VMAT2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: VMAT2_HUMAN
• UniProt AC: Q05940
• Protein Name: Synaptic vesicular amine transporter
• Gene Name: SLC18A2
• Organism: Homo sapiens (Human).
• Sequence Length: 514
• Subcellular Localization: Cytoplasmic vesicle membrane; Multi-pass membrane protein.
• Protein Description: Involved in the ATP-dependent vesicular transport of biogenic amine neurotransmitters. Pumps cytosolic monoamines including dopamine, norepinephrine, serotonin, and histamine into synaptic vesicles. Requisite for vesicular amine storage prior to secretion via exocytosis..
• Protein Sequence: MALSELALVRWLQESRRSRKLILFIVFLALLLDNMLLTVVVPIIPSYLYSIKHEKNATEIQTARPVHTASISDSFQSIFSYYDNSTMVTGNATRDLTLHQTATQHMVTNASAVPSDCPSEDKDLLNENVQVGLLFASKATVQLITNPFIGLLTNRIGYPIPIFAGFCIMFVSTIMFAFSSSYAFLLIARSLQGIGSSCSSVAGMGMLASVYTDDEERGNVMGIALGGLAMGVLVGPPFGSVLYEFVGKTAPFLVLAALVLLDGAIQLFVLQPSRVQPESQKGTPLTTLLKDPYILIAAGSICFANMGIAMLEPALPIWMMETMCSRKWQLGVAFLPASISYLIGTNIFGILAHKMGRWLCALLGMIIVGVSILCIPFAKNIYGLIAPNFGVGFAIGMVDSSMMPIMGYLVDLRHVSVYGSVYAIADVAFCMGYAIGPSAGGAIAKAIGFPWLMTIIGIIDILFAPLCFFLRSPPAKEEKMAILMDHNCPIKTKMYTQNNIQSYPIGEDEESESD

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
15	Phosphorylation	LVRWLQESRRSRKLI HHHHHHHHHHHHHHH	21.74	-
18	Phosphorylation	WLQESRRSRKLILFI HHHHHHHHHHHHHHH	32.43	-
50	Phosphorylation	IIPSYLYSIKHEKNA CCHHHHHHHCCCCCC	23.67	24719451
84	N-linked_Glycosylation	SIFSYYDNSTMVTGN HHHHCCCCCCEEECC	24.21	UniProtKB CARBOHYD
91	N-linked_Glycosylation	NSTMVTGNATRDLTL CCCEEECCCCCCEEE	28.86	UniProtKB CARBOHYD
111	Phosphorylation	QHMVTNASAVPSDCP CHHHHCCCCCCCCCC	31.69	22210691
119	Phosphorylation	AVPSDCPSEDKDLLN CCCCCCCCCCHHHCC	65.83	22210691
240	Phosphorylation	LVGPPFGSVLYEFVG CCCCCCHHHHHHHHC	14.88	22817900
279	Phosphorylation	PSRVQPESQKGTPLT HHHCCCCCCCCCCCH	43.82	-
283	Phosphorylation	QPESQKGTPLTTLLK CCCCCCCCCCHHHHC	23.35	-
286	Phosphorylation	SQKGTPLTTLLKDPY CCCCCCCHHHHCCCE	19.32	-
287	Phosphorylation	QKGTPLTTLLKDPYI CCCCCCHHHHCCCEE	37.46	-
479	Acetylation	SPPAKEEKMAILMDH CCCCHHHHHHHCCCC	34.42	25953088
511	Phosphorylation	PIGEDEESESD---- CCCCCCCCCCC----	40.11	28270605
513	Phosphorylation	GEDEESESD------ CCCCCCCCC------	58.88	28270605

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
15	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
18	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
511	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
511	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
511	S	Phosphorylation	Kinase	CK1_GROUP	-	PhosphoELM
511	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
513	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
513	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
513	S	Phosphorylation	Kinase	CK1_GROUP	-	PhosphoELM
513	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of VMAT2_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 VMAT2_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of VMAT2_HUMAN !!

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
• D00197: Reserpine (JP16/USP/INN); Apoplon (TN); Serpalan (TN)
• D08575: Tetrabenazine (JAN/INN); Nitoman (TN); Xenazine (TN)
• D10170: Tedatioxetine (USAN)
• D10171: Tedatioxetine hydrobromide (USAN)
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240, AND MASSSPECTROMETRY.
PubMed: 19690332

"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-511 AND SER-513, ANDMASS SPECTROMETRY.
PubMed: 18088087