CPLM-002706

Genbank Nucleotide ID

Guanine nucleotide-binding protein G(k) subunit alpha

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
29	NLREDGEKAAKEVKL	ubiquitination	[1, 2, 3]
35	EKAAKEVKLLLLGAG	ubiquitination	[1, 4, 5]
46	LGAGESGKSTIVKQM	ubiquitination	[5, 6]
92	IRAMGRLKIDFGEAA	ubiquitination	[1, 2, 3, 4, 5, 7, 8, 9]
128	PELAGVIKRLWRDGG	ubiquitination	[1, 7, 8, 9]
192	VETHFTFKDLYFKMF	ubiquitination	[1, 2, 3, 4, 5, 9]
197	TFKDLYFKMFDVGGQ	ubiquitination	[1, 2, 5, 9]
248	NRMHESMKLFDSICN	ubiquitination	[4, 5]
257	FDSICNNKWFTETSI	ubiquitination	[2]
277	KKDLFEEKIKRSPLT	ubiquitination	[4, 9]
349	VIIKNNLKECGLY**	ubiquitination	[2, 3, 6, 7, 9, 10]

[1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[7] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[9] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[10] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]

Functional Description

Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G(k) is the stimulatory G protein of receptor- regulated K(+) channels. The active GTP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.

NP_BIND 40 47 GTP (By similarity).
NP_BIND 175 181 GTP (By similarity).
NP_BIND 200 204 GTP (By similarity).
NP_BIND 269 272 GTP (By similarity).
METAL 47 47 Magnesium (By similarity).
METAL 181 181 Magnesium (By similarity).
BINDING 326 326 GTP; via amide nitrogen (By similarity).
MOD_RES 178 178 ADP-ribosylarginine; by cholera toxin (By
MOD_RES 351 351 ADP-ribosylcysteine; by pertussis toxin
LIPID 2 2 N-myristoyl glycine (By similarity).
LIPID 3 3 S-palmitoyl cysteine (By similarity).

3D-structure; ADP-ribosylation; Cell cycle; Cell division; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; GTP-binding; Lipoprotein; Magnesium; Membrane; Metal-binding; Myristate; Nucleotide-binding; Palmitate; Reference proteome; Transducer.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005813; C:centrosome; IDA:UniProtKB.
GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO:0005794; C:Golgi apparatus; IEA:Compara.
GO:0005834; C:heterotrimeric G-protein complex; IBA:RefGenome.
GO:0045121; C:membrane raft; IEA:Compara.
GO:0030496; C:midbody; IDA:UniProtKB.
GO:0042588; C:zymogen granule; IEA:Compara.
GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:RefGenome.
GO:0031821; F:G-protein coupled serotonin receptor binding; IBA:RefGenome.
GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO:0003924; F:GTPase activity; IBA:RefGenome.
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO:0004871; F:signal transducer activity; IBA:RefGenome.
GO:0007193; P:adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway; TAS:Reactome.
GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO:0051301; P:cell division; IDA:UniProtKB.
GO:0007194; P:negative regulation of adenylate cyclase activity; TAS:ProtInc.
GO:0030168; P:platelet activation; TAS:Reactome.
GO:0007268; P:synaptic transmission; TAS:Reactome.
GO:0006810; P:transport; NAS:ProtInc.
GO:0006906; P:vesicle fusion; IEA:Compara.

IPR001408; Gprotein_alpha_I.
IPR001019; Gprotein_alpha_su.
IPR011025; GproteinA_insert.
IPR027417; P-loop_NTPase.

PR00318; GPROTEINA.
PR00441; GPROTEINAI.