GNB5

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2PBI

Identifiers

Aliases

GNB5, guanine nucleotide binding protein (G protein), beta 5, GB5, G protein subunit beta 5

External IDs

MGI: 101848 HomoloGene: 40714 GeneCards: GNB5

Gene ontology
Molecular function	• G-protein gamma-subunit binding • chaperone binding • protein binding • signal transducer activity • GTPase activity • GTPase activator activity
Cellular component	• photoreceptor inner segment • membrane • myelin sheath • plasma membrane • photoreceptor outer segment • nucleus • cytosol
Biological process	• positive regulation of GTPase activity • G-protein coupled receptor signaling pathway • negative regulation of voltage-gated calcium channel activity • signal transduction • protein folding
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


10681


14697

Ensembl


ENSG00000069966


ENSMUSG00000032192

UniProt


O14775


P62881

RefSeq (mRNA)


NM_006578 NM_016194


NM_010313 NM_138719

RefSeq (protein)


NP_006569.1 NP_057278.2 NP_006569.1


NP_034443.1 NP_619733.1

Location (UCSC)

Chr 15: 52.12 – 52.19 Mb

Chr 9: 75.31 – 75.34 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Guanine nucleotide-binding protein subunit beta-5 is a protein that in humans is encoded by the GNB5 gene.^[3] Alternatively spliced transcript variants encoding different isoforms exist.^[4]

Function

Heterotrimeric guanine nucleotide-binding proteins (G proteins), which integrate signals between receptors and effector proteins, are composed of an alpha, a beta, and a gamma subunit. These subunits are encoded by families of related genes. This gene encodes a beta subunit. Beta subunits are important regulators of alpha subunits, as well as of certain signal transduction receptors and effectors.^[4]

GNB5 has been shown to differentially control RGS protein stability and membrane anchor binding, and therefore is involved in the control of complex neuronal G protein signaling pathways.^[5]

Interactions

GNB5 has been shown to interact with:

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Jones PG, Lombardi SJ, Cockett MI (Jun 1998). "Cloning and tissue distribution of the human G protein beta 5 cDNA". Biochim. Biophys. Acta. 1402 (3): 288–91. doi:10.1016/S0167-4889(98)00017-2. PMID 9606987.
1 2 "Entrez Gene: GNB5 guanine nucleotide binding protein (G protein), beta 5".
1 2 Masuho I, Wakasugi-Masuho H, Posokhova EN, Patton JR, Martemyanov KA (June 2011). "Type 5 G protein beta subunit (Gbeta5) controls the interaction of regulator of G protein signaling 9 (RGS9) with membrane anchors". J. Biol. Chem. 286 (24): 21806–13. doi:10.1074/jbc.M111.241513. PMC 3122235. PMID 21511947.
↑ Yan K, Kalyanaraman V, Gautam N (March 1996). "Differential ability to form the G protein betagamma complex among members of the beta and gamma subunit families". J. Biol. Chem. 271 (12): 7141–6. doi:10.1074/jbc.271.12.7141. PMID 8636150.
↑ Blake BL, Wing MR, Zhou JY, Lei Q, Hillmann JR, Behe CI, Morris RA, Harden TK, Bayliss DA, Miller RJ, Siderovski DP (December 2001). "G beta association and effector interaction selectivities of the divergent G gamma subunit G gamma(13)". J. Biol. Chem. 276 (52): 49267–74. doi:10.1074/jbc.M106565200. PMID 11675383.
↑ Levay K, Cabrera JL, Satpaev DK, Slepak VZ (March 1999). "Gbeta5 prevents the RGS7-Galphao interaction through binding to a distinct Ggamma-like domain found in RGS7 and other RGS proteins". Proc. Natl. Acad. Sci. U.S.A. 96 (5): 2503–7. doi:10.1073/pnas.96.5.2503. PMC 26814. PMID 10051672.
↑ Posner BA, Gilman AG, Harris BA (October 1999). "Regulators of G protein signaling 6 and 7. Purification of complexes with gbeta5 and assessment of their effects on g protein-mediated signaling pathways". J. Biol. Chem. 274 (43): 31087–93. doi:10.1074/jbc.274.43.31087. PMID 10521509.

Downes GB, Gautam N (1999). "The G protein subunit gene families". Genomics. 62 (3): 544–52. doi:10.1006/geno.1999.5992. PMID 10644457.
Yan K, Kalyanaraman V, Gautam N (1996). "Differential ability to form the G protein betagamma complex among members of the beta and gamma subunit families". J. Biol. Chem. 271 (12): 7141–6. doi:10.1074/jbc.271.12.7141. PMID 8636150.
Watson AJ, Aragay AM, Slepak VZ, Simon MI (1996). "A novel form of the G protein beta subunit Gbeta5 is specifically expressed in the vertebrate retina". J. Biol. Chem. 271 (45): 28154–60. doi:10.1074/jbc.271.45.28154. PMID 8910430.
Gold SJ, Ni YG, Dohlman HG, Nestler EJ (1997). "Regulators of G-protein signaling (RGS) proteins: region-specific expression of nine subtypes in rat brain". J. Neurosci. 17 (20): 8024–37. PMID 9315921.
Snow BE, Krumins AM, Brothers GM, Lee SF, Wall MA, Chung S, Mangion J, Arya S, Gilman AG, Siderovski DP (1998). "A G protein gamma subunit-like domain shared between RGS11 and other RGS proteins specifies binding to Gbeta5 subunits". Proc. Natl. Acad. Sci. U.S.A. 95 (22): 13307–12. doi:10.1073/pnas.95.22.13307. PMC 23793. PMID 9789084.
Levay K, Cabrera JL, Satpaev DK, Slepak VZ (1999). "Gbeta5 prevents the RGS7-Galphao interaction through binding to a distinct Ggamma-like domain found in RGS7 and other RGS proteins". Proc. Natl. Acad. Sci. U.S.A. 96 (5): 2503–7. doi:10.1073/pnas.96.5.2503. PMC 26814. PMID 10051672.
Snow BE, Betts L, Mangion J, Sondek J, Siderovski DP (1999). "Fidelity of G protein beta-subunit association by the G protein gamma-subunit-like domains of RGS6, RGS7, and RGS11". Proc. Natl. Acad. Sci. U.S.A. 96 (11): 6489–94. doi:10.1073/pnas.96.11.6489. PMC 26909. PMID 10339615.
Posner BA, Gilman AG, Harris BA (1999). "Regulators of G protein signaling 6 and 7. Purification of complexes with gbeta5 and assessment of their effects on g protein-mediated signaling pathways". J. Biol. Chem. 274 (43): 31087–93. doi:10.1074/jbc.274.43.31087. PMID 10521509.
Hartley JL, Temple GF, Brasch MA (2000). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948. PMID 11076863.
Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Böcher M, Blöcker H, Bauersachs S, Blum H, Lauber J, Düsterhöft A, Beyer A, Köhrer K, Strack N, Mewes HW, Ottenwälder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.
Simpson JC, Wellenreuther R, Poustka A, Pepperkok R, Wiemann S (2000). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287–92. doi:10.1093/embo-reports/kvd058. PMC 1083732. PMID 11256614.
Blake BL, Wing MR, Zhou JY, Lei Q, Hillmann JR, Behe CI, Morris RA, Harden TK, Bayliss DA, Miller RJ, Siderovski DP (2001). "G beta association and effector interaction selectivities of the divergent G gamma subunit G gamma(13)". J. Biol. Chem. 276 (52): 49267–74. doi:10.1074/jbc.M106565200. PMID 11675383.
Hu G, Wensel TG (2002). "R9AP, a membrane anchor for the photoreceptor GTPase accelerating protein, RGS9-1". Proc. Natl. Acad. Sci. U.S.A. 99 (15): 9755–60. doi:10.1073/pnas.152094799. PMC 125004. PMID 12119397.
Ajit SK, Young KH (2004). "Enhancement of pheromone response by RGS9 and Gbeta5 in yeast". Biochem. Biophys. Res. Commun. 324 (2): 686–91. doi:10.1016/j.bbrc.2004.09.100. PMID 15474482.
Wiemann S, Arlt D, Huber W, Wellenreuther R, Schleeger S, Mehrle A, Bechtel S, Sauermann M, Korf U, Pepperkok R, Sültmann H, Poustka A (2004). "From ORFeome to biology: a functional genomics pipeline". Genome Res. 14 (10B): 2136–44. doi:10.1101/gr.2576704. PMC 528930. PMID 15489336.

Intracellular signaling peptides and proteins

MAP

see MAP kinase pathway

Calcium

G protein

Heterotrimeric

cAMP:	Heterotrimeric G protein Gs/Gi Adenylate cyclase cAMP 3',5'-cyclic-AMP phosphodiesterase Protein kinase A

cGMP:	Transducin Gustducin Guanylate cyclase cGMP 3',5'-cyclic-GMP phosphodiesterase Protein kinase G

G alpha subunit G_α GNAO1 GNAI1 GNAI2 GNAI3 GNAT1 GNAT2 GNAT3 GNAZ GNAS GNAL GNAQ GNA11 GNA12 GNA13 GNA14 GNA15/GNA16

G beta-gamma complex G_β GNB1 GNB2 GNB3 GNB4 GNB5 G_γ GNGT1 GNGT2 GNG2 GNG3 GNG4 GNG5 GNG7 GNG8 GNG10 GNG11 GNG12 GNG13 BSCL2

G protein-coupled receptor kinase AMP-activated protein kinase

Monomeric

Cyclin

Lipid

Other protein kinase

Serine/threonine:	Casein kinase 1 2 eIF-2 kinase EIF2AK3 Glycogen synthase kinase GSK1 GSK2 GSK-3 GSK3A GSK3B IκB kinase CHUK IKK2 IKBKG Interleukin-1 receptor-associated kinase IRAK1 IRAK2 IRAK3 IRAK4 Lim kinase LIMK1 LIMK2 p21-activated kinases PAK1 PAK2 PAK3 PAK4 Rho-associated protein kinase ROCK1 ROCK2 Ribosomal s6 kinase RPS6KA1

Tyrosine:	ZAP70 Focal adhesion protein-tyrosine kinase PTK2 PTK2B BTK

both	Dual-specificity kinase

Other protein phosphatase

Serine/threonine:	Protein phosphatase 2

Tyrosine:	protein tyrosine phosphatase: Receptor-like protein tyrosine phosphatase Sh2 domain-containing protein tyrosine phosphatase

both:	Dual-specificity phosphatase

Apoptosis

see apoptosis signaling pathway

GTP-binding protein regulators

see GTP-binding protein regulators

Other

see also deficiencies of intracellular signaling peptides and proteins

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GNB5

Function

Interactions

References

Further reading