RIC8_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RIC8_DROME
• UniProt AC: Q9W358
• Protein Name: Synembryn
• Gene Name: ric8a
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 573
• Subcellular Localization: Cytoplasm, cell cortex . Localizes to the cell cortex.
• Protein Description: Guanine nucleotide exchange factor (GEF), which can activate some, but not all, G-alpha proteins independently of G-protein coupled receptors. Acts by exchanging bound GDP for free GTP. Plays a key role in asymmetric spindle positioning, a step for asymmetric cell division that generates cell diversity during development by activating G(i) alpha protein independently of G-protein coupled receptors. In addition to its GEF activity, it plays an essential role in cortical subcellular localization of heterotrimeric G proteins, suggesting it acts as a facilitator of G-alpha function through control of its membrane targeting and/or assembling of associated components rather than a GEF. Also required during gastrulation and sensory organ precursors (SOP) formation..
• Protein Sequence: METEHLKRLEAKEADHIPAILDEFNTKNADLLVFDSFRTDNLWHELWLAIFGILDDQRLSHLHTQCLNTVRILTRDEFSLQTNYIEQEVNTLLKLARIEAGSLKLPATPDELKQEEREEPQLEPSQAQSEVIAEALKCLCNLVYQSSDCRRQCLRQHCLDAILKRVASSMRHPCALEYYDMKLLFLLTALEPAARSRLQIDLNGLTYMTKWLDDKLGEDSVGEEQLNIICELLKVMFNVTSAPDKSPNEYEIQSLHLTGVLRELLLRFGDLATEKDRAVVTHAINLLTNISGSCLTELTLRCSNAELESHKEREQDNEKEKDTEAGAGAKPRECCSQCFEKRNVRSLDVLLRYLRQSLAQQEAEASSHELLSPVLTVLVKCARSDRVMRHYLRQEILPPLRDVSQRPEVGQELRNHLCRFLTLPAMILRDLSAELLFVLCKENVGRMIKYTGYGNAAGLFAKRGILDCRRVEGTDYSSDSEDSDTEEYKQQQQGINPVLGCVEPRSKSHLDDISEEQKEYEAMQLVNLIEQLRQGGIVKPAMIDKDGRPQPLEHILQLQEELPQQQLDQKRKT

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
102	Phosphorylation	LARIEAGSLKLPATP HHHHHHCCCCCCCCH	29.40	22817900
108	Phosphorylation	GSLKLPATPDELKQE CCCCCCCCHHHHHHH	29.36	19429919
476	Phosphorylation	RRVEGTDYSSDSEDS EEECCCCCCCCCCCC	15.20	19429919
477	Phosphorylation	RVEGTDYSSDSEDSD EECCCCCCCCCCCCC	30.40	19429919
478	Phosphorylation	VEGTDYSSDSEDSDT ECCCCCCCCCCCCCH	38.64	19429919
480	Phosphorylation	GTDYSSDSEDSDTEE CCCCCCCCCCCCHHH	45.30	19429919
483	Phosphorylation	YSSDSEDSDTEEYKQ CCCCCCCCCHHHHHH	42.24	19429919
485	Phosphorylation	SDSEDSDTEEYKQQQ CCCCCCCHHHHHHHH	34.37	19429919
506	Phosphorylation	LGCVEPRSKSHLDDI HHCCCCCCHHHCCCC	49.58	19429919
508	Phosphorylation	CVEPRSKSHLDDISE CCCCCCHHHCCCCCH	30.45	19429919
520	Phosphorylation	ISEEQKEYEAMQLVN CCHHHHHHHHHHHHH	18.94	19429919
539	Acetylation	LRQGGIVKPAMIDKD HHCCCCCCCCEECCC	25.74	21791702

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

Oops, there are no upstream regulatory protein records of RIC8_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RIC8_DROME !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RIC8_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CSN4_DROME	CSN4	physical	14605208
GNAL_DROME	cta	physical	24006487
GNAI_DROME	Galphai	physical	16228011
GNAI_DROME	Galphai	physical	16228012

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477; SER-478; SER-480AND SER-483, AND MASS SPECTROMETRY.
PubMed: 18327897