GBG12_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GBG12_HUMAN
• UniProt AC: Q9UBI6
• Protein Name: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-12
• Gene Name: GNG12
• Organism: Homo sapiens (Human).
• Sequence Length: 72
• Subcellular Localization: Cell membrane ; Lipid-anchor ; Cytoplasmic side .
• Protein Description: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction..
• Protein Sequence: MSSKTASTNNIAQARRTVQQLRLEASIERIKVSKASADLMSYCEEHARSDPLLIGIPTSENPFKDKKTCIIL

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	------MSSKTASTN ------CCCCCCCCC	40.31	7493986
2	Acetylation	------MSSKTASTN ------CCCCCCCCC	40.31	7493986
3	Phosphorylation	-----MSSKTASTNN -----CCCCCCCCCC	32.50	23403867
4	Acetylation	----MSSKTASTNNI ----CCCCCCCCCCH	40.58	27452117
4	Malonylation	----MSSKTASTNNI ----CCCCCCCCCCH	40.58	32601280
4	Ubiquitination	----MSSKTASTNNI ----CCCCCCCCCCH	40.58	-
4	Ubiquitination	----MSSKTASTNNI ----CCCCCCCCCCH	40.58	23000965
5	Phosphorylation	---MSSKTASTNNIA ---CCCCCCCCCCHH	27.99	23403867
7	Phosphorylation	-MSSKTASTNNIAQA -CCCCCCCCCCHHHH	36.58	29255136
8	Phosphorylation	MSSKTASTNNIAQAR CCCCCCCCCCHHHHH	29.80	29255136
26	Phosphorylation	QQLRLEASIERIKVS HHHHHHHHHHHHHHC	18.66	30266825
31	Ubiquitination	EASIERIKVSKASAD HHHHHHHHHCHHHHH	46.83	23000965
34	Ubiquitination	IERIKVSKASADLMS HHHHHHCHHHHHHHH	49.72	23000965
34	Acetylation	IERIKVSKASADLMS HHHHHHCHHHHHHHH	49.72	26051181
34	Malonylation	IERIKVSKASADLMS HHHHHHCHHHHHHHH	49.72	32601280
34	Ubiquitination	IERIKVSKASADLMS HHHHHHCHHHHHHHH	49.72	21890473
36	Phosphorylation	RIKVSKASADLMSYC HHHHCHHHHHHHHHH	26.50	28258704
41	Phosphorylation	KASADLMSYCEEHAR HHHHHHHHHHHHHHH	33.65	30576142
42	Phosphorylation	ASADLMSYCEEHARS HHHHHHHHHHHHHHC	7.01	21082442
43	S-nitrosylation	SADLMSYCEEHARSD HHHHHHHHHHHHHCC	3.77	2212679
49	Phosphorylation	YCEEHARSDPLLIGI HHHHHHHCCCEEEEC	44.34	30266825
58	Phosphorylation	PLLIGIPTSENPFKD CEEEECCCCCCCCCC	46.91	25850435
59	Phosphorylation	LLIGIPTSENPFKDK EEEECCCCCCCCCCC	29.98	25850435
64	Ubiquitination	PTSENPFKDKKTCII CCCCCCCCCCCCEEE	70.65	23000965
64	Ubiquitination	PTSENPFKDKKTCII CCCCCCCCCCCCEEE	70.65	-
66	Ubiquitination	SENPFKDKKTCIIL- CCCCCCCCCCEEEC-	51.04	23000965
66	Ubiquitination	SENPFKDKKTCIIL- CCCCCCCCCCEEEC-	51.04	-
67	Ubiquitination	ENPFKDKKTCIIL-- CCCCCCCCCEEEC--	59.78	23000965
69	Geranylgeranylation	PFKDKKTCIIL---- CCCCCCCEEEC----	2.21	24023390
69	Methylation	PFKDKKTCIIL---- CCCCCCCEEEC----	2.21	24023390
69	Geranylgeranylation	PFKDKKTCIIL---- CCCCCCCEEEC----	2.21	24023390

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

Oops, there are no upstream regulatory protein records of GBG12_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GBG12_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of GBG12_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GBB1_HUMAN	GNB1	physical	19168127
GBB2_HUMAN	GNB2	physical	19168127
GBB3_HUMAN	GNB3	physical	19168127
MET_HUMAN	MET	physical	22939629
RAP1A_HUMAN	RAP1A	physical	22939629
GBB3_HUMAN	GNB3	physical	22940628
GBB2_HUMAN	GNB2	physical	23326349
MEF2A_HUMAN	MEF2A	physical	23326349
TBP_HUMAN	TBP	physical	23326349

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASSSPECTROMETRY.
PubMed: 18669648

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26, AND MASSSPECTROMETRY.
PubMed: 17081983

"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42, AND MASSSPECTROMETRY.
PubMed: 17053785