HUMAN:SYUA

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	SNCA (synonyms: NACP, PARK1)
Protein Name(s)	Alpha-synuclein Non-A beta component of AD amyloid Non-A4 component of amyloid precursor NACP
External Links
UniProt	P37840
EMBL	L08850 L36674 L36675 D31839 U46901 U46897 U46898 U46899 AF163864 AF163864 AY049786 AK290169 CR457058 DQ088379 CH471057 BC013293 BC108275
CCDS	CCDS3634.1 CCDS43252.1
PIR	A49669 S56746
RefSeq	NP_000336.1 NP_001139526.1 NP_001139527.1 NP_009292.1
UniGene	Hs.21374
PDB	1XQ8 2JN5 2KKW 2M55 2X6M 3Q25 3Q26 3Q27 3Q28 3Q29 4BXL
PDBsum	1XQ8 2JN5 2KKW 2M55 2X6M 3Q25 3Q26 3Q27 3Q28 3Q29 4BXL
DisProt	DP00070
ProteinModelPortal	P37840
SMR	P37840
BioGrid	112506
DIP	DIP-35354N
IntAct	P37840
MINT	MINT-2515483
STRING	9606.ENSP00000338345
BindingDB	P37840
ChEMBL	CHEMBL6152
TCDB	1.C.77.1.1
PhosphoSite	P37840
DMDM	586067
MaxQB	P37840
PaxDb	P37840
PRIDE	P37840
DNASU	6622
Ensembl	ENST00000336904 ENST00000345009 ENST00000394986 ENST00000394989 ENST00000394991 ENST00000420646 ENST00000505199 ENST00000506244 ENST00000508895 ENST00000618500
GeneID	6622
KEGG	hsa:6622
UCSC	uc003hsp.3
CTD	6622
GeneCards	GC04M090646
GeneReviews	SNCA
HGNC	HGNC:11138
HPA	CAB010877 HPA005459
MIM	127750 163890 168600 168601 605543
neXtProt	NX_P37840
Orphanet	1648 171695 2828
PharmGKB	PA35986
eggNOG	NOG44393
GeneTree	ENSGT00390000016161
HOGENOM	HOG000008691
HOVERGEN	HBG000481
InParanoid	P37840
KO	K04528
OMA	QEGILQD
OrthoDB	EOG7034KG
PhylomeDB	P37840
TreeFam	TF332776
Reactome	REACT_75925
SignaLink	P37840
ChiTaRS	SNCA
EvolutionaryTrace	P37840
GeneWiki	Alpha-synuclein
GenomeRNAi	6622
NextBio	25791
PMAP-CutDB	P37840
PRO	PR:P37840
Proteomes	UP000005640
Bgee	P37840
CleanEx	HS_SNCA
ExpressionAtlas	P37840
Genevestigator	P37840
GO	GO:0015629 GO:0030424 GO:0005938 GO:0030054 GO:0005737 GO:0030659 GO:0005829 GO:0005576 GO:0043205 GO:0005794 GO:0030426 GO:0016234 GO:0005764 GO:0005739 GO:0005640 GO:0005634 GO:0048471 GO:0005886 GO:0005840 GO:0005791 GO:0008021 GO:0043195 GO:0043014 GO:0005509 GO:0005507 GO:0043027 GO:0045502 GO:0008198 GO:0042393 GO:0030544 GO:0042802 GO:0019894 GO:0000287 GO:0016491 GO:0005543 GO:0051219 GO:0048156 GO:0044212 GO:0008270 GO:0006919 GO:0008344 GO:0007568 GO:0048148 GO:0071280 GO:0071872 GO:0044344 GO:0034599 GO:0042416 GO:0051583 GO:0043206 GO:0006631 GO:0060291 GO:0001774 GO:0042775 GO:0007006 GO:0043066 GO:0043154 GO:0045963 GO:0051585 GO:0045920 GO:0035067 GO:0031115 GO:1902957 GO:0032769 GO:0043524 GO:0051622 GO:0010642 GO:0001933 GO:0051612 GO:0070495 GO:0000122 GO:0032410 GO:0006638 GO:0055114 GO:0006644 GO:0043065 GO:0045807 GO:1903284 GO:1903285 GO:0060732 GO:0001956 GO:0033138 GO:0071902 GO:0001921 GO:0051281 GO:0031648 GO:0031623 GO:0050812 GO:0014059 GO:0060079 GO:0014048 GO:0040012 GO:0048169 GO:0043030 GO:0010517 GO:1903426 GO:1903421 GO:0042493 GO:0034341 GO:0070555 GO:0010040 GO:0032496 GO:0032026 GO:0050808 GO:0048488
Gene3D	1.10.287.700
InterPro	IPR001058 IPR002460
PANTHER	PTHR13820
Pfam	PF01387
PRINTS	PR01212 PR01211

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0001934	positive regulation of protein phosphorylation	PMID:21127069^[1]	ECO:0000269			P		Fig 4a and 4b show that levels of phosphorylated tau were higher in the brains of alpha-synuclein +/+ genotype compared to the alpha-synuclein -/- genotype. Also, a western blot of brain samples using pS262 polyclonal anitbody specific for phosphorylated tau produced a band 3.2 times less intense in alpha-synuclein -/- gentoypes compared to alpha-synuclein +/+ genotypes.	complete
	GO:0045860	positive regulation of protein kinase activity	PMID:21127069^[1]	ECO:0000269			P		Fig 5b shows the relative phosphorylation of recombinant human tau by recombinant protein kinase A. The phosphorylation of tau at Ser262 is increased in the presence of alpha-synuclein compared to controls.	complete
enables	GO:0003779	actin binding	PMID:18331289^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P60709	F		Seeded From UniProt	complete
involved_in	GO:0051621	regulation of norepinephrine uptake	PMID:18331289^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P60709	P	part_of:(GO:0022898)	Seeded From UniProt	complete
involved_in	GO:0022898	regulation of transmembrane transporter activity	PMID:18331289^[2]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P60709	P	has_regulation_target:(UniProtKB:P23975) regulates_transport_of:(CHEBI:33569)	Seeded From UniProt	complete
involved_in	GO:0045921	positive regulation of exocytosis	PMID:30404828^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016079	synaptic vesicle exocytosis	PMID:28288128^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016082	synaptic vesicle priming	PMID:30404828^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051262	protein tetramerization	PMID:21841800^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035493	SNARE complex assembly	PMID:20798282^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0000149	SNARE binding	PMID:20798282^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0050729	positive regulation of inflammatory response	PMID:25533483^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(GO:0033554) occurs_in:(UBERON:0003883)	Seeded From UniProt	complete
involved_in	GO:1901216	positive regulation of neuron death	PMID:25533483^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(GO:0033554) occurs_in:(UBERON:0003883)	Seeded From UniProt	complete
involved_in	GO:1905606	regulation of presynapse assembly	PMID:25533483^[7]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:Q21053	P	occurs_in:(CL:0000108) has_input:(UniProtKB:Q96QK1)	Seeded From UniProt	complete
enables	GO:0030544	Hsp70 protein binding	PMID:18975920^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0DMV9	F		Seeded From UniProt	complete
enables	GO:1903136	cuprous ion binding	PMID:25495902^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1904715	negative regulation of chaperone-mediated autophagy	PMID:20697033^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000700)	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:23983262^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:24936070^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24936070^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:24936070^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:24936070^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:24936070^[12]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25561023^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:25561023^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	PMID:15863497^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1901215	negative regulation of neuron death	PMID:15863497^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15863497^[14]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005543	phospholipid binding	PMID:17222866^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0016234	inclusion body	PMID:17222866^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0099512	supramolecular fiber	PMID:17222866^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0099512	supramolecular fiber	PMID:23507046^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1903285	positive regulation of hydrogen peroxide catabolic process	PMID:23507046^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034599	cellular response to oxidative stress	PMID:23507046^[16]	ECO:0000305	curator inference used in manual assertion	GO:1903284	P		Seeded From UniProt	complete
involved_in	GO:1903284	positive regulation of glutathione peroxidase activity	PMID:23507046^[16]	ECO:0000314	direct assay evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P07203)	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:17222866^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:24403142^[17]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071902	positive regulation of protein serine/threonine kinase activity	PMID:21127069^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051219	phosphoprotein binding	PMID:21127069^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0048156	tau protein binding	PMID:21127069^[1]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0033138	positive regulation of peptidyl-serine phosphorylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:O55042	P		Seeded From UniProt	complete
involved_in	GO:0032769	negative regulation of monooxygenase activity	PMID:11943812^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031115	negative regulation of microtubule polymerization	PMID:21127069^[1]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006919	activation of cysteine-type endopeptidase activity involved in apoptotic process	PMID:21050448^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071280	cellular response to copper ion	PMID:21320589^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070555	response to interleukin-1	PMID:12406186^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0070495	negative regulation of thrombin-activated receptor signaling pathway	PMID:12239163^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
NOT\|enables	GO:0060961	phospholipase D inhibitor activity	PMID:19146388^[23]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0060732	positive regulation of inositol phosphate biosynthetic process	PMID:15641770^[24]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0055114	oxidation-reduction process	PMID:21320589^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
NOT\|involved_in	GO:0055074	calcium ion homeostasis	PMID:12239163^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051622	negative regulation of norepinephrine uptake	PMID:17156375^[25]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051612	negative regulation of serotonin uptake	PMID:16882008^[26]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051585	negative regulation of dopamine uptake involved in synaptic transmission	PMID:12958153^[27]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051281	positive regulation of release of sequestered calcium ion into cytosol	PMID:15641770^[24]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048488	synaptic vesicle endocytosis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:O55042	P		Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:20039155^[28]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0048156	tau protein binding	PMID:17408955^[29]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0045920	negative regulation of exocytosis	PMID:12239163^[22]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045807	positive regulation of endocytosis	PMID:18980610^[30]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0070840	dynein complex binding	PMID:16176937^[31]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q5XIL8	F		Seeded From UniProt	complete
part_of	GO:0099512	supramolecular fiber	PMID:18346205^[32]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0043154	negative regulation of cysteine-type endopeptidase activity involved in apoptotic process	PMID:10818098^[33]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	PMID:10818098^[33]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0043027	cysteine-type endopeptidase inhibitor activity involved in apoptotic process	PMID:10818098^[33]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0043014	alpha-tubulin binding	PMID:11698390^[34]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P68363	F		Seeded From UniProt	complete
enables	GO:0042393	histone binding	PMID:16959795^[35]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0035067	negative regulation of histone acetylation	PMID:16959795^[35]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034341	response to interferon-gamma	PMID:19157893^[36]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032496	response to lipopolysaccharide	PMID:12406186^[21]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032410	negative regulation of transporter activity	PMID:16882008^[26]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0032026	response to magnesium ion	PMID:11850416^[37]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0031648	protein destabilization	PMID:21320589^[20]	ECO:0000314	direct assay evidence used in manual assertion		P	happens_during:(GO:0071280)	Seeded From UniProt	complete
involved_in	GO:0031623	receptor internalization	PMID:18980610^[30]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0031092	platelet alpha granule membrane	PMID:12239163^[22]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0030544	Hsp70 protein binding	PMID:18975920^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0DMV8	F		Seeded From UniProt	complete
part_of	GO:0030426	growth cone	PMID:12958153^[27]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030424	axon	PMID:12958153^[27]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019894	kinesin binding	PMID:16176937^[31]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q2PQA9	F		Seeded From UniProt	complete
enables	GO:0016491	oxidoreductase activity	PMID:21320589^[20]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(CHEBI:18243)	Seeded From UniProt	complete
part_of	GO:0016234	inclusion body	PMID:20039155^[28]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0015629	actin cytoskeleton	PMID:17408955^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0010642	negative regulation of platelet-derived growth factor receptor signaling pathway	PMID:12239163^[22]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010517	regulation of phospholipase activity	PMID:15641770^[24]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010040	response to iron(II) ion	PMID:11850416^[37]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:11850416^[37]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008198	ferrous iron binding	PMID:11850416^[37]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005938	cell cortex	PMID:19157893^[36]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:15641770^[24]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:12958153^[27]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:8248242^[38]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:12406186^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16959795^[35]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:17408955^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:12958153^[27]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:12406186^[21]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:16959795^[35]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:17408955^[29]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:11312271^[39]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:11850416^[37]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005507	copper ion binding	PMID:21319811^[40]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0005507	copper ion binding	PMID:21320589^[20]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
NOT\|enables	GO:0005504	fatty acid binding	PMID:16687662^[41]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0001921	positive regulation of receptor recycling	PMID:18980610^[30]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0000287	magnesium ion binding	PMID:11850416^[37]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25732184^[42]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840	F	occurs_in:(GO:0005737)\|occurs_in:(GO:0097413)	Seeded From UniProt	complete
	GO:0035543	positive regulation of SNARE complex assembly	PMID:20798282^[6]	ECO:0000314			P		Figure 1 shows the immunoprecipitation of α-Synuclein/α-S/alpha-Synuclein/Snca of Homo sapiens in transgenic Mus musculus with SNARE complexes immunoprecipitated with SNAP-25 to measure the activity.	complete CACAO 13462
enables	GO:0042802	identical protein binding	PMID:25643172^[43]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840	F	occurs_in:(GO:0005737)\|occurs_in:(GO:0097413)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24983211^[44]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840	F	occurs_in:(GO:0005737)\|occurs_in:(GO:0097413)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24895406^[45]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840	F	occurs_in:(GO:0005737)\|occurs_in:(GO:0097413)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24374342^[46]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840	F	occurs_in:(GO:0005737)\|occurs_in:(GO:0097413)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23927048^[47]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840	F	occurs_in:(GO:0005737)\|occurs_in:(GO:0097413)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:22119730^[48]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840	F	occurs_in:(GO:0005737)\|occurs_in:(GO:0097413)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21443877^[49]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840	F	occurs_in:(GO:0005737)\|occurs_in:(GO:0097413)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19875982^[50]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840	F	occurs_in:(GO:0005737)\|occurs_in:(GO:0097413)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19745811^[51]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840	F	occurs_in:(GO:0005737)\|occurs_in:(GO:0097413)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18614564^[52]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840	F	occurs_in:(GO:0005737)\|occurs_in:(GO:0097413)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16764865^[53]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840	F	occurs_in:(GO:0005737)\|occurs_in:(GO:0097413)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16330551^[54]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840	F	occurs_in:(GO:0005737)\|occurs_in:(GO:0097413)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:15502874^[55]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840	F	occurs_in:(GO:0005737)\|occurs_in:(GO:0097413)	Seeded From UniProt	complete
involved_in	GO:0006915	apoptotic process	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0043027	P		Seeded From UniProt	complete
part_of	GO:0098794	postsynapse	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0060079	C		Seeded From UniProt	complete
involved_in	GO:2000377	regulation of reactive oxygen species metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0061024	membrane organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0060291	long-term synaptic potentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0060079	excitatory postsynaptic potential	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0051259	protein complex oligomerization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0050812	regulation of acyl-CoA biosynthetic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0050808	synapse organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0050806	positive regulation of synaptic transmission	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0048489	synaptic vesicle transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0048488	synaptic vesicle endocytosis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0048169	regulation of long-term neuronal synaptic plasticity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0048168	regulation of neuronal synaptic plasticity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0046928	regulation of neurotransmitter secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
part_of	GO:0045202	synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	C		Seeded From UniProt	complete
involved_in	GO:0043524	negative regulation of neuron apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0043030	regulation of macrophage activation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	F		Seeded From UniProt	complete
involved_in	GO:0042775	mitochondrial ATP synthesis coupled electron transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0042493	response to drug	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0042417	dopamine metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0042416	dopamine biosynthetic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
enables	GO:0042393	histone binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	F		Seeded From UniProt	complete
involved_in	GO:0040012	regulation of locomotion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0035493	SNARE complex assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0034599	cellular response to oxidative stress	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0033138	positive regulation of peptidyl-serine phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
part_of	GO:0030672	synaptic vesicle membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	C		Seeded From UniProt	complete
part_of	GO:0016234	inclusion body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	C		Seeded From UniProt	complete
involved_in	GO:0014059	regulation of dopamine secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0014048	regulation of glutamate secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0008344	adult locomotory behavior	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0007268	chemical synaptic transmission	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0007006	mitochondrial membrane organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0006644	phospholipid metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0006638	neutral lipid metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0006631	fatty acid metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	C		Seeded From UniProt	complete
involved_in	GO:0001963	synaptic transmission, dopaminergic	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0001956	positive regulation of neurotransmitter secretion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:0001774	microglial cell activation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:O55042 ensembl:ENSMUSP00000109907	P		Seeded From UniProt	complete
involved_in	GO:1904307	response to desipramine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	P		Seeded From UniProt	complete
involved_in	GO:1901215	negative regulation of neuron death	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	P		Seeded From UniProt	complete
involved_in	GO:1901214	regulation of neuron death	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	P		Seeded From UniProt	complete
part_of	GO:0098793	presynapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
enables	GO:0048487	beta-tubulin binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	F		Seeded From UniProt	complete
involved_in	GO:0048148	behavioral response to cocaine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	P		Seeded From UniProt	complete
enables	GO:0047485	protein N-terminus binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	F		Seeded From UniProt	complete
involved_in	GO:0045963	negative regulation of dopamine metabolic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	P		Seeded From UniProt	complete
involved_in	GO:0044344	cellular response to fibroblast growth factor stimulus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	P		Seeded From UniProt	complete
part_of	GO:0043679	axon terminus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
involved_in	GO:0043524	negative regulation of neuron apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	P		Seeded From UniProt	complete
enables	GO:0043274	phospholipase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	F		Seeded From UniProt	complete
part_of	GO:0043231	intracellular membrane-bounded organelle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0043195	terminal bouton	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0043025	neuronal cell body	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
involved_in	GO:0042220	response to cocaine	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	P		Seeded From UniProt	complete
part_of	GO:0030659	cytoplasmic vesicle membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0030426	growth cone	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
enables	GO:0019904	protein domain specific binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	F		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	F		Seeded From UniProt	complete
part_of	GO:0008021	synaptic vesicle	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
enables	GO:0008017	microtubule binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	F		Seeded From UniProt	complete
involved_in	GO:0007568	aging	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0005840	ribosome	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0005791	rough endoplasmic reticulum	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0005759	mitochondrial matrix	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0005758	mitochondrial intermembrane space	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0005743	mitochondrial inner membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0005741	mitochondrial outer membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0005640	nuclear outer membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	C		Seeded From UniProt	complete
enables	GO:0005543	phospholipid binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	F		Seeded From UniProt	complete
involved_in	GO:0001933	negative regulation of protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P37377 ensembl:ENSRNOP00000030609	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002460	C		Seeded From UniProt	complete
involved_in	GO:0014059	regulation of dopamine secretion	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002460	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:27018801^[56]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840-1	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25732184^[42]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840-1	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:24895406^[45]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840-1	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18550842^[57]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P37840-1	F		Seeded From UniProt	complete
involved_in	GO:1903421	regulation of synaptic vesicle recycling	PMID:23983262^[11]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0001774	microglial cell activation	PMID:24252804^[58]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	has_input:(UniProtKB:Q9UBK2)	Seeded From UniProt	complete
part_of	GO:0005739	mitochondrion	PMID:24252804^[58]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	part_of:(CL:0000700)	Seeded From UniProt	complete
enables	GO:0044212	transcription regulatory region DNA binding	PMID:24252804^[58]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	has_input:(UniProtKB:Q9UBK2)	Seeded From UniProt	complete
involved_in	GO:0043065	positive regulation of apoptotic process	PMID:24252804^[58]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000122	negative regulation of transcription by RNA polymerase II	PMID:24252804^[58]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1902957	negative regulation of mitochondrial electron transport, NADH to ubiquinone	PMID:24252804^[58]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
colocalizes_with	GO:0005747	mitochondrial respiratory chain complex I	PMID:24252804^[58]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:1903426	regulation of reactive oxygen species biosynthetic process	PMID:24252804^[58]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005764	lysosome	PMID:24477431^[59]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0071872	cellular response to epinephrine stimulus	PMID:21320589^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051583	dopamine uptake involved in synaptic transmission	PMID:21320589^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0097435	supramolecular fiber organization	PMID:21320589^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0042416	dopamine biosynthetic process	PMID:21320589^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0014059	regulation of dopamine secretion	PMID:21320589^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0044267	cellular protein metabolic process	Reactome:R-HSA-392499	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-5661161 Reactome:R-HSA-5661157 Reactome:R-HSA-5660757 Reactome:R-HSA-5660753 Reactome:R-HSA-5660752 Reactome:R-HSA-5658496 Reactome:R-HSA-5658104	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-977136 Reactome:R-HSA-976734	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0964 UniProtKB-SubCell:SL-0243	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
part_of	GO:0045202	synapse	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0770 UniProtKB-SubCell:SL-0258	C		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		Seeded From UniProt	complete
part_of	GO:0030054	cell junction	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0965	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472 UniProtKB-SubCell:SL-0162	C		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 Qureshi, HY & Paudel, HK (2011) Parkinsonian neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and alpha-synuclein mutations promote Tau protein phosphorylation at Ser262 and destabilize microtubule cytoskeleton in vitro. J. Biol. Chem. 286 5055-68 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Jeannotte, AM & Sidhu, A (2008) Regulated interactions of the norepineprhine transporter by the actin and microtubule cytoskeletons. J. Neurochem. 105 1668-82 PubMed GONUTS page
↑ ^3.0 ^3.1 Huang, CC et al. (2018) Soluble α-synuclein facilitates priming and fusion by releasing Ca from the thapsigargin-sensitive Ca pool in PC12 cells. J. Cell. Sci. 131 PubMed GONUTS page
↑ Logan, T et al. (2017) α-Synuclein promotes dilation of the exocytotic fusion pore. Nat. Neurosci. 20 681-689 PubMed GONUTS page
↑ Bartels, T et al. (2011) α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 477 107-10 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Burré, J et al. (2010) Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro. Science 329 1663-7 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Dhungel, N et al. (2015) Parkinson's disease genes VPS35 and EIF4G1 interact genetically and converge on α-synuclein. Neuron 85 76-87 PubMed GONUTS page
↑ ^8.0 ^8.1 Luk, KC et al. (2008) Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly. Biochemistry 47 12614-25 PubMed GONUTS page
↑ De Ricco, R et al. (2015) Differences in the binding of copper(I) to α- and β-synuclein. Inorg Chem 54 265-72 PubMed GONUTS page
↑ Alvarez-Erviti, L et al. (2010) Chaperone-mediated autophagy markers in Parkinson disease brains. Arch. Neurol. 67 1464-72 PubMed GONUTS page
↑ ^11.0 ^11.1 Oueslati, A et al. (2013) Polo-like kinase 2 regulates selective autophagic α-synuclein clearance and suppresses its toxicity in vivo. Proc. Natl. Acad. Sci. U.S.A. 110 E3945-54 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 ^12.4 Khalaf, O et al. (2014) The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity. J. Biol. Chem. 289 21856-76 PubMed GONUTS page
↑ ^13.0 ^13.1 Tsigelny, IF et al. (2015) Molecular determinants of α-synuclein mutants' oligomerization and membrane interactions. ACS Chem Neurosci 6 403-16 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 Sung, JY et al. (2005) Proteolytic cleavage of extracellular secreted {alpha}-synuclein via matrix metalloproteinases. J. Biol. Chem. 280 25216-24 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 ^15.3 Volles, MJ & Lansbury, PT Jr (2007) Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity. J. Mol. Biol. 366 1510-22 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 Koo, HJ et al. (2013) α-Synuclein-mediated defense against oxidative stress via modulation of glutathione peroxidase. Biochim. Biophys. Acta 1834 972-6 PubMed GONUTS page
↑ Skibinski, G et al. (2014) Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies. J. Neurosci. 34 418-33 PubMed GONUTS page
↑ Perez, RG et al. (2002) A role for alpha-synuclein in the regulation of dopamine biosynthesis. J. Neurosci. 22 3090-9 PubMed GONUTS page
↑ Khandelwal, PJ et al. (2010) Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model. Mol Neurodegener 5 47 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 ^20.3 ^20.4 ^20.5 ^20.6 ^20.7 ^20.8 ^20.9 Meloni, G & Vašák, M (2011) Redox activity of α-synuclein-Cu is silenced by Zn₇-metallothionein-3. Free Radic. Biol. Med. 50 1471-9 PubMed GONUTS page
↑ ^21.0 ^21.1 ^21.2 ^21.3 Tanji, K et al. (2002) Upregulation of alpha-synuclein by lipopolysaccharide and interleukin-1 in human macrophages. Pathol. Int. 52 572-7 PubMed GONUTS page
↑ ^22.0 ^22.1 ^22.2 ^22.3 ^22.4 Park, SM et al. (2002) Evidence that alpha-synuclein functions as a negative regulator of Ca(++)-dependent alpha-granule release from human platelets. Blood 100 2506-14 PubMed GONUTS page
↑ Rappley, I et al. (2009) Evidence that alpha-synuclein does not inhibit phospholipase D. Biochemistry 48 1077-83 PubMed GONUTS page
↑ ^24.0 ^24.1 ^24.2 ^24.3 Narayanan, V et al. (2005) Fluorescence studies suggest a role for alpha-synuclein in the phosphatidylinositol lipid signaling pathway. Biochemistry 44 462-70 PubMed GONUTS page
↑ Wersinger, C et al. (2006) Attenuation of the norepinephrine transporter activity and trafficking via interactions with alpha-synuclein. Eur. J. Neurosci. 24 3141-52 PubMed GONUTS page
↑ ^26.0 ^26.1 Wersinger, C et al. (2006) Modulation of the trafficking of the human serotonin transporter by human alpha-synuclein. Eur. J. Neurosci. 24 55-64 PubMed GONUTS page
↑ ^27.0 ^27.1 ^27.2 ^27.3 ^27.4 Wersinger, C et al. (2003) Modulation of dopamine transporter function by alpha-synuclein is altered by impairment of cell adhesion and by induction of oxidative stress. FASEB J. 17 2151-3 PubMed GONUTS page
↑ ^28.0 ^28.1 Pountney, DL et al. (2011) Association of metallothionein-III with oligodendroglial cytoplasmic inclusions in multiple system atrophy. Neurotox Res 19 115-22 PubMed GONUTS page
↑ ^29.0 ^29.1 ^29.2 ^29.3 Esposito, A et al. (2007) alpha-Synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton. Neurobiol. Dis. 26 521-31 PubMed GONUTS page
↑ ^30.0 ^30.1 ^30.2 Ben Gedalya, T et al. (2009) Alpha-synuclein and polyunsaturated fatty acids promote clathrin-mediated endocytosis and synaptic vesicle recycling. Traffic 10 218-34 PubMed GONUTS page
↑ ^31.0 ^31.1 Utton, MA et al. (2005) Molecular motors implicated in the axonal transport of tau and alpha-synuclein. J. Cell. Sci. 118 4645-54 PubMed GONUTS page
↑ Gerard, M et al. (2008) FK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53T. J. Neurochem. 106 121-33 PubMed GONUTS page
↑ ^33.0 ^33.1 ^33.2 da Costa, CA et al. (2000) Wild-type but not Parkinson's disease-related ala-53 --> Thr mutant alpha -synuclein protects neuronal cells from apoptotic stimuli. J. Biol. Chem. 275 24065-9 PubMed GONUTS page
↑ Alim, MA et al. (2002) Tubulin seeds alpha-synuclein fibril formation. J. Biol. Chem. 277 2112-7 PubMed GONUTS page
↑ ^35.0 ^35.1 ^35.2 ^35.3 Kontopoulos, E et al. (2006) Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity. Hum. Mol. Genet. 15 3012-23 PubMed GONUTS page
↑ ^36.0 ^36.1 Dinh, K et al. (2009) Fluorescence microscopy and 3D image reconstruction of cytokine initiated disruption of the Parkinson disease associated proteins alpha-synuclein, tau and ubiquitin in cultured glial cells. Cytokine 45 179-83 PubMed GONUTS page
↑ ^37.0 ^37.1 ^37.2 ^37.3 ^37.4 ^37.5 Golts, N et al. (2002) Magnesium inhibits spontaneous and iron-induced aggregation of alpha-synuclein. J. Biol. Chem. 277 16116-23 PubMed GONUTS page
↑ Uéda, K et al. (1993) Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 90 11282-6 PubMed GONUTS page
↑ Nielsen, MS et al. (2001) Ca2+ binding to alpha-synuclein regulates ligand binding and oligomerization. J. Biol. Chem. 276 22680-4 PubMed GONUTS page
↑ Dudzik, CG et al. (2011) Coordination features and affinity of the Cu²+ site in the α-synuclein protein of Parkinson's disease. Biochemistry 50 1771-7 PubMed GONUTS page
↑ Lücke, C et al. (2006) Interactions between fatty acids and alpha-synuclein. J. Lipid Res. 47 1714-24 PubMed GONUTS page
↑ ^42.0 ^42.1 Roberts, RF et al. (2015) Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson's disease brain. Brain 138 1642-57 PubMed GONUTS page
↑ Galvagnion, C et al. (2015) Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation. Nat. Chem. Biol. 11 229-34 PubMed GONUTS page
↑ Yin, G et al. (2014) α-Synuclein interacts with the switch region of Rab8a in a Ser129 phosphorylation-dependent manner. Neurobiol. Dis. 70 149-61 PubMed GONUTS page
↑ ^45.0 ^45.1 Plotegher, N et al. (2014) The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicity. Hum. Mol. Genet. 23 5615-29 PubMed GONUTS page
↑ Lorenzen, N et al. (2014) The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes. FEBS Lett. 588 497-502 PubMed GONUTS page
↑ Coelho-Cerqueira, E et al. (2013) α-Synuclein as an intrinsically disordered monomer--fact or artefact? FEBS J. 280 4915-27 PubMed GONUTS page
↑ Herrera, F & Outeiro, TF (2012) α-Synuclein modifies huntingtin aggregation in living cells. FEBS Lett. 586 7-12 PubMed GONUTS page
↑ Caruana, M et al. (2011) Inhibition and disaggregation of α-synuclein oligomers by natural polyphenolic compounds. FEBS Lett. 585 1113-20 PubMed GONUTS page
↑ Roodveldt, C et al. (2009) Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hip. EMBO J. 28 3758-70 PubMed GONUTS page
↑ Karpinar, DP et al. (2009) Pre-fibrillar alpha-synuclein variants with impaired beta-structure increase neurotoxicity in Parkinson's disease models. EMBO J. 28 3256-68 PubMed GONUTS page
↑ McFarland, MA et al. (2008) Proteomics analysis identifies phosphorylation-dependent alpha-synuclein protein interactions. Mol. Cell Proteomics 7 2123-37 PubMed GONUTS page
↑ Du, HN et al. (2006) Acceleration of alpha-synuclein aggregation by homologous peptides. FEBS Lett. 580 3657-64 PubMed GONUTS page
↑ Lee, CH et al. (2006) Dequalinium-induced protofibril formation of alpha-synuclein. J. Biol. Chem. 281 3463-72 PubMed GONUTS page
↑ Shendelman, S et al. (2004) DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation. PLoS Biol. 2 e362 PubMed GONUTS page
↑ Tuttle, MD et al. (2016) Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein. Nat. Struct. Mol. Biol. 23 409-15 PubMed GONUTS page
↑ Vilar, M et al. (2008) The fold of alpha-synuclein fibrils. Proc. Natl. Acad. Sci. U.S.A. 105 8637-42 PubMed GONUTS page
↑ ^58.0 ^58.1 ^58.2 ^58.3 ^58.4 ^58.5 ^58.6 ^58.7 Dias, V et al. (2013) The role of oxidative stress in Parkinson's disease. J Parkinsons Dis 3 461-91 PubMed GONUTS page
↑ Murphy, KE et al. (2014) Reduced glucocerebrosidase is associated with increased α-synuclein in sporadic Parkinson's disease. Brain 137 834-48 PubMed GONUTS page

[PMID:21127069-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 Qureshi, HY & Paudel, HK (2011) Parkinsonian neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) and alpha-synuclein mutations promote Tau protein phosphorylation at Ser262 and destabilize microtubule cytoskeleton in vitro. J. Biol. Chem. 286 5055-68 PubMed GONUTS page

[PMID:18331289-2] 2.0 ^2.1 ^2.2 Jeannotte, AM & Sidhu, A (2008) Regulated interactions of the norepineprhine transporter by the actin and microtubule cytoskeletons. J. Neurochem. 105 1668-82 PubMed GONUTS page

[PMID:30404828-3] 3.0 ^3.1 Huang, CC et al. (2018) Soluble α-synuclein facilitates priming and fusion by releasing Ca from the thapsigargin-sensitive Ca pool in PC12 cells. J. Cell. Sci. 131 PubMed GONUTS page

[PMID:28288128-4] Logan, T et al. (2017) α-Synuclein promotes dilation of the exocytotic fusion pore. Nat. Neurosci. 20 681-689 PubMed GONUTS page

[PMID:21841800-5] Bartels, T et al. (2011) α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation. Nature 477 107-10 PubMed GONUTS page

[PMID:20798282-6] 6.0 ^6.1 ^6.2 Burré, J et al. (2010) Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro. Science 329 1663-7 PubMed GONUTS page

[PMID:25533483-7] 7.0 ^7.1 ^7.2 Dhungel, N et al. (2015) Parkinson's disease genes VPS35 and EIF4G1 interact genetically and converge on α-synuclein. Neuron 85 76-87 PubMed GONUTS page

[PMID:18975920-8] 8.0 ^8.1 Luk, KC et al. (2008) Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly. Biochemistry 47 12614-25 PubMed GONUTS page

[PMID:25495902-9] De Ricco, R et al. (2015) Differences in the binding of copper(I) to α- and β-synuclein. Inorg Chem 54 265-72 PubMed GONUTS page

[PMID:20697033-10] Alvarez-Erviti, L et al. (2010) Chaperone-mediated autophagy markers in Parkinson disease brains. Arch. Neurol. 67 1464-72 PubMed GONUTS page

[PMID:23983262-11] 11.0 ^11.1 Oueslati, A et al. (2013) Polo-like kinase 2 regulates selective autophagic α-synuclein clearance and suppresses its toxicity in vivo. Proc. Natl. Acad. Sci. U.S.A. 110 E3945-54 PubMed GONUTS page

[PMID:24936070-12] 12.0 ^12.1 ^12.2 ^12.3 ^12.4 Khalaf, O et al. (2014) The H50Q mutation enhances α-synuclein aggregation, secretion, and toxicity. J. Biol. Chem. 289 21856-76 PubMed GONUTS page

[PMID:25561023-13] 13.0 ^13.1 Tsigelny, IF et al. (2015) Molecular determinants of α-synuclein mutants' oligomerization and membrane interactions. ACS Chem Neurosci 6 403-16 PubMed GONUTS page

[PMID:15863497-14] 14.0 ^14.1 ^14.2 Sung, JY et al. (2005) Proteolytic cleavage of extracellular secreted {alpha}-synuclein via matrix metalloproteinases. J. Biol. Chem. 280 25216-24 PubMed GONUTS page

[PMID:17222866-15] 15.0 ^15.1 ^15.2 ^15.3 Volles, MJ & Lansbury, PT Jr (2007) Relationships between the sequence of alpha-synuclein and its membrane affinity, fibrillization propensity, and yeast toxicity. J. Mol. Biol. 366 1510-22 PubMed GONUTS page

[PMID:23507046-16] 16.0 ^16.1 ^16.2 ^16.3 Koo, HJ et al. (2013) α-Synuclein-mediated defense against oxidative stress via modulation of glutathione peroxidase. Biochim. Biophys. Acta 1834 972-6 PubMed GONUTS page

[PMID:24403142-17] Skibinski, G et al. (2014) Mutant LRRK2 toxicity in neurons depends on LRRK2 levels and synuclein but not kinase activity or inclusion bodies. J. Neurosci. 34 418-33 PubMed GONUTS page

[PMID:11943812-18] Perez, RG et al. (2002) A role for alpha-synuclein in the regulation of dopamine biosynthesis. J. Neurosci. 22 3090-9 PubMed GONUTS page

[PMID:21050448-19] Khandelwal, PJ et al. (2010) Parkinson-related parkin reduces α-Synuclein phosphorylation in a gene transfer model. Mol Neurodegener 5 47 PubMed GONUTS page

[PMID:21320589-20] 20.0 ^20.1 ^20.2 ^20.3 ^20.4 ^20.5 ^20.6 ^20.7 ^20.8 ^20.9 Meloni, G & Vašák, M (2011) Redox activity of α-synuclein-Cu is silenced by Zn₇-metallothionein-3. Free Radic. Biol. Med. 50 1471-9 PubMed GONUTS page

[PMID:12406186-21] 21.0 ^21.1 ^21.2 ^21.3 Tanji, K et al. (2002) Upregulation of alpha-synuclein by lipopolysaccharide and interleukin-1 in human macrophages. Pathol. Int. 52 572-7 PubMed GONUTS page

[PMID:12239163-22] 22.0 ^22.1 ^22.2 ^22.3 ^22.4 Park, SM et al. (2002) Evidence that alpha-synuclein functions as a negative regulator of Ca(++)-dependent alpha-granule release from human platelets. Blood 100 2506-14 PubMed GONUTS page

[PMID:19146388-23] Rappley, I et al. (2009) Evidence that alpha-synuclein does not inhibit phospholipase D. Biochemistry 48 1077-83 PubMed GONUTS page

[PMID:15641770-24] 24.0 ^24.1 ^24.2 ^24.3 Narayanan, V et al. (2005) Fluorescence studies suggest a role for alpha-synuclein in the phosphatidylinositol lipid signaling pathway. Biochemistry 44 462-70 PubMed GONUTS page

[PMID:17156375-25] Wersinger, C et al. (2006) Attenuation of the norepinephrine transporter activity and trafficking via interactions with alpha-synuclein. Eur. J. Neurosci. 24 3141-52 PubMed GONUTS page

[PMID:16882008-26] 26.0 ^26.1 Wersinger, C et al. (2006) Modulation of the trafficking of the human serotonin transporter by human alpha-synuclein. Eur. J. Neurosci. 24 55-64 PubMed GONUTS page

[PMID:12958153-27] 27.0 ^27.1 ^27.2 ^27.3 ^27.4 Wersinger, C et al. (2003) Modulation of dopamine transporter function by alpha-synuclein is altered by impairment of cell adhesion and by induction of oxidative stress. FASEB J. 17 2151-3 PubMed GONUTS page

[PMID:20039155-28] 28.0 ^28.1 Pountney, DL et al. (2011) Association of metallothionein-III with oligodendroglial cytoplasmic inclusions in multiple system atrophy. Neurotox Res 19 115-22 PubMed GONUTS page

[PMID:17408955-29] 29.0 ^29.1 ^29.2 ^29.3 Esposito, A et al. (2007) alpha-Synuclein and its disease-related mutants interact differentially with the microtubule protein tau and associate with the actin cytoskeleton. Neurobiol. Dis. 26 521-31 PubMed GONUTS page

[PMID:18980610-30] 30.0 ^30.1 ^30.2 Ben Gedalya, T et al. (2009) Alpha-synuclein and polyunsaturated fatty acids promote clathrin-mediated endocytosis and synaptic vesicle recycling. Traffic 10 218-34 PubMed GONUTS page

[PMID:16176937-31] 31.0 ^31.1 Utton, MA et al. (2005) Molecular motors implicated in the axonal transport of tau and alpha-synuclein. J. Cell. Sci. 118 4645-54 PubMed GONUTS page

[PMID:18346205-32] Gerard, M et al. (2008) FK506 binding protein 12 differentially accelerates fibril formation of wild type alpha-synuclein and its clinical mutants A30P or A53T. J. Neurochem. 106 121-33 PubMed GONUTS page

[PMID:10818098-33] 33.0 ^33.1 ^33.2 da Costa, CA et al. (2000) Wild-type but not Parkinson's disease-related ala-53 --> Thr mutant alpha -synuclein protects neuronal cells from apoptotic stimuli. J. Biol. Chem. 275 24065-9 PubMed GONUTS page

[PMID:11698390-34] Alim, MA et al. (2002) Tubulin seeds alpha-synuclein fibril formation. J. Biol. Chem. 277 2112-7 PubMed GONUTS page

[PMID:16959795-35] 35.0 ^35.1 ^35.2 ^35.3 Kontopoulos, E et al. (2006) Alpha-synuclein acts in the nucleus to inhibit histone acetylation and promote neurotoxicity. Hum. Mol. Genet. 15 3012-23 PubMed GONUTS page

[PMID:19157893-36] 36.0 ^36.1 Dinh, K et al. (2009) Fluorescence microscopy and 3D image reconstruction of cytokine initiated disruption of the Parkinson disease associated proteins alpha-synuclein, tau and ubiquitin in cultured glial cells. Cytokine 45 179-83 PubMed GONUTS page

[PMID:11850416-37] 37.0 ^37.1 ^37.2 ^37.3 ^37.4 ^37.5 Golts, N et al. (2002) Magnesium inhibits spontaneous and iron-induced aggregation of alpha-synuclein. J. Biol. Chem. 277 16116-23 PubMed GONUTS page

[PMID:8248242-38] Uéda, K et al. (1993) Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease. Proc. Natl. Acad. Sci. U.S.A. 90 11282-6 PubMed GONUTS page

[PMID:11312271-39] Nielsen, MS et al. (2001) Ca2+ binding to alpha-synuclein regulates ligand binding and oligomerization. J. Biol. Chem. 276 22680-4 PubMed GONUTS page

[PMID:21319811-40] Dudzik, CG et al. (2011) Coordination features and affinity of the Cu²+ site in the α-synuclein protein of Parkinson's disease. Biochemistry 50 1771-7 PubMed GONUTS page

[PMID:16687662-41] Lücke, C et al. (2006) Interactions between fatty acids and alpha-synuclein. J. Lipid Res. 47 1714-24 PubMed GONUTS page

[PMID:25732184-42] 42.0 ^42.1 Roberts, RF et al. (2015) Direct visualization of alpha-synuclein oligomers reveals previously undetected pathology in Parkinson's disease brain. Brain 138 1642-57 PubMed GONUTS page

[PMID:25643172-43] Galvagnion, C et al. (2015) Lipid vesicles trigger α-synuclein aggregation by stimulating primary nucleation. Nat. Chem. Biol. 11 229-34 PubMed GONUTS page

[PMID:24983211-44] Yin, G et al. (2014) α-Synuclein interacts with the switch region of Rab8a in a Ser129 phosphorylation-dependent manner. Neurobiol. Dis. 70 149-61 PubMed GONUTS page

[PMID:24895406-45] 45.0 ^45.1 Plotegher, N et al. (2014) The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicity. Hum. Mol. Genet. 23 5615-29 PubMed GONUTS page

[PMID:24374342-46] Lorenzen, N et al. (2014) The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes. FEBS Lett. 588 497-502 PubMed GONUTS page

[PMID:23927048-47] Coelho-Cerqueira, E et al. (2013) α-Synuclein as an intrinsically disordered monomer--fact or artefact? FEBS J. 280 4915-27 PubMed GONUTS page

[PMID:22119730-48] Herrera, F & Outeiro, TF (2012) α-Synuclein modifies huntingtin aggregation in living cells. FEBS Lett. 586 7-12 PubMed GONUTS page

[PMID:21443877-49] Caruana, M et al. (2011) Inhibition and disaggregation of α-synuclein oligomers by natural polyphenolic compounds. FEBS Lett. 585 1113-20 PubMed GONUTS page

[PMID:19875982-50] Roodveldt, C et al. (2009) Chaperone proteostasis in Parkinson's disease: stabilization of the Hsp70/alpha-synuclein complex by Hip. EMBO J. 28 3758-70 PubMed GONUTS page

[PMID:19745811-51] Karpinar, DP et al. (2009) Pre-fibrillar alpha-synuclein variants with impaired beta-structure increase neurotoxicity in Parkinson's disease models. EMBO J. 28 3256-68 PubMed GONUTS page

[PMID:18614564-52] McFarland, MA et al. (2008) Proteomics analysis identifies phosphorylation-dependent alpha-synuclein protein interactions. Mol. Cell Proteomics 7 2123-37 PubMed GONUTS page

[PMID:16764865-53] Du, HN et al. (2006) Acceleration of alpha-synuclein aggregation by homologous peptides. FEBS Lett. 580 3657-64 PubMed GONUTS page

[PMID:16330551-54] Lee, CH et al. (2006) Dequalinium-induced protofibril formation of alpha-synuclein. J. Biol. Chem. 281 3463-72 PubMed GONUTS page

[PMID:15502874-55] Shendelman, S et al. (2004) DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-synuclein aggregate formation. PLoS Biol. 2 e362 PubMed GONUTS page

[PMID:27018801-56] Tuttle, MD et al. (2016) Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein. Nat. Struct. Mol. Biol. 23 409-15 PubMed GONUTS page

[PMID:18550842-57] Vilar, M et al. (2008) The fold of alpha-synuclein fibrils. Proc. Natl. Acad. Sci. U.S.A. 105 8637-42 PubMed GONUTS page

[PMID:24252804-58] 58.0 ^58.1 ^58.2 ^58.3 ^58.4 ^58.5 ^58.6 ^58.7 Dias, V et al. (2013) The role of oxidative stress in Parkinson's disease. J Parkinsons Dis 3 461-91 PubMed GONUTS page

[PMID:24477431-59] Murphy, KE et al. (2014) Reduced glucocerebrosidase is associated with increased α-synuclein in sporadic Parkinson's disease. Brain 137 834-48 PubMed GONUTS page

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HUMAN:SYUA

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