GNB2

Protein-coding gene in the species Homo sapiens
GNB2
Identifiers
AliasesGNB2, G protein subunit beta 2, SSS4, SSS4; NEDHYDF, HG2C1
External IDsOMIM: 139390 MGI: 95784 HomoloGene: 68451 GeneCards: GNB2
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for GNB2
Genomic location for GNB2
Band7q22.1Start100,673,567 bp[1]
End100,679,174 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • anterior pituitary

  • stromal cell of endometrium

  • ganglionic eminence

  • right uterine tube

  • skin of abdomen

  • left uterine tube

  • gastric mucosa

  • right lung

  • canal of the cervix

  • right adrenal gland
    n/a
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein-containing complex binding
  • calcium channel regulator activity
  • signal transducer activity
  • protein binding
  • GTPase activity
  • GTPase binding
Cellular component
  • cytoplasm
  • cell body
  • vesicle
  • membrane
  • focal adhesion
  • myelin sheath
  • plasma membrane
  • lysosomal membrane
  • perinuclear region of cytoplasm
  • extracellular exosome
  • cytosol
  • extracellular space
  • protein-containing complex
Biological process
  • G protein-coupled receptor signaling pathway
  • cellular response to glucagon stimulus
  • signal transduction
  • protein folding
  • regulation of molecular function
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

2783

14693

Ensembl

ENSG00000172354

n/a

UniProt

P62879

P62880

RefSeq (mRNA)

NM_005273

NM_010312

RefSeq (protein)

NP_005264

NP_034442

Location (UCSC)Chr 7: 100.67 – 100.68 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2 is a protein that in humans is encoded by the GNB2 gene.[4][5]

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. This gene contains a trinucleotide (CCG) repeat length polymorphism in its 5' UTR.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000172354 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ Glockner G, Scherer S, Schattevoy R, Boright A, Weber J, Tsui LC, Rosenthal A (Dec 1998). "Large-scale sequencing of two regions in human chromosome 7q22: analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17 genes". Genome Res. 8 (10): 1060–73. doi:10.1101/gr.8.10.1060. PMC 310788. PMID 9799793.
  5. ^ a b "Entrez Gene: GNB2 guanine nucleotide binding protein (G protein), beta polypeptide 2".

Further reading

  • Downes GB, Gautam N (2000). "The G protein subunit gene families". Genomics. 62 (3): 544–52. doi:10.1006/geno.1999.5992. PMID 10644457.
  • Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
  • Lovett M, Kere J, Hinton LM (1991). "Direct selection: a method for the isolation of cDNAs encoded by large genomic regions". Proc. Natl. Acad. Sci. U.S.A. 88 (21): 9628–32. Bibcode:1991PNAS...88.9628L. doi:10.1073/pnas.88.21.9628. PMC 52771. PMID 1946378.
  • Blatt C, Eversole-Cire P, Cohn VH, et al. (1988). "Chromosomal localization of genes encoding guanine nucleotide-binding protein subunits in mouse and human". Proc. Natl. Acad. Sci. U.S.A. 85 (20): 7642–6. Bibcode:1988PNAS...85.7642B. doi:10.1073/pnas.85.20.7642. PMC 282248. PMID 2902634.
  • Fong HK, Amatruda TT, Birren BW, Simon MI (1987). "Distinct forms of the beta subunit of GTP-binding regulatory proteins identified by molecular cloning". Proc. Natl. Acad. Sci. U.S.A. 84 (11): 3792–6. Bibcode:1987PNAS...84.3792F. doi:10.1073/pnas.84.11.3792. PMC 304962. PMID 3108879.
  • Gao B, Gilman AG, Robishaw JD (1987). "A second form of the beta subunit of signal-transducing G proteins". Proc. Natl. Acad. Sci. U.S.A. 84 (17): 6122–5. Bibcode:1987PNAS...84.6122G. doi:10.1073/pnas.84.17.6122. PMC 299020. PMID 3114742.
  • Buhl AM, Osawa S, Johnson GL (1995). "Mitogen-activated protein kinase activation requires two signal inputs from the human anaphylatoxin C5a receptor". J. Biol. Chem. 270 (34): 19828–32. doi:10.1074/jbc.270.34.19828. PMID 7649993.
  • Ray K, Kunsch C, Bonner LM, Robishaw JD (1995). "Isolation of cDNA clones encoding eight different human G protein gamma subunits, including three novel forms designated the gamma 4, gamma 10, and gamma 11 subunits". J. Biol. Chem. 270 (37): 21765–71. doi:10.1074/jbc.270.37.21765. PMID 7665596.
  • Pumiglia KM, LeVine H, Haske T, et al. (1995). "A direct interaction between G-protein beta gamma subunits and the Raf-1 protein kinase". J. Biol. Chem. 270 (24): 14251–4. doi:10.1074/jbc.270.24.14251. PMID 7782277.
  • Ueda N, Iñiguez-Lluhi JA, Lee E, et al. (1994). "G protein beta gamma subunits. Simplified purification and properties of novel isoforms". J. Biol. Chem. 269 (6): 4388–95. doi:10.1016/S0021-9258(17)41792-3. PMID 8308009.
  • Liang JJ, Cockett M, Khawaja XZ (1998). "Immunohistochemical localization of G protein beta1, beta2, beta3, beta4, beta5, and gamma3 subunits in the adult rat brain". J. Neurochem. 71 (1): 345–55. doi:10.1046/j.1471-4159.1998.71010345.x. PMID 9648884. S2CID 83954980.
  • Kleiderlein JJ, Nisson PE, Jessee J, et al. (1999). "CCG repeats in cDNAs from human brain". Hum. Genet. 103 (6): 666–73. doi:10.1007/s004390050889. PMID 9921901. S2CID 23696667.
  • Asano T, Morishita R, Ueda H, Kato K (1999). "Selective association of G protein beta(4) with gamma(5) and gamma(12) subunits in bovine tissues". J. Biol. Chem. 274 (30): 21425–9. doi:10.1074/jbc.274.30.21425. PMID 10409705.
  • Suzuki H, Fukunishi Y, Kagawa I, et al. (2001). "Protein-protein interaction panel using mouse full-length cDNAs". Genome Res. 11 (10): 1758–65. doi:10.1101/gr.180101. PMC 311163. PMID 11591653.
  • Blake BL, Wing MR, Zhou JY, et al. (2002). "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.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Cuello F, Schulze RA, Heemeyer F, et al. (2003). "Activation of heterotrimeric G proteins by a high energy phosphate transfer via nucleoside diphosphate kinase (NDPK) B and Gbeta subunits. Complex formation of NDPK B with Gbeta gamma dimers and phosphorylation of His-266 IN Gbeta". J. Biol. Chem. 278 (9): 7220–6. doi:10.1074/jbc.M210304200. PMID 12486123.
  • Sprague RS, Bowles EA, Olearczyk JJ, et al. (2003). "The role of G protein beta subunits in the release of ATP from human erythrocytes". J. Physiol. Pharmacol. 53 (4 Pt 1): 667–74. PMID 12512701.
  • v
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  • 1b9x: STRUCTURAL ANALYSIS OF PHOSDUCIN AND ITS PHOSPHORYLATION-REGULATED INTERACTION WITH TRANSDUCIN
    1b9x: STRUCTURAL ANALYSIS OF PHOSDUCIN AND ITS PHOSPHORYLATION-REGULATED INTERACTION WITH TRANSDUCIN
  • 1b9y: STRUCTURAL ANALYSIS OF PHOSDUCIN AND ITS PHOSPHORYLATION-REGULATED INTERACTION WITH TRANSDUCIN BETA-GAMMA
    1b9y: STRUCTURAL ANALYSIS OF PHOSDUCIN AND ITS PHOSPHORYLATION-REGULATED INTERACTION WITH TRANSDUCIN BETA-GAMMA
  • 1gg2: G PROTEIN HETEROTRIMER MUTANT GI_ALPHA_1(G203A) BETA_1 GAMMA_2 WITH GDP BOUND
    1gg2: G PROTEIN HETEROTRIMER MUTANT GI_ALPHA_1(G203A) BETA_1 GAMMA_2 WITH GDP BOUND
  • 1got: HETEROTRIMERIC COMPLEX OF A GT-ALPHA/GI-ALPHA CHIMERA AND THE GT-BETA-GAMMA SUBUNITS
    1got: HETEROTRIMERIC COMPLEX OF A GT-ALPHA/GI-ALPHA CHIMERA AND THE GT-BETA-GAMMA SUBUNITS
  • 1gp2: G PROTEIN HETEROTRIMER GI_ALPHA_1 BETA_1 GAMMA_2 WITH GDP BOUND
    1gp2: G PROTEIN HETEROTRIMER GI_ALPHA_1 BETA_1 GAMMA_2 WITH GDP BOUND
  • 1omw: Crystal Structure of the complex between G Protein-Coupled Receptor Kinase 2 and Heterotrimeric G Protein beta 1 and gamma 2 subunits
    1omw: Crystal Structure of the complex between G Protein-Coupled Receptor Kinase 2 and Heterotrimeric G Protein beta 1 and gamma 2 subunits
  • 1tbg: BETA-GAMMA DIMER OF THE HETEROTRIMERIC G-PROTEIN TRANSDUCIN
    1tbg: BETA-GAMMA DIMER OF THE HETEROTRIMERIC G-PROTEIN TRANSDUCIN
  • 1xhm: The Crystal Structure of a Biologically Active Peptide (SIGK) Bound to a G Protein Beta:Gamma Heterodimer
    1xhm: The Crystal Structure of a Biologically Active Peptide (SIGK) Bound to a G Protein Beta:Gamma Heterodimer
  • 2bcj: Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-q and Gbetagamma Subunits
    2bcj: Crystal Structure of G Protein-Coupled Receptor Kinase 2 in Complex with Galpha-q and Gbetagamma Subunits
  • 2trc: PHOSDUCIN/TRANSDUCIN BETA-GAMMA COMPLEX
    2trc: PHOSDUCIN/TRANSDUCIN BETA-GAMMA COMPLEX
  • v
  • t
  • e
MAP
  • see MAP kinase pathway
Calcium
G protein
Heterotrimeric
cAMP:
cGMP:
Monomeric
Cyclin
Lipid
Other protein kinase
Serine/threonine:
Tyrosine:
Serine/threonine/tyrosine
Arginine
Other protein phosphatase
Serine/threonine:
Tyrosine:
both:
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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