RAB10_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAB10_MOUSE
• UniProt AC: P61027
• Protein Name: Ras-related protein Rab-10
• Gene Name: Rab10
• Organism: Mus musculus (Mouse).
• Sequence Length: 200
• Subcellular Localization: Cytoplasmic vesicle membrane ; Lipid-anchor ; Cytoplasmic side . Golgi apparatus, trans-Golgi network membrane . Endosome membrane . Recycling endosome membrane . Cytoplasmic vesicle, phagosome membrane . Cell projection, cilium . Endoplasmic reticulum me
• 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 set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (By similarity). That Rab is mainly involved in the biosynthetic transport of proteins from the Golgi to the plasma membrane. Regulates, for instance, SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane. In parallel, it regulates the transport of TLR4, a toll-like receptor to the plasma membrane and therefore may be important for innate immune response. Plays also a specific role in asymmetric protein transport to the plasma membrane within the polarized neuron and epithelial cells. In neurons, it is involved in axonogenesis through regulation of vesicular membrane trafficking toward the axonal plasma membrane while in epithelial cells, it regulates transport from the Golgi to the basolateral membrane. Moreover, may play a role in the basolateral recycling pathway and in phagosome maturation. Finally, may play a role in endoplasmic reticulum dynamics and morphology controlling tubulation along microtubules and tubules fusion..
• Protein Sequence: MAKKTYDLLFKLLLIGDSGVGKTCVLFRFSDDAFNTTFISTIGIDFKIKTVELQGKKIKLQIWDTAGQERFHTITTSYYRGAMGIMLVYDITNGKSFENISKWLRNIDEHANEDVERMLLGNKCDMDDKRVVPKGKGEQIAREHGIRFFETSAKANINIEKAFLTLAEDILRKTPVKEPNSENVDISSGGGVTGWKSKCC

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
5	Phosphorylation	---MAKKTYDLLFKL ---CCHHHHHHHHHH	22.89	28066266
6	Phosphorylation	--MAKKTYDLLFKLL --CCHHHHHHHHHHH	17.30	28066266
18	Phosphorylation	KLLLIGDSGVGKTCV HHHHHCCCCCCCEEE	30.11	29472430
40	Phosphorylation	AFNTTFISTIGIDFK CCCCEEEEEEEECEE	15.13	26643407
41	Phosphorylation	FNTTFISTIGIDFKI CCCEEEEEEEECEEE	20.57	26643407
73	Phosphorylation	AGQERFHTITTSYYR CCCCCEEEEECHHCC	19.80	26824392
75	Phosphorylation	QERFHTITTSYYRGA CCCEEEEECHHCCCC	15.73	19060867
76	Phosphorylation	ERFHTITTSYYRGAM CCEEEEECHHCCCCC	15.75	25777480
77	Phosphorylation	RFHTITTSYYRGAMG CEEEEECHHCCCCCE	16.12	25777480
78	Phosphorylation	FHTITTSYYRGAMGI EEEEECHHCCCCCEE	8.62	25777480
79	Phosphorylation	HTITTSYYRGAMGIM EEEECHHCCCCCEEE	11.44	25777480
102	Ubiquitination	KSFENISKWLRNIDE CCHHHHHHHHHCHHH	46.58	22790023
102	Acetylation	KSFENISKWLRNIDE CCHHHHHHHHHCHHH	46.58	23236377
129	Acetylation	NKCDMDDKRVVPKGK CCCCCCCCCCCCCCC	42.71	7970347
154	Ubiquitination	RFFETSAKANINIEK EEEECCCCCCCCHHH	41.56	22790023
177	Ubiquitination	ILRKTPVKEPNSENV HHHHCCCCCCCCCCC	69.52	22790023
181	Phosphorylation	TPVKEPNSENVDISS CCCCCCCCCCCCCCC	41.06	29472430
187	Phosphorylation	NSENVDISSGGGVTG CCCCCCCCCCCCCCC	20.61	25521595
188	Phosphorylation	SENVDISSGGGVTGW CCCCCCCCCCCCCCC	41.62	25521595
193	Phosphorylation	ISSGGGVTGWKSKCC CCCCCCCCCCCCCCC	40.37	28066266
199	Geranylgeranylation	VTGWKSKCC------ CCCCCCCCC------	4.26	-
200	Geranylgeranylation	TGWKSKCC------- CCCCCCCC-------	7.79	-

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
73	T	Phosphorylation	Kinase	LRRK2	Q5S006	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
73	T	Phosphorylation	Phosphorylation of Thr-73 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.	26824392

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RAB10_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RAB10_MOUSE !!

Drug and Disease Associations

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