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

Overview
SNCB a member of the synuclein family. Abundantly expressed in the brain. Inhibits phospholipase D2 selectively. May play a role in neuronal plasticity, is abundant in neurofibrillary lesions of Alzheimer's patients. Highly expressed in the substantia nigra of the brain, a region of neuronal degeneration in patients with Parkinson disease. Note: This description may include information from UniProtKB.
Protein type: Adaptor/scaffold
Cellular Component: Golgi apparatus; growth cone; mitochondrion; cell soma; cytoplasm; nucleolus; terminal button; nucleus
Molecular Function: phospholipase inhibitor activity; beta-tubulin binding; calcium ion binding; alpha-tubulin binding
Biological Process: synaptic transmission; negative regulation of catalytic activity; synapse organization and biogenesis; negative regulation of neuron apoptosis; dopamine metabolic process
Reference #:  Q16143 (UniProtKB)
Alt. Names/Synonyms: Beta-synuclein; SNCB; synuclein, beta; SYUB
Gene Symbols: SNCB
Molecular weight: 14,288 Da
Basal Isoelectric point: 4.41  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

SNCB

Protein Structure Not Found.


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

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

Show Multiple Sequence Alignment


 SS 

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


 MS 

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


       human

 
0 2 K6-ac __MDVFMkGLSMAkE
0 12 K12-ac MkGLSMAkEGVVAAA
0 1 K12 MkGLSMAKEGVVAAA
0 1 K12 MkGLSMAKEGVVAAA
1 0 T27 EKTKQGVTEAAEKTK
0 1 K32 GVTEAAEKTKEGVLy
0 11 Y39-p KTKEGVLyVGSKTRE
0 3 S42 EGVLyVGSKTREGVV
0 2 K43 GVLyVGSKTREGVVQ
0 2 T44 VLyVGSKTREGVVQG
0 2 E46 yVGSKTREGVVQGVA
0 1 K58 GVASVAEKTKEQASH
0 1 S64 EKTKEQASHLGGAVF
0 1 S72 HLGGAVFSGAGNIAA
1 0 S118-p LMEPEGEsYEDPPQE
0 1 P122 EGEsYEDPPQEEyQE
1 1 Y127-p EDPPQEEyQEYEPEA
  mouse

 
K6 __MDVFMKGLSMAkE
K12 MKGLSMAKEGVVAAA
K12-m1 MKGLSMAkEGVVAAA
K12-ub MKGLSMAkEGVVAAA
T27 EKTKQGVTEAAEKTK
K32 GVTEAAEKTKEGVLy
Y39-p KTKEGVLyVGsKtsG
S42-p EGVLyVGsKtsGVVQ
K43 GVLyVGsKtsGVVQG
T44-p VLyVGsKtsGVVQGV
S45-p LyVGsKtsGVVQGVA
K57-ub GVASVAEkTKEQAsH
S63-p EkTKEQAsHLGGAVF
S71-p HLGGAVFsGAGNIAA
S117 LMEPEGESYEDsPQE
S121-p EGESYEDsPQEEyQE
Y126-p EDsPQEEyQEYEPEA
  rat

 
K6-ac __MDVFMkGLSMAKE
K12 MkGLSMAKEGVVAAA
K12 MkGLSMAKEGVVAAA
K12 MkGLSMAKEGVVAAA
T27-gl EKTKQGVtEAAEkTK
K32-ub GVtEAAEkTKEGVLy
Y39-p kTKEGVLyVGskTKE
S42-p EGVLyVGskTKEGVV
K43-ub GVLyVGskTKEGVVQ
T44 VLyVGskTKEGVVQG
E46 yVGskTKEGVVQGVA
K58 GVASVAEKTKEQASH
S64 EKTKEQASHLGGAVF
S72 HLGGAVFSGAGNIAA
S118 LMEPEGESYEDSPQE
S122 EGESYEDSPQEEYQE
Y127 EDSPQEEYQEYEPEA
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