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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q5T481: Variant p.Ser635Ala

RNA-binding protein 20
Gene: RBM20
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Variant information Variant position: help 635 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 Alanine (A) at position 635 (S635A, p.Ser635Ala). 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 small size and hydrophobic (A) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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
Variant description: help In CMD1DD; causes the formation of anomalous isoforms in TTN (Titin); impaired localization to the nucleus, leading to mislocalization to the cytoplasm. Any additional useful information about the variant.


Sequence information Variant position: help 635 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1227 The length of the canonical sequence.
Location on the sequence: help SQRERDMFREADRYGPERPR S RSPVSRSLSPRSHTPSFTSC 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                         SQRERDMFREADRYGPERPRSRSPVSRSLSPRSHTPSFTSC

Mouse                         SQRERDMLREADRYGPERPRSRSPMSRSLSPRSHS------

Rat                           SQRERCMLREADRYGPERPRSRSPMSRSLSPRSHS------

Pig                           SQRERDMFREADRYGPERPRSRSPVSRSLSPRSHTPSFTSC
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 1 – 1227 RNA-binding protein 20
Region 624 – 906 Disordered
Region 628 – 655 RS
Modified residue 635 – 635 Phosphoserine
Modified residue 637 – 637 Phosphoserine
Modified residue 640 – 640 Phosphoserine
Modified residue 642 – 642 Phosphoserine



Literature citations
RBM20, a gene for hereditary cardiomyopathy, regulates titin splicing.
Guo W.; Schafer S.; Greaser M.L.; Radke M.H.; Liss M.; Govindarajan T.; Maatz H.; Schulz H.; Li S.; Parrish A.M.; Dauksaite V.; Vakeel P.; Klaassen S.; Gerull B.; Thierfelder L.; Regitz-Zagrosek V.; Hacker T.A.; Saupe K.W.; Dec G.W.; Ellinor P.T.; MacRae C.A.; Spallek B.; Fischer R.; Perrot A.; Ozcelik C.; Saar K.; Hubner N.; Gotthardt M.;
Nat. Med. 18:766-773(2012)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; FUNCTION; VARIANT CMD1DD ALA-635; CHARACTERIZATION OF VARIANT CMD1DD ALA-635; Proteome-wide quantitative RNA-interactome capture identifies phosphorylation sites with regulatory potential in RBM20.
Vieira-Vieira C.H.; Dauksaite V.; Sporbert A.; Gotthardt M.; Selbach M.;
Mol. Cell 0:0-0(2022)
Cited for: FUNCTION; SUBCELLULAR LOCATION; PHOSPHORYLATION AT SER-635 SER-660; SER-679; SER-742; SER-865; SER-876; SER-980; SER-1060; SER-1080; SER-1120 AND SER-1210; CHARACTERIZATION OF VARIANT CMD1DD ALA-635; MUTAGENESIS OF SER-660; SER-679; GLU-685; SER-742; SER-876; SER-980; SER-1060; SER-1080; SER-1120 AND SER-1210;
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.