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SYP (human)

Overview SYP Possibly involved in structural functions as organizing other membrane components or in targeting the vesicles to the plasma membrane. Involved in the regulation of short-term and long-term synaptic plasticity. Homohexamer or homotetramer. Interacts with SRCIN1. Characteristic of a type of small (30-80 nm) neurosecretory vesicles, including presynaptic vesicles, but also vesicles of various neuroendocrine cells of both neuronal and epithelial phenotype. Belongs to the synaptophysin/synaptobrevin family. Note: This description may include information from UniProtKB. Protein type: Membrane protein, integral; Vesicle protein Cellular Component: presynaptic membrane; protein complex; presynaptic active zone; cell junction; integral to synaptic vesicle membrane Molecular Function: identical protein binding; transporter activity; cholesterol binding; syntaxin-1 binding; SH2 domain binding; calcium ion binding Biological Process: regulation of long-term neuronal synaptic plasticity; synaptic vesicle maturation; synaptic vesicle membrane organization and biogenesis; endocytosis; regulation of short-term neuronal synaptic plasticity Reference #:  P08247 (UniProtKB) Alt. Names/Synonyms: Major synaptic vesicle protein p38; MRXSYP; Synaptophysin; SYP; SYPH Gene Symbols: SYP Molecular weight: 33,845 Da Basal Isoelectric point: 4.66  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below SYP

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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

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	129		Y81-p	PFRLHQVyFDAPTCR
0	2		T86	QVyFDAPTCRGGTTK
0	1		R88	yFDAPTCRGGTTKVF
0	1		T186	EMPVCRQTGNTCKEL
0	1		Y250-p	QPAPGDAyGDAGYGQ
1	1		Y268	GYGPQDSYGPQGGYQ
1	1		Y278	QGGYQPDYGQPAGSG

	mouse
Y81-p	PFRLHQVyFDAPsCV
S86-p	QVyFDAPsCVkGGTT
K89-u	FDAPsCVkGGTTKIF
T187-p	EMPMCRQtGNTCKEL
Y251	QPAPGDAYGDAGYGQ
Y269-p	GYGPQDSyGPQGGYQ
Y279-p	QGGYQPDyGQPASGG

	rat
Y75-p	PFRLHQVyFDAPSCV
S80	QVyFDAPSCVKGGTT
K83	FDAPSCVKGGTTKIF
T181	EMPMCRQTGNTCKEL
Y245	QPAPGDAYGDAGYGQ
Y263-p	GYGPQDSyGPQGGYQ
Y273-p	QGGYQPDyGQPASGG

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