TCDB is operated by the Saier Lab Bioinformatics Group
TCIDNameDomainKingdom/PhylumProtein(s)
*1.C.77.1.1









α-synuclein (140 aas). In addition to β-amyloid, the cellular prion protein, PrPC  binds α-synuclein, which is responsible for neurodegenerative synucleopathies (Urrea et al. 2017). β-barrel channels such as α-hemolysin may serve as sensitive probes of α-synuclein (α-syn) interactions with membranes as well as model systems for studies of channel-assisted protein transport (Gurnev et al. 2014).  α-synuclein interacts with membranes to affect Ca2+ signalling, and the oligomeric β-sheet-rich α-synuclein leads to Ca2+ dysregulation and Ca2+-dependent cell death (Angelova et al. 2016).

Eukaryota
Metazoa
α-synuclein of Homo sapiens (EAX06036)
*1.C.77.1.2









β-synuclein of 134 aas.  The expression of β-synuclein can be regulated by Ca2+-dependent protein kinase G (PKG)-activation via stimulation of NMDA receptors (TC# 1.A.10) and voltage-operated Ca2+ channels (TC# 1.A.1) in the endoplasmic reticulum in the dorsal striatum (Yang and Choe 2014). Also forms a complex with the Slick/Slack channel, presumably to regulate its channel activity (Rizzi et al. 2015).

Eukaryota
Metazoa
beta-synuclein of Homo sapiens
*1.C.77.1.3









γ-synuclein, of 127 aas, (also designated synuclein-γ (SNCG) is implicated in both neurodegenerative diseases and cancer. Overexpression of SNCG in cancer cells is linked to tumor progression and chemoresistance (Liu et al. 2016).

Eukaryota
Metazoa
gamma-synuclein of Homo sapiens