dbPTM

GNAI1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GNAI1_HUMAN
UniProt AC	P63096
Protein Name	Guanine nucleotide-binding protein G(i) subunit alpha-1
Gene Name	GNAI1
Organism	Homo sapiens (Human).
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. [PubMed: 8774883]
Protein Sequence	MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	N-myristoyl glycine	------MGCTLSAED ------CCCCCCHHH	17.08	-
2	Myristoylation	------MGCTLSAED ------CCCCCCHHH	17.08	20213681
3	S-palmitoylation	-----MGCTLSAEDK -----CCCCCCHHHH	3.14	-
15	Ubiquitination	EDKAAVERSKMIDRN HHHHHHHHHHHHCHH	34.67	30230243
17	Ubiquitination	KAAVERSKMIDRNLR HHHHHHHHHHCHHHH	46.20	-
29	Ubiquitination	NLREDGEKAAREVKL HHHHHHHHHHHHHHH	53.53	21906983
35	Ubiquitination	EKAAREVKLLLLGAG HHHHHHHHHHEECCC	28.76	21906983
40	Ubiquitination	EVKLLLLGAGESGKS HHHHHEECCCCCCCH	31.35	23000965
40	Ubiquitination	EVKLLLLGAGESGKS HHHHHEECCCCCCCH	31.35	21890473
44	Phosphorylation	LLLGAGESGKSTIVK HEECCCCCCCHHHHH	51.07	20873877
46	Ubiquitination	LGAGESGKSTIVKQM ECCCCCCCHHHHHHH	54.42	23000965
47	Phosphorylation	GAGESGKSTIVKQMK CCCCCCCHHHHHHHH	27.22	20873877
48	Phosphorylation	AGESGKSTIVKQMKI CCCCCCHHHHHHHHH	33.02	29514088
51	Ubiquitination	SGKSTIVKQMKIIHE CCCHHHHHHHHHHHH	40.60	23000965
54	Ubiquitination	STIVKQMKIIHEAGY HHHHHHHHHHHHCCC	35.69	22817900
61	Phosphorylation	KIIHEAGYSEEECKQ HHHHHCCCCHHHHHH	21.69	28152594
62	Phosphorylation	IIHEAGYSEEECKQY HHHHCCCCHHHHHHC	37.30	28152594
67	Acetylation	GYSEEECKQYKAVVY CCCHHHHHHCCCHHC	61.00	26051181
67	Ubiquitination	GYSEEECKQYKAVVY CCCHHHHHHCCCHHC	61.00	30230243
76	Ubiquitination	YKAVVYSNTIQSIIA CCCHHCCHHHHHHHH	24.42	23000965
80	Ubiquitination	VYSNTIQSIIAIIRA HCCHHHHHHHHHHHH	16.47	23000965
92	Ubiquitination	IRAMGRLKIDFGDSA HHHHCCCCCCCCCCC	38.58	21890473
92	Ubiquitination	IRAMGRLKIDFGDSA HHHHCCCCCCCCCCC	38.58	23000965
98	Phosphorylation	LKIDFGDSARADDAR CCCCCCCCCCHHHHH	21.75	29759185
128	Ubiquitination	AELAGVIKRLWKDSG HHHHHHHHHHHHCCC	38.75	23000965
132	Ubiquitination	GVIKRLWKDSGVQAC HHHHHHHHCCCHHHH	46.75	23000965
140	Ubiquitination	DSGVQACFNRSREYQ CCCHHHHHHCCCCEE	10.76	23000965
140	Ubiquitination	DSGVQACFNRSREYQ CCCHHHHHHCCCCEE	10.76	21890473
143	Phosphorylation	VQACFNRSREYQLND HHHHHHCCCCEECCC	30.48	28152594
145	Ubiquitination	ACFNRSREYQLNDSA HHHHCCCCEECCCCH	38.59	21890473
145	Ubiquitination	ACFNRSREYQLNDSA HHHHCCCCEECCCCH	38.59	21890473
146	Phosphorylation	CFNRSREYQLNDSAA HHHCCCCEECCCCHH	19.72	28152594
151	Phosphorylation	REYQLNDSAAYYLND CCEECCCCHHHHHCC	17.46	28152594
155	Phosphorylation	LNDSAAYYLNDLDRI CCCCHHHHHCCHHHH	8.36	-
178	ADP-ribosylation	QQDVLRTRVKTTGIV HHHHHHHHHCCCCEE	22.85	-
178	ADP-ribosylation	QQDVLRTRVKTTGIV HHHHHHHHHCCCCEE	22.85	-
180	Ubiquitination	DVLRTRVKTTGIVET HHHHHHHCCCCEEEE	36.76	30230243
192	Ubiquitination	VETHFTFKDLHFKMF EEEEEEECCEEEEEE	57.21	23000965
192	Ubiquitination	VETHFTFKDLHFKMF EEEEEEECCEEEEEE	57.21	21890473
196	Ubiquitination	FTFKDLHFKMFDVGG EEECCEEEEEEECCC	8.79	23000965
196	Ubiquitination	FTFKDLHFKMFDVGG EEECCEEEEEEECCC	8.79	21890473
197	Ubiquitination	TFKDLHFKMFDVGGQ EECCEEEEEEECCCC	28.10	23000965
197	Ubiquitination	TFKDLHFKMFDVGGQ EECCEEEEEEECCCC	28.10	21890473
204	Deamidation	KMFDVGGQRSERKKW EEEECCCCCCCHHHH	39.54	24141704
204	Deamidated glutamine	KMFDVGGQRSERKKW EEEECCCCCCCHHHH	39.54	-
206	Phosphorylation	FDVGGQRSERKKWIH EECCCCCCCHHHHHH	33.59	23401153
225	Ubiquitination	VTAIIFCVALSDYDL HHHHHHHHHCCCCCE	4.12	21890473
225	Ubiquitination	VTAIIFCVALSDYDL HHHHHHHHHCCCCCE	4.12	21890473
227	Ubiquitination	AIIFCVALSDYDLVL HHHHHHHCCCCCEEE	1.67	22817900
228	Ubiquitination	IIFCVALSDYDLVLA HHHHHHCCCCCEEEC	25.12	22817900
248	Ubiquitination	NRMHESMKLFDSICN HHHHHHHHHHHHHHC	56.11	21890473
248	Ubiquitination	NRMHESMKLFDSICN HHHHHHHHHHHHHHC	56.11	23000965
252	Phosphorylation	ESMKLFDSICNNKWF HHHHHHHHHHCCCCC	23.00	20873877
260	Ubiquitination	ICNNKWFTDTSIILF HHCCCCCCCCEEEEE	36.93	32142685
260	Phosphorylation	ICNNKWFTDTSIILF HHCCCCCCCCEEEEE	36.93	28857561
262	Phosphorylation	NNKWFTDTSIILFLN CCCCCCCCEEEEEEE	20.83	28857561
265	Ubiquitination	WFTDTSIILFLNKKD CCCCCEEEEEEEHHH	1.92	33845483
271	Ubiquitination	IILFLNKKDLFEEKI EEEEEEHHHHHHHHH	59.60	-
277	Ubiquitination	KKDLFEEKIKKSPLT HHHHHHHHHHCCCCE	53.26	21890473
277	Ubiquitination	KKDLFEEKIKKSPLT HHHHHHHHHHCCCCE	53.26	21890473
278	Ubiquitination	KDLFEEKIKKSPLTI HHHHHHHHHCCCCEE	8.43	33845483
279	Ubiquitination	DLFEEKIKKSPLTIC HHHHHHHHCCCCEEE	59.26	22817900
280	Ubiquitination	LFEEKIKKSPLTICY HHHHHHHCCCCEEEC	61.86	22817900
293	Ubiquitination	CYPEYAGSNTYEEAA ECCCCCCCCCHHHHH	20.16	33845483
297	Ubiquitination	YAGSNTYEEAAAYIQ CCCCCCHHHHHHHHH	38.84	33845483
312	Ubiquitination	CQFEDLNKRKDTKEI HHHHHHHCCCCCCCE	69.03	32142685
317	Ubiquitination	LNKRKDTKEIYTHFT HHCCCCCCCEECEEE	52.85	33845483
320	Phosphorylation	RKDTKEIYTHFTCAT CCCCCCEECEEEECC	8.68	28152594
330	Ubiquitination	FTCATDTKNVQFVFD EEECCCCCCCEEEHH	58.91	33845483
345	Ubiquitination	AVTDVIIKNNLKDCG HHHHHHHHCCCCCCC	28.76	33845483
349	Ubiquitination	VIIKNNLKDCGLF-- HHHHCCCCCCCCC--	53.77	33845483
351	ADP-ribosylation	IKNNLKDCGLF---- HHCCCCCCCCC----	4.95	-
351	ADP-ribosylation	IKNNLKDCGLF---- HHCCCCCCCCC----	4.95	-
351	S-palmitoylation	IKNNLKDCGLF---- HHCCCCCCCCC----	4.95	29575903

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of GNAI1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
2	G	Myristoylation	20213681
Myristoylation at Gly-2 is required for membrane anchoring before palmitoylation.
2	G	Palmitoylation	20213681
Myristoylation at Gly-2 is required for membrane anchoring before palmitoylation.
3	C	Palmitoylation	-
Palmitoylation at Cys-3 varies with membrane lipid composition.
204	Q	Amidation	24141704
(Microbial infection) Deamidated at Gln-204 by Photorhabdus asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby activating RhoA.

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of GNAI1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GPSM3_HUMAN	GPSM3	physical	14656218
GPSM1_HUMAN	GPSM1	physical	14530282
NGB_HUMAN	NGB	physical	12860983
ADCY5_HUMAN	ADCY5	physical	9748257
RGS14_HUMAN	RGS14	physical	11387333
RGS12_HUMAN	RGS12	physical	11387333
IGF1R_HUMAN	IGF1R	physical	10644671
RGS10_HUMAN	RGS10	physical	9207071
PRGR_HUMAN	PGR	physical	16484338
RGS14_HUMAN	RGS14	physical	19899154
PTH1R_HUMAN	PTH1R	physical	16099817
GNAI3_HUMAN	GNAI3	physical	22939629
GNAI2_HUMAN	GNAI2	physical	22939629
NCF1_HUMAN	NCF1	physical	16782902
NCF2_HUMAN	NCF2	physical	16782902
NUCB1_HUMAN	NUCB1	physical	21988832
RAGP1_HUMAN	RANGAP1	physical	21988832
RGS14_HUMAN	RGS14	physical	21988832
RIC8A_HUMAN	RIC8A	physical	21988832
THAP7_HUMAN	THAP7	physical	21988832
RGS17_HUMAN	RGS17	physical	25416956
GPSM3_HUMAN	GPSM3	physical	25416956
GBG4_HUMAN	GNG4	physical	26186194
GNAT3_HUMAN	GNAT3	physical	26186194
GNAI3_HUMAN	GNAI3	physical	26186194
GNAO_HUMAN	GNAO1	physical	26186194
RGS12_HUMAN	RGS12	physical	26186194
RIC8A_HUMAN	RIC8A	physical	26186194
RGS14_HUMAN	RGS14	physical	26186194
MTHR_HUMAN	MTHFR	physical	26186194
GBG10_HUMAN	GNG10	physical	26186194
GDS1_HUMAN	RAP1GDS1	physical	26186194
GNA13_HUMAN	GNA13	physical	26186194
GBB4_HUMAN	GNB4	physical	26186194
GBG5_HUMAN	GNG5	physical	26186194
PDE3B_HUMAN	PDE3B	physical	26186194
ABCA3_HUMAN	ABCA3	physical	26186194
DDRGK_HUMAN	DDRGK1	physical	26186194
VPP2_HUMAN	ATP6V0A2	physical	26186194
GPSM1_HUMAN	GPSM1	physical	26186194
GBG7_HUMAN	GNG7	physical	26186194
CNEP1_HUMAN	CTDNEP1	physical	26186194
PSMD3_HUMAN	PSMD3	physical	26344197
GNAI3_HUMAN	GNAI3	physical	28514442
GNAO_HUMAN	GNAO1	physical	28514442
RGS12_HUMAN	RGS12	physical	28514442
GNAT3_HUMAN	GNAT3	physical	28514442
GBB4_HUMAN	GNB4	physical	28514442
GPSM1_HUMAN	GPSM1	physical	28514442
GBG5_HUMAN	GNG5	physical	28514442
MTHR_HUMAN	MTHFR	physical	28514442
RGS14_HUMAN	RGS14	physical	28514442
RIC8A_HUMAN	RIC8A	physical	28514442
GBG7_HUMAN	GNG7	physical	28514442
GBB1_HUMAN	GNB1	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.

Regulatory Network of GNAI1_HUMAN

Related Literatures of Post-Translational Modification

Myristoylation
Reference	PubMed
"Strategy for comprehensive identification of human N-myristoylatedproteins using an insect cell-free protein synthesis system."; Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,Tsunasawa S., Utsumi T.; Proteomics 10:1780-1793(2010). Cited for: MYRISTOYLATION AT GLY-2.	20213681 [Abstract]

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