dbPTM

RAB3I_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RAB3I_MOUSE
UniProt AC	Q68EF0
Protein Name	Rab-3A-interacting protein
Gene Name	Rab3ip {ECO:0000312\|EMBL:AAH80289.1}
Organism	Mus musculus (Mouse).
Sequence Length	428
Subcellular Localization	Cytoplasm. Nucleus. Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Predominantly cytoplasmic but a small proportion colocalizes with SSX2 in the nucleus. Activation of protein kinase C results in redistribution to the periphery of lamellipo
Protein Description	Guanine nucleotide exchange factor (GEF) which may activate RAB8A and RAB8B. Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form. Mediates the release of GDP from RAB8A and RAB8B but not from RAB3A or RAB5. Modulates actin organization and promotes polarized transport of RAB8A-specific vesicles to the cell surface. Together with RAB11A, RAB8A, 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 (By similarity)..
Protein Sequence	MANDPLEGFHEVNLASPTSPDLLGVCDPGTQEQTTSPSVIYRPHPSTLCAAPLQANALDLSDLPTQPVYSSPRHFNCAEVSNISAHAPDPASSVPSAVASGLTKLTSRKDSCNAEREFLQGATITEASAGNDDIFGLSTDSLSRLRSPSVLEVREKGYERLKEELAKAQREAHKMVREANVKQATAEKQLKEAQGKIDVLQAEVAALKTLVLSSSPTSPTQEPLAAAKTPFKRGHTRNKSTSSAMGGSHQDLSVIQPIVKDCKEADLSLYNEFRSWKDEPTMDRTCPFLDKIYQEDIFPCLTFAKSELASAVLEAVENNTLSIEPVGLQPIRFVKASAVECGGPKKCALTGQSKPCRHRIRLGDSSCCYYISPFCRYRITSVCNFFTYIRYIQQGLVKQQDVDQMFWEVMQLRKEMSLAKLGYFKEEL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
69	Phosphorylation	DLPTQPVYSSPRHFN HCCCCCCCCCCCCCC	15.32	-
111	Phosphorylation	KLTSRKDSCNAEREF HHHCCCCCCHHHHHH	16.59	26239621
123	Phosphorylation	REFLQGATITEASAG HHHHHCCEEEECCCC	34.94	23984901
125	Phosphorylation	FLQGATITEASAGND HHHCCEEEECCCCCC	22.57	23984901
128	Phosphorylation	GATITEASAGNDDIF CCEEEECCCCCCCCC	30.40	23984901
138	Phosphorylation	NDDIFGLSTDSLSRL CCCCCCCCHHHHHCC	30.46	30352176
141	Phosphorylation	IFGLSTDSLSRLRSP CCCCCHHHHHCCCCC	28.47	23335269
143	Phosphorylation	GLSTDSLSRLRSPSV CCCHHHHHCCCCCCH	32.97	23335269
147	Phosphorylation	DSLSRLRSPSVLEVR HHHHCCCCCCHHHHH	26.56	24068923
149	Phosphorylation	LSRLRSPSVLEVREK HHCCCCCCHHHHHHH	40.35	26239621
191	Methylation	ATAEKQLKEAQGKID HHHHHHHHHHCCCHH	48.81	-
196	Methylation	QLKEAQGKIDVLQAE HHHHHCCCHHHHHHH	24.53	-
209	Phosphorylation	AEVAALKTLVLSSSP HHHHHHHHHHHCCCC	23.97	28833060
213	Phosphorylation	ALKTLVLSSSPTSPT HHHHHHHCCCCCCCC	22.69	28833060
214	Phosphorylation	LKTLVLSSSPTSPTQ HHHHHHCCCCCCCCC	35.85	25521595
215	Phosphorylation	KTLVLSSSPTSPTQE HHHHHCCCCCCCCCC	28.90	25521595
217	Phosphorylation	LVLSSSPTSPTQEPL HHHCCCCCCCCCCCH	49.65	24925903
218	Phosphorylation	VLSSSPTSPTQEPLA HHCCCCCCCCCCCHH	29.36	25521595
220	Phosphorylation	SSSPTSPTQEPLAAA CCCCCCCCCCCHHHC	45.38	25521595
229	Phosphorylation	EPLAAAKTPFKRGHT CCHHHCCCCCCCCCC	29.27	-
240	Phosphorylation	RGHTRNKSTSSAMGG CCCCCCCCCCCCCCC	36.75	25521595
241	Phosphorylation	GHTRNKSTSSAMGGS CCCCCCCCCCCCCCC	28.45	25521595
242	Phosphorylation	HTRNKSTSSAMGGSH CCCCCCCCCCCCCCH	24.16	25521595
243	Phosphorylation	TRNKSTSSAMGGSHQ CCCCCCCCCCCCCHH	23.51	27742792
248	Phosphorylation	TSSAMGGSHQDLSVI CCCCCCCCHHHHHHH	16.55	25521595
253	Phosphorylation	GGSHQDLSVIQPIVK CCCHHHHHHHHHHHC	26.01	25619855
335	Malonylation	LQPIRFVKASAVECG CCCEEEEEEEEEECC	33.63	32601280
423	Phosphorylation	MSLAKLGYFKEEL-- HHHHHHCCCHHCC--	23.16	25266776

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
240	S	Phosphorylation	Kinase	STK38	Q91VJ4	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RAB3I_MOUSE !!

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 RAB3I_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of RAB3I_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of RAB3I_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240 AND SER-242, ANDMASS SPECTROMETRY.	17242355 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-217, AND MASSSPECTROMETRY.	17114649 [Abstract]