dbPTM

GNAQ_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GNAQ_HUMAN
UniProt AC	P50148
Protein Name	Guanine nucleotide-binding protein G(q) subunit alpha
Gene Name	GNAQ
Organism	Homo sapiens (Human).
Sequence Length	359
Subcellular Localization	Nucleus. Membrane. Nucleus membrane. Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes..
Protein Description	Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Regulates B-cell selection and survival and is required to prevent B-cell-dependent autoimmunity. Regulates chemotaxis of BM-derived neutrophils and dendritic cells (in vitro) (By similarity)..
Protein Sequence	MTLESIMACCLSEEAKEARRINDEIERQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFENPYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPAYLPTQQDVLRVRVPTTGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	S-palmitoylation	TLESIMACCLSEEAK CHHHHHHHHCCHHHH	1.01	19801377
10	S-palmitoylation	LESIMACCLSEEAKE HHHHHHHHCCHHHHH	3.21	19801377
16	Ubiquitination	CCLSEEAKEARRIND HHCCHHHHHHHHHCH	56.01	-
50	Phosphorylation	LLLGTGESGKSTFIK HHHHCCCCCCHHHHE	53.52	-
52	Ubiquitination	LGTGESGKSTFIKQM HHCCCCCCHHHHEEE	56.45	-
53	Phosphorylation	GTGESGKSTFIKQMR HCCCCCCHHHHEEEE	31.88	17531806
65	Phosphorylation	QMRIIHGSGYSDEDK EEEEECCCCCCHHHC	22.01	28270605
67	Phosphorylation	RIIHGSGYSDEDKRG EEECCCCCCHHHCCC	18.04	28270605
68	Phosphorylation	IIHGSGYSDEDKRGF EECCCCCCHHHCCCC	37.74	28270605
72	Ubiquitination	SGYSDEDKRGFTKLV CCCCHHHCCCCHHHH	52.99	-
80	Phosphorylation	RGFTKLVYQNIFTAM CCCHHHHHHHHHHHH	13.28	18083107
85	Phosphorylation	LVYQNIFTAMQAMIR HHHHHHHHHHHHHHH	19.88	22210691
101	Phosphorylation	MDTLKIPYKYEHNKA HHHCCCCCCCCCCHH	29.67	26657352
102	Acetylation	DTLKIPYKYEHNKAH HHCCCCCCCCCCHHH	38.52	19608861
102	Ubiquitination	DTLKIPYKYEHNKAH HHCCCCCCCCCCHHH	38.52	19608861
103	Phosphorylation	TLKIPYKYEHNKAHA HCCCCCCCCCCHHHH	19.31	26657352
107	Ubiquitination	PYKYEHNKAHAQLVR CCCCCCCHHHHHHHH	43.38	-
120	Ubiquitination	VREVDVEKVSAFENP HHCCCHHHHHCCCCH	41.14	-
122	Phosphorylation	EVDVEKVSAFENPYV CCCHHHHHCCCCHHH	38.00	25599653
128	Phosphorylation	VSAFENPYVDAIKSL HHCCCCHHHHHHHHH	23.65	25599653
144	S-palmitoylation	NDPGIQECYDRRREY CCCCHHHHHHHHHHE	2.16	29575903
154	Phosphorylation	RRREYQLSDSTKYYL HHHHEECCCCCCCCC	17.62	17056873
158	Ubiquitination	YQLSDSTKYYLNDLD EECCCCCCCCCCCHH	35.53	-
183	ADP-ribosylation	QQDVLRVRVPTTGII CCCEEEEECCCCCEE	23.43	-
183	ADP-ribosylation	QQDVLRVRVPTTGII CCCEEEEECCCCCEE	23.43	-
187	Phosphorylation	LRVRVPTTGIIEYPF EEEECCCCCEEECCC	21.95	-
198	Phosphorylation	EYPFDLQSVIFRMVD ECCCCHHHHEEEEEC	25.20	-
209	Deamidation	RMVDVGGQRSERRKW EEECCCCCCCHHHHH	39.54	24141704
209	Deamidated glutamine	RMVDVGGQRSERRKW EEECCCCCCCHHHHH	39.54	-
209	Formation of an isopeptide bond	RMVDVGGQRSERRKW EEECCCCCCCHHHHH	39.54	-
252	Ubiquitination	ENRMEESKALFRTII CCCHHHHHHHHHHHH	53.00	21906983
291	Phosphorylation	MYSHLVDYFPEYDGP HHHHHHHHCCCCCCC	17.35	-
345	Ubiquitination	RFVFAAVKDTILQLN HHHHHHHHHHHHHHC	44.41	-
354	Ubiquitination	TILQLNLKEYNLV-- HHHHHCCHHCCCC--	58.01	21906983

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
53	S	Phosphorylation	Kinase	YPKA	-	PSP
53	S	Phosphorylation	Kinase	YPKA	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
209	Q	Amidation		24141704
(Microbial infection) Deamidated at Gln-209 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 GNAQ_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PK3CA_HUMAN	PIK3CA	physical	12704201
P85A_HUMAN	PIK3R1	physical	12704201
GNAS3_HUMAN	GNAS	physical	22939629
GNAS2_HUMAN	GNAS	physical	22939629
ALEX_HUMAN	GNAS	physical	22939629
GNAS1_HUMAN	GNAS	physical	22939629
PPT1_HUMAN	PPT1	physical	21988832
5NT3A_HUMAN	NT5C3A	physical	21988832
LUM_HUMAN	LUM	physical	21988832
RIC8A_HUMAN	RIC8A	physical	16629901
RIC8B_HUMAN	RIC8B	physical	12652642

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
163000	Capillary malformations, congenital (CMC)
185300	Sturge-Weber syndrome (SWS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GNAQ_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102, AND MASS SPECTROMETRY.	19608861 [Abstract]

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