GBG_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GBG_YEAST
• UniProt AC: P18852
• Protein Name: Guanine nucleotide-binding protein subunit gamma
• Gene Name: STE18
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 110
• Subcellular Localization: Membrane; Lipid-anchor.
• Protein Description: Implicated in the pheromone A- and alpha-factor response pathway. The beta and gamma chains of the putative yeast mating response pathway G protein play a positive role in initiation of the mating response..
• Protein Sequence: MTSVQNSPRLQQPQEQQQQQQQLSLKIKQLKLKRINELNNKLRKELSRERITASNACLTIINYTSNTKDYTLPELWGYPVAGSNHFIEGLKNAQKNSQMSNSNSVCCTLM

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	------MTSVQNSPR ------CCCCCCCCC	37.29	28152593
3	Phosphorylation	-----MTSVQNSPRL -----CCCCCCCCCC	22.02	28152593
7	Phosphorylation	-MTSVQNSPRLQQPQ -CCCCCCCCCCCCHH	8.36	24909858
24	Phosphorylation	QQQQQQLSLKIKQLK HHHHHHHHHHHHHHH	24.23	19823750
26	Ubiquitination	QQQQLSLKIKQLKLK HHHHHHHHHHHHHHH	44.47	23749301
41	Ubiquitination	RINELNNKLRKELSR HHHHHHHHHHHHHHH	48.90	23749301
83	Phosphorylation	WGYPVAGSNHFIEGL HCCCCCCCHHHHHHH	19.86	21440633
106	S-palmitoylation	MSNSNSVCCTLM--- CCCCCCCCCCCC---	1.15	-
106	S-palmitoylation	MSNSNSVCCTLM--- CCCCCCCCCCCC---	1.15	10523659
107	Methylation	SNSNSVCCTLM---- CCCCCCCCCCC----	2.83	10523659
107	Farnesylation	SNSNSVCCTLM---- CCCCCCCCCCC----	2.83	10523659
107	S-palmitoylation	SNSNSVCCTLM---- CCCCCCCCCCC----	2.83	10712512
107	Farnesylation	SNSNSVCCTLM---- CCCCCCCCCCC----	2.83	10523659

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GBG_YEAST !!

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GBB_YEAST	STE4	physical	10688190
GBB_YEAST	STE4	physical	8417317
FAR1_YEAST	FAR1	physical	9822386
GBB_YEAST	STE4	physical	8649369
AKR1_YEAST	AKR1	physical	8649369
STE5_YEAST	STE5	genetic	8289786
STE12_YEAST	STE12	genetic	9286665
GBB_YEAST	STE4	genetic	1297344
GBB_YEAST	STE4	physical	11283351
GBB_YEAST	STE4	genetic	9732267
GBB_YEAST	STE4	physical	11557045
CYAA_YEAST	CYR1	physical	12905884

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Palmitoylation

"Dual lipid modification motifs in G(alpha) and G(gamma) subunits arerequired for full activity of the pheromone response pathway inSaccharomyces cerevisiae.";
Manahan C.L., Patnana M., Blumer K.J., Linder M.E.;
Mol. Biol. Cell 11:957-968(2000).
Cited for: ISOPRENYLATION AT CYS-107, AND PALMITOYLATION AT CYS-106.
PubMed: 10712512

"Dual lipid modification of the yeast gamma subunit Ste18p determinesmembrane localization of Gbetagamma.";
Hirschman J.E., Jenness D.D.;
Mol. Cell. Biol. 19:7705-7711(1999).
Cited for: ISOPRENYLATION AT CYS-107, PALMITOYLATION AT CYS-106, AND MUTAGENESISOF CYS-106.
PubMed: 10523659

Prenylation

"Dual lipid modification motifs in G(alpha) and G(gamma) subunits arerequired for full activity of the pheromone response pathway inSaccharomyces cerevisiae.";
Manahan C.L., Patnana M., Blumer K.J., Linder M.E.;
Mol. Biol. Cell 11:957-968(2000).
Cited for: ISOPRENYLATION AT CYS-107, AND PALMITOYLATION AT CYS-106.
PubMed: 10712512

"Dual lipid modification of the yeast gamma subunit Ste18p determinesmembrane localization of Gbetagamma.";
Hirschman J.E., Jenness D.D.;
Mol. Cell. Biol. 19:7705-7711(1999).
Cited for: ISOPRENYLATION AT CYS-107, PALMITOYLATION AT CYS-106, AND MUTAGENESISOF CYS-106.
PubMed: 10523659