PPM1B

PPM1B
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases PPM1B, PP2C-beta, PP2C-beta-X, PP2CB, PP2CBETA, PPC2BETAX, protein phosphatase, Mg2+/Mn2+ dependent 1B
External IDs MGI: 101841 HomoloGene: 2027 GeneCards: PPM1B
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

5495

19043

Ensembl

ENSG00000138032

ENSMUSG00000061130

UniProt

O75688

P36993

RefSeq (mRNA)

NM_001033556
NM_001033557
NM_002706
NM_177968
NM_177969

NM_001159496
NM_001159497
NM_001159498
NM_011151

RefSeq (protein)

NP_001028729.1
NP_002697.1
NP_808907.1
NP_808908.1

NP_001152969.1
NP_001152970.1
NP_035281.1

Location (UCSC) Chr 2: 44.17 – 44.24 Mb Chr 17: 84.96 – 85.02 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Protein phosphatase 1B is an enzyme that in humans is encoded by the PPM1B gene.[3][4]

Function

The protein encoded by this gene is a member of the PP2C family of Ser/Thr protein phosphatases. PP2C family members are known to be negative regulators of cell stress response pathways. This phosphatase has been shown to dephosphorylate cyclin-dependent kinases (CDKs), and thus may be involved in cell cycle control. Overexpression of this phosphatase is reported to cause cell-growth arrest or cell death. Alternative splicing results in multiple transcript variants encoding different isoforms. Additional transcript variants have been described, but currently do not represent full-length sequences.[4]

Interactions

PPM1B has been shown to interact with:

References

  1. "Human PubMed Reference:".
  2. "Mouse PubMed Reference:".
  3. Marley AE, Kline A, Crabtree G, Sullivan JE, Beri RK (August 1998). "The cloning expression and tissue distribution of human PP2Cbeta". FEBS Lett. 431 (1): 121–4. doi:10.1016/S0014-5793(98)00708-X. PMID 9684878.
  4. 1 2 "Entrez Gene: PPM1B protein phosphatase 1B (formerly 2C), magnesium-dependent, beta isoform".
  5. 1 2 Cheng A, Kaldis P, Solomon MJ (November 2000). "Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C alpha and beta 2 isoforms". J. Biol. Chem. 275 (44): 34744–9. doi:10.1074/jbc.M006210200. PMID 10934208.
  6. 1 2 3 Prajapati S, Verma U, Yamamoto Y, Kwak YT, Gaynor RB (January 2004). "Protein phosphatase 2Cbeta association with the IkappaB kinase complex is involved in regulating NF-kappaB activity". J. Biol. Chem. 279 (3): 1739–46. doi:10.1074/jbc.M306273200. PMID 14585847.
  7. Hanada M, Ninomiya-Tsuji J, Komaki K, Ohnishi M, Katsura K, Kanamaru R, Matsumoto K, Tamura S (February 2001). "Regulation of the TAK1 signaling pathway by protein phosphatase 2C". J. Biol. Chem. 276 (8): 5753–9. doi:10.1074/jbc.M007773200. PMID 11104763.
  8. Tasdelen I, van Beekum O, Gorbenko O, Fleskens V, van den Broek NJ, Koppen A, Hamers N, Berger R, Coffer PJ, Brenkman AB, Kalkhoven E. "The serine/threonine phosphatase PPM1B (PP2Cβ) selectively modulates PPARγ activity". Biochem. J. 451 (1): 45–53. doi:10.1042/BJ20121113. PMID 23320500.

Further reading


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