dbPTM

RAB8B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAB8B_HUMAN
UniProt AC	Q92930
Protein Name	Ras-related protein Rab-8B
Gene Name	RAB8B
Organism	Homo sapiens (Human).
Sequence Length	207
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side . Cytoplasmic vesicle, phagosome . Cytoplasmic vesicle, phagosome membrane Lipid-anchor Cytoplasmic side . Recruited to phagosomes containing S.aureus or M.tuberculosis.
Protein Description	The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab may be involved in polarized vesicular trafficking and neurotransmitter release. May participate in cell junction dynamics in Sertoli cells (By similarity)..
Protein Sequence	MAKTYDYLFKLLLIGDSGVGKTCLLFRFSEDAFNTTFISTIGIDFKIRTIELDGKKIKLQIWDTAGQERFRTITTAYYRGAMGIMLVYDITNEKSFDNIKNWIRNIEEHASSDVERMILGNKCDMNDKRQVSKERGEKLAIDYGIKFLETSAKSSANVEEAFFTLARDIMTKLNRKMNDSNSAGAGGPVKITENRSKKTSFFRCSLL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Acetylation	-----MAKTYDYLFK -----CCCCHHHHHH	46.44	19608861
3	Ubiquitination	-----MAKTYDYLFK -----CCCCHHHHHH	46.44	23000965
4	Phosphorylation	----MAKTYDYLFKL ----CCCCHHHHHHH	16.46	28796482
5	Phosphorylation	---MAKTYDYLFKLL ---CCCCHHHHHHHH	11.24	25884760
7	Phosphorylation	-MAKTYDYLFKLLLI -CCCCHHHHHHHHHH	12.01	28152594
13	Ubiquitination	DYLFKLLLIGDSGVG HHHHHHHHHCCCCCC	6.28	23000965
17	Phosphorylation	KLLLIGDSGVGKTCL HHHHHCCCCCCCEEE	30.11	23911959
19	Ubiquitination	LLIGDSGVGKTCLLF HHHCCCCCCCEEEEE	9.11	21890473
40	Phosphorylation	FNTTFISTIGIDFKI CCCCEEEEEEEEEEE	20.57	-
47	Ubiquitination	TIGIDFKIRTIELDG EEEEEEEEEEEEECC	4.79	24816145
49	Phosphorylation	GIDFKIRTIELDGKK EEEEEEEEEEECCEE	23.44	22985185
57	Ubiquitination	IELDGKKIKLQIWDT EEECCEEEEEEEECC	6.49	25015289
64	Phosphorylation	IKLQIWDTAGQERFR EEEEEECCCCHHHHH	20.07	28857561
72	Phosphorylation	AGQERFRTITTAYYR CCHHHHHHHHHHHHH	21.69	23898821
74	Phosphorylation	QERFRTITTAYYRGA HHHHHHHHHHHHHCC	12.54	29978859
75	Phosphorylation	ERFRTITTAYYRGAM HHHHHHHHHHHHCCC	14.60	29978859
77	Phosphorylation	FRTITTAYYRGAMGI HHHHHHHHHHCCCEE	7.51	28060719
78	Phosphorylation	RTITTAYYRGAMGIM HHHHHHHHHCCCEEE	10.50	-
94	Ubiquitination	VYDITNEKSFDNIKN EEECCCCCCHHHHHH	59.50	23000965
95	Ubiquitination	YDITNEKSFDNIKNW EECCCCCCHHHHHHH	31.49	24816145
100	Ubiquitination	EKSFDNIKNWIRNIE CCCHHHHHHHHHHHH	53.11	23000965
111	Phosphorylation	RNIEEHASSDVERMI HHHHHHCCCHHHHHH	29.04	29255136
111	O-linked_Glycosylation	RNIEEHASSDVERMI HHHHHHCCCHHHHHH	29.04	30379171
112	Phosphorylation	NIEEHASSDVERMIL HHHHHCCCHHHHHHH	46.59	29255136
112	O-linked_Glycosylation	NIEEHASSDVERMIL HHHHHCCCHHHHHHH	46.59	30379171
122	Ubiquitination	ERMILGNKCDMNDKR HHHHHCCCCCCCCCC	29.79	29967540
128	Ubiquitination	NKCDMNDKRQVSKER CCCCCCCCCHHHHHH	39.46	24816145
132	Phosphorylation	MNDKRQVSKERGEKL CCCCCHHHHHHHHHH	22.06	-
138	Ubiquitination	VSKERGEKLAIDYGI HHHHHHHHHHHHHHH	46.15	25015289
143	Phosphorylation	GEKLAIDYGIKFLET HHHHHHHHHHHHHHH	18.03	22964224
153	Ubiquitination	KFLETSAKSSANVEE HHHHHCCCCCCCHHH	44.72	29967540
164	Phosphorylation	NVEEAFFTLARDIMT CHHHHHHHHHHHHHH	17.04	29255136
176	Ubiquitination	IMTKLNRKMNDSNSA HHHHHHHHCCCCCCC	40.77	24816145
180	Phosphorylation	LNRKMNDSNSAGAGG HHHHCCCCCCCCCCC	27.90	29255136
182	Phosphorylation	RKMNDSNSAGAGGPV HHCCCCCCCCCCCCE	31.84	29255136
190	Ubiquitination	AGAGGPVKITENRSK CCCCCCEEECCCCCC	47.22	33845483
200	Phosphorylation	ENRSKKTSFFRCSLL CCCCCCCEEEEEECC	31.13	21712546
204	Methylation	KKTSFFRCSLL---- CCCEEEEEECC----	2.58	-
204	Geranylgeranylation	KKTSFFRCSLL---- CCCEEEEEECC----	2.58	-

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
72	T	Phosphorylation	Kinase	LRRK2	Q5S007	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
72	T	Phosphorylation		29125462
Phosphorylation of Thr-72 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 RAB8B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CADH1_HUMAN	CDH1	physical	12639940
CADH2_HUMAN	CDH2	physical	12639940
TES_HUMAN	TES	physical	12639940
CTNB1_HUMAN	CTNNB1	physical	12639940
PLAK_HUMAN	JUP	physical	12639940
ZO1_HUMAN	TJP1	physical	12639940
ITB1_HUMAN	ITGB1	physical	12639940
VIME_HUMAN	VIM	physical	12639940
OCLN_HUMAN	OCLN	physical	12639940
TBG1_HUMAN	TUBG1	physical	12639940
ACTB_HUMAN	ACTB	physical	12639940
PAXI_HUMAN	PXN	physical	12639940
TBA1A_HUMAN	TUBA1A	physical	12639940
TBB5_HUMAN	TUBB	physical	12639940
A4_HUMAN	APP	physical	21832049
GDIA_HUMAN	GDI1	physical	26344197
GDIB_HUMAN	GDI2	physical	26344197
HCD2_HUMAN	HSD17B10	physical	26344197
MILK2_HUMAN	MICALL2	physical	28514442
RAB8A_HUMAN	RAB8A	physical	28514442
GDIA_HUMAN	GDI1	physical	28514442
MILK1_HUMAN	MICALL1	physical	28514442
MICA3_HUMAN	MICAL3	physical	28514442
SYTL4_HUMAN	SYTL4	physical	28514442
UH1BL_HUMAN	UHRF1BP1L	physical	28514442
RAE1_HUMAN	CHM	physical	28514442
FLNC_HUMAN	FLNC	physical	28514442
SYNM_HUMAN	NARS2	physical	28514442
RAE2_HUMAN	CHML	physical	28514442
MOCS1_HUMAN	MOCS1	physical	28514442
RAB13_HUMAN	RAB13	physical	28514442
NOCT_HUMAN	CCRN4L	physical	28514442
MSS4_HUMAN	RABIF	physical	28514442
CTU2_HUMAN	CTU2	physical	28514442
GDIB_HUMAN	GDI2	physical	28514442
FLNA_HUMAN	FLNA	physical	28514442

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.

Regulatory Network of RAB8B_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-5, AND MASSSPECTROMETRY.	19534553 [Abstract]

show