PPP2CB

Enzyme found in humans
PPP2CB
Identifiers
AliasesPPP2CB, PP2Abeta, PP2CB, protein phosphatase 2 catalytic subunit beta
External IDsOMIM: 176916; MGI: 1321161; HomoloGene: 37889; GeneCards: PPP2CB; OMA:PPP2CB - orthologs
Gene location (Human)
Chromosome 8 (human)
Chr.Chromosome 8 (human)[1]
Chromosome 8 (human)
Genomic location for PPP2CB
Genomic location for PPP2CB
Band8p12Start30,774,457 bp[1]
End30,814,314 bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for PPP2CB
Genomic location for PPP2CB
Band8 A4|8 20.63 cMStart34,089,653 bp[2]
End34,109,469 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • pons

  • superior vestibular nucleus

  • subthalamic nucleus

  • lateral nuclear group of thalamus

  • optic nerve

  • postcentral gyrus

  • external globus pallidus

  • bronchial epithelial cell

  • jejunal mucosa

  • pars reticulata
Top expressed in
  • spermatid

  • molar

  • granulocyte

  • spermatocyte

  • left colon

  • seminiferous tubule

  • ventricular zone

  • medial ganglionic eminence

  • parotid gland

  • endothelial cell of lymphatic vessel
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • phosphoprotein phosphatase activity
  • metal ion binding
  • protein binding
  • hydrolase activity
  • protein serine/threonine phosphatase activity
  • protein C-terminus binding
  • tau protein binding
Cellular component
  • cytoplasm
  • cytosol
  • spindle pole
  • protein phosphatase type 2A complex
  • chromosome
  • chromosome, centromeric region
  • extracellular exosome
  • cytoskeleton
  • nucleus
Biological process
  • response to antibiotic
  • response to endoplasmic reticulum stress
  • apoptotic mitochondrial changes
  • regulation of gene expression
  • response to hydrogen peroxide
  • proteasome-mediated ubiquitin-dependent protein catabolic process
  • protein dephosphorylation
  • negative regulation of Ras protein signal transduction
  • response to lead ion
  • peptidyl-threonine dephosphorylation
  • peptidyl-serine dephosphorylation
  • positive regulation of microtubule binding
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5516

19053

Ensembl

ENSG00000104695

ENSMUSG00000009630

UniProt

P62714

P62715

RefSeq (mRNA)

NM_004156
NM_001009552

NM_017374

RefSeq (protein)

NP_001009552

NP_059070

Location (UCSC)Chr 8: 30.77 – 30.81 MbChr 8: 34.09 – 34.11 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform is an enzyme that in humans is encoded by the PPP2CB gene.[5]

Function

This gene encodes the phosphatase 2A catalytic subunit. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. This gene encodes a beta isoform of the catalytic subunit. Two transcript variants encoding the same protein have been identified for this gene.[6]

Interactions

PPP2CB has been shown to interact with TLX1,[7] PPP2R1B[8] and PPP2R1A.[8][9]

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000104695 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000009630 – 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. ^ Jones TA, Barker HM, da Cruz e Silva EF, Mayer-Jaekel RE, Hemmings BA, Spurr NK, Sheer D, Cohen PT (April 1993). "Localization of the genes encoding the catalytic subunits of protein phosphatase 2A to human chromosome bands 5q23-->q31 and 8p12-->p11.2, respectively". Cytogenetics and Cell Genetics. 63 (1): 35–41. doi:10.1159/000133497. PMID 8383590.
  6. ^ "Entrez Gene: PPP2CB protein phosphatase 2 (formerly 2A), catalytic subunit, beta isoform".
  7. ^ Kawabe T, Muslin AJ, Korsmeyer SJ (Jan 1997). "HOX11 interacts with protein phosphatases PP2A and PP1 and disrupts a G2/M cell-cycle checkpoint". Nature. 385 (6615): 454–8. Bibcode:1997Natur.385..454K. doi:10.1038/385454a0. PMID 9009195. S2CID 608633.
  8. ^ a b Zhou J, Pham HT, Ruediger R, Walter G (Jan 2003). "Characterization of the Aalpha and Abeta subunit isoforms of protein phosphatase 2A: differences in expression, subunit interaction, and evolution". The Biochemical Journal. 369 (Pt 2): 387–98. doi:10.1042/BJ20021244. PMC 1223084. PMID 12370081.
  9. ^ Goudreault M, D'Ambrosio LM, Kean MJ, Mullin MJ, Larsen BG, Sanchez A, Chaudhry S, Chen GI, Sicheri F, Nesvizhskii AI, Aebersold R, Raught B, Gingras AC (Jan 2009). "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein". Molecular & Cellular Proteomics. 8 (1): 157–71. doi:10.1074/mcp.M800266-MCP200. PMC 2621004. PMID 18782753.

Further reading

  • Zolnierowicz S (Oct 2000). "Type 2A protein phosphatase, the complex regulator of numerous signaling pathways". Biochemical Pharmacology. 60 (8): 1225–35. doi:10.1016/S0006-2952(00)00424-X. PMID 11007961.
  • Goedert M, Cohen ES, Jakes R, Cohen P (Nov 1992). "p42 MAP kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1. Implications for Alzheimer's disease [corrected]". FEBS Letters. 312 (1): 95–9. doi:10.1016/0014-5793(92)81418-L. PMID 1330687. S2CID 34940651.
  • Khew-Goodall Y, Mayer RE, Maurer F, Stone SR, Hemmings BA (Jan 1991). "Structure and transcriptional regulation of protein phosphatase 2A catalytic subunit genes". Biochemistry. 30 (1): 89–97. doi:10.1021/bi00215a014. PMID 1846293.
  • Pallas DC, Shahrik LK, Martin BL, Jaspers S, Miller TB, Brautigan DL, Roberts TM (Jan 1990). "Polyoma small and middle T antigens and SV40 small t antigen form stable complexes with protein phosphatase 2A". Cell. 60 (1): 167–76. doi:10.1016/0092-8674(90)90726-U. PMID 2153055. S2CID 2007706.
  • Virshup DM, Kauffman MG, Kelly TJ (Dec 1989). "Activation of SV40 DNA replication in vitro by cellular protein phosphatase 2A". The EMBO Journal. 8 (12): 3891–8. doi:10.1002/j.1460-2075.1989.tb08568.x. PMC 402079. PMID 2555176.
  • Arino J, Woon CW, Brautigan DL, Miller TB, Johnson GL (Jun 1988). "Human liver phosphatase 2A: cDNA and amino acid sequence of two catalytic subunit isotypes". Proceedings of the National Academy of Sciences of the United States of America. 85 (12): 4252–6. Bibcode:1988PNAS...85.4252A. doi:10.1073/pnas.85.12.4252. PMC 280405. PMID 2837763.
  • Hemmings BA, Wernet W, Mayer R, Maurer F, Hofsteenge J, Stone SR (Dec 1988). "The nucleotide sequence of the cDNA encoding the human lung protein phosphatase 2A beta catalytic subunit". Nucleic Acids Research. 16 (23): 11366. doi:10.1093/nar/16.23.11366. PMC 339017. PMID 2849765.
  • Favre B, Zolnierowicz S, Turowski P, Hemmings BA (Jun 1994). "The catalytic subunit of protein phosphatase 2A is carboxyl-methylated in vivo". The Journal of Biological Chemistry. 269 (23): 16311–7. doi:10.1016/S0021-9258(17)34009-7. PMID 8206937.
  • Keranen LM, Dutil EM, Newton AC (Dec 1995). "Protein kinase C is regulated in vivo by three functionally distinct phosphorylations". Current Biology. 5 (12): 1394–1403. Bibcode:1995CBio....5.1394K. doi:10.1016/S0960-9822(95)00277-6. PMID 8749392. S2CID 15610228.
  • Tung HY, De Rocquigny H, Zhao LJ, Cayla X, Roques BP, Ozon R (Jan 1997). "Direct activation of protein phosphatase-2A0 by HIV-1 encoded protein complex NCp7:vpr". FEBS Letters. 401 (2–3): 197–201. doi:10.1016/S0014-5793(96)01470-6. PMID 9013886. S2CID 23293768.
  • Nagase T, Murakami T, Nozaki H, Inoue R, Nishito Y, Tanabe O, Usui H, Takeda M (Jul 1997). "Tissue and subcellular distributions, and characterization of rat brain protein phosphatase 2A containing a 72-kDa delta/B" subunit". Journal of Biochemistry. 122 (1): 178–87. doi:10.1093/oxfordjournals.jbchem.a021726. PMID 9276686.
  • Ruediger R, Brewis N, Ohst K, Walter G (Nov 1997). "Increasing the ratio of PP2A core enzyme to holoenzyme inhibits Tat-stimulated HIV-1 transcription and virus production". Virology. 238 (2): 432–43. doi:10.1006/viro.1997.8873. PMID 9400615.
  • Hsu W, Zeng L, Costantini F (Feb 1999). "Identification of a domain of Axin that binds to the serine/threonine protein phosphatase 2A and a self-binding domain". The Journal of Biological Chemistry. 274 (6): 3439–45. doi:10.1074/jbc.274.6.3439. PMID 9920888.
  • Ogris E, Du X, Nelson KC, Mak EK, Yu XX, Lane WS, Pallas DC (May 1999). "A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A". The Journal of Biological Chemistry. 274 (20): 14382–91. doi:10.1074/jbc.274.20.14382. PMC 3503312. PMID 10318862.
  • De Baere I, Derua R, Janssens V, Van Hoof C, Waelkens E, Merlevede W, Goris J (Dec 1999). "Purification of porcine brain protein phosphatase 2A leucine carboxyl methyltransferase and cloning of the human homologue". Biochemistry. 38 (50): 16539–47. doi:10.1021/bi991646a. PMID 10600115.
  • Götz J, Probst A, Mistl C, Nitsch RM, Ehler E (May 2000). "Distinct role of protein phosphatase 2A subunit Calpha in the regulation of E-cadherin and beta-catenin during development". Mechanisms of Development. 93 (1–2): 83–93. doi:10.1016/S0925-4773(00)00267-7. PMID 10781942. S2CID 496289.
  • Lüss H, Klein-Wiele O, Bokník P, Herzig S, Knapp J, Linck B, Müller FU, Scheld HH, Schmid C, Schmitz W, Neumann J (Dec 2000). "Regional expression of protein phosphatase type 1 and 2A catalytic subunit isoforms in the human heart". Journal of Molecular and Cellular Cardiology. 32 (12): 2349–59. doi:10.1006/jmcc.2000.1265. PMID 11113010.
  • v
  • t
  • e
  • 2iae: Crystal structure of a protein phosphatase 2A (PP2A) holoenzyme.
    2iae: Crystal structure of a protein phosphatase 2A (PP2A) holoenzyme.
  • 2ie3: Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor-inducing Toxins
    2ie3: Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor-inducing Toxins
  • 2ie4: Structure of the Protein Phosphatase 2A Core Enzyme Bound to okadaic acid
    2ie4: Structure of the Protein Phosphatase 2A Core Enzyme Bound to okadaic acid
  • 2npp: Structure of the Protein Phosphatase 2A Holoenzyme
    2npp: Structure of the Protein Phosphatase 2A Holoenzyme
  • 2nyl: Crystal structure of Protein Phosphatase 2A (PP2A) holoenzyme with the catalytic subunit carboxyl terminus truncated
    2nyl: Crystal structure of Protein Phosphatase 2A (PP2A) holoenzyme with the catalytic subunit carboxyl terminus truncated
  • 2nym: Crystal Structure of Protein Phosphatase 2A (PP2A) with C-terminus truncated catalytic subunit
    2nym: Crystal Structure of Protein Phosphatase 2A (PP2A) with C-terminus truncated catalytic subunit
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