GNAO_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GNAO_RAT
• UniProt AC: P59215
• Protein Name: Guanine nucleotide-binding protein G(o) subunit alpha
• Gene Name: Gnao1
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 354
• Subcellular Localization: Cell membrane . Membrane ; Lipid-anchor .
• Protein Description: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(o) protein function is not clear. Stimulated by RGS14 (By similarity)..
• Protein Sequence: MGCTLSAEERAALERSKAIEKNLKEDGISAAKDVKLLLLGAGESGKSTIVKQMKIIHEDGFSGEDVKQYKPVVYSNTIQSLAAIVRAMDTLGVEYGDKERKADSKMVCDVVSRMEDTEPFSAELLSAMMRLWGDSGIQECFNRSREYQLNDSAKYYLDSLDRIGAADYQPTEQDILRTRVKTTGIVETHFTFKNLHFRLFDVGGQRSERKKWIHCFEDVTAIIFCVALSGYDQVLHEDETTNRMHESLMLFDSICNNKFFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYPGSNTYEDAAAYIQTQFESKNRSPNKEIYCHMTCATDTNNIQVVFDAVTDIIIANNLRGCGLY

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	N-myristoyl glycine	------MGCTLSAEE ------CCCCCCHHH	17.08	-
2	Myristoylation	------MGCTLSAEE ------CCCCCCHHH	17.08	8484716
3	S-palmitoylation	-----MGCTLSAEER -----CCCCCCHHHH	3.14	8146194
21	Ubiquitination	ERSKAIEKNLKEDGI HHHHHHHHHHHHCCC	62.56	-
24	Acetylation	KAIEKNLKEDGISAA HHHHHHHHHCCCCHH	64.25	22902405
24	Ubiquitination	KAIEKNLKEDGISAA HHHHHHHHHCCCCHH	64.25	-
29	Phosphorylation	NLKEDGISAAKDVKL HHHHCCCCHHHHHEE	27.92	25403869
32	Ubiquitination	EDGISAAKDVKLLLL HCCCCHHHHHEEEEE	63.87	-
32	Acetylation	EDGISAAKDVKLLLL HCCCCHHHHHEEEEE	63.87	22902405
35	Acetylation	ISAAKDVKLLLLGAG CCHHHHHEEEEECCC	43.48	22902405
35	Ubiquitination	ISAAKDVKLLLLGAG CCHHHHHEEEEECCC	43.48	-
46	Ubiquitination	LGAGESGKSTIVKQM ECCCCCCCCHHHEEE	54.42	-
51	Ubiquitination	SGKSTIVKQMKIIHE CCCCHHHEEEEEECC	40.60	-
54	Acetylation	STIVKQMKIIHEDGF CHHHEEEEEECCCCC	35.69	22902405
54	Ubiquitination	STIVKQMKIIHEDGF CHHHEEEEEECCCCC	35.69	-
62	Phosphorylation	IIHEDGFSGEDVKQY EECCCCCCCCHHHHH	46.96	25403869
67	Ubiquitination	GFSGEDVKQYKPVVY CCCCCHHHHHCCEEE	61.30	-
69	Phosphorylation	SGEDVKQYKPVVYSN CCCHHHHHCCEEEHH	16.13	-
70	Ubiquitination	GEDVKQYKPVVYSNT CCHHHHHCCEEEHHH	28.92	-
74	Phosphorylation	KQYKPVVYSNTIQSL HHHCCEEEHHHHHHH	9.09	-
75	Phosphorylation	QYKPVVYSNTIQSLA HHCCEEEHHHHHHHH	18.85	-
95	Phosphorylation	MDTLGVEYGDKERKA HHHHCCCCCCCCCCC	28.37	-
98	Acetylation	LGVEYGDKERKADSK HCCCCCCCCCCCCCC	55.87	22902405
98	Ubiquitination	LGVEYGDKERKADSK HCCCCCCCCCCCCCC	55.87	-
101	Acetylation	EYGDKERKADSKMVC CCCCCCCCCCCCEEH	58.60	22902405
101	Ubiquitination	EYGDKERKADSKMVC CCCCCCCCCCCCEEH	58.60	-
105	Ubiquitination	KERKADSKMVCDVVS CCCCCCCCEEHHHHH	35.58	-
105	Acetylation	KERKADSKMVCDVVS CCCCCCCCEEHHHHH	35.58	22902405
140	S-nitrosylation	GDSGIQECFNRSREY CCCHHHHHHHHCCCC	1.78	22178444
140	S-nitrosocysteine	GDSGIQECFNRSREY CCCHHHHHHHHCCCC	1.78	-
144	Phosphorylation	IQECFNRSREYQLND HHHHHHHCCCCCCCC	30.48	-
147	Phosphorylation	CFNRSREYQLNDSAK HHHHCCCCCCCCHHH	19.72	-
154	Ubiquitination	YQLNDSAKYYLDSLD CCCCCHHHHHHHCHH	38.08	-
154	Acetylation	YQLNDSAKYYLDSLD CCCCCHHHHHHHCHH	38.08	22902405
155	Phosphorylation	QLNDSAKYYLDSLDR CCCCHHHHHHHCHHH	14.69	-
156	Phosphorylation	LNDSAKYYLDSLDRI CCCHHHHHHHCHHHC	11.88	-
159	Phosphorylation	SAKYYLDSLDRIGAA HHHHHHHCHHHCCCC	29.58	22673903
168	Phosphorylation	DRIGAADYQPTEQDI HHCCCCCCCCCHHHH	16.21	-
181	Ubiquitination	DILRTRVKTTGIVET HHHHHHHCCCCEEEE	36.76	-
205	Formation of an isopeptide bond	RLFDVGGQRSERKKW EEEECCCCCCCHHHH	39.54	-
207	Phosphorylation	FDVGGQRSERKKWIH EECCCCCCCHHHHCH	33.59	27097102
253	Phosphorylation	ESLMLFDSICNNKFF HHHHHHHHHHCCCEE	23.00	27097102
272 (in isoform 2)	Acetylation	-	59.60	-
272	Ubiquitination	IILFLNKKDLFGEKI HEEEEEHHHHCCCHH	59.60	-
278	Acetylation	KKDLFGEKIKKSPLT HHHHCCCHHCCCCCE	61.27	22902405
297	Phosphorylation	EYPGSNTYEDAAAYI CCCCCCCHHHHHHHH	18.96	-
346	Deamidated asparagine	VTDIIIANNLRGCGL HHHHEEECCCCCCCC	37.35	-
346	Deamidation	VTDIIIANNLRGCGL HHHHEEECCCCCCCC	37.35	9990023

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

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
346	N	Amidation	Deamidation of Asn-346 converts alpha-1 to alpha-3.	9990023

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ZBT16_HUMAN	ZBTB16	physical	18262754

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Deamidation

"Posttranslational modification of Galphao1 generates Galphao3, anabundant G protein in brain.";
Exner T., Jensen O.N., Mann M., Kleuss C., Nurnberg B.;
Proc. Natl. Acad. Sci. U.S.A. 96:1327-1332(1999).
Cited for: DEAMIDATION AT ASN-346.
PubMed: 9990023

Myristoylation

"A novel N-terminal motif for palmitoylation of G-protein alphasubunits.";
Parenti M., Vigano M.A., Newman C.M.H., Milligan G., Magee A.I.;
Biochem. J. 291:349-353(1993).
Cited for: MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-3, AND ABSENCE OFPALMITOYLATION AT CYS-351.
PubMed: 8484716

Palmitoylation

"A novel N-terminal motif for palmitoylation of G-protein alphasubunits.";
Parenti M., Vigano M.A., Newman C.M.H., Milligan G., Magee A.I.;
Biochem. J. 291:349-353(1993).
Cited for: MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-3, AND ABSENCE OFPALMITOYLATION AT CYS-351.
PubMed: 8484716