RAB35_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RAB35_MOUSE
• UniProt AC: Q6PHN9
• Protein Name: Ras-related protein Rab-35
• Gene Name: Rab35
• Organism: Mus musculus (Mouse).
• Sequence Length: 201
• Subcellular Localization: Cell membrane ; Lipid-anchor ; Cytoplasmic side . Membrane, clathrin-coated pit . Cytoplasmic vesicle, clathrin-coated vesicle . Endosome . Melanosome . Present on sorting endosomes and recycling endosome tubules. Tends to be enriched in PIP2-positiv
• 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 the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes..
• Protein Sequence: MARDYDHLFKLLIIGDSGVGKSSLLLRFADNTFSGSYITTIGVDFKIRTVEINGEKVKLQIWDTAGQERFRTITSTYYRGTHGVIVVYDVTSAESFVNVKRWLHEINQNCDDVCRILVGNKNDDPERKVVETEDAYKFAGQMGIQLFETSAKENVNVEEMFNCITELVLRAKKDNLAKQQQQQQNDVVKLTKNSKRKKRCC

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	---MARDYDHLFKLL ---CCCCHHHHEEEE	10.33	25367039
17	Phosphorylation	KLLIIGDSGVGKSSL EEEEECCCCCCCCHH	30.11	20469934
37	Phosphorylation	DNTFSGSYITTIGVD CCCCCCCEEEEEEEE	13.05	29514104
72	Phosphorylation	AGQERFRTITSTYYR CCHHHEEEEEEEECC	26.37	29125462
74	Phosphorylation	QERFRTITSTYYRGT HHHEEEEEEEECCCC	17.88	26643407
75	Phosphorylation	ERFRTITSTYYRGTH HHEEEEEEEECCCCC	15.57	26643407
75	Other	ERFRTITSTYYRGTH HHEEEEEEEECCCCC	15.57	-
76	Phosphorylation	RFRTITSTYYRGTHG HEEEEEEEECCCCCE	18.87	26643407
77	Phosphorylation	FRTITSTYYRGTHGV EEEEEEEECCCCCEE	7.31	26643407
78	Phosphorylation	RTITSTYYRGTHGVI EEEEEEECCCCCEEE	11.58	26643407
136	Phosphorylation	VVETEDAYKFAGQMG EEEHHHHHHHHHHHH	20.97	22817900
163	Glutathionylation	NVEEMFNCITELVLR CHHHHHHHHHHHHHH	2.52	24333276
178	Ubiquitination	AKKDNLAKQQQQQQN HHHHHHHHHHHHHHH	52.37	-
189	Ubiquitination	QQQNDVVKLTKNSKR HHHHHHHHHHHCCCC	50.73	-
200	Geranylgeranylation	NSKRKKRCC------ CCCCCCCCC------	4.42	-
201	Geranylgeranylation	SKRKKRCC------- CCCCCCCC-------	7.89	-

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	Q5S006	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RAB35_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 RAB35_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RAB35_MOUSE !!

Drug and Disease Associations

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