RAB3B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAB3B_HUMAN
• UniProt AC: P20337
• Protein Name: Ras-related protein Rab-3B
• Gene Name: RAB3B
• Organism: Homo sapiens (Human).
• Sequence Length: 219
• Subcellular Localization: Cell membrane ; Lipid-anchor ; Cytoplasmic side . Golgi apparatus . Colocalizes with GAS8/DRC4 in the Golgi apparatus.
• Protein Description: Protein transport. Probably involved in vesicular traffic (By similarity)..
• Protein Sequence: MASVTDGKTGVKDASDQNFDYMFKLLIIGNSSVGKTSFLFRYADDTFTPAFVSTVGIDFKVKTVYRHEKRVKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWATQIKTYSWDNAQVILVGNKCDMEEERVVPTEKGQLLAEQLGFDFFEASAKENISVRQAFERLVDAICDKMSDSLDTDPSMLGSSKNTRLSDTPPLLQQNCSC

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
2	Acetylation	------MASVTDGKT ------CCCCCCCCC	16.83	-
3	O-linked_Glycosylation	-----MASVTDGKTG -----CCCCCCCCCC	25.01	30379171
8	Malonylation	MASVTDGKTGVKDAS CCCCCCCCCCCCCCC	44.94	26320211
8	Ubiquitination	MASVTDGKTGVKDAS CCCCCCCCCCCCCCC	44.94	33845483
12	Ubiquitination	TDGKTGVKDASDQNF CCCCCCCCCCCCCCC	49.25	22817900
21	Phosphorylation	ASDQNFDYMFKLLII CCCCCCCEEEEEEEE	10.58	-
22	Sulfoxidation	SDQNFDYMFKLLIIG CCCCCCEEEEEEEEC	2.28	30846556
72	Ubiquitination	YRHEKRVKLQIWDTA EECCCEEEEEEECCC	38.41	-
72	Malonylation	YRHEKRVKLQIWDTA EECCCEEEEEEECCC	38.41	26320211
78	Phosphorylation	VKLQIWDTAGQERYR EEEEEECCCCHHHHH	20.07	28857561
84	Phosphorylation	DTAGQERYRTITTAY CCCCHHHHHHHHHHH	16.03	19060867
86	Phosphorylation	AGQERYRTITTAYYR CCHHHHHHHHHHHHH	17.46	29125462
88	Phosphorylation	QERYRTITTAYYRGA HHHHHHHHHHHHHCC	12.54	-
89	Phosphorylation	ERYRTITTAYYRGAM HHHHHHHHHHHHCCC	14.60	24961811
91	Phosphorylation	YRTITTAYYRGAMGF HHHHHHHHHHCCCEE	7.51	21951684
92	Phosphorylation	RTITTAYYRGAMGFI HHHHHHHHHCCCEEE	10.50	21951684
102	Phosphorylation	AMGFILMYDITNEES CCEEEEEEECCCHHH	10.76	21951684
149	Ubiquitination	ERVVPTEKGQLLAEQ CEECCCHHHHHHHHH	55.20	21906983
184	S-nitrosylation	ERLVDAICDKMSDSL HHHHHHHHHHCHHCC	4.39	22178444
184	S-nitrosocysteine	ERLVDAICDKMSDSL HHHHHHHHHHCHHCC	4.39	-
188	Phosphorylation	DAICDKMSDSLDTDP HHHHHHCHHCCCCCH	29.77	22617229
190	Phosphorylation	ICDKMSDSLDTDPSM HHHHCHHCCCCCHHH	22.34	28355574
193	Phosphorylation	KMSDSLDTDPSMLGS HCHHCCCCCHHHCCC	55.92	23403867
196	Phosphorylation	DSLDTDPSMLGSSKN HCCCCCHHHCCCCCC	29.46	29514088
200	Phosphorylation	TDPSMLGSSKNTRLS CCHHHCCCCCCCCCC	33.89	29514088
201	Phosphorylation	DPSMLGSSKNTRLSD CHHHCCCCCCCCCCC	28.29	29514088
202	Ubiquitination	PSMLGSSKNTRLSDT HHHCCCCCCCCCCCC	65.13	21906983
217	Geranylgeranylation	PPLLQQNCSC----- CHHHHHCCCC-----	3.69	-
219	Methylation	LLQQNCSC------- HHHHCCCC-------	7.62	-
219	Geranylgeranylation	LLQQNCSC------- HHHHCCCC-------	7.62	-

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	Q5S007	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
86	T	Phosphorylation	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 inhibitor GDI2.	29125462

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RAB3B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GDIA_HUMAN	GDI1	physical	11741295
PIGR_HUMAN	PIGR	physical	11832247

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.