8OY1

Structure of the human Guanine Nucleotide-Binding Protein G(K) Subunit Alpha

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000139	cellular_component	Golgi membrane
A	0001664	molecular_function	G protein-coupled receptor binding
A	0003924	molecular_function	GTPase activity
A	0005515	molecular_function	protein binding
A	0005525	molecular_function	GTP binding
A	0005654	cellular_component	nucleoplasm
A	0005730	cellular_component	nucleolus
A	0005737	cellular_component	cytoplasm
A	0005765	cellular_component	lysosomal membrane
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0005794	cellular_component	Golgi apparatus
A	0005813	cellular_component	centrosome
A	0005834	cellular_component	heterotrimeric G-protein complex
A	0005856	cellular_component	cytoskeleton
A	0005886	cellular_component	plasma membrane
A	0007165	biological_process	signal transduction
A	0007186	biological_process	G protein-coupled receptor signaling pathway
A	0007188	biological_process	adenylate cyclase-modulating G protein-coupled receptor signaling pathway
A	0007193	biological_process	adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway
A	0007194	biological_process	negative regulation of adenylate cyclase activity
A	0007212	biological_process	G protein-coupled dopamine receptor signaling pathway
A	0016020	cellular_component	membrane
A	0016239	biological_process	positive regulation of macroautophagy
A	0019001	molecular_function	guanyl nucleotide binding
A	0019003	molecular_function	GDP binding
A	0030496	cellular_component	midbody
A	0031683	molecular_function	G-protein beta/gamma-subunit complex binding
A	0046039	biological_process	GTP metabolic process
A	0046872	molecular_function	metal ion binding
A	0051301	biological_process	cell division
A	0070062	cellular_component	extracellular exosome

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0007744|PDB:2IHB, ECO:0007744|PDB:2ODE, ECO:0007744|PDB:2V4Z, ECO:0007744|PDB:4G5O, ECO:0007744|PDB:4G5R, ECO:0007744|PDB:4G5S

Chain	Residue	Details
A	GLU43
A	LEU175
A	ASN269

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:19478087, ECO:0007744|PDB:2V4Z

Chain	Residue	Details
A	SER47
A	THR181

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744|PDB:2V4Z, ECO:0007744|PDB:4G5O, ECO:0007744|PDB:4G5R, ECO:0007744|PDB:4G5S

Chain	Residue	Details
A	ASP150

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000305|PubMed:19478087, ECO:0007744|PDB:2V4Z

Chain	Residue	Details
A	ASP200

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0007744|PDB:2IHB, ECO:0007744|PDB:2ODE, ECO:0007744|PDB:2V4Z, ECO:0007744|PDB:4G5O, ECO:0007744|PDB:4G5R

Chain	Residue	Details
A	ALA326

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: ADP-ribosylarginine; by cholera toxin => ECO:0000250

Chain	Residue	Details
A	ARG178

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Deamidated glutamine; by Photorhabdus PAU_02230 => ECO:0000269|PubMed:24141704

Chain	Residue	Details
A	GLN204

---