RB11B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RB11B_MOUSE
• UniProt AC: P46638
• Protein Name: Ras-related protein Rab-11B
• Gene Name: Rab11b
• Organism: Mus musculus (Mouse).
• Sequence Length: 218
• Subcellular Localization: Recycling endosome membrane ; Lipid-anchor ; Cytoplasmic side . Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmic vesicle, phagosome membrane; Lipid-anchor; Cytoplasmic side. Recruited to p
• 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. That Rab plays a role in endocytic recycling, regulating apical recycling of several transmembrane proteins including cystic fibrosis transmembrane conductance regulator/CFTR, epithelial sodium channel/ENaC, potassium voltage-gated channel, and voltage-dependent L-type calcium channel. May also regulate constitutive and regulated secretion, like insulin granule exocytosis. Required for melanosome transport and release from melanocytes. Also regulates V-ATPase intracellular transport in response to extracellular acidosis..
• Protein Sequence: MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNNLSFIETSALDSTNVEEAFKNILTEIYRIVSQKQIADRAAHDESPGNNVVDISVPPTTDGQRPNKLQCCQSL

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
2	Acetylation	------MGTRDDEYD ------CCCCHHHCC	29.47	-
3	Phosphorylation	-----MGTRDDEYDY -----CCCCHHHCCE	29.62	22499769
4	Citrullination	----MGTRDDEYDYL ----CCCCHHHCCEE	43.59	-
4	Citrullination	----MGTRDDEYDYL ----CCCCHHHCCEE	43.59	24463520
8	Phosphorylation	MGTRDDEYDYLFKVV CCCCHHHCCEEEEEE	19.51	22499769
10	Phosphorylation	TRDDEYDYLFKVVLI CCHHHCCEEEEEEEE	17.09	28066266
20	Phosphorylation	KVVLIGDSGVGKSNL EEEEECCCCCCHHHH	30.11	25338131
24	Succinylation	IGDSGVGKSNLLSRF ECCCCCCHHHHHHHH	33.49	23806337
24	Acetylation	IGDSGVGKSNLLSRF ECCCCCCHHHHHHHH	33.49	23806337
24	Ubiquitination	IGDSGVGKSNLLSRF ECCCCCCHHHHHHHH	33.49	-
40	Phosphorylation	RNEFNLESKSTIGVE CCCCCCCCCCEEEEE	34.76	-
42	Phosphorylation	EFNLESKSTIGVEFA CCCCCCCCEEEEEEE	34.24	26824392
43	Phosphorylation	FNLESKSTIGVEFAT CCCCCCCEEEEEEEE	26.03	19060867
52	Phosphorylation	GVEFATRSIQVDGKT EEEEEEEEEEECCEE	17.02	-
73	Phosphorylation	DTAGQERYRAITSAY CCCCHHHHHHHHHHH	12.02	29514104
77	Phosphorylation	QERYRAITSAYYRGA HHHHHHHHHHHHHHH	13.30	26745281
78	Phosphorylation	ERYRAITSAYYRGAV HHHHHHHHHHHHHHH	14.25	26824392
80	Phosphorylation	YRAITSAYYRGAVGA HHHHHHHHHHHHHHH	8.08	28066266
115	Phosphorylation	ELRDHADSNIVIMLV HHHHCCCCCEEEEEE	29.28	22817900
145	Ubiquitination	EARAFAEKNNLSFIE HHHHHHHHCCCCEEE	47.94	22790023
179	Ubiquitination	IYRIVSQKQIADRAA HHHHHCHHHHHHHHC	35.84	22790023
190	Phosphorylation	DRAAHDESPGNNVVD HHHCCCCCCCCCEEE	44.13	25521595
214	Geranylgeranylation	QRPNKLQCCQSL--- CCCCCCCCCCCC---	3.10	-
215	Methylation	RPNKLQCCQSL---- CCCCCCCCCCC----	1.66	-
215	Geranylgeranylation	RPNKLQCCQSL---- CCCCCCCCCCC----	1.66	-

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

Oops, there are no upstream regulatory protein records of RB11B_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RB11B_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 RB11B_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of RB11B_MOUSE !!

Drug and Disease Associations

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