VAMP8_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VAMP8_MOUSE
• UniProt AC: O70404
• Protein Name: Vesicle-associated membrane protein 8 {ECO:0000303|PubMed:15363411}
• Gene Name: Vamp8 {ECO:0000312|MGI:MGI:1336882}
• Organism: Mus musculus (Mouse).
• Sequence Length: 101
• Subcellular Localization: Lysosome membrane ; Single-pass type IV membrane protein . Late endosome membrane ; Single-pass type IV membrane protein . Early endosome membrane ; Single-pass type IV membrane protein . Cell membrane ; Single-pass type IV membrane protein . Perinuc
• Protein Description: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. VAMP8 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane via its interaction with the STX17-SNAP29 binary t-SNARE complex (By similarity). Also required for dense-granule secretion in platelets (By similarity). Plays also a role in regulated enzyme secretion in pancreatic acinar cells. [PubMed: 15363411 Involved in the abscission of the midbody during cell division, which leads to completely separate daughter cells (By similarity Involved in the homotypic fusion of early and late endosomes (By similarity]
• Protein Sequence: MEEASGSAGNDRVRNLQSEVEGVKNIMTQNVERILSRGENLDHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVIICVIVLIIVILIILFATGTIPT

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEEASGSA -------CCCCCCCC	10.68	-
5	Phosphorylation	---MEEASGSAGNDR ---CCCCCCCCCCHH	36.24	26745281
7	Phosphorylation	-MEEASGSAGNDRVR -CCCCCCCCCCHHHH	30.43	26745281
18	Phosphorylation	DRVRNLQSEVEGVKN HHHHHHHHHHHHHHH	46.94	25521595
24	Ubiquitination	QSEVEGVKNIMTQNV HHHHHHHHHHHHHHH	52.17	22790023
28	Phosphorylation	EGVKNIMTQNVERIL HHHHHHHHHHHHHHH	17.13	-
47	Ubiquitination	NLDHLRNKTEDLEAT CHHHHHHHHHHHHHH	47.02	22790023
48	Phosphorylation	LDHLRNKTEDLEATS HHHHHHHHHHHHHHH	37.98	25619855
54	Phosphorylation	KTEDLEATSEHFKTT HHHHHHHHHHHHHHH	25.85	26824392
55	Phosphorylation	TEDLEATSEHFKTTS HHHHHHHHHHHHHHH	35.80	25521595
59	Ubiquitination	EATSEHFKTTSQKVA HHHHHHHHHHHHHHH	53.45	22790023
62	Phosphorylation	SEHFKTTSQKVARKF HHHHHHHHHHHHHHH	32.98	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of VAMP8_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of VAMP8_MOUSE !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of VAMP8_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of VAMP8_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND MASSSPECTROMETRY.
PubMed: 19144319