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Protein Page:
SNCA (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
SNCA a member of the synuclein family. Abundantly expressed in the brain. Inhibits phospholipase D2 selectively. May integrate presynaptic signaling and membrane trafficking. Implicated in the pathogenesis of Parkinson's disease. A major component of amyloid plaques in the brains of patients with Alzheimer's disease. Two alternatively spliced isoforms transcripts have been identified. Note: This description may include information from UniProtKB.
Protein type: Adaptor/scaffold
Cellular Component: Golgi apparatus; nuclear outer membrane; rough endoplasmic reticulum; mitochondrion; lysosome; extracellular region; fibril; terminal button; cell cortex; inclusion body; cytosol; actin cytoskeleton; platelet alpha granule membrane; synaptic vesicle; growth cone; axon; perinuclear region of cytoplasm; cytoplasm; plasma membrane; ribosome; nucleus; cell junction
Molecular Function: identical protein binding; protein domain specific binding; zinc ion binding; histone binding; kinesin binding; microtubule binding; ferrous iron binding; caspase inhibitor activity; beta-tubulin binding; magnesium ion binding; phosphoprotein binding; protein N-terminus binding; Hsp70 protein binding; calcium ion binding; oxidoreductase activity; dynein binding; protein binding; phospholipase binding; copper ion binding; phospholipid binding; tau protein binding; fatty acid binding; alpha-tubulin binding
Biological Process: regulation of long-term neuronal synaptic plasticity; negative regulation of serotonin uptake; regulation of acyl-CoA biosynthetic process; adult locomotory behavior; negative regulation of norepinephrine uptake; mitochondrial membrane organization and biogenesis; microglial cell activation; positive regulation of endocytosis; response to lipopolysaccharide; negative regulation of caspase activity; negative regulation of monooxygenase activity; dopamine biosynthetic process; fatty acid metabolic process; positive regulation of neurotransmitter secretion; regulation of dopamine secretion; negative regulation of histone acetylation; negative regulation of dopamine uptake; calcium ion homeostasis; negative regulation of exocytosis; response to magnesium ion; negative regulation of protein amino acid phosphorylation; behavioral response to cocaine; phospholipid metabolic process; receptor internalization; fibril organization and biogenesis; synapse organization and biogenesis; dopamine uptake; negative regulation of neuron apoptosis; response to iron(II) ion; positive regulation of receptor recycling; aging; caspase activation; response to drug; neutral lipid metabolic process; protein destabilization; regulation of glutamate secretion; regulation of macrophage activation; negative regulation of microtubule polymerization; positive regulation of peptidyl-serine phosphorylation; organelle ATP synthesis coupled electron transport; negative regulation of dopamine metabolic process; regulation of locomotion; synaptic vesicle endocytosis; positive regulation of release of sequestered calcium ion into cytosol; regulation of excitatory postsynaptic membrane potential; negative regulation of transporter activity; negative regulation of apoptosis
Reference #:  P37840 (UniProtKB)
Alt. Names/Synonyms: Alpha-synuclein; alpha-synuclein, isoform NACP140; MGC110988; NACP; non A-beta component of AD amyloid; Non-A beta component of AD amyloid; non-A4 component of amyloid; Non-A4 component of amyloid precursor; PARK1; PARK4; PD1; SNCA; synuclein, alpha (non A4 component of amyloid precursor); SYUA
Gene Symbols: SNCA
Molecular weight: 14,460 Da
Basal Isoelectric point: 4.67  Predict pI for various phosphorylation states
CST Pathways:  Parkinson's Disease
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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SNCA

Protein Structure Not Found.


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Sites Implicated In
apoptosis, altered: Y39‑p
apoptosis, induced: S87‑p, S129‑p
apoptosis, inhibited: S129‑p
activity, induced: S129‑p
activity, inhibited: Y125‑p
intracellular localization: S129‑p
molecular association, regulation: Y39‑p, S129‑p
phosphorylation: Y39‑p
protein conformation: S129‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K6 __MDVFMKGLSkAkE
1 0 K6-sm __MDVFMkGLSkAkE
1 0 K10-sm VFMkGLSkAkEGVVA
0 1 K12 MkGLSkAKEGVVAAA
0 1 K12-ub MkGLSkAkEGVVAAA
1 0 K12-sm MkGLSkAkEGVVAAA
0 1 K21-ub GVVAAAEkTkQGVAE
1 0 K21-sm GVVAAAEkTkQGVAE
0 3 K23-ub VAAAEkTkQGVAEAA
1 0 K23-sm VAAAEkTkQGVAEAA
1 0 K34-sm AEAAGKTkEGVLyVG
2 12 Y39-p KTkEGVLyVGSKTkE
0 2 K43 GVLyVGSKTkEGVVH
0 1 K45 LyVGSKTKEGVVHGV
1 0 K45-sm LyVGSKTkEGVVHGV
0 1 T54 GVVHGVATVAEkTkE
0 1 T54-ga GVVHGVAtVAEkTkE
0 1 K58-ac GVAtVAEkTkEQVTN
0 1 T59 VAtVAEkTkEQVTNV
1 0 K60-sm AtVAEkTkEQVTNVG
1 1 T72 NVGGAVVTGVTAVAQ
1 0 K80-sm GVTAVAQkTVEGAGs
4 0 S87-p kTVEGAGsIAAATGF
0 1 S87-gl kTVEGAGsIAAATGF
0 1 K96-ac AAATGFVkKDQLGkN
0 1 K96 AAATGFVKKDQLGkN
2 0 K96-sm AAATGFVkKDQLGkN
2 0 K102-sm VkKDQLGkNEEGAPQ
6 0 Y125-p VDPDNEAyEMPsEEG
31 3 S129-p NEAyEMPsEEGyQDy
2 0 Y133-p EMPsEEGyQDyEPEA
2 0 Y136-p sEEGyQDyEPEA___
  mouse

 
K6-ub __MDVFMkGLSKAkE
K6 __MDVFMKGLSKAkE
K10 VFMkGLSKAkEGVVA
K12-m1 MkGLSKAkEGVVAAA
K12 MkGLSKAKEGVVAAA
K12 MkGLSKAKEGVVAAA
K21 GVVAAAEKTKQGVAE
K21 GVVAAAEKTKQGVAE
K23 VAAAEKTKQGVAEAA
K23 VAAAEKTKQGVAEAA
K34 AEAAGKTKEGVLyVG
Y39-p KTKEGVLyVGSKTkE
K43 GVLyVGSKTkEGVVH
K45-m1 LyVGSKTkEGVVHGV
K45 LyVGSKTKEGVVHGV
T54-gl GVVHGVTtVAEKtKE
T54 GVVHGVTTVAEKtKE
K58 GVTtVAEKtKEQVTN
T59-gl VTtVAEKtKEQVTNV
K60 TtVAEKtKEQVTNVG
T72-gl NVGGAVVtGVTAVAQ
K80 GVTAVAQKTVEGAGN
N87 KTVEGAGNIAAATGF
N87 KTVEGAGNIAAATGF
K96 AAATGFVKKDQMGKG
K96-ub AAATGFVkKDQMGKG
K96 AAATGFVKKDQMGKG
K102 VkKDQMGKGEEGYPQ
Y125 VDPGSEAYEMPsEEG
S129-p SEAYEMPsEEGYQDY
Y133 EMPsEEGYQDYEPEA
Y136 sEEGYQDYEPEA___
  rat

 
K6 __MDVFMKGLSKAKE
K6 __MDVFMKGLSKAKE
K10 VFMKGLSKAKEGVVA
K12 MKGLSKAKEGVVAAA
K12 MKGLSKAKEGVVAAA
K12 MKGLSKAKEGVVAAA
K21 GVVAAAEKTKQGVAE
K21 GVVAAAEKTKQGVAE
K23 VAAAEKTKQGVAEAA
K23 VAAAEKTKQGVAEAA
K34 AEAAGKTKEGVLyVG
Y39-p KTKEGVLyVGSkTKE
K43-ub GVLyVGSkTKEGVVH
K45 LyVGSkTKEGVVHGV
K45 LyVGSkTKEGVVHGV
T54 GVVHGVTTVAEKTKE
T54 GVVHGVTTVAEKTKE
K58 GVTTVAEKTKEQVTN
T59 VTTVAEKTKEQVTNV
K60 TTVAEKTKEQVTNVG
T72-gl NVGGAVVtGVTAVAQ
K80 GVTAVAQKTVEGAGN
N87 KTVEGAGNIAAATGF
N87 KTVEGAGNIAAATGF
K96 AAATGFVKKDQMGKG
K96 AAATGFVKKDQMGKG
K96 AAATGFVKKDQMGKG
K102 VKKDQMGKGEEGYPQ
Y125 VDPSSEAYEMPSEEG
S129 SEAYEMPSEEGYQDY
Y133 EMPSEEGYQDYEPEA
Y136 SEEGYQDYEPEA___
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