dbPTM

RAB8A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAB8A_HUMAN
UniProt AC	P61006
Protein Name	Ras-related protein Rab-8A
Gene Name	RAB8A
Organism	Homo sapiens (Human).
Sequence Length	207
Subcellular Localization	Cell membrane Lipid-anchor Cytoplasmic side . Golgi apparatus . Recycling endosome membrane . Cell projection, cilium . Cytoplasmic vesicle, phagosome . Cytoplasmic vesicle, phagosome membrane Lipid-anchor Cytoplasmic side . Cytoplasm, cytoskeleto
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 is involved in polarized vesicular trafficking and neurotransmitter release. Together with RAB11A, RAB3IP, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. [PubMed: 20890297 Together with MYO5B and RAB11A participates in epithelial cell polarization]
Protein Sequence	MAKTYDYLFKLLLIGDSGVGKTCVLFRFSEDAFNSTFISTIGIDFKIRTIELDGKRIKLQIWDTAGQERFRTITTAYYRGAMGIMLVYDITNEKSFDNIRNWIRNIEEHASADVEKMILGNKCDVNDKRQVSKERGEKLALDYGIKFMETSAKANINVENAFFTLARDIKAKMDKKLEGNSPQGSNQGVKITPDQQKRSSFFRCVLL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Ubiquitination	-----MAKTYDYLFK -----CCCCHHHHHH	46.44	-
3	Acetylation	-----MAKTYDYLFK -----CCCCHHHHHH	46.44	-
3	Ubiquitination	-----MAKTYDYLFK -----CCCCHHHHHH	46.44	-
3	Acetylation	-----MAKTYDYLFK -----CCCCHHHHHH	46.44	25953088
4	Phosphorylation	----MAKTYDYLFKL ----CCCCHHHHHHH	16.46	28796482
5	Phosphorylation	---MAKTYDYLFKLL ---CCCCHHHHHHHH	11.24	25884760
7	Phosphorylation	-MAKTYDYLFKLLLI -CCCCHHHHHHHHHH	12.01	28152594
17	Phosphorylation	KLLLIGDSGVGKTCV HHHHHCCCCCCCEEE	30.11	23911959
23	S-palmitoylation	DSGVGKTCVLFRFSE CCCCCCEEEEEEECC	2.59	29575903
49	Phosphorylation	GIDFKIRTIELDGKR CEEEEEEEEEECCEE	23.44	22985185
64	Phosphorylation	IKLQIWDTAGQERFR EEEEEECCCCHHHHH	20.07	28857561
72	Phosphorylation	AGQERFRTITTAYYR CCHHHHHHHHHHHHH	21.69	26824392
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	-
111	Phosphorylation	RNIEEHASADVEKMI HCHHHHCCCCHHHHH	27.23	25159151
116	Ubiquitination	HASADVEKMILGNKC HCCCCHHHHHHCCCC	30.96	21906983
116	Ubiquitination	HASADVEKMILGNKC HCCCCHHHHHHCCCC	30.96	-
122	Ubiquitination	EKMILGNKCDVNDKR HHHHHCCCCCCCCCC	29.98	-
132	Phosphorylation	VNDKRQVSKERGEKL CCCCCHHHHHHHHHH	22.06	-
138	Ubiquitination	VSKERGEKLALDYGI HHHHHHHHHHHHHHH	41.71	-
138	Ubiquitination	VSKERGEKLALDYGI HHHHHHHHHHHHHHH	41.71	21906983
162 (in isoform 2)	Phosphorylation	-	7.88	30622161
164 (in isoform 2)	Phosphorylation	-	17.04	30622161
164	Phosphorylation	NVENAFFTLARDIKA CHHHHHHHHHHHHHH	17.04	30266825
176	Ubiquitination	IKAKMDKKLEGNSPQ HHHHHHHHCCCCCCC	47.72	-
181	Phosphorylation	DKKLEGNSPQGSNQG HHHCCCCCCCCCCCC	29.47	29255136
185	Phosphorylation	EGNSPQGSNQGVKIT CCCCCCCCCCCCCCC	22.26	29255136
190	Ubiquitination	QGSNQGVKITPDQQK CCCCCCCCCCCCHHH	47.92	21906983
192	Phosphorylation	SNQGVKITPDQQKRS CCCCCCCCCCHHHCC	18.33	25159151
197	Ubiquitination	KITPDQQKRSSFFRC CCCCCHHHCCCCEEE	48.92	-
199	Phosphorylation	TPDQQKRSSFFRCVL CCCHHHCCCCEEEEE	38.23	24702127
200	Phosphorylation	PDQQKRSSFFRCVLL CCHHHCCCCEEEEEC	32.22	23312004
204	Geranylgeranylation	KRSSFFRCVLL---- HCCCCEEEEEC----	1.82	8375503
204	Geranylgeranylation	KRSSFFRCVLL---- HCCCCEEEEEC----	1.82	8375503
204	Methylation	KRSSFFRCVLL---- HCCCCEEEEEC----	1.82	-

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
72	T	Phosphorylation	Kinase	LRRK2	Q5S007	Uniprot
72	T	Phosphorylation	Kinase	TAK1	O43318	PSP
72	T	Phosphorylation	Kinase	MST3	Q9Y6E0	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
72	T	Phosphorylation		26824392
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 RAB8A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BAG6_HUMAN	BAG6	physical	16169070
SYTL4_HUMAN	SYTL4	physical	11773082
M4K2_HUMAN	MAP4K2	physical	8643544
TFR1_HUMAN	TFRC	physical	20085643
OPTN_HUMAN	OPTN	physical	20085643
SYUA_HUMAN	SNCA	physical	15207266
RB11B_HUMAN	RAB11B	physical	22939629
RRBP1_HUMAN	RRBP1	physical	22939629
EHD1_HUMAN	EHD1	physical	17507647
EHD3_HUMAN	EHD3	physical	17507647
OPTN_HUMAN	OPTN	physical	23357852
SYTL4_HUMAN	SYTL4	physical	23140275
TFR1_HUMAN	TFRC	physical	22854040
ODFP2_HUMAN	ODF2	physical	17646400
ANXA4_HUMAN	ANXA4	physical	26344197
GDIA_HUMAN	GDI1	physical	26344197
GDIB_HUMAN	GDI2	physical	26344197
HCD2_HUMAN	HSD17B10	physical	26344197
RAB10_HUMAN	RAB10	physical	26344197
SDHB_HUMAN	SDHB	physical	26344197
EXOC6_HUMAN	EXOC6	physical	26553929
SYTL4_HUMAN	SYTL4	physical	26553929
RAB3B_HUMAN	RAB3B	physical	26553929
STX3_HUMAN	STX3	physical	26553929
MTMR4_HUMAN	MTMR4	physical	27432908
STOM_HUMAN	STOM	physical	27173435
ARMC8_HUMAN	ARMC8	physical	27173435
RBP10_HUMAN	RANBP10	physical	27173435
WDR26_HUMAN	WDR26	physical	27173435
BBS1_HUMAN	BBS1	physical	27173435
MICA1_MOUSE	Mical1	physical	26833786
MILK1_MOUSE	Micall1	physical	26833786
MILK2_MOUSE	Micall2	physical	26833786
OPTN_MOUSE	Optn	physical	26833786
EH1L1_MOUSE	Ehbp1l1	physical	26833786
EH1L1_HUMAN	EHBP1L1	physical	26833786
BIN1_HUMAN	BIN1	physical	26833786

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 RAB8A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-185, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-185 ANDTHR-192, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-185, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"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-181 AND SER-185, ANDMASS SPECTROMETRY.	18088087 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-185, ANDMASS SPECTROMETRY.	17081983 [Abstract]
Prenylation
Reference	PubMed
"Isoprenylation of Rab proteins possessing a C-terminal CaaX motif."; Joberty G., Tavitian A., Zahraoui A.; FEBS Lett. 330:323-328(1993). Cited for: ISOPRENYLATION AT CYS-204.	8375503 [Abstract]

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