GNAI1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GNAI1_MOUSE
• UniProt AC: B2RSH2
• Protein Name: Guanine nucleotide-binding protein G(i) subunit alpha-1
• Gene Name: Gnai1
• Organism: Mus musculus (Mouse).
• Sequence Length: 354
• Subcellular Localization: Nucleus . Cytoplasm . Cell membrane ; Peripheral membrane protein ; Cytoplasmic side . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cell cortex . Membrane ; Lipid-anchor . Localizes in the centrosomes of interphase
• Protein Description: Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins (By similarity). Signaling is mediated via effector proteins, such as adenylate cyclase. Inhibits adenylate cyclase activity, leading to decreased intracellular cAMP levels (By similarity). The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. Required for normal cytokinesis during mitosis. Required for cortical dynein-dynactin complex recruitment during metaphase (By similarity)..
• Protein Sequence: MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF

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	------MGCTLSAED ------CCCCCCHHH	17.08	-
3	S-palmitoylation	-----MGCTLSAEDK -----CCCCCCHHHH	3.14	-
17	Ubiquitination	KAAVERSKMIDRNLR HHHHHHHHHHCHHHH	46.20	27667366
29	Ubiquitination	NLREDGEKAAREVKL HHHHHHHHHHHHHHH	53.53	22790023
35	Ubiquitination	EKAAREVKLLLLGAG HHHHHHHHHHEECCC	28.76	-
35	Acetylation	EKAAREVKLLLLGAG HHHHHHHHHHEECCC	28.76	-
44	Phosphorylation	LLLGAGESGKSTIVK HEECCCCCCCHHHHH	51.07	22817900
46	Ubiquitination	LGAGESGKSTIVKQM ECCCCCCCHHHHHHH	54.42	27667366
47	Phosphorylation	GAGESGKSTIVKQMK CCCCCCCHHHHHHHH	27.22	29899451
48	Phosphorylation	AGESGKSTIVKQMKI CCCCCCHHHHHHHHH	33.02	-
51	Ubiquitination	SGKSTIVKQMKIIHE CCCHHHHHHHHHHHH	40.60	27667366
54	Ubiquitination	STIVKQMKIIHEAGY HHHHHHHHHHHHCCC	35.69	22790023
67	Ubiquitination	GYSEEECKQYKAVVY CCCHHHHHHCCCHHC	61.00	22790023
92	Ubiquitination	IRAMGRLKIDFGDSA HHHHCCCCCCCCCCC	38.58	22790023
98	Phosphorylation	LKIDFGDSARADDAR CCCCCCCCCCHHHHH	21.75	20415495
128	Acetylation	AELAGVIKRLWKDSG HHHHHHHHHHHHCCC	38.75	15604649
132	Ubiquitination	GVIKRLWKDSGVQAC HHHHHHHHCCCHHHH	46.75	22790023
167	Nitration	DRIAQPNYIPTQQDV HHHCCCCCCCCHHHH	18.24	-
180	Ubiquitination	DVLRTRVKTTGIVET HHHHHHHCCCCEEEE	36.76	-
187	Phosphorylation	KTTGIVETHFTFKDL CCCCEEEEEEEECCE	16.05	-
190	Phosphorylation	GIVETHFTFKDLHFK CEEEEEEEECCEEEE	23.36	-
192	Ubiquitination	VETHFTFKDLHFKMF EEEEEEECCEEEEEE	57.21	-
197	Ubiquitination	TFKDLHFKMFDVGGQ EECCEEEEEEECCCC	28.10	-
206	Phosphorylation	FDVGGQRSERKKWIH EECCCCCCCHHHHHH	33.59	22817900
248	Ubiquitination	NRMHESMKLFDSICN HHHHHHHHHHHHHHC	56.11	-
252	Phosphorylation	ESMKLFDSICNNKWF HHHHHHHHHHCCCCC	23.00	22324799
271	Ubiquitination	IILFLNKKDLFEEKI EEEEEEHHHHHHHHH	59.60	27667366
277	Ubiquitination	KKDLFEEKIKKSPLT HHHHHHHHHHCCCCE	53.26	27667366
290	Phosphorylation	LTICYPEYAGSNTYE CEEECCCCCCCCCHH	16.26	-
293	Phosphorylation	CYPEYAGSNTYEEAA ECCCCCCCCCHHHHH	20.16	-
312	Ubiquitination	CQFEDLNKRKDTKEI HHHHHHHCCCCCCCE	69.03	-
345	Ubiquitination	AVTDVIIKNNLKDCG HHHHHHHHCCCCCCC	28.76	-
349	Ubiquitination	VIIKNNLKDCGLF-- HHHHCCCCCCCCC--	53.77	-
351	S-palmitoylation	IKNNLKDCGLF---- HHCCCCCCCCC----	4.95	28680068

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

Oops, there are no upstream regulatory protein records of GNAI1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
2	G	Myristoylation	Myristoylation at Gly-2 is required for membrane anchoring before palmitoylation.	-
2	G	Palmitoylation	Myristoylation at Gly-2 is required for membrane anchoring before palmitoylation.	-
3	C	Palmitoylation	Palmitoylation at Cys-3 varies with membrane lipid composition.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of GNAI1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of GNAI1_MOUSE !!

Drug and Disease Associations

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