GNA11_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GNA11_HUMAN
• UniProt AC: P29992
• Protein Name: Guanine nucleotide-binding protein subunit alpha-11
• Gene Name: GNA11
• Organism: Homo sapiens (Human).
• Sequence Length: 359
• Subcellular Localization: Cell membrane ; Lipid-anchor . Cytoplasm . In testicular cells, expressed exclusively in the cytoplasm.
• Protein Description: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Acts as an activator of phospholipase C..
• Protein Sequence: MTLESMMACCLSDEVKESKRINAEIEKQLRRDKRDARRELKLLLLGTGESGKSTFIKQMRIIHGAGYSEEDKRGFTKLVYQNIFTAMQAMIRAMETLKILYKYEQNKANALLIREVDVEKVTTFEHQYVSAIKTLWEDPGIQECYDRRREYQLSDSAKYYLTDVDRIATLGYLPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNENRMEESKALFRTIITYPWFQNSSVILFLNKKDLLEDKILYSHLVDYFPEFDGPQRDAQAAREFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV

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	Phosphorylation	------MTLESMMAC ------CCHHHHHHH	38.95	29083192
5	Phosphorylation	---MTLESMMACCLS ---CCHHHHHHHHHC	19.57	29083192
9	S-palmitoylation	TLESMMACCLSDEVK CHHHHHHHHHCHHHH	0.99	21044946
10	S-palmitoylation	LESMMACCLSDEVKE HHHHHHHHHCHHHHH	2.71	21044946
16	Ubiquitination	CCLSDEVKESKRINA HHHCHHHHHHHHHCH	54.98	32015554
18	Phosphorylation	LSDEVKESKRINAEI HCHHHHHHHHHCHHH	22.86	29083192
20	Methylation	DEVKESKRINAEIEK HHHHHHHHHCHHHHH	36.35	-
27	Ubiquitination	RINAEIEKQLRRDKR HHCHHHHHHHHHCHH	61.36	23000965
33	Ubiquitination	EKQLRRDKRDARREL HHHHHHCHHHHHHHH	50.82	23000965
41	Ubiquitination	RDARRELKLLLLGTG HHHHHHHHHHHHHCC	32.13	30230243
50	Phosphorylation	LLLGTGESGKSTFIK HHHHCCCCCCHHHHE	53.52	-
52	Ubiquitination	LGTGESGKSTFIKQM HHCCCCCCHHHHEEE	56.45	30230243
53	Phosphorylation	GTGESGKSTFIKQMR HCCCCCCHHHHEEEE	31.88	17531806
57	Ubiquitination	SGKSTFIKQMRIIHG CCCHHHHEEEEECCC	33.57	30230243
68	Phosphorylation	IIHGAGYSEEDKRGF ECCCCCCCHHHHCCC	33.32	-
72	Ubiquitination	AGYSEEDKRGFTKLV CCCCHHHHCCCHHHH	58.67	30230243
77	Ubiquitination	EDKRGFTKLVYQNIF HHHCCCHHHHHHHHH	33.42	30230243
80	Phosphorylation	RGFTKLVYQNIFTAM CCCHHHHHHHHHHHH	13.28	18083107
98	Ubiquitination	IRAMETLKILYKYEQ HHHHHHHHHHHHHHH	37.78	23000965
102	Neddylation	ETLKILYKYEQNKAN HHHHHHHHHHHHCCC	38.58	32015554
102	Ubiquitination	ETLKILYKYEQNKAN HHHHHHHHHHHHCCC	38.58	23000965
102	Sumoylation	ETLKILYKYEQNKAN HHHHHHHHHHHHCCC	38.58	-
102	Acetylation	ETLKILYKYEQNKAN HHHHHHHHHHHHCCC	38.58	27452117
107	Ubiquitination	LYKYEQNKANALLIR HHHHHHHCCCEEEEE	42.59	23000965
120	Ubiquitination	IREVDVEKVTTFEHQ EEEECHHHCCCCHHH	44.74	30230243
133	Ubiquitination	HQYVSAIKTLWEDPG HHHHHHHHHHHCCCC	36.96	29967540
144	S-palmitoylation	EDPGIQECYDRRREY CCCCHHHHHHHHHHE	2.16	29575903
151	Phosphorylation	CYDRRREYQLSDSAK HHHHHHHEECCCCCC	16.97	-
154	Phosphorylation	RRREYQLSDSAKYYL HHHHEECCCCCCEEE	17.62	17646429
158	Ubiquitination	YQLSDSAKYYLTDVD EECCCCCCEEECCHH	38.08	23000965
159	Phosphorylation	QLSDSAKYYLTDVDR ECCCCCCEEECCHHH	11.92	20068231
160	Phosphorylation	LSDSAKYYLTDVDRI CCCCCCEEECCHHHH	11.47	20068231
162	Phosphorylation	DSAKYYLTDVDRIAT CCCCEEECCHHHHHC	20.18	20068231
169	Phosphorylation	TDVDRIATLGYLPTQ CCHHHHHCCCCCCCC	20.53	27050516
183	ADP-ribosylation	QQDVLRVRVPTTGII CCCEEEEECCCCCEE	23.43	-
183	ADP-ribosylation	QQDVLRVRVPTTGII CCCEEEEECCCCCEE	23.43	-
187	Phosphorylation	LRVRVPTTGIIEYPF EEEECCCCCEEECCC	21.95	-
209	Deamidation	RMVDVGGQRSERRKW EEECCCCCCCHHHHH	39.54	24141704
209	Deamidated glutamine	RMVDVGGQRSERRKW EEECCCCCCCHHHHH	39.54	-
252	Ubiquitination	ENRMEESKALFRTII CCCHHHHHHHHHHHH	53.00	21906983
282	Ubiquitination	KKDLLEDKILYSHLV HHHHHHCHHHHHHHH	25.82	30230243
291	Phosphorylation	LYSHLVDYFPEFDGP HHHHHHHHCCCCCCC	17.35	-
322	Ubiquitination	DLNPDSDKIIYSHFT CCCCCCCCEEEEECE	34.65	30230243
345	Ubiquitination	RFVFAAVKDTILQLN HHHHHHHHHHHHHHC	44.41	21963094
354	Ubiquitination	TILQLNLKEYNLV-- HHHHHCCHHCCCC--	58.01	21906983
356	Phosphorylation	LQLNLKEYNLV---- HHHCCHHCCCC----	16.53	27642862

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

Oops, there are no upstream regulatory protein records of GNA11_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
209	Q	Amidation	(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.	24141704

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of GNA11_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EDNRA_HUMAN	EDNRA	physical	10789830
EDNRB_HUMAN	EDNRB	physical	10789830
GNAS3_HUMAN	GNAS	physical	22939629
GNAS2_HUMAN	GNAS	physical	22939629
ALEX_HUMAN	GNAS	physical	22939629
GNAS1_HUMAN	GNAS	physical	22939629
NHRF1_HUMAN	SLC9A3R1	physical	12193606
CXCR5_HUMAN	CXCR5	physical	23773523

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 145981: Hypocalciuric hypercalcemia, familial 2 (HHC2)
• 615361: Hypocalcemia, autosomal dominant 2 (HYPOC2)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Palmitoylation

"Site-specific analysis of protein S-acylation by resin-assistedcapture.";
Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A.,Stamler J.S., Casey P.J.;
J. Lipid Res. 52:393-398(2011).
Cited for: PALMITOYLATION AT CYS-9 AND CYS-10.
PubMed: 21044946