PLCB2

Protein-coding gene in the species Homo sapiens

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; OMA:PLCB2 - orthologs
| Gene location (Human)

Chr.| Chromosome 15 (human)[1]

Band| 15q15.1| Start| 40,278,176 bp[1]
End| 40,307,935 bp[1]
| Gene location (Mouse)

Chr.| Chromosome 2 (mouse)[2]

Band| 2 E5|2 59.43 cM| Start| 118,537,998 bp[2]
End| 118,558,919 bp[2]
| RNA expression pattern

Bgee| | Human| Mouse (ortholog)

|

| Top expressed in

* granulocyte

* monocyte

* spleen

* blood

* bone marrow cell

* lymph node

* appendix

* upper lobe of left lung

* right lung

* C1 segment

| Top expressed in

* granulocyte

* thymus

* female urethra

* male urethra

* lumbar subsegment of spinal cord

* blood

* spermatocyte

* spleen

* ascending aorta

* aortic valve

More reference expression data
BioGPS| |

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

Species| Human| Mouse
Entrez| |

5330

18796

Ensembl| |

ENSG00000137841

ENSMUSG00000040061

UniProt| |

Q00722

A3KGF7

RefSeq (mRNA)| |

NM_001284297
NM_001284298
NM_001284299
NM_004573

NM_001290790
NM_177568

RefSeq (protein)| |

NP_001271226
NP_001271227
NP_001271228
NP_004564

NP_001277719
NP_808236

Location (UCSC)| Chr 15: 40.28 – 40.31 Mb| Chr 2: 118.54 – 118.56 Mb
PubMed search| [3]| [4]
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

[edit]

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

[edit]

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

## References

[edit]

1. ^ a b c GRCh38: Ensembl release 89: ENSG00000137841 - Ensembl, May 2017
2. ^ a b c 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.
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.
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 45169136.1–2&rft.pages=48-9&rft.date=1999-03&rft_id=https://api.semanticscholar.org/CorpusID:45169136#id-name=S2CID&rft_id=info:pmid/9925923&rft_id=info:doi/10.1159/000015166&rft.aulast=Park&rft.aufirst=SH&rft.au=Ryu,+SH&rft.au=Suh,+PG&rft.au=Kim,+H&rfr_id=info:sid/en.wikipedia.org:PLCB2" class="Z3988">
7. ^ "Entrez Gene: PLCB2 phospholipase C, beta 2".
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.
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.

## Further reading

[edit]

* 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 19529677.3–4&rft.pages=184-92&rft.date=1998&rft_id=https://api.semanticscholar.org/CorpusID:19529677#id-name=S2CID&rft_id=info:pmid/9730685&rft_id=info:doi/10.1159/000026336&rft.aulast=Mayne&rft.aufirst=M&rft.au=Bratanich,+AC&rft.au=Chen,+P&rft.au=Rana,+F&rft.au=Nath,+A&rft.au=Power,+C&rfr_id=info:sid/en.wikipedia.org:PLCB2" class="Z3988">
* 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. S2CID 25410140.
* 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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* t
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PDB gallery

* 2fju: Activated Rac1 bound to its effector phospholipase C beta 2

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Hydrolase: esterases (EC 3.1)

3.1.1: Carboxylic
ester hydrolases|

* Cholinesterase
* Acetylcholinesterase
* Butyrylcholinesterase
* Pectinesterase
* 6-phosphogluconolactonase
* PAF acetylhydrolase

* Lipase
* Bile salt-dependent
* Gastric/Lingual
* Pancreatic
* Lysosomal
* Hormone-sensitive
* Endothelial
* Hepatic
* Lipoprotein
* Monoacylglycerol
* Diacylglycerol

* Phospholipase
* A1
* A2
* B

* Cutinase
* PETase

3.1.2: Thioesterase|

* Palmitoyl protein thioesterase
* Ubiquitin carboxy-terminal hydrolase L1
* 4-hydroxybenzoyl-CoA thioesterase

3.1.3: Phosphatase|

* Alkaline phosphatase
* ALPI
* ALPL
* ALPP
* Acid phosphatase (Prostatic)/Tartrate-resistant acid phosphatase/Purple acid phosphatases
* Nucleotidase
* Glucose 6-phosphatase
* Fructose 1,6-bisphosphatase
* Calcineurin
* Protein phosphatase
* PP2A
* OCRL
* Pyruvate dehydrogenase phosphatase
* Fructose 6-P,2-kinase:fructose 2,6-bisphosphatase
* PTEN
* Phytase
* Beta-propeller phytase
* Inositol-phosphate phosphatase
* IMPA1, IMPA2, IMPA3
* Protein phosphatase: Protein tyrosine phosphatase
* Protein serine/threonine phosphatase
* Dual-specificity phosphatase

3.1.4:
Phosphodiesterase|

* Autotaxin
* Phospholipase
* C
* D
* Sphingomyelin phosphodiesterase
* 1
* PDE1
* PDE2
* PDE3
* PDE4A/PDE4B
* PDE5
* Lecithinase (Clostridium perfringens alpha toxin)
* Cyclic nucleotide phosphodiesterase

3.1.6: Sulfatase|

* arylsulfatase
* Arylsulfatase A
* Arylsulfatase B
* Arylsulfatase L
* Steroid sulfatase
* Galactosamine-6 sulfatase
* Iduronate-2-sulfatase
* N-acetylglucosamine-6-sulfatase

Nuclease (includes
deoxyribonuclease
and ribonuclease)|

| 3.1.11-16:
Exonuclease|

| Exodeoxyribonuclease|

* RecBCD

|

Exoribonuclease|

* Oligonucleotidase

3.1.21-31:
Endonuclease|

| Endodeoxyribonuclease|

* Deoxyribonuclease I
* Deoxyribonuclease II
* Deoxyribonuclease IV
* Restriction enzyme;see {{Restriction enzyme}}
* UvrABC endonuclease

|

Endoribonuclease|

* RNase III
* Drosha: Microprocessor complex
* Dicer: RNA-induced silencing complex
* RNase H
* 1
* 2A
* 2B
* 2C
* RNase P
* RNase A
* RNase Z
* RNase E
* 1
* 2
* 3
* 4/5
* RNase T1

either deoxy- or ribo-  |

* Nuclease S1
* Mung bean nuclease
* Serratia marcescens nuclease
* Micrococcal nuclease

* v
* t
* e

Enzymes

Activity|

* Active site
* Binding site
* Catalytic triad
* Oxyanion hole
* Enzyme promiscuity
* Diffusion-limited enzyme
* 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)

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