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

 SYUA_MOUSE              Reviewed;         140 AA.
O55042; Q3U130; Q9CXF8; Q9EQC3; Q9QUR3;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 2.
30-AUG-2017, entry version 151.
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=Syn;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9648883;
Hsu L.J., Mallory M., Xia Y., Veinbergs I., Hashimoto M.,
Yoshimoto M., Thal L.J., Saitoh T., Masliah E.;
"Expression pattern of synucleins (non-Abeta component of Alzheimer's
disease amyloid precursor protein/alpha-synuclein) during murine brain
development.";
J. Neurochem. 71:338-344(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=ICR;
PubMed=9601701; DOI=10.1097/00001756-199804200-00051;
Hong L., Ko H.W., Gwag B.J., Joe E., Lee S., Kim Y.T., Suh Y.-H.;
"The cDNA cloning and ontogeny of mouse alpha-synuclein.";
NeuroReport 9:1239-1243(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and Sv129/Ola; TISSUE=Brain;
Fog J.U., Kallunki P.;
"Genomic cloning of the mouse alpha-synuclein and analysis of the
promoter.";
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J, and NOD; TISSUE=Liver, and Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-54.
STRAIN=129/SvJ;
PubMed=12732244; DOI=10.1016/S0306-4522(03)00036-8;
Schlueter O.M., Fornai F., Alessandri M.G., Takamori S., Geppert M.,
Jahn R., Suedhof T.C.;
"Role of alpha-synuclein in 1-methyl-4-phenyl-1,2,3,6-
tetrahydropyridine-induced parkinsonism in mice.";
Neuroscience 118:985-1002(2003).
[8]
PROTEIN SEQUENCE OF 61-96, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
[9]
PHOSPHORYLATION AT SER-129.
PubMed=19004816; DOI=10.1074/jbc.C800206200;
Inglis K.J., Chereau D., Brigham E.F., Chiou S.S., Schobel S.,
Frigon N.L., Yu M., Caccavello R.J., Nelson S., Motter R., Wright S.,
Chian D., Santiago P., Soriano F., Ramos C., Powell K.,
Goldstein J.M., Babcock M., Yednock T., Bard F., Basi G.S., Sham H.,
Chilcote T.J., McConlogue L., Griswold-Prenner I., Anderson J.P.;
"Polo-like kinase 2 (PLK2) phosphorylates alpha-synuclein at serine
129 in central nervous system.";
J. Biol. Chem. 284:2598-2602(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: May be involved in the regulation of dopamine release
and transport.
-!- SUBUNIT: Interacts with UCHL1. {ECO:0000250}.
-!- INTERACTION:
P55258:Rab8a; NbExp=2; IntAct=EBI-2310271, EBI-398411;
Q61327:Slc6a3; NbExp=5; IntAct=EBI-2310271, EBI-7839708;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000250|UniProtKB:P37840}. Membrane
{ECO:0000250|UniProtKB:P37840}. Nucleus
{ECO:0000250|UniProtKB:P37840}. Cell junction, synapse
{ECO:0000250|UniProtKB:P37840}. Secreted
{ECO:0000250|UniProtKB:P37840}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O55042-1; Sequence=Displayed;
Name=2;
IsoId=O55042-2; Sequence=VSP_025018, VSP_025019;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylated, predominantly on serine residues.
Phosphorylated on Tyr-125 upon osmotic stress (By similarity).
{ECO:0000250}.
-!- 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:0000250}.
-!- SIMILARITY: Belongs to the synuclein family. {ECO:0000305}.
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EMBL; AF044672; AAC00521.1; -; mRNA.
EMBL; AF033261; AAD11254.1; -; mRNA.
EMBL; AF179273; AAD56908.1; -; mRNA.
EMBL; AF179272; AAD56907.1; -; Genomic_DNA.
EMBL; AF179268; AAD56907.1; JOINED; Genomic_DNA.
EMBL; AF179269; AAD56907.1; JOINED; Genomic_DNA.
EMBL; AF179270; AAD56907.1; JOINED; Genomic_DNA.
EMBL; AF179271; AAD56907.1; JOINED; Genomic_DNA.
EMBL; AF163865; AAG30304.1; -; Genomic_DNA.
EMBL; AK014472; BAB29375.1; -; mRNA.
EMBL; AK156316; BAE33670.1; -; mRNA.
EMBL; BC046764; AAH46764.1; -; mRNA.
EMBL; AF277451; AAG44833.1; -; Genomic_DNA.
CCDS; CCDS20201.1; -. [O55042-1]
RefSeq; NP_001035916.1; NM_001042451.2. [O55042-1]
RefSeq; NP_033247.1; NM_009221.2. [O55042-1]
UniGene; Mm.17484; -.
ProteinModelPortal; O55042; -.
SMR; O55042; -.
BioGrid; 203365; 17.
IntAct; O55042; 8.
MINT; MINT-2736846; -.
STRING; 10090.ENSMUSP00000109907; -.
iPTMnet; O55042; -.
PhosphoSitePlus; O55042; -.
MaxQB; O55042; -.
PaxDb; O55042; -.
PeptideAtlas; O55042; -.
PRIDE; O55042; -.
Ensembl; ENSMUST00000114268; ENSMUSP00000109907; ENSMUSG00000025889. [O55042-1]
Ensembl; ENSMUST00000163779; ENSMUSP00000126067; ENSMUSG00000025889. [O55042-1]
GeneID; 20617; -.
KEGG; mmu:20617; -.
UCSC; uc009cdn.2; mouse. [O55042-1]
UCSC; uc009cdp.2; mouse. [O55042-2]
CTD; 6622; -.
MGI; MGI:1277151; Snca.
eggNOG; ENOG410IWI2; Eukaryota.
eggNOG; ENOG4111TDZ; LUCA.
GeneTree; ENSGT00390000016161; -.
HOGENOM; HOG000008691; -.
HOVERGEN; HBG000481; -.
InParanoid; O55042; -.
KO; K04528; -.
OMA; SEAYEMP; -.
OrthoDB; EOG091G11PA; -.
PhylomeDB; O55042; -.
TreeFam; TF332776; -.
PMAP-CutDB; O55042; -.
PRO; PR:O55042; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000025889; -.
CleanEx; MM_SNCA; -.
Genevisible; O55042; MM.
GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0005938; C:cell cortex; ISO:MGI.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005856; C:cytoskeleton; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISS:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0030426; C:growth cone; ISO:MGI.
GO; GO:0016234; C:inclusion body; IDA:ParkinsonsUK-UCL.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IMP:ParkinsonsUK-UCL.
GO; GO:0005640; C:nuclear outer membrane; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0031092; C:platelet alpha granule membrane; IEA:Ensembl.
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; ISO:MGI.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
GO; GO:0050544; F:arachidonic acid binding; IDA:MGI.
GO; GO:0048487; F:beta-tubulin binding; IEA:Ensembl.
GO; GO:0005509; F:calcium ion binding; ISO:MGI.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:1903136; F:cuprous ion binding; ISO:MGI.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:MGI.
GO; GO:0070840; F:dynein complex binding; ISO:MGI.
GO; GO:0008198; F:ferrous iron binding; ISO:MGI.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0030544; F:Hsp70 protein binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IDA:MGI.
GO; GO:0019894; F:kinesin binding; ISO:MGI.
GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
GO; GO:0016491; F:oxidoreductase activity; ISO:MGI.
GO; GO:0043274; F:phospholipase binding; IEA:Ensembl.
GO; GO:0005543; F:phospholipid binding; ISO:MGI.
GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
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; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; ISO:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:0008344; P:adult locomotory behavior; IGI:MGI.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0048148; P:behavioral response to cocaine; IEA:Ensembl.
GO; GO:0071280; P:cellular response to copper ion; ISO:MGI.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; IMP:MGI.
GO; GO:0007268; P:chemical synaptic transmission; IGI:MGI.
GO; GO:0042416; P:dopamine biosynthetic process; IMP:MGI.
GO; GO:0042417; P:dopamine metabolic process; IGI:MGI.
GO; GO:0060079; P:excitatory postsynaptic potential; IMP:MGI.
GO; GO:0006631; P:fatty acid metabolic process; IMP:MGI.
GO; GO:0060291; P:long-term synaptic potentiation; IMP:MGI.
GO; GO:0061024; P:membrane organization; IMP:MGI.
GO; GO:0001774; P:microglial cell activation; IMP:MGI.
GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IMP:MGI.
GO; GO:0007006; P:mitochondrial membrane organization; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:1904715; P:negative regulation of chaperone-mediated autophagy; ISO:MGI.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
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; ISO:MGI.
GO; GO:0045920; P:negative regulation of exocytosis; ISO:MGI.
GO; GO:0035067; P:negative regulation of histone acetylation; ISO:MGI.
GO; GO:0031115; P:negative regulation of microtubule polymerization; ISO:MGI.
GO; GO:0032769; P:negative regulation of monooxygenase activity; ISO:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IGI:MGI.
GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
GO; GO:0051622; P:negative regulation of norepinephrine uptake; ISO:MGI.
GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; ISO:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0051612; P:negative regulation of serotonin uptake; ISO:MGI.
GO; GO:0070495; P:negative regulation of thrombin-activated receptor signaling pathway; ISO:MGI.
GO; GO:0032410; P:negative regulation of transporter activity; ISO:MGI.
GO; GO:0006638; P:neutral lipid metabolic process; IMP:MGI.
GO; GO:0055114; P:oxidation-reduction process; ISO:MGI.
GO; GO:0006644; P:phospholipid metabolic process; IMP:MGI.
GO; GO:0045807; P:positive regulation of endocytosis; ISO:MGI.
GO; GO:1903284; P:positive regulation of glutathione peroxidase activity; ISO:MGI.
GO; GO:1903285; P:positive regulation of hydrogen peroxide catabolic process; ISO:MGI.
GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; ISO:MGI.
GO; GO:0001956; P:positive regulation of neurotransmitter secretion; IDA:MGI.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0001921; P:positive regulation of receptor recycling; ISO:MGI.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI.
GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:MGI.
GO; GO:0031648; P:protein destabilization; ISO:MGI.
GO; GO:0031623; P:receptor internalization; ISO:MGI.
GO; GO:0050812; P:regulation of acyl-CoA biosynthetic process; IDA:MGI.
GO; GO:0014059; P:regulation of dopamine secretion; IGI:MGI.
GO; GO:0014048; P:regulation of glutamate secretion; IMP:MGI.
GO; GO:0040012; P:regulation of locomotion; IMP:MGI.
GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; IMP:MGI.
GO; GO:0043030; P:regulation of macrophage activation; IMP:MGI.
GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IMP:MGI.
GO; GO:0046928; P:regulation of neurotransmitter secretion; IMP:MGI.
GO; GO:0010517; P:regulation of phospholipase activity; ISO:MGI.
GO; GO:1905606; P:regulation of presynapse assembly; ISO:MGI.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:ParkinsonsUK-UCL.
GO; GO:0042493; P:response to drug; IMP:MGI.
GO; GO:0034341; P:response to interferon-gamma; ISO:MGI.
GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
GO; GO:0010040; P:response to iron(II) ion; ISO:MGI.
GO; GO:0032496; P:response to lipopolysaccharide; ISO:MGI.
GO; GO:0032026; P:response to magnesium ion; ISO:MGI.
GO; GO:0050808; P:synapse organization; IGI:MGI.
GO; GO:0001963; P:synaptic transmission, dopaminergic; IMP:MGI.
GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:UniProtKB.
GO; GO:0048489; P:synaptic vesicle transport; IMP:MGI.
InterPro; IPR001058; Synuclein.
InterPro; IPR002460; Synuclein_alpha.
PANTHER; PTHR13820; PTHR13820; 1.
PANTHER; PTHR13820:SF12; PTHR13820:SF12; 1.
Pfam; PF01387; Synuclein; 1.
PRINTS; PR01212; ASYNUCLEIN.
PRINTS; PR01211; SYNUCLEIN.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell junction; Complete proteome;
Copper; Cytoplasm; Direct protein sequencing; Membrane; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Secreted;
Synapse; Ubl conjugation.
CHAIN 1 140 Alpha-synuclein.
/FTId=PRO_0000184026.
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:0000250}.
METAL 50 50 Copper. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:P37840}.
MOD_RES 125 125 Phosphotyrosine; by FYN.
{ECO:0000250|UniProtKB:P37840}.
MOD_RES 129 129 Phosphoserine; by PLK2.
{ECO:0000269|PubMed:19004816}.
VAR_SEQ 103 121 GEEGYPQEGILEDMPVDPG -> VWLPVLCSVITLDTMSLH
A (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_025018.
VAR_SEQ 122 140 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_025019.
CONFLICT 58 58 K -> T (in Ref. 1; AAC00521).
{ECO:0000305}.
SEQUENCE 140 AA; 14485 MW; 1FFD19D7E15E636C CRC64;
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVTTVAEKTK
EQVTNVGGAV VTGVTAVAQK TVEGAGNIAA ATGFVKKDQM GKGEEGYPQE GILEDMPVDP
GSEAYEMPSE EGYQDYEPEA


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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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