VAMP8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VAMP8_HUMAN
• UniProt AC: Q9BV40
• Protein Name: Vesicle-associated membrane protein 8 {ECO:0000303|PubMed:12130530}
• Gene Name: VAMP8 {ECO:0000303|PubMed:12130530}
• Organism: Homo sapiens (Human).
• Sequence Length: 100
• Subcellular Localization: Lysosome membrane ; Single-pass type IV membrane protein . Early endosome membrane ; Single-pass type IV membrane protein . Late 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. [PubMed: 23217709]
• Protein Sequence: MEEASEGGGNDRVRNLQSEVEGVKNIMTQNVERILARGENLEHLRNKTEDLEATSEHFKTTSQKVARKFWWKNVKMIVLICVIVFIIILFIVLFATGAFS

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	-------MEEASEGG -------CCCHHCCC	10.68	25944712
1	Sulfoxidation	-------MEEASEGG -------CCCHHCCC	10.68	28465586
5	Phosphorylation	---MEEASEGGGNDR ---CCCHHCCCCCHH	39.80	23401153
12	Methylation	SEGGGNDRVRNLQSE HCCCCCHHHHHHHHH	33.04	115919741
18	Phosphorylation	DRVRNLQSEVEGVKN HHHHHHHHHHHHHHH	46.94	23401153
24	Ubiquitination	QSEVEGVKNIMTQNV HHHHHHHHHHHHHCH	52.17	21906983
28	Phosphorylation	EGVKNIMTQNVERIL HHHHHHHHHCHHHHH	17.13	20068231
47	Acetylation	NLEHLRNKTEDLEAT CHHHHHHHHHHHHHH	47.02	26822725
47	Ubiquitination	NLEHLRNKTEDLEAT CHHHHHHHHHHHHHH	47.02	21890473
48	Phosphorylation	LEHLRNKTEDLEATS HHHHHHHHHHHHHHH	37.98	23911959
54	Phosphorylation	KTEDLEATSEHFKTT HHHHHHHHHHHHHHH	25.85	23401153
55	Phosphorylation	TEDLEATSEHFKTTS HHHHHHHHHHHHHHH	35.80	23401153
59	Ubiquitination	EATSEHFKTTSQKVA HHHHHHHHHHHHHHH	53.45	21906983
60	Phosphorylation	ATSEHFKTTSQKVAR HHHHHHHHHHHHHHH	30.64	25954137
61	Phosphorylation	TSEHFKTTSQKVARK HHHHHHHHHHHHHHH	29.74	25954137
62	Phosphorylation	SEHFKTTSQKVARKF HHHHHHHHHHHHHHH	32.98	23312004
64	Ubiquitination	HFKTTSQKVARKFWW HHHHHHHHHHHHHHH	37.31	21890473

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
-	K	Ubiquitination	E3 ubiquitin ligase	MARCHF9	Q86YJ5	PMID:19457934

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of VAMP8_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STX7_RAT	Stx7	physical	11101518
VTI1A_RAT	Vti1a	physical	11101518
STX8_RAT	Stx8	physical	11101518
STX7_HUMAN	STX7	physical	11101518
VTI1A_HUMAN	VTI1A	physical	11101518
STX8_HUMAN	STX8	physical	11101518
UBP8_HUMAN	USP8	physical	18388320
STABP_HUMAN	STAMBP	physical	18388320
STX6_HUMAN	STX6	physical	19557002
STX7_HUMAN	STX7	physical	19557002
STX8_HUMAN	STX8	physical	19557002

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330