RAB13_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAB13_MOUSE
• UniProt AC: Q9DD03
• Protein Name: Ras-related protein Rab-13
• Gene Name: Rab13
• Organism: Mus musculus (Mouse).
• Sequence Length: 202
• Subcellular Localization: Cell membrane ; Lipid-anchor ; Cytoplasmic side . Cytoplasmic vesicle membrane ; Lipid-anchor ; Cytoplasmic side . Cell junction, tight junction . Golgi apparatus, trans-Golgi network membrane . Recycling endosome membrane . Cell projection, lamellipodium
• 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 endocytic recycling and regulates the transport to the plasma membrane of transmembrane proteins like the tight junction protein OCLN/occludin. Thereby, it regulates the assembly and the activity of tight junctions. Moreover, it may also regulate tight junction assembly by activating the PKA signaling pathway and by reorganizing the actin cytoskeleton through the activation of the downstream effectors PRKACA and MICALL2 respectively. Through its role in tight junction assembly, may play a role in the establishment of Sertoli cell barrier. Plays also a role in angiogenesis through regulation of endothelial cells chemotaxis. Also involved in neurite outgrowth. Has also been proposed to play a role in post-Golgi membrane trafficking from the TGN to the recycling endosome. Finally, it has been involved in insulin-induced transport to the plasma membrane of the glucose transporter GLUT4 and therefore may play a role in glucose homeostasis..
• Protein Sequence: MAKAYDHLFKLLLIGDSGVGKTCLIIRFAEDNFNSTYISTIGIDFKIRTVDIEGKRIKLQVWDTAGQERFKTITTAYYRGAMGIILVYDITDEKSFENIQNWMKSIKENASAGVERLLLGNKCDMEAKRQVQREQAEKLAREHRIRFFETSAKSSVNVDEAFSSLARDILLKTGGRRSGTNSKPSSTGLKTSDKKKNKCLLG

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	---MAKAYDHLFKLL ---CHHHHHHHHHHH	11.82	24719451
17	Phosphorylation	KLLLIGDSGVGKTCL HHHHHCCCCCCCEEE	30.11	29472430
37	Phosphorylation	EDNFNSTYISTIGID CCCCCCCEEEEEEEE	7.84	29514104
77	Phosphorylation	FKTITTAYYRGAMGI HHHHHHHHHCCCCEE	7.51	29514104
178	Phosphorylation	LKTGGRRSGTNSKPS HHCCCCCCCCCCCCC	48.92	26824392
180	Phosphorylation	TGGRRSGTNSKPSST CCCCCCCCCCCCCCC	37.25	29472430
182	Phosphorylation	GRRSGTNSKPSSTGL CCCCCCCCCCCCCCC	45.86	23140645
185	Phosphorylation	SGTNSKPSSTGLKTS CCCCCCCCCCCCCCC	44.24	29514104
199	Methylation	SDKKKNKCLLG---- CCCCCCCCCCC----	5.47	-
199	Geranylgeranylation	SDKKKNKCLLG---- CCCCCCCCCCC----	5.47	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RAB13_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RAB13_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RAB13_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MILK2_MOUSE	Micall2	physical	16525024

Drug and Disease Associations

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