Variant position: 53 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 140 The length of the canonical sequence.
Location on the sequence:
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 TKEGVLYVGSKTKEGVVHGV ATVAEKTKEQVTNVGGAVVTG
Gorilla TKEGVLYVGSKTKEGVVHGV ATVAEKTKEQVTNVGGAVVTG
Rhesus macaque TKEGVLYVGSKTKEGVVHGV ATVAEKTKEQVTNVGGAVVTG
Chimpanzee TKEGVLYVGSKTKEGVVHGV ATVAEKTKEQVTNVGGAVVTG
Mouse TKEGVLYVGSKTKEGVVHGV TTVAEKTKEQVTNVGGAVVTG
Rat TKEGVLYVGSKTKEGVVHGV TTVAEKTKEQVTNVGGAVVTG
Pig TKEGVLYVGSKTKEGVVHGV TTVAEKTKEQVTNVGEAVVTG
Bovine TKEGVLYVGSKTKEGVVHGV TTVAEKTKEQVTNVGEAVVTG
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.
Type Positions Description
1 – 140 Alpha-synuclein
42 – 56 3; approximate
20 – 67 4 X 11 AA tandem repeats of [EGS]-K-T-K-[EQ]-[GQ]-V-X(4)
50 – 50 Copper
41 – 54 Missing. In isoform 2-5.
35 – 35 E -> K. No effect on oligomerization.
39 – 39 Y -> F. No effect on osmotic stress-induced phosphorylation.
50 – 50 H -> A. Impairs copper-binding.
57 – 57 E -> K. Increases oligomerization.
38 – 55
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.;
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;
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.