dbPTM

VATB2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	VATB2_MOUSE
UniProt AC	P62814
Protein Name	V-type proton ATPase subunit B, brain isoform
Gene Name	Atp6v1b2
Organism	Mus musculus (Mouse).
Sequence Length	511
Subcellular Localization	Endomembrane system Peripheral membrane protein. Melanosome. Endomembrane.
Protein Description	Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells..
Protein Sequence	MALRAMRGIVNGAAPELPVPTGGPMAGAREQALAVSRNYLSQPRLTYKTVSGVNGPLVILDHVKFPRYAEIVHLTLPDGTKRSGQVLEVSGSKAVVQVFEGTSGIDAKKTSCEFTGDILRTPVSEDMLGRVFNGSGKPIDRGPVVLAEDFLDIMGQPINPQCRIYPEEMIQTGISAIDGMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSKDVVDYSEENFAIVFAAMGVNMETARFFKSDFEENGSMDNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGYMYTDLATIYERAGRVEGRNGSITQIPILTMPNDDITHPIPDLTGYITEGQIYVDRQLHNRQIYPPINVLPSLSRLMKSAIGEGMTRKDHADVSNQLYACYAIGKDVQAMKAVVGEEALTSDDLLYLEFLQKFEKNFITQGPYENRTVYETLDIGWQLLRIFPKEMLKRIPQSTLSEFYPRDSAKH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
41	Phosphorylation	AVSRNYLSQPRLTYK HHHCHHHCCCCCEEE	27.98	24719451
48	Phosphoglycerylation	SQPRLTYKTVSGVNG CCCCCEEEEECCCCC	36.90	-
64	Ubiquitination	LVILDHVKFPRYAEI EEEEECCCCCCCEEE	46.35	22790023
68	Nitration	DHVKFPRYAEIVHLT ECCCCCCCEEEEEEE	14.61	-
81	Ubiquitination	LTLPDGTKRSGQVLE EECCCCCCCCCCEEE	50.53	22790023
90	Phosphorylation	SGQVLEVSGSKAVVQ CCCEEEEECCEEEEE	28.15	25338131
92	Phosphorylation	QVLEVSGSKAVVQVF CEEEEECCEEEEEEE	15.22	29899451
103	Phosphorylation	VQVFEGTSGIDAKKT EEEEECCCCCCCCCC	44.61	24719451
108	Ubiquitination	GTSGIDAKKTSCEFT CCCCCCCCCCEEEEC	53.49	22790023
108	Acetylation	GTSGIDAKKTSCEFT CCCCCCCCCCEEEEC	53.49	19847547
109	Ubiquitination	TSGIDAKKTSCEFTG CCCCCCCCCEEEECC	47.60	-
109	Acetylation	TSGIDAKKTSCEFTG CCCCCCCCCEEEECC	47.60	19847557
109	Malonylation	TSGIDAKKTSCEFTG CCCCCCCCCEEEECC	47.60	26320211
111	Phosphorylation	GIDAKKTSCEFTGDI CCCCCCCEEEECCCC	22.11	19060867
112	S-nitrosylation	IDAKKTSCEFTGDIL CCCCCCEEEECCCCC	6.37	24895380
137	Ubiquitination	RVFNGSGKPIDRGPV HHCCCCCCCCCCCCE	40.26	22790023
162	Glutathionylation	GQPINPQCRIYPEEM CCCCCCCCCCCHHHH	2.77	24333276
188	Ubiquitination	NSIARGQKIPIFSAA CHHHCCCCCCEEECC	53.96	22790023
207	S-nitrosylation	NEIAAQICRQAGLVK HHHHHHHHHHCCCCC	1.43	24926564
207	Glutathionylation	NEIAAQICRQAGLVK HHHHHHHHHHCCCCC	1.43	24333276
207	S-palmitoylation	NEIAAQICRQAGLVK HHHHHHHHHHCCCCC	1.43	26165157
214	Ubiquitination	CRQAGLVKKSKDVVD HHHCCCCCCCCCCCC	57.27	27667366
289	S-nitrosylation	AEFLAYQCEKHVLVI HHHHHHHHHCCEEEE	4.98	24895380
403	Ubiquitination	PSLSRLMKSAIGEGM HHHHHHHHHHHCCCC	41.13	22790023
403	Acetylation	PSLSRLMKSAIGEGM HHHHHHHHHHHCCCC	41.13	7614155
404	Phosphorylation	SLSRLMKSAIGEGMT HHHHHHHHHHCCCCC	15.91	19144319
445	Phosphorylation	VVGEEALTSDDLLYL HHCCCCCCCCHHHHH	36.84	29899451
446	Phosphorylation	VGEEALTSDDLLYLE HCCCCCCCCHHHHHH	29.94	20415495
451	Phosphorylation	LTSDDLLYLEFLQKF CCCCHHHHHHHHHHH	16.10	20415495
460	Ubiquitination	EFLQKFEKNFITQGP HHHHHHHHHCCCCCC	61.36	22790023
468	Phosphorylation	NFITQGPYENRTVYE HCCCCCCCCCCCHHH	32.43	25367039
489	Ubiquitination	QLLRIFPKEMLKRIP HHHHHCCHHHHHCCC	45.03	22790023
498	Phosphorylation	MLKRIPQSTLSEFYP HHHCCCHHHHHHHCC	26.43	25521595
499	Phosphorylation	LKRIPQSTLSEFYPR HHCCCHHHHHHHCCC	29.11	20415495
501	Phosphorylation	RIPQSTLSEFYPRDS CCCHHHHHHHCCCCC	26.25	20415495
504	Phosphorylation	QSTLSEFYPRDSAKH HHHHHHHCCCCCCCC	8.03	29899451
504	Nitration	QSTLSEFYPRDSAKH HHHHHHHCCCCCCCC	8.03	-

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
Oops, there are no upstream regulatory protein records of VATB2_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of VATB2_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of VATB2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of VATB2_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of VATB2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-404, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-498, AND MASSSPECTROMETRY.	17114649 [Abstract]