PPM1B

Protein-coding gene in the species Homo sapiens
PPM1B
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2P8E

Identifiers
AliasesPPM1B, PP2C-beta, PP2C-beta-X, PP2CB, PP2CBETA, PPC2BETAX, protein phosphatase, Mg2+/Mn2+ dependent 1B
External IDsOMIM: 603770; MGI: 101841; HomoloGene: 2027; GeneCards: PPM1B; OMA:PPM1B - orthologs
Gene location (Human)
Chromosome 2 (human)
Chr.Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for PPM1B
Genomic location for PPM1B
Band2p21Start44,167,969 bp[1]
End44,244,384 bp[1]
Gene location (Mouse)
Chromosome 17 (mouse)
Chr.Chromosome 17 (mouse)[2]
Chromosome 17 (mouse)
Genomic location for PPM1B
Genomic location for PPM1B
Band17 E4|17 55.13 cMStart85,264,169 bp[2]
End85,331,419 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • secondary oocyte

  • Epithelium of choroid plexus

  • retinal pigment epithelium

  • gastrocnemius muscle

  • biceps brachii

  • Skeletal muscle tissue of rectus abdominis

  • muscle of thigh

  • Skeletal muscle tissue of biceps brachii

  • deltoid muscle

  • glutes
Top expressed in
  • neural layer of retina

  • ankle

  • spermatid

  • muscle of thigh

  • digastric muscle

  • temporal muscle

  • saccule

  • sternocleidomastoid muscle

  • body of femur

  • cerebellar cortex
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein binding
  • magnesium ion binding
  • manganese ion binding
  • protein serine/threonine phosphatase activity
  • phosphoprotein phosphatase activity
  • catalytic activity
  • cation binding
  • hydrolase activity
  • metal ion binding
Cellular component
  • membrane
  • cytoplasm
  • nucleolus
  • cytosol
  • nucleus
Biological process
  • protein dephosphorylation
  • negative regulation of I-kappaB kinase/NF-kappaB signaling
  • negative regulation of defense response to virus
  • N-terminal protein myristoylation
  • peptidyl-threonine dephosphorylation
  • negative regulation of interferon-beta production
  • negative regulation of NIK/NF-kappaB signaling
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
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
NP_002697
NP_808907
NP_808908

NP_001152968
NP_001152969
NP_001152970
NP_035281

Location (UCSC)Chr 2: 44.17 – 44.24 MbChr 17: 85.26 – 85.33 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Protein phosphatase 1B is an enzyme that in humans is encoded by the PPM1B gene.[5][6]

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.[6]

Interactions

PPM1B has been shown to interact with:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000138032 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000061130 – 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. ^ 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. S2CID 84075989.
  6. ^ a b "Entrez Gene: PPM1B protein phosphatase 1B (formerly 2C), magnesium-dependent, beta isoform".
  7. ^ a b 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.
  8. ^ a b c 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.
  9. ^ 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.
  10. ^ 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 (2013). "The serine/threonine phosphatase PPM1B (PP2Cβ) selectively modulates PPARγ activity". Biochem. J. 451 (1): 45–53. doi:10.1042/BJ20121113. PMID 23320500.

Further reading

  • Hishiya A, Ohnishi M, Tamura S, Nakamura F (1999). "Protein phosphatase 2C inactivates F-actin binding of human platelet moesin". J. Biol. Chem. 274 (38): 26705–12. doi:10.1074/jbc.274.38.26705. PMID 10480873.
  • Cheng A, Ross KE, Kaldis P, Solomon MJ (2000). "Dephosphorylation of cyclin-dependent kinases by type 2C protein phosphatases". Genes Dev. 13 (22): 2946–57. doi:10.1101/gad.13.22.2946. PMC 317162. PMID 10580002.
  • Cheng A, Kaldis P, Solomon MJ (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.
  • Hanada M, Ninomiya-Tsuji J, Komaki K, Ohnishi M, Katsura K, Kanamaru R, Matsumoto K, Tamura S (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.
  • Parvari R, Brodyansky I, Elpeleg O, Moses S, Landau D, Hershkovitz E (2001). "A recessive contiguous gene deletion of chromosome 2p16 associated with cystinuria and a mitochondrial disease". Am. J. Hum. Genet. 69 (4): 869–75. doi:10.1086/323624. PMC 1226072. PMID 11524703.
  • Seroussi E, Shani N, Ben-Meir D, Chajut A, Divinski I, Faier S, Gery S, Karby S, Kariv-Inbal Z, Sella O, Smorodinsky NI, Lavi S (2001). "Uniquely conserved non-translated regions are involved in generation of the two major transcripts of protein phosphatase 2Cbeta". J. Mol. Biol. 312 (3): 439–51. doi:10.1006/jmbi.2001.4967. PMID 11563908.
  • Prajapati S, Verma U, Yamamoto Y, Kwak YT, Gaynor RB (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.
  • Parvari R, Gonen Y, Alshafee I, Buriakovsky S, Regev K, Hershkovitz E (2005). "The 2p21 deletion syndrome: characterization of the transcription content". Genomics. 86 (2): 195–211. doi:10.1016/j.ygeno.2005.04.001. PMID 15913950.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
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  • 2p8e: Crystal structure of the serine/threonine phosphatase domain of human PPM1B
    2p8e: Crystal structure of the serine/threonine phosphatase domain of human PPM1B


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