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Alpha-synuclein (Non-A beta component of AD amyloid) (Non-A4 component of amyloid precursor) (NACP)

 SYUA_HUMAN              Reviewed;         140 AA.
P37840; A8K2A4; Q13701; Q4JHI3; Q6IAU6;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 1.
25-OCT-2017, entry version 207.
RecName: Full=Alpha-synuclein;
AltName: Full=Non-A beta component of AD amyloid;
AltName: Full=Non-A4 component of amyloid precursor;
Short=NACP;
Name=SNCA; Synonyms=NACP, PARK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 61-95.
TISSUE=Brain;
PubMed=8248242; DOI=10.1073/pnas.90.23.11282;
Ueda K., Fukushima H., Masliah E., Xia Y., Iwai A., Yoshimoto M.,
Otero D.A., Kondo J., Ihara Y., Saitoh T.;
"Molecular cloning of cDNA encoding an unrecognized component of
amyloid in Alzheimer disease.";
Proc. Natl. Acad. Sci. U.S.A. 90:11282-11286(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2-4 AND 2-5).
PubMed=7601450; DOI=10.1016/0888-7543(95)80208-4;
Campion D., Martin C., Heilig R., Charbonnier F., Moreau V.,
Flaman J.-M., Petit J.-L., Hannequin D., Brice A., Frebourg T.;
"The NACP/synuclein gene: chromosomal assignment and screening for
alterations in Alzheimer disease.";
Genomics 26:254-257(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2-4).
TISSUE=Brain;
PubMed=7802671; DOI=10.1006/bbrc.1994.2816;
Ueda K., Saitoh T., Mori H.;
"Tissue-dependent alternative splicing of mRNA for NACP, the precursor
of non-A beta component of Alzheimer's disease amyloid.";
Biochem. Biophys. Res. Commun. 205:1366-1372(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Xia Y., Silva R.D., Chen X.H., Saitoh T.;
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2-4).
PubMed=11156617; DOI=10.1101/gr.165801;
Touchman J.W., Dehejia A., Chiba-Falek O., Cabin D.E., Schwartz J.R.,
Orrison B.M., Polymeropoulos M.H., Nussbaum R.L.;
"Human and mouse alpha-synuclein genes: comparative genomic sequence
analysis and identification of a novel gene regulatory element.";
Genome Res. 11:78-86(2001).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Hu X., Xu Y., Peng X., Yuan J., Qiang B.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
PROTEIN SEQUENCE OF 59-96, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[13]
PHOSPHORYLATION AT SER-87 AND SER-129 BY CK1 AND CK2.
PubMed=10617630; DOI=10.1074/jbc.275.1.390;
Okochi M., Walter J., Koyama A., Nakajo S., Baba M., Iwatsubo T.,
Meijer L., Kahle P.J., Haass C.;
"Constitutive phosphorylation of the Parkinson's disease associated
alpha-synuclein.";
J. Biol. Chem. 275:390-397(2000).
[14]
PHOSPHORYLATION BY G-PROTEIN COUPLED RECEPTOR KINASE.
PubMed=10852916; DOI=10.1074/jbc.M003542200;
Pronin A.N., Morris A.J., Surguchov A., Benovic J.L.;
"Synucleins are a novel class of substrates for G protein-coupled
receptor kinases.";
J. Biol. Chem. 275:26515-26522(2000).
[15]
PHOSPHORYLATION AT TYR-125 BY FYN.
PubMed=11162638; DOI=10.1006/bbrc.2000.4253;
Nakamura T., Yamashita H., Takahashi T., Nakamura S.;
"Activated Fyn phosphorylates alpha-synuclein at tyrosine residue
125.";
Biochem. Biophys. Res. Commun. 280:1085-1092(2001).
[16]
INTERACTION WITH PHOSPHOLIPASE D.
PubMed=11821392; DOI=10.1074/jbc.M110414200;
Ahn B.H., Rhim H., Kim S.Y., Sung Y.M., Lee M.Y., Choi J.Y.,
Wolozin B., Chang J.S., Lee Y.H., Kwon T.K., Chung K.C., Yoon S.H.,
Hahn S.J., Kim M.S., Jo Y.H., Min do S.;
"Alpha-synuclein interacts with phospholipase D isozymes and inhibits
pervanadate-induced phospholipase D activation in human embryonic
kidney-293 cells.";
J. Biol. Chem. 277:12334-12342(2002).
[17]
PHOSPHORYLATION AT SER-129.
PubMed=11813001; DOI=10.1038/ncb748;
Fujiwara H., Hasegawa M., Dohmae N., Kawashima A., Masliah E.,
Goldberg M.S., Shen J., Takio K., Iwatsubo T.;
"alpha-Synuclein is phosphorylated in synucleinopathy lesions.";
Nat. Cell Biol. 4:160-164(2002).
[18]
INTERACTION WITH HISTONES, AND SUBCELLULAR LOCATION.
PubMed=12859192; DOI=10.1021/bi0341152;
Goers J., Manning-Bog A.B., McCormack A.L., Millett I.S., Doniach S.,
Di Monte D.A., Uversky V.N., Fink A.L.;
"Nuclear localization of alpha-synuclein and its interaction with
histones.";
Biochemistry 42:8465-8471(2003).
[19]
ROLE OF THE C-TERMINUS IN FIBRILLOGENESIS.
PubMed=12859200; DOI=10.1021/bi027363r;
Murray I.V., Giasson B.I., Quinn S.M., Koppaka V., Axelsen P.H.,
Ischiropoulos H., Trojanowski J.Q., Lee V.M.;
"Role of alpha-synuclein carboxy-terminus on fibril formation in
vitro.";
Biochemistry 42:8530-8540(2003).
[20]
REVIEW.
PubMed=12558071; DOI=10.2174/1566524033361690;
Alves da Costa C.;
"Recent advances on alpha-synuclein cell biology: functions and
dysfunctions.";
Curr. Mol. Med. 3:17-24(2003).
[21]
MUTAGENESIS OF TYR-39; TYR-125; TYR-133 AND TYR-136, CHARACTERIZATION
OF VARIANT THR-53, AND PHOSPHORYLATION AT TYR-125.
PubMed=12893833; DOI=10.1074/jbc.M213217200;
Takahashi T., Yamashita H., Nagano Y., Nakamura T., Ohmori H.,
Avraham H., Avraham S., Yasuda M., Matsumoto M.;
"Identification and characterization of a novel Pyk2/related adhesion
focal tyrosine kinase-associated protein that inhibits alpha-synuclein
phosphorylation.";
J. Biol. Chem. 278:42225-42233(2003).
[22]
SUBCELLULAR LOCATION.
PubMed=15282274; DOI=10.1523/JNEUROSCI.1594-04.2004;
Fortin D.L., Troyer M.D., Nakamura K., Kubo S., Anthony M.D.,
Edwards R.H.;
"Lipid rafts mediate the synaptic localization of alpha-synuclein.";
J. Neurosci. 24:6715-6723(2004).
[23]
FIBRILS FORMATION, DOMAIN NAC, AND MUTAGENESIS OF 67-GLY--VAL-71;
71-VAL--VAL-82; 76-ALA-VAL-77; VAL-77; ALA-78 AND 85-ALA--PHE-94.
PubMed=19722699; DOI=10.1021/bi900539p;
Waxman E.A., Mazzulli J.R., Giasson B.I.;
"Characterization of hydrophobic residue requirements for alpha-
synuclein fibrillization.";
Biochemistry 48:9427-9436(2009).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
COPPER-BINDING, AND MUTAGENESIS OF ASP-2 AND HIS-50.
PubMed=21319811; DOI=10.1021/bi101912q;
Dudzik C.G., Walter E.D., Millhauser G.L.;
"Coordination features and affinity of the Cu(2)+ site in the alpha-
synuclein protein of Parkinson's disease.";
Biochemistry 50:1771-1777(2011).
[26]
ACETYLATION AT MET-1.
PubMed=22407793; DOI=10.1002/pro.2056;
Trexler A.J., Rhoades E.;
"N-Terminal acetylation is critical for forming alpha-helical oligomer
of alpha-synuclein.";
Protein Sci. 21:601-605(2012).
[27]
STRUCTURE BY NMR IN COMPLEX WITH DETERGENT MICELLES.
PubMed=15615727; DOI=10.1074/jbc.M411805200;
Ulmer T.S., Bax A., Cole N.B., Nussbaum R.L.;
"Structure and dynamics of micelle-bound human alpha-synuclein.";
J. Biol. Chem. 280:9595-9603(2005).
[28]
VARIANT PARK1 THR-53.
PubMed=9197268; DOI=10.1126/science.276.5321.2045;
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.;
"Mutation in the alpha-synuclein gene identified in families with
Parkinson's disease.";
Science 276:2045-2047(1997).
[29]
VARIANT PARK1 PRO-30.
PubMed=9462735; DOI=10.1038/ng0298-106;
Krueger R., Kuhn W., Mueller T., Woitalla D., Graeber M., Koesel S.,
Przuntek H., Epplen J.T., Schoels L., Riess O.;
"Ala30Pro mutation in the gene encoding alpha-synuclein in Parkinson's
disease.";
Nat. Genet. 18:106-108(1998).
[30]
VARIANT PARK1/DLB LYS-46.
PubMed=14755719; DOI=10.1002/ana.10795;
Zarranz J.J., Alegre J., Gomez-Esteban J.C., Lezcano E., Ros R.,
Ampuero I., Vidal L., Hoenicka J., Rodriguez O., Atares B.,
Llorens V., Gomez Tortosa E., del Ser T., Munoz D.G., de Yebenes J.G.;
"The new mutation, E46K, of alpha-synuclein causes Parkinson and Lewy
body dementia.";
Ann. Neurol. 55:164-173(2004).
[31]
CHARACTERIZATION OF VARIANT LYS-46.
PubMed=15498564; DOI=10.1016/j.febslet.2004.09.038;
Choi W., Zibaee S., Jakes R., Serpell L.C., Davletov B.,
Crowther R.A., Goedert M.;
"Mutation E46K increases phospholipid binding and assembly into
filaments of human alpha-synuclein.";
FEBS Lett. 576:363-368(2004).
[32]
VARIANT PARK1 GLN-50.
PubMed=23457019; DOI=10.1002/mds.25421;
Appel-Cresswell S., Vilarino-Guell C., Encarnacion M., Sherman H.,
Yu I., Shah B., Weir D., Thompson C., Szu-Tu C., Trinh J., Aasly J.O.,
Rajput A., Rajput A.H., Jon Stoessl A., Farrer M.J.;
"Alpha-synuclein p.H50Q, a novel pathogenic mutation for Parkinson's
disease.";
Mov. Disord. 28:811-813(2013).
[33]
VARIANT PARK1 GLN-50, AND CHARACTERIZATION OF VARIANT PARK1 GLN-50.
PubMed=23427326; DOI=10.1212/WNL.0b013e31828727ba;
Proukakis C., Dudzik C.G., Brier T., MacKay D.S., Cooper J.M.,
Millhauser G.L., Houlden H., Schapira A.H.;
"A novel alpha-synuclein missense mutation in Parkinson disease.";
Neurology 80:1062-1064(2013).
[34]
CHARACTERIZATION OF VARIANT PARK1 GLN-50, SUBCELLULAR LOCATION,
SUBUNIT, AND PHOSPHORYLATION AT SER-129.
PubMed=24936070; DOI=10.1074/jbc.M114.553297;
Khalaf O., Fauvet B., Oueslati A., Dikiy I., Mahul-Mellier A.L.,
Ruggeri F.S., Mbefo M.K., Vercruysse F., Dietler G., Lee S.J.,
Eliezer D., Lashuel H.A.;
"The H50Q mutation enhances alpha-synuclein aggregation, secretion,
and toxicity.";
J. Biol. Chem. 289:21856-21876(2014).
[35]
CHARACTERIZATION OF VARIANTS PARK1 PRO-30; LYS-46; GLN-50 AND THR-53,
MUTAGENESIS OF GLU-35 AND GLU-57, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=25561023; DOI=10.1021/cn500332w;
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.;
"Molecular determinants of alpha-synuclein mutants' oligomerization
and membrane interactions.";
ACS Chem. Neurosci. 6:403-416(2015).
-!- FUNCTION: May be involved in the regulation of dopamine release
and transport. Induces fibrillization of microtubule-associated
protein tau. Reduces neuronal responsiveness to various apoptotic
stimuli, leading to a decreased caspase-3 activation.
-!- SUBUNIT: Soluble monomer which can form filamentous aggregates.
Interacts with UCHL1 (By similarity). Interacts with phospholipase
D and histones. {ECO:0000250, ECO:0000269|PubMed:11821392,
ECO:0000269|PubMed:12859192, ECO:0000269|PubMed:15615727,
ECO:0000269|PubMed:24936070, ECO:0000269|PubMed:25561023}.
-!- INTERACTION:
Self; NbExp=35; IntAct=EBI-985879, EBI-985879;
P00519-1:ABL1; NbExp=6; IntAct=EBI-985879, EBI-5278159;
P00519-2:ABL1; NbExp=5; IntAct=EBI-985879, EBI-9254597;
P49841:GSK3B; NbExp=2; IntAct=EBI-985879, EBI-373586;
P08107:HSPA1B; NbExp=7; IntAct=EBI-985879, EBI-629985;
P42858:HTT; NbExp=4; IntAct=EBI-985879, EBI-466029;
Q5S007:LRRK2; NbExp=6; IntAct=EBI-985879, EBI-5323863;
P10636-8:MAPT; NbExp=3; IntAct=EBI-985879, EBI-366233;
P00414:MT-CO3; NbExp=3; IntAct=EBI-985879, EBI-3932264;
Q9UI14:RABAC1; NbExp=4; IntAct=EBI-985879, EBI-712367;
Q01959:SLC6A3; NbExp=3; IntAct=EBI-985879, EBI-6661445;
Q61327:Slc6a3 (xeno); NbExp=5; IntAct=EBI-985879, EBI-7839708;
Q9Y6H5:SNCAIP; NbExp=22; IntAct=EBI-985879, EBI-717182;
Q9Y6H5-2:SNCAIP; NbExp=2; IntAct=EBI-985879, EBI-15577909;
P17600:SYN1; NbExp=2; IntAct=EBI-985879, EBI-717274;
Q04917:YWHAH; NbExp=9; IntAct=EBI-9684465, EBI-306940;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:24936070, ECO:0000269|PubMed:25561023}.
Membrane {ECO:0000269|PubMed:24936070}. Nucleus
{ECO:0000269|PubMed:12859192, ECO:0000269|PubMed:24936070}. Cell
junction, synapse {ECO:0000269|PubMed:15282274}. Secreted
{ECO:0000269|PubMed:24936070}. Note=Membrane-bound in dopaminergic
neurons. {ECO:0000269|PubMed:15282274}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=NACP140;
IsoId=P37840-1; Sequence=Displayed;
Name=2-4; Synonyms=NACP112;
IsoId=P37840-2; Sequence=VSP_006364;
Name=2-5;
IsoId=P37840-3; Sequence=VSP_006363;
-!- TISSUE SPECIFICITY: Expressed principally in brain but is also
expressed in low concentrations in all tissues examined except in
liver. Concentrated in presynaptic nerve terminals.
-!- DOMAIN: The 'non A-beta component of Alzheimer disease amyloid
plaque' domain (NAC domain) is involved in fibrils formation. The
middle hydrophobic region forms the core of the filaments. The C-
terminus may regulate aggregation and determine the diameter of
the filaments. {ECO:0000269|PubMed:19722699}.
-!- PTM: 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. {ECO:0000269|PubMed:10617630,
ECO:0000269|PubMed:10852916, ECO:0000269|PubMed:11162638,
ECO:0000269|PubMed:11813001, ECO:0000269|PubMed:12893833,
ECO:0000269|PubMed:24936070}.
-!- PTM: 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.
-!- PTM: Ubiquitinated. The predominant conjugate is the
diubiquitinated form (By similarity). {ECO:0000250}.
-!- PTM: Acetylation at Met-1 seems to be important for proper folding
and native oligomeric structure. {ECO:0000269|PubMed:22407793}.
-!- DISEASE: Note=Genetic alterations of SNCA resulting in aberrant
polymerization into fibrils, are associated with several
neurodegenerative diseases (synucleinopathies). SNCA fibrillar
aggregates represent the major non A-beta component of Alzheimer
disease amyloid plaque, and a major component of Lewy body
inclusions. They are also found within Lewy body (LB)-like
intraneuronal inclusions, glial inclusions and axonal spheroids in
neurodegeneration with brain iron accumulation type 1.
-!- DISEASE: Parkinson disease 1, autosomal dominant (PARK1)
[MIM:168601]: A complex neurodegenerative disorder characterized
by bradykinesia, resting tremor, muscular rigidity and postural
instability. Additional features are characteristic postural
abnormalities, dysautonomia, dystonic cramps, and dementia. The
pathology of Parkinson disease involves the loss of dopaminergic
neurons in the substantia nigra and the presence of Lewy bodies
(intraneuronal accumulations of aggregated proteins), in surviving
neurons in various areas of the brain. The disease is progressive
and usually manifests after the age of 50 years, although early-
onset cases (before 50 years) are known. The majority of the cases
are sporadic suggesting a multifactorial etiology based on
environmental and genetic factors. However, some patients present
with a positive family history for the disease. Familial forms of
the disease usually begin at earlier ages and are associated with
atypical clinical features. {ECO:0000269|PubMed:14755719,
ECO:0000269|PubMed:23427326, ECO:0000269|PubMed:23457019,
ECO:0000269|PubMed:24936070, ECO:0000269|PubMed:25561023,
ECO:0000269|PubMed:9197268, ECO:0000269|PubMed:9462735}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Parkinson disease 4, autosomal dominant (PARK4)
[MIM:605543]: A complex neurodegenerative disorder with
manifestations ranging from typical Parkinson disease to dementia
with Lewy bodies. Clinical features include parkinsonian symptoms
(resting tremor, rigidity, postural instability and bradykinesia),
dementia, diffuse Lewy body pathology, autonomic dysfunction,
hallucinations and paranoia. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Dementia Lewy body (DLB) [MIM:127750]: A
neurodegenerative disorder characterized by mental impairment
leading to dementia, parkinsonism, fluctuating cognitive function,
visual hallucinations, falls, syncopal episodes, and sensitivity
to neuroleptic medication. Brainstem or cortical intraneuronal
accumulations of aggregated proteins (Lewy bodies) are the only
essential pathologic features. Patients may also have hippocampal
and neocortical senile plaques, sometimes in sufficient number to
fulfill the diagnostic criteria for Alzheimer disease.
{ECO:0000269|PubMed:14755719}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the synuclein family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/snca/";
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EMBL; L08850; AAA16117.1; -; mRNA.
EMBL; L36674; AAA98493.1; -; mRNA.
EMBL; L36675; AAA98487.1; -; mRNA.
EMBL; D31839; BAA06625.1; -; mRNA.
EMBL; U46901; AAC02114.1; -; Genomic_DNA.
EMBL; U46897; AAC02114.1; JOINED; Genomic_DNA.
EMBL; U46898; AAC02114.1; JOINED; Genomic_DNA.
EMBL; U46899; AAC02114.1; JOINED; Genomic_DNA.
EMBL; AF163864; AAG30302.1; -; Genomic_DNA.
EMBL; AF163864; AAG30303.1; -; Genomic_DNA.
EMBL; AY049786; AAL15443.1; -; mRNA.
EMBL; AK290169; BAF82858.1; -; mRNA.
EMBL; CR457058; CAG33339.1; -; mRNA.
EMBL; DQ088379; AAY88735.1; -; Genomic_DNA.
EMBL; CH471057; EAX06036.1; -; Genomic_DNA.
EMBL; BC013293; AAH13293.1; -; mRNA.
EMBL; BC108275; AAI08276.1; -; mRNA.
CCDS; CCDS3634.1; -. [P37840-1]
CCDS; CCDS43252.1; -. [P37840-2]
PIR; A49669; A49669.
PIR; S56746; S56746.
RefSeq; NP_000336.1; NM_000345.3. [P37840-1]
RefSeq; NP_001139526.1; NM_001146054.1. [P37840-1]
RefSeq; NP_001139527.1; NM_001146055.1. [P37840-1]
RefSeq; NP_009292.1; NM_007308.2. [P37840-2]
RefSeq; XP_011530510.1; XM_011532208.2. [P37840-1]
RefSeq; XP_016864051.1; XM_017008562.1. [P37840-1]
RefSeq; XP_016864052.1; XM_017008563.1. [P37840-1]
UniGene; Hs.21374; -.
PDB; 1XQ8; NMR; -; A=1-140.
PDB; 2JN5; NMR; -; A=1-12.
PDB; 2KKW; NMR; -; A=1-140.
PDB; 2M55; NMR; -; B=1-19.
PDB; 2N0A; NMR; -; A/B/C/D/E/F/G/H/I/J=1-140.
PDB; 2X6M; X-ray; 1.62 A; B=132-140.
PDB; 3Q25; X-ray; 1.90 A; A=1-19.
PDB; 3Q26; X-ray; 1.54 A; A=10-42.
PDB; 3Q27; X-ray; 1.30 A; A=32-57.
PDB; 3Q28; X-ray; 1.60 A; A=58-79.
PDB; 3Q29; X-ray; 2.30 A; A/C=1-19.
PDB; 4BXL; NMR; -; C=35-56.
PDB; 4R0U; X-ray; 1.38 A; A=72-78.
PDB; 4R0W; X-ray; 1.50 A; A=70-76.
PDB; 4RIK; X-ray; 1.85 A; A=69-77.
PDB; 4RIL; EM; 1.43 A; A=68-78.
PDB; 4ZNN; EM; 1.41 A; A=47-56.
PDB; 5CRW; X-ray; 1.60 A; B=31-41.
PDBsum; 1XQ8; -.
PDBsum; 2JN5; -.
PDBsum; 2KKW; -.
PDBsum; 2M55; -.
PDBsum; 2N0A; -.
PDBsum; 2X6M; -.
PDBsum; 3Q25; -.
PDBsum; 3Q26; -.
PDBsum; 3Q27; -.
PDBsum; 3Q28; -.
PDBsum; 3Q29; -.
PDBsum; 4BXL; -.
PDBsum; 4R0U; -.
PDBsum; 4R0W; -.
PDBsum; 4RIK; -.
PDBsum; 4RIL; -.
PDBsum; 4ZNN; -.
PDBsum; 5CRW; -.
DisProt; DP00070; -.
ProteinModelPortal; P37840; -.
SMR; P37840; -.
BioGrid; 112506; 470.
CORUM; P37840; -.
DIP; DIP-35354N; -.
IntAct; P37840; 262.
MINT; MINT-2515483; -.
STRING; 9606.ENSP00000338345; -.
BindingDB; P37840; -.
ChEMBL; CHEMBL6152; -.
TCDB; 1.C.77.1.1; the synuclein (synuclein) family.
iPTMnet; P37840; -.
PhosphoSitePlus; P37840; -.
BioMuta; SNCA; -.
DMDM; 586067; -.
EPD; P37840; -.
MaxQB; P37840; -.
PaxDb; P37840; -.
PeptideAtlas; P37840; -.
PRIDE; P37840; -.
TopDownProteomics; P37840-1; -. [P37840-1]
DNASU; 6622; -.
Ensembl; ENST00000336904; ENSP00000338345; ENSG00000145335. [P37840-1]
Ensembl; ENST00000345009; ENSP00000343683; ENSG00000145335. [P37840-2]
Ensembl; ENST00000394986; ENSP00000378437; ENSG00000145335. [P37840-1]
Ensembl; ENST00000394989; ENSP00000378440; ENSG00000145335. [P37840-3]
Ensembl; ENST00000394991; ENSP00000378442; ENSG00000145335. [P37840-1]
Ensembl; ENST00000420646; ENSP00000396241; ENSG00000145335. [P37840-2]
Ensembl; ENST00000505199; ENSP00000421485; ENSG00000145335. [P37840-3]
Ensembl; ENST00000506244; ENSP00000422238; ENSG00000145335. [P37840-1]
Ensembl; ENST00000508895; ENSP00000426955; ENSG00000145335. [P37840-1]
Ensembl; ENST00000618500; ENSP00000484044; ENSG00000145335. [P37840-3]
GeneID; 6622; -.
KEGG; hsa:6622; -.
UCSC; uc003hso.3; human. [P37840-1]
CTD; 6622; -.
DisGeNET; 6622; -.
EuPathDB; HostDB:ENSG00000145335.15; -.
GeneCards; SNCA; -.
GeneReviews; SNCA; -.
HGNC; HGNC:11138; SNCA.
HPA; CAB010877; -.
HPA; HPA005459; -.
MalaCards; SNCA; -.
MIM; 127750; phenotype.
MIM; 163890; gene.
MIM; 168600; phenotype.
MIM; 168601; phenotype.
MIM; 605543; phenotype.
neXtProt; NX_P37840; -.
OpenTargets; ENSG00000145335; -.
Orphanet; 1648; Dementia with Lewy body.
Orphanet; 171695; Parkinsonian-pyramidal syndrome.
Orphanet; 2828; Young adult-onset Parkinsonism.
PharmGKB; PA35986; -.
eggNOG; ENOG410IWI2; Eukaryota.
eggNOG; ENOG4111TDZ; LUCA.
GeneTree; ENSGT00390000016161; -.
HOGENOM; HOG000008691; -.
HOVERGEN; HBG000481; -.
InParanoid; P37840; -.
KO; K04528; -.
OMA; SEAYEMP; -.
OrthoDB; EOG091G11PA; -.
PhylomeDB; P37840; -.
TreeFam; TF332776; -.
Reactome; R-HSA-977225; Amyloid fiber formation.
SignaLink; P37840; -.
SIGNOR; P37840; -.
ChiTaRS; SNCA; human.
EvolutionaryTrace; P37840; -.
GeneWiki; Alpha-synuclein; -.
GenomeRNAi; 6622; -.
PMAP-CutDB; P37840; -.
PRO; PR:P37840; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000145335; -.
CleanEx; HS_SNCA; -.
ExpressionAtlas; P37840; baseline and differential.
Genevisible; P37840; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:ParkinsonsUK-UCL.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0030426; C:growth cone; IDA:UniProtKB.
GO; GO:0016234; C:inclusion body; IDA:UniProtKB.
GO; GO:0005764; C:lysosome; TAS:ParkinsonsUK-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; TAS:ParkinsonsUK-UCL.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005640; C:nuclear outer membrane; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0098794; C:postsynapse; IEA:GOC.
GO; GO:0005840; C:ribosome; IEA:Ensembl.
GO; GO:0005791; C:rough endoplasmic reticulum; IEA:Ensembl.
GO; GO:0099512; C:supramolecular fiber; IDA:UniProtKB.
GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
GO; GO:0043014; F:alpha-tubulin binding; IPI:UniProtKB.
GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO; GO:1903136; F:cuprous ion binding; IMP:CAFA.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0070840; F:dynein complex binding; IPI:UniProtKB.
GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0019894; F:kinesin binding; IPI:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
GO; GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
GO; GO:0043274; F:phospholipase binding; IEA:Ensembl.
GO; GO:0005543; F:phospholipid binding; IDA:ParkinsonsUK-UCL.
GO; GO:0051219; F:phosphoprotein binding; IDA:BHF-UCL.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0048156; F:tau protein binding; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; TAS:ParkinsonsUK-UCL.
GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL.
GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0071280; P:cellular response to copper ion; IDA:UniProtKB.
GO; GO:0071872; P:cellular response to epinephrine stimulus; TAS:UniProtKB.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; IC:ParkinsonsUK-UCL.
GO; GO:0042416; P:dopamine biosynthetic process; TAS:UniProtKB.
GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; TAS:UniProtKB.
GO; GO:0060079; P:excitatory postsynaptic potential; IEA:Ensembl.
GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl.
GO; GO:0060291; P:long-term synaptic potentiation; IEA:Ensembl.
GO; GO:0001774; P:microglial cell activation; TAS:ParkinsonsUK-UCL.
GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IEA:Ensembl.
GO; GO:0007006; P:mitochondrial membrane organization; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:1904715; P:negative regulation of chaperone-mediated autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0045963; P:negative regulation of dopamine metabolic process; IEA:Ensembl.
GO; GO:0051585; P:negative regulation of dopamine uptake involved in synaptic transmission; IDA:UniProtKB.
GO; GO:0045920; P:negative regulation of exocytosis; IMP:UniProtKB.
GO; GO:0035067; P:negative regulation of histone acetylation; IDA:UniProtKB.
GO; GO:0031115; P:negative regulation of microtubule polymerization; IDA:BHF-UCL.
GO; GO:1902957; P:negative regulation of mitochondrial electron transport, NADH to ubiquinone; TAS:ParkinsonsUK-UCL.
GO; GO:0032769; P:negative regulation of monooxygenase activity; IDA:BHF-UCL.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:1901215; P:negative regulation of neuron death; IDA:ParkinsonsUK-UCL.
GO; GO:0051622; P:negative regulation of norepinephrine uptake; IDA:UniProtKB.
GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0051612; P:negative regulation of serotonin uptake; IDA:UniProtKB.
GO; GO:0070495; P:negative regulation of thrombin-activated receptor signaling pathway; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ParkinsonsUK-UCL.
GO; GO:0032410; P:negative regulation of transporter activity; IDA:UniProtKB.
GO; GO:0006638; P:neutral lipid metabolic process; IEA:Ensembl.
GO; GO:0055114; P:oxidation-reduction process; IDA:UniProtKB.
GO; GO:0006644; P:phospholipid metabolic process; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:ParkinsonsUK-UCL.
GO; GO:0045807; P:positive regulation of endocytosis; IDA:UniProtKB.
GO; GO:1903284; P:positive regulation of glutathione peroxidase activity; IDA:ParkinsonsUK-UCL.
GO; GO:1903285; P:positive regulation of hydrogen peroxide catabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IDA:ParkinsonsUK-UCL.
GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; IDA:UniProtKB.
GO; GO:1901216; P:positive regulation of neuron death; IDA:ParkinsonsUK-UCL.
GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:BHF-UCL.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:BHF-UCL.
GO; GO:0001921; P:positive regulation of receptor recycling; IDA:UniProtKB.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:UniProtKB.
GO; GO:0031648; P:protein destabilization; IDA:UniProtKB.
GO; GO:0031623; P:receptor internalization; IDA:UniProtKB.
GO; GO:0050812; P:regulation of acyl-CoA biosynthetic process; IEA:Ensembl.
GO; GO:0014059; P:regulation of dopamine secretion; TAS:UniProtKB.
GO; GO:0014048; P:regulation of glutamate secretion; IEA:Ensembl.
GO; GO:0040012; P:regulation of locomotion; IEA:Ensembl.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IEA:Ensembl.
GO; GO:0043030; P:regulation of macrophage activation; IEA:Ensembl.
GO; GO:0010517; P:regulation of phospholipase activity; IDA:UniProtKB.
GO; GO:1905606; P:regulation of presynapse assembly; IGI:ParkinsonsUK-UCL.
GO; GO:1903426; P:regulation of reactive oxygen species biosynthetic process; TAS:ParkinsonsUK-UCL.
GO; GO:1903421; P:regulation of synaptic vesicle recycling; TAS:ParkinsonsUK-UCL.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0034341; P:response to interferon-gamma; IDA:UniProtKB.
GO; GO:0070555; P:response to interleukin-1; IDA:UniProtKB.
GO; GO:0010040; P:response to iron(II) ion; IDA:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0032026; P:response to magnesium ion; IDA:UniProtKB.
GO; GO:0097435; P:supramolecular fiber organization; TAS:UniProtKB.
GO; GO:0050808; P:synapse organization; IEA:Ensembl.
GO; GO:0048488; P:synaptic vesicle endocytosis; ISS:UniProtKB.
InterPro; IPR001058; Synuclein.
InterPro; IPR002460; Synuclein_alpha.
PANTHER; PTHR13820; PTHR13820; 1.
PANTHER; PTHR13820:SF5; PTHR13820:SF5; 1.
Pfam; PF01387; Synuclein; 1.
PRINTS; PR01212; ASYNUCLEIN.
PRINTS; PR01211; SYNUCLEIN.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Alzheimer disease;
Amyloid; Cell junction; Complete proteome; Copper; Cytoplasm;
Direct protein sequencing; Disease mutation; Membrane; Metal-binding;
Neurodegeneration; Nucleus; Parkinson disease; Parkinsonism;
Phosphoprotein; Reference proteome; Repeat; Secreted; Synapse;
Ubl conjugation.
CHAIN 1 140 Alpha-synuclein.
/FTId=PRO_0000184022.
REPEAT 20 30 1.
REPEAT 31 41 2.
REPEAT 42 56 3; approximate.
REPEAT 57 67 4.
REGION 20 67 4 X 11 AA tandem repeats of [EGS]-K-T-K-
[EQ]-[GQ]-V-X(4).
METAL 2 2 Copper. {ECO:0000305}.
METAL 50 50 Copper. {ECO:0000305}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:22407793}.
MOD_RES 87 87 Phosphoserine.
{ECO:0000269|PubMed:10617630}.
MOD_RES 125 125 Phosphotyrosine; by FYN.
{ECO:0000269|PubMed:11162638,
ECO:0000269|PubMed:12893833}.
MOD_RES 129 129 Phosphoserine; by BARK1, PLK2, CK2, CK1
and GRK5. {ECO:0000269|PubMed:10617630,
ECO:0000269|PubMed:11813001,
ECO:0000269|PubMed:24936070}.
VAR_SEQ 41 54 Missing (in isoform 2-5).
{ECO:0000303|PubMed:7601450}.
/FTId=VSP_006363.
VAR_SEQ 103 130 Missing (in isoform 2-4).
{ECO:0000303|PubMed:7601450,
ECO:0000303|PubMed:7802671}.
/FTId=VSP_006364.
VARIANT 30 30 A -> P (in PARK1; no effect on
oligomerization; dbSNP:rs104893878).
{ECO:0000269|PubMed:25561023,
ECO:0000269|PubMed:9462735}.
/FTId=VAR_007957.
VARIANT 46 46 E -> K (in PARK1 and DLB; significant
increase in binding to negatively charged
phospholipid liposomes; increases
oligomerization; dbSNP:rs104893875).
{ECO:0000269|PubMed:14755719,
ECO:0000269|PubMed:15498564,
ECO:0000269|PubMed:25561023}.
/FTId=VAR_022703.
VARIANT 50 50 H -> Q (in PARK1; no effect on protein
structure; no effect on phosphorylation
of the protein; no effect on
membrane- and lipid-binding; increases
oligomerization; increases fibril
formation; increases secretion of the
protein; impairs copper-binding;
dbSNP:rs201106962).
{ECO:0000269|PubMed:23427326,
ECO:0000269|PubMed:23457019,
ECO:0000269|PubMed:24936070,
ECO:0000269|PubMed:25561023}.
/FTId=VAR_070171.
VARIANT 53 53 A -> T (in PARK1; no effect on osmotic
stress-induced phosphorylation; increases
oligomerization; dbSNP:rs104893877).
{ECO:0000269|PubMed:12893833,
ECO:0000269|PubMed:25561023,
ECO:0000269|PubMed:9197268}.
/FTId=VAR_007454.
MUTAGEN 2 2 D->A: Impairs copper-binding.
{ECO:0000269|PubMed:21319811}.
MUTAGEN 35 35 E->K: No effect on oligomerization.
{ECO:0000269|PubMed:25561023}.
MUTAGEN 39 39 Y->F: No effect on osmotic stress-induced
phosphorylation.
{ECO:0000269|PubMed:12893833}.
MUTAGEN 50 50 H->A: Impairs copper-binding.
{ECO:0000269|PubMed:21319811}.
MUTAGEN 57 57 E->K: Increases oligomerization.
{ECO:0000269|PubMed:25561023}.
MUTAGEN 67 71 Missing: Reduces polymerization into
amyloid fibrils.
{ECO:0000269|PubMed:19722699}.
MUTAGEN 71 82 Missing: Impairs polymerization into
amyloid fibrils.
{ECO:0000269|PubMed:19722699}.
MUTAGEN 76 77 Missing: Impairs polymerization into
amyloid fibrils.
{ECO:0000269|PubMed:19722699}.
MUTAGEN 76 76 Missing: Does not affect polymerization
into amyloid fibrils.
MUTAGEN 77 77 Missing: Does not affect polymerization
into amyloid fibrils.
{ECO:0000269|PubMed:19722699}.
MUTAGEN 78 78 Missing: Does not affect polymerization
into amyloid fibrils.
{ECO:0000269|PubMed:19722699}.
MUTAGEN 85 94 Missing: Reduces polymerization into
amyloid fibrils.
{ECO:0000269|PubMed:19722699}.
MUTAGEN 125 125 Y->F: Abolishes osmotic stress-induced
phosphorylation.
{ECO:0000269|PubMed:12893833}.
MUTAGEN 133 133 Y->F: No effect on osmotic stress-induced
phosphorylation.
{ECO:0000269|PubMed:12893833}.
MUTAGEN 136 136 Y->F: No effect on osmotic stress-induced
phosphorylation.
{ECO:0000269|PubMed:12893833}.
HELIX 3 11 {ECO:0000244|PDB:3Q25}.
HELIX 17 19 {ECO:0000244|PDB:2N0A}.
HELIX 21 32 {ECO:0000244|PDB:3Q26}.
HELIX 41 44 {ECO:0000244|PDB:3Q27}.
STRAND 45 47 {ECO:0000244|PDB:4BXL}.
HELIX 52 55 {ECO:0000244|PDB:3Q27}.
HELIX 66 68 {ECO:0000244|PDB:3Q28}.
STRAND 70 78 {ECO:0000244|PDB:2N0A}.
STRAND 80 83 {ECO:0000244|PDB:2N0A}.
STRAND 88 98 {ECO:0000244|PDB:2N0A}.
STRAND 110 113 {ECO:0000244|PDB:1XQ8}.
TURN 120 122 {ECO:0000244|PDB:1XQ8}.
TURN 124 126 {ECO:0000244|PDB:1XQ8}.
TURN 133 136 {ECO:0000244|PDB:2N0A}.
SEQUENCE 140 AA; 14460 MW; 6BB2F12128931663 CRC64;
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK
EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP
DNEAYEMPSE EGYQDYEPEA


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10-002-38060 alpha-Synuclein A30P human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38062 alpha-Synuclein 112 human - NACP112; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38067 alpha-Synuclein E46K human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38059 alpha-Synuclein A53T human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38061 alpha-Synuclein A30P_A53T human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38068 alpha-Synuclein 1-95 (Syn 1-95) human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38065 alpha-Synuclein (tri-NAC) human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-663-45667 alpha-Synuclein Human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 0.1 mg
10-002-38064 alpha-Synuclein 96-140 (Syn 96-140) human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-663-45667 alpha-Synuclein Human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 0.02 mg
10-002-38063 alpha-Synuclein 61-140 (Syn 61-140) human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-663-45667 alpha-Synuclein Human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38066 alpha-Synuclein 1-60 (Syn 1-60) human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
20-002-35023 alpha-Synuclein (anti-alpha-Synuclein. 61-95 aa. clone 5C2) - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP Monoclonal 0.1 ml
20-272-192257 alpha Synuclein - Mouse monoclonal [4B12] to alpha Synuclein; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP Monoclonal 0.1 ml
18-272-196445 alpha Synuclein - Rabbit polyclonal to alpha Synuclein; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP Polyclonal 0.5 ml
20-272-192256 alpha Synuclein - Mouse monoclonal [4D6] to alpha Synuclein; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP Monoclonal 0.1 ml
18-272-196446 alpha Synuclein prediluted - Rabbit polyclonal to alpha Synuclein prediluted; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP Polyclonal 7 ml


 

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