dbPTM

RAB3A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAB3A_MOUSE
UniProt AC	P63011
Protein Name	Ras-related protein Rab-3A
Gene Name	Rab3a
Organism	Mus musculus (Mouse).
Sequence Length	220
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side .
Protein Description	Involved in exocytosis by regulating a late step in synaptic vesicle fusion. Could play a role in neurotransmitter release by regulating membrane flow in the nerve terminal (By similarity)..
Protein Sequence	MASATDSRYGQKESSDQNFDYMFKILIIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTIYRNDKRIKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWSTQIKTYSWDNAQVLLVGNKCDMEDERVVSSERGRQLADHLGFEFFEASAKDNINVKQTFERLVDVICEKMSESLDTADPAVTGAKQGPQLTDQQAPPHQDCAC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MASATDSRYGQK ---CCCCCCCCCCCC	31.82	22324799
7	Phosphorylation	-MASATDSRYGQKES -CCCCCCCCCCCCCC	24.05	22817900
12	Ubiquitination	TDSRYGQKESSDQNF CCCCCCCCCCCCCCC	56.02	22790023
14	Phosphorylation	SRYGQKESSDQNFDY CCCCCCCCCCCCCCE	46.37	25521595
15	Phosphorylation	RYGQKESSDQNFDYM CCCCCCCCCCCCCEE	44.28	22817900
31	Phosphorylation	KILIIGNSSVGKTSF EEEEECCCCCCCEEE	22.61	20415495
32	Phosphorylation	ILIIGNSSVGKTSFL EEEECCCCCCCEEEE	38.60	20415495
37	Phosphorylation	NSSVGKTSFLFRYAD CCCCCCEEEEEEECC	24.36	15648052
42	Phosphorylation	KTSFLFRYADDSFTP CEEEEEEECCCCCCC	13.67	29899451
63	Phosphorylation	GIDFKVKTIYRNDKR CCCEEEEEEEECCCE	26.65	22324799
86	Phosphorylation	AGQERYRTITTAYYR CCHHHHHHHHHHHHH	17.46	29125462
91	Phosphorylation	YRTITTAYYRGAMGF HHHHHHHHHHCCCEE	7.51	29514104
136	Ubiquitination	QVLLVGNKCDMEDER EEEEEECCCCCCCCE	26.19	22790023
167	Ubiquitination	EFFEASAKDNINVKQ EEHHHHHCCCCCHHH	49.14	22790023
173	Ubiquitination	AKDNINVKQTFERLV HCCCCCHHHHHHHHH	38.85	22790023
184	S-nitrosylation	ERLVDVICEKMSESL HHHHHHHHHHHHHCC	4.06	22588120
186	Ubiquitination	LVDVICEKMSESLDT HHHHHHHHHHHCCCC	43.23	22790023
188	Phosphorylation	DVICEKMSESLDTAD HHHHHHHHHCCCCCC	34.79	25521595
190	Phosphorylation	ICEKMSESLDTADPA HHHHHHHCCCCCCCC	25.00	25521595
193	Phosphorylation	KMSESLDTADPAVTG HHHHCCCCCCCCCCC	37.95	24925903
199	Phosphorylation	DTADPAVTGAKQGPQ CCCCCCCCCCCCCCC	33.26	29899451
218	Geranylgeranylation	QAPPHQDCAC----- CCCCCCCCCC-----	3.15	-
218	S-palmitoylation	QAPPHQDCAC----- CCCCCCCCCC-----	3.15	28680068
220	Geranylgeranylation	PPHQDCAC------- CCCCCCCC-------	7.82	-
220	Methylation	PPHQDCAC------- CCCCCCCC-------	7.82	-

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
86	T	Phosphorylation	Kinase	LRRK2	Q5S006	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
86	T	Phosphorylation		29125462
Phosphorylation of Thr-86 in the switch II region by LRRK2 prevents the association of RAB regulatory proteins, including CHM, CHML and RAB GDP dissociation inhibitors GDI1 and GDI2.

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 RAB3A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SYUA_HUMAN	SNCA	physical	15099020
RP3A_MOUSE	Rph3a	physical	15099020

Drug and Disease Associations

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

Regulatory Network of RAB3A_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-188, AND MASSSPECTROMETRY.	17114649 [Abstract]
"Quantitative analysis of both protein expression and serine /threonine post-translational modifications through stable isotopelabeling with dithiothreitol."; Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,Hart G.W., Burlingame A.L.; Proteomics 5:388-398(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND MASSSPECTROMETRY.	15648052 [Abstract]

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