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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P37840: Variant p.Ala53Thr

Alpha-synuclein
Gene: SNCA
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Variant information Variant position: help 53 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 Alanine (A) to Threonine (T) at position 53 (A53T, p.Ala53Thr). 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 hydrophobic (A) to medium size and polar (T) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 PARK1; no effect on osmotic stress-induced phosphorylation; increases oligomerization. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 53 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 140 The length of the canonical sequence.
Location on the sequence: help TKEGVLYVGSKTKEGVVHGV A TVAEKTKEQVTNVGGAVVTG 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                         TKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTG

Gorilla                       TKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTG

Rhesus macaque                TKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTG

Chimpanzee                    TKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTG

Mouse                         TKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTG

Rat                           TKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTG

Pig                           TKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGEAVVTG

Bovine                        TKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGEAVVTG
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 – 140 Alpha-synuclein
Repeat 42 – 56 3; approximate
Region 20 – 67 4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4)
Binding site 50 – 50
Alternative sequence 41 – 54 Missing. In isoform 2-5.
Mutagenesis 35 – 35 E -> K. No effect on oligomerization.
Mutagenesis 39 – 39 Y -> F. No effect on osmotic stress-induced phosphorylation.
Mutagenesis 50 – 50 H -> A. Impairs copper-binding.
Mutagenesis 57 – 57 E -> K. Increases oligomerization.
Helix 52 – 55



Literature citations
Identification and characterization of a novel Pyk2/related adhesion focal tyrosine kinase-associated protein that inhibits alpha-synuclein phosphorylation.
Takahashi T.; Yamashita H.; Nagano Y.; Nakamura T.; Ohmori H.; Avraham H.; Avraham S.; Yasuda M.; Matsumoto M.;
J. Biol. Chem. 278:42225-42233(2003)
Cited for: MUTAGENESIS OF TYR-39; TYR-125; TYR-133 AND TYR-136; CHARACTERIZATION OF VARIANT THR-53; PHOSPHORYLATION AT TYR-125; Mutation in the alpha-synuclein gene identified in families with Parkinson's disease.
Polymeropoulos M.H.; Lavedan C.; Leroy E.; Ide S.E.; Dehejia A.; Dutra A.; Pike B.; Root H.; Rubenstein J.; Boyer R.; Stenroos E.S.; Chandrasekharappa S.; Athanassiadou A.; Papapetropoulos T.; Johnson W.G.; Lazzarini A.M.; Duvoisin R.C.; di Iorio G.; Golbe L.I.; Nussbaum R.L.;
Science 276:2045-2047(1997)
Cited for: VARIANT PARK1 THR-53; Molecular determinants of alpha-synuclein mutants' oligomerization and membrane interactions.
Tsigelny I.F.; Sharikov Y.; Kouznetsova V.L.; Greenberg J.P.; Wrasidlo W.; Overk C.; Gonzalez T.; Trejo M.; Spencer B.; Kosberg K.; Masliah E.;
ACS Chem. Neurosci. 6:403-416(2015)
Cited for: CHARACTERIZATION OF VARIANTS PARK1 PRO-30; LYS-46; GLN-50 AND THR-53; MUTAGENESIS OF GLU-35 AND GLU-57; SUBCELLULAR LOCATION; SUBUNIT;
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.