RIC8B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RIC8B_HUMAN
• UniProt AC: Q9NVN3
• Protein Name: Synembryn-B
• Gene Name: RIC8B
• Organism: Homo sapiens (Human).
• Sequence Length: 520
• 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 by exchanging bound GDP for free GTP. Able to potentiate G(olf)-alpha-dependent cAMP accumulation suggesting that it may be an important component for odorant signal transduction..
• Protein Sequence: MDEERALYIVRAGEAGAIERVLRDYSDKHRATFKFESTDEDKRKKLCEGIFKVLIKDIPTTCQVSCLEVLRILSRDKKVLVPVTTKENMQILLRLAKLNELDDSLEKVSEFPVIVESLKCLCNIVFNSQMAQQLSLELNLAAKLCNLLRKCKDRKFINDIKCFDLRLLFLLSLLHTDIRSQLRYELQGLPLLTQILESAFSIKWTDEYESAIDHNGPPLSPQETDCAIEALKALFNVTVDSWKVHKESDSHQFRVMAAVLRHCLLIVGPTEDKTEELHSNAVNLLSNVPVSCLDVLICPLTHEETAQEATTLDELPSNKTAEKETVLKNNTMVYNGMNMEAIHVLLNFMEKRIDKGSSYREGLTPVLSLLTECSRAHRNIRKFLKDQVLPPLRDVTNRPEVGSTVRNKLVRLMTHVDLGVKQIAAEFLFVLCKERVDSLLKYTGYGNAAGLLAARGLLAGGRGDNWYSEDEDTDTEEYKNAKPKEELLKPMGLKPDGTITPLEEALNQYSVIEETSSDTD

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
37	Phosphorylation	RATFKFESTDEDKRK CEEEEEECCCHHHHH	44.27	-
38	Phosphorylation	ATFKFESTDEDKRKK EEEEEECCCHHHHHH	35.89	-
109	Phosphorylation	DDSLEKVSEFPVIVE CHHHHHHHCCHHHHH	44.58	23403867
201	Phosphorylation	QILESAFSIKWTDEY HHHHHCCCCCCCHHH	23.99	24719451
323	Acetylation	PSNKTAEKETVLKNN CCCCCCCCHHHHCCC	57.11	23236377
357	Phosphorylation	EKRIDKGSSYREGLT HHHCCCCCHHHCCCH	29.91	24719451
368	Phosphorylation	EGLTPVLSLLTECSR CCCHHHHHHHHHHHH	22.90	24719451
414	Phosphorylation	NKLVRLMTHVDLGVK HHHHHHHHHHCCCHH	24.28	-
438	Phosphorylation	LCKERVDSLLKYTGY HHHHHHHHHHHHCCC	32.51	24719451
443	Phosphorylation	VDSLLKYTGYGNAAG HHHHHHHCCCCCHHH	23.49	-
467	Phosphorylation	GGRGDNWYSEDEDTD CCCCCCCCCCCCCCC	14.40	26657352
468	Phosphorylation	GRGDNWYSEDEDTDT CCCCCCCCCCCCCCH	30.13	30175587
473	Phosphorylation	WYSEDEDTDTEEYKN CCCCCCCCCHHHHHH	42.65	22617229
475	Phosphorylation	SEDEDTDTEEYKNAK CCCCCCCHHHHHHCC	32.58	23663014
478	Phosphorylation	EDTDTEEYKNAKPKE CCCCHHHHHHCCCHH	11.87	23403867
509	Phosphorylation	LEEALNQYSVIEETS HHHHHHHCCHHHCCC	12.11	27251275
510	Phosphorylation	EEALNQYSVIEETSS HHHHHHCCHHHCCCC	13.57	27732954
515	Phosphorylation	QYSVIEETSSDTD-- HCCHHHCCCCCCC--	22.27	27732954
516	Phosphorylation	YSVIEETSSDTD--- CCHHHCCCCCCC---	29.51	27732954
517	Phosphorylation	SVIEETSSDTD---- CHHHCCCCCCC----	52.53	27732954
519	Phosphorylation	IEETSSDTD------ HHCCCCCCC------	45.62	27732954

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

Oops, there are no upstream regulatory protein records of RIC8B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RIC8B_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of RIC8B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GNAS3_HUMAN	GNAS	physical	12652642
GNAS2_HUMAN	GNAS	physical	12652642
ALEX_HUMAN	GNAS	physical	12652642
GNAS1_HUMAN	GNAS	physical	12652642
GNAQ_HUMAN	GNAQ	physical	12652642
GNAS3_HUMAN	GNAS	physical	28514442
GNAS2_HUMAN	GNAS	physical	28514442
ALEX_HUMAN	GNAS	physical	28514442
GNAS1_HUMAN	GNAS	physical	28514442

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-468 AND THR-473, ANDMASS SPECTROMETRY.
PubMed: 19690332