GNAT3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GNAT3_HUMAN
• UniProt AC: A8MTJ3
• Protein Name: Guanine nucleotide-binding protein G(t) subunit alpha-3
• Gene Name: GNAT3
• Organism: Homo sapiens (Human).
• Sequence Length: 354
• Subcellular Localization: Cytoplasm . Dual ditribution pattern; plasmalemmal pattern with apical region localization and cytosolic pattern with localization throughout the cytoplasm.
• Protein Description: Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction. Transduction by this alpha subunit involves coupling of specific cell-surface receptors with a cGMP-phosphodiesterase; Activation of phosphodiesterase lowers intracellular levels of cAMP and cGMP which may open a cyclic nucleotide-suppressible cation channel leading to influx of calcium, ultimately leading to release of neurotransmitter. Indeed, denatonium and strychnine induce transient reduction in cAMP and cGMP in taste tissue, whereas this decrease is inhibited by GNAT3 antibody. Gustducin heterotrimer transduces response to bitter and sweet compounds via regulation of phosphodiesterase for alpha subunit, as well as via activation of phospholipase C for beta and gamma subunits, with ultimate increase inositol trisphosphate and increase of intracellular Calcium. GNAT3 can functionally couple to taste receptors to transmit intracellular signal: receptor heterodimer TAS1R2/TAS1R3 senses sweetness and TAS1R1/TAS1R3 transduces umami taste, whereas the T2R family GPCRs act as bitter sensors. Functions also as lumenal sugar sensors in the gut to control the expression of the Na+-glucose transporter SGLT1 in response to dietaty sugar, as well as the secretion of Glucagon-like peptide-1, GLP-1 and glucose-dependent insulinotropic polypeptide, GIP. Thus, may modulate the gut capacity to absorb sugars, with implications in malabsorption syndromes and diet-related disorders including diabetes and obesity..
• Protein Sequence: MGSGISSESKESAKRSKELEKKLQEDAERDARTVKLLLLGAGESGKSTIVKQMKIIHKNGYSEQECMEFKAVIYSNTLQSILAIVKAMTTLGIDYVNPRSAEDQRQLYAMANTLEDGGMTPQLAEVIKRLWRDPGIQACFERASEYQLNDSAAYYLNDLDRITASGYVPNEQDVLHSRVKTTGIIETQFSFKDLHFRMFDVGGQRSERKKWIHCFEGVTCIIFCAALSAYDMVLVEDEEVNRMHESLHLFNSICNHKYFSTTSIVLFLNKKDIFQEKVTKVHLSICFPEYTGPNTFEDAGNYIKNQFLDLNLKKEDKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF

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	Myristoylation	------MGSGISSES ------CCCCCCHHH	34.28	-
35	Acetylation	ERDARTVKLLLLGAG HHHHHHHHHHHHCCC	32.57	163903
44	Phosphorylation	LLLGAGESGKSTIVK HHHCCCCCCCHHHHH	51.07	20873877
46	Ubiquitination	LGAGESGKSTIVKQM HCCCCCCCHHHHHHE	54.42	21890473
46	Ubiquitination	LGAGESGKSTIVKQM HCCCCCCCHHHHHHE	54.42	23000965
47	Phosphorylation	GAGESGKSTIVKQMK CCCCCCCHHHHHHEE	27.22	20873877
48	Phosphorylation	AGESGKSTIVKQMKI CCCCCCHHHHHHEEE	33.02	29514088
51	Ubiquitination	SGKSTIVKQMKIIHK CCCHHHHHHEEEECC	40.60	23000965
54	Ubiquitination	STIVKQMKIIHKNGY HHHHHHEEEECCCCC	35.69	22817900
89	Phosphorylation	LAIVKAMTTLGIDYV HHHHHHHHHCCCCCC	24.59	-
90	Phosphorylation	AIVKAMTTLGIDYVN HHHHHHHHCCCCCCC	15.20	-
95	Phosphorylation	MTTLGIDYVNPRSAE HHHCCCCCCCCCCHH	10.54	-
108	Phosphorylation	AEDQRQLYAMANTLE HHHHHHHHHHHHCHH	5.98	21214269
113	Phosphorylation	QLYAMANTLEDGGMT HHHHHHHCHHCCCCC	23.22	21214269
155	Phosphorylation	LNDSAAYYLNDLDRI CCCCHHHHCCCHHHE	8.36	-
190	Phosphorylation	GIIETQFSFKDLHFR CEEEEEEEECCCEEE	22.90	24719451
206	Phosphorylation	FDVGGQRSERKKWIH EECCCCCCCHHHHCH	33.59	23401153
321	Phosphorylation	KEDKEIYSHMTCATD CCCHHHHHHCCCCCC	16.67	22210691
327	Phosphorylation	YSHMTCATDTQNVKF HHHCCCCCCCCCCCC	41.55	22210691
345	Ubiquitination	AVTDIIIKENLKDCG HHHHHHHHHHHCCCC	30.09	32015554

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

Oops, there are no upstream regulatory protein records of GNAT3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GNAT3_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 GNAT3_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of GNAT3_HUMAN !!

Drug and Disease Associations

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