PLCB2

PLCB2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2FJU, 2ZKM
Identifiers
Aliases	PLCB2, PLC-beta-2, phospholipase C beta 2
External IDs	OMIM: 604114 MGI: 107465 HomoloGene: 20957 GeneCards: PLCB2
Gene location (Human)
Chr.	Chromosome 15 (human)[1]
End	40,307,935 bp[1]
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)[2]
End	118,558,919 bp[2]
RNA expression pattern
	Top expressed in
	monocyte; ; spleen; ; blood; ; bone marrow cells; ; lymph node; ; appendix; ; upper lobe of left lung; ; right lung; ; gallbladder; ; right uterine tube;
	Top expressed in
	thymus; ; female urethra; ; male urethra; ; blood; ; spermatocyte; ; spleen; ; ascending aorta; ; aortic valve; ; seminiferous tubule; ; bone marrow;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	phosphoric diester hydrolase activity; phospholipase C activity; calcium ion binding; hydrolase activity; signal transducer activity; metal ion binding; phosphatidylinositol phospholipase C activity;
Cellular component	cytoplasm; cytosol;
Biological process	lipid catabolic process; sensory perception of bitter taste; phospholipid metabolic process; intracellular signal transduction; inositol phosphate metabolic process; activation of phospholipase C activity; signal transduction; lipid metabolism; Wnt signaling pathway, calcium modulating pathway; G protein-coupled receptor signaling pathway; inositol trisphosphate biosynthetic process; phosphatidylinositol-mediated signaling; release of sequestered calcium ion into cytosol;
	Sources:Amigo / QuickGO
Orthologs
	5330
	18796
	ENSG00000137841
	ENSMUSG00000040061
	Q00722
	A3KGF7
	NM_001284297; NM_001284298; NM_001284299; NM_004573
	NM_001290790; NM_177568
	NP_001271226; NP_001271227; NP_001271228; NP_004564
	NP_001277719; NP_808236
	Wikidata
View/Edit Human	View/Edit Mouse

1-Phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2 is an enzyme that in humans is encoded by the PLCB2 gene.[5][6][7]

Function

The gene codes for the enzyme phospholipase C β2. The enzyme catalyzes the formation of inositol 1,4,5-trisphosphate and diacylglycerol from phosphatidylinositol 4,5-bisphosphate. This reaction uses calcium as a cofactor and plays an important role in the intracellular transduction of many extracellular signals. This gene is activated by two G-protein alpha subunits, alpha-q and alpha-11, as well as G-beta gamma subunits.

Interactions

PLCB2 has been shown to interact with MAP2K3[8] and TRPM7.[9]

References

GRCh38: Ensembl release 89: ENSG00000137841 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000040061 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Park D, Jhon DY, Kriz R, Knopf J, Rhee SG (Sep 1992). "Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2". J. Biol. Chem. 267 (23): 16048–55. doi:10.1016/S0021-9258(18)41963-1. PMID 1644792.
Park SH, Ryu SH, Suh PG, Kim H (Mar 1999). "Assignment1 of human PLCB2 encoding PLC beta2 to human chromosome 15q15 by fluorescence in situ hybridization". Cytogenet. Cell Genet. 83 (1–2): 48–9. doi:10.1159/000015166. PMID 9925923. S2CID 45169136.
"Entrez Gene: PLCB2 phospholipase C, beta 2".
Barr AJ, Marjoram R, Xu J, Snyderman R (Apr 2002). "Phospholipase C-beta 2 interacts with mitogen-activated protein kinase kinase 3". Biochem. Biophys. Res. Commun. 293 (1): 647–52. doi:10.1016/S0006-291X(02)00259-0. PMID 12054652.
Runnels LW, Yue L, Clapham DE (May 2002). "The TRPM7 channel is inactivated by PIP(2) hydrolysis". Nat. Cell Biol. 4 (5): 329–36. doi:10.1038/ncb781. PMID 11941371. S2CID 21592843.

Cefai D, Debre P, Kaczorek M, Idziorek T, Autran B, Bismuth G (1990). "Human immunodeficiency virus-1 glycoproteins gp120 and gp160 specifically inhibit the CD3/T cell-antigen receptor phosphoinositide transduction pathway". J. Clin. Invest. 86 (6): 2117–24. doi:10.1172/JCI114950. PMC 329852. PMID 1979339.
Zauli G, Previati M, Caramelli E, Bassini A, Falcieri E, Gibellini D, Bertolaso L, Bosco D, Robuffo I, Capitani S (1995). "Exogenous human immunodeficiency virus type-1 Tat protein selectively stimulates a phosphatidylinositol-specific phospholipase C nuclear pathway in the Jurkat T cell line". Eur. J. Immunol. 25 (9): 2695–700. doi:10.1002/eji.1830250944. PMID 7589147. S2CID 20562627.
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.
Chen P, Mayne M, Power C, Nath A (1997). "The Tat protein of HIV-1 induces tumor necrosis factor-alpha production. Implications for HIV-1-associated neurological diseases". J. Biol. Chem. 272 (36): 22385–8. doi:10.1074/jbc.272.36.22385. PMID 9278385.
Darè E, Kifor O, Brown EM, Weber G (1998). "Characterization of the phosphatidylinositol-specific phospholipase C isozymes present in the bovine parathyroid and in human kidney HEK293 cells stably transfected with the human parathyroid Ca2+-sensing receptor". J. Mol. Endocrinol. 21 (1): 7–17. doi:10.1677/jme.0.0210007. PMID 9723859.
Mayne M, Bratanich AC, Chen P, Rana F, Nath A, Power C (1998). "HIV-1 tat molecular diversity and induction of TNF-alpha: implications for HIV-induced neurological disease". Neuroimmunomodulation. 5 (3–4): 184–92. doi:10.1159/000026336. PMID 9730685. S2CID 19529677.
Haughey NJ, Holden CP, Nath A, Geiger JD (1999). "Involvement of inositol 1,4,5-trisphosphate-regulated stores of intracellular calcium in calcium dysregulation and neuron cell death caused by HIV-1 protein tat". J. Neurochem. 73 (4): 1363–74. doi:10.1046/j.1471-4159.1999.0731363.x. PMID 10501179.
Mayne M, Holden CP, Nath A, Geiger JD (2000). "Release of calcium from inositol 1,4,5-trisphosphate receptor-regulated stores by HIV-1 Tat regulates TNF-alpha production in human macrophages". J. Immunol. 164 (12): 6538–42. doi:10.4049/jimmunol.164.12.6538. PMID 10843712.
Tang Y, Tang J, Chen Z, Trost C, Flockerzi V, Li M, Ramesh V, Zhu MX (2000). "Association of mammalian trp4 and phospholipase C isozymes with a PDZ domain-containing protein, NHERF". J. Biol. Chem. 275 (48): 37559–64. doi:10.1074/jbc.M006635200. PMID 10980202.
Caricasole A, Sala C, Roncarati R, Formenti E, Terstappen GC (2000). "Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1)". Biochim. Biophys. Acta. 1517 (1): 63–72. doi:10.1016/S0167-4781(00)00260-8. PMID 11118617.
Singer AU, Waldo GL, Harden TK, Sondek J (2002). "A unique fold of phospholipase C-beta mediates dimerization and interaction with G alpha q". Nat. Struct. Biol. 9 (1): 32–6. doi:10.1038/nsb731. PMID 11753430. S2CID 13301839.
Runnels LW, Yue L, Clapham DE (2002). "The TRPM7 channel is inactivated by PIP(2) hydrolysis". Nat. Cell Biol. 4 (5): 329–36. doi:10.1038/ncb781. PMID 11941371. S2CID 21592843.
Scarlata S (2002). "Regulation of the lateral association of phospholipase Cbeta2 and G protein subunits by lipid rafts". Biochemistry. 41 (22): 7092–9. doi:10.1021/bi025625j. PMID 12033943.
Bertagnolo V, Marchisio M, Pierpaoli S, Colamussi ML, Brugnoli F, Visani G, Zauli G, Capitani S (2002). "Selective up-regulation of phospholipase C-beta2 during granulocytic differentiation of normal and leukemic hematopoietic progenitors". J. Leukoc. Biol. 71 (6): 957–65. doi:10.1189/jlb.71.6.957. PMID 12050180. S2CID 37477730.
Barr AJ, Marjoram R, Xu J, Snyderman R (2002). "Phospholipase C-beta 2 interacts with mitogen-activated protein kinase kinase 3". Biochem. Biophys. Res. Commun. 293 (1): 647–52. doi:10.1016/S0006-291X(02)00259-0. PMID 12054652.
Buck E, Schatz P, Scarlata S, Iyengar R (2002). "Role of dynamic interactions in effective signal transfer for Gbeta stimulation of phospholipase C-beta 2". J. Biol. Chem. 277 (51): 49707–15. doi:10.1074/jbc.M205553200. PMID 12388553.
Bennasser Y, Badou A, Tkaczuk J, Bahraoui E (2002). "Signaling pathways triggered by HIV-1 Tat in human monocytes to induce TNF-alpha". Virology. 303 (1): 174–80. doi:10.1006/viro.2002.1676. PMID 12482669.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000137841 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000040061 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1644792-5] Park D, Jhon DY, Kriz R, Knopf J, Rhee SG (Sep 1992). "Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2". J. Biol. Chem. 267 (23): 16048–55. doi:10.1016/S0021-9258(18)41963-1. PMID 1644792.

[pmid9925923-6] Park SH, Ryu SH, Suh PG, Kim H (Mar 1999). "Assignment1 of human PLCB2 encoding PLC beta2 to human chromosome 15q15 by fluorescence in situ hybridization". Cytogenet. Cell Genet. 83 (1–2): 48–9. doi:10.1159/000015166. PMID 9925923. S2CID 45169136.

[entrez-7] "Entrez Gene: PLCB2 phospholipase C, beta 2".

[pmid12054652-8] Barr AJ, Marjoram R, Xu J, Snyderman R (Apr 2002). "Phospholipase C-beta 2 interacts with mitogen-activated protein kinase kinase 3". Biochem. Biophys. Res. Commun. 293 (1): 647–52. doi:10.1016/S0006-291X(02)00259-0. PMID 12054652.

[pmid11941371-9] Runnels LW, Yue L, Clapham DE (May 2002). "The TRPM7 channel is inactivated by PIP(2) hydrolysis". Nat. Cell Biol. 4 (5): 329–36. doi:10.1038/ncb781. PMID 11941371. S2CID 21592843.

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

PLCB2

Function

Interactions

References

Further reading