UNIPROT #

P37840

PROTEIN NAME

Phospho-alpha Synuclein (S129)

SYNONYMS

Alpha synuclein antibody; Alpha-synuclein antibody; Alpha-synuclein, isoform NACP140 antibody; alphaSYN antibody; MGC105443 antibody; MGC110988 antibody; MGC127560 antibody; MGC64356 antibody; NACP antibody; Non A beta component of AD amyloid antibody; Non A4 component of amyloid antibody; Non A4 component of amyloid precursor antibody; Non-A beta component of AD amyloid antibody; Non-A-beta component of alzheimers disease amyloid , precursor of antibody; Non-A4 component of amyloid precursor antibody; Non-A4 component of amyloid, precursor of antibody; OTTHUMP00000218549 antibody; OTTHUMP00000218551 antibody; OTTHUMP00000218552 antibody; OTTHUMP00000218553 antibody; OTTHUMP00000218554 antibody; PARK 1 antibody; PARK 4 antibody; PARK1 antibody; PARK4 antibody; Parkinson disease (autosomal dominant, Lewy body) 4 antibody; Parkinson disease familial 1 antibody; SNCA antibody; Snca synuclein, alpha (non A4 component of amyloid precursor) antibody; SYN antibody; Synuclein alpha antibody; Synuclein alpha 140 antibody; Synuclein, alpha (non A4 component of amyloid precursor) antibody; SYUA_HUMAN antibody

SEQUENCE SIMILARITIES

Belongs to the synuclein family.

TISSUE SPECIFICITY

Highly expressed in presynaptic terminals in the central nervous system. Expressed principally in brain.

POST-TRANSLATIONAL MODIFICATION

Phosphorylated, predominantly on serine residues. Phosphorylation by CK1 appears to occur on residues distinct from the residue phosphorylated by other kinases. Phosphorylation of Ser-129 is selective and extensive in synucleinopathy lesions. In vitro, phosphorylation at Ser-129 promoted insoluble fibril formation. Phosphorylated on Tyr-125 by a PTK2B-dependent pathway upon osmotic stress.; Hallmark lesions of neurodegenerative synucleinopathies contain alpha-synuclein that is modified by nitration of tyrosine residues and possibly by dityrosine cross-linking to generated stable oligomers.; Ubiquitinated. The predominant conjugate is the diubiquitinated form (By similarity).; Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.

SUBCELLULAR LOCATION

Nucleus. Cytosol. Secreted. Membrane.

FUNCTION

The synuclein family members, including α-synuclein (also designated NACP for non-β-Amyloid component) and β-synuclein, are predominantly expressed in the brain and are speculated to be involved in synaptic regulation and neuronal plasticity. α-synuclein is localized to neuronal cell bodies and synapses. α-synuclein was first identified as a component of Alzheimer's disease amyloid plaques. Abnormal platelet function in Alzheimer's disease has been demonstrated. During megakaryocytic differentiation α-synuclein has been found to be upregulated, while β-synuclein is downregulated, indicating that coordinate expression of synucleins may be important during hematopoetic cell differentiation. A mutant form of α-synuclein has been found in patients with early onset Parkinson's disease.