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

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  1235
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  2214
The length of the canonical sequence.

Location on the sequence:   AGRMVKKGLASPTAITPVAS  P ICGKTRGTTPVSKPLEDIEA
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                         AGRMVKKGLASPTAITPVASPICGKTRGTTPVSKPLEDIEA

Mouse                         AGRMVKKGLASPTSITPISSPLCSKSRGTTPVSKPLEDIEA

Bovine                        AGRMVKRGLASPTAITPVASPVSSKARGTTPVSRPLEDIEA

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 1 – 2214 Supervillin
Modified residue 1225 – 1225 Phosphoserine
Modified residue 1230 – 1230 Phosphothreonine
Modified residue 1234 – 1234 Phosphoserine


Literature citations

Cloning, characterization, and chromosomal localization of human supervillin (SVIL).
Pope R.K.; Pestonjamasp K.N.; Smith K.P.; Wulfkuhle J.D.; Strassel C.P.; Lawrence J.B.; Luna E.J.;
Genomics 52:342-351(1998)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2); VARIANTS ALA-189 AND ALA-1235; INTERACTION WITH ACTIN; SUBCELLULAR LOCATION; TISSUE SPECIFICITY;

Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton.
Oh S.W.; Pope R.K.; Smith K.P.; Crowley J.L.; Nebl T.; Lawrence J.B.; Luna E.J.;
J. Cell Sci. 116:2261-2275(2003)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); FUNCTION (ISOFORM 1); VARIANTS ALA-189; ILE-422 AND ALA-1235;

A quantitative atlas of mitotic phosphorylation.
Dephoure N.; Zhou C.; Villen J.; Beausoleil S.A.; Bakalarski C.E.; Elledge S.J.; Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-221; SER-245; SER-920; THR-1111; SER-1120; SER-1225 AND SER-1322; PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 AND SER-270 (ISOFORMS 2 AND SV3); VARIANT [LARGE SCALE ANALYSIS] ALA-1235; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
Olsen J.V.; Vermeulen M.; Santamaria A.; Kumar C.; Miller M.L.; Jensen L.J.; Gnad F.; Cox J.; Jensen T.S.; Nigg E.A.; Brunak S.; Mann M.;
Sci. Signal. 3:RA3-RA3(2010)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-221; SER-245; SER-270; SER-707; SER-914; SER-920; SER-924; SER-968; SER-1120; SER-1225; THR-1230 AND SER-1322; PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 AND SER-270 (ISOFORMS 2 AND SV3); VARIANT [LARGE SCALE ANALYSIS] ALA-1235; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
Rigbolt K.T.; Prokhorova T.A.; Akimov V.; Henningsen J.; Johansen P.T.; Kratchmarova I.; Kassem M.; Mann M.; Olsen J.V.; Blagoev B.;
Sci. Signal. 4:RS3-RS3(2011)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-707; SER-914 AND SER-968; PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261 AND SER-270 (ISOFORMS 2 AND SV3); VARIANT [LARGE SCALE ANALYSIS] ALA-1235; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];

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