PPM1B

PPM1B
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2P8E
Identifiers
Aliases	PPM1B , PP2C-beta, PP2C-beta-X, PP2CB, PP2CBETA, PPC2BETAX, protein phosphatase, Mg2+/Mn2+ dependent 1B
External IDs	OMIM: 603770 MGI: 101841 HomoloGene: 2027 GeneCards: PPM1B
Gene location (Human)
Chr.	Chromosome 2 (human)
End	44,244,384 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	85,331,419 bp
RNA expression pattern
	Top expressed in
	secondary oocyte; ; retinal pigment epithelium; ; gastrocnemius muscle; ; biceps brachii; ; deltoid muscle; ; vastus lateralis muscle; ; optic nerve; ; internal globus pallidus; ; tibialis anterior muscle; ; popliteal artery;
	Top expressed in
	ankle; ; spermatid; ; digastric muscle; ; temporal muscle; ; saccule; ; sternocleidomastoid muscle; ; body of femur; ; cerebellar cortex; ; superior cervical ganglion; ; endocardial cushion;
	More reference expression data
	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
	5495
	19043
	ENSG00000138032
	ENSMUSG00000061130
	O75688
	P36993
	NM_001033556 ; NM_001033557 ; NM_002706 ; NM_177968 ; NM_177969 Contents Function ; Interactions ; References ; Further reading ;
	NM_001159496 ; NM_001159497 ; NM_001159498 ; NM_011151
	NP_001028729 ; NP_002697 ; NP_808907 ; NP_808908
	NP_001152968 ; NP_001152969 ; NP_001152970 ; NP_035281
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 04, 2023

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:

Related Research Articles

Cyclin-dependent kinase 2, also known as cell division protein kinase 2, or Cdk2, is an enzyme that in humans is encoded by the CDK2 gene. The protein encoded by this gene is a member of the cyclin-dependent kinase family of Ser/Thr protein kinases. This protein kinase is highly similar to the gene products of S. cerevisiae cdc28, and S. pombe cdc2, also known as Cdk1 in humans. It is a catalytic subunit of the cyclin-dependent kinase complex, whose activity is restricted to the G1-S phase of the cell cycle, where cells make proteins necessary for mitosis and replicate their DNA. This protein associates with and is regulated by the regulatory subunits of the complex including cyclin E or A. Cyclin E binds G1 phase Cdk2, which is required for the transition from G1 to S phase while binding with Cyclin A is required to progress through the S phase. Its activity is also regulated by phosphorylation. Multiple alternatively spliced variants and multiple transcription initiation sites of this gene have been reported. The role of this protein in G1-S transition has been recently questioned as cells lacking Cdk2 are reported to have no problem during this transition.

Cyclin-dependent kinase 4 also known as cell division protein kinase 4 is an enzyme that in humans is encoded by the CDK4 gene. CDK4 is a member of the cyclin-dependent kinase family.

Cell division protein kinase 6 (CDK6) is an enzyme encoded by the CDK6 gene. It is regulated by cyclins, more specifically by Cyclin D proteins and Cyclin-dependent kinase inhibitor proteins. The protein encoded by this gene is a member of the cyclin-dependent kinase, (CDK) family, which includes CDK4. CDK family members are highly similar to the gene products of Saccharomyces cerevisiae cdc28, and Schizosaccharomyces pombe cdc2, and are known to be important regulators of cell cycle progression in the point of regulation named R or restriction point.

Cyclin-dependent kinase 1 also known as CDK1 or cell division cycle protein 2 homolog is a highly conserved protein that functions as a serine/threonine protein kinase, and is a key player in cell cycle regulation. It has been highly studied in the budding yeast S. cerevisiae, and the fission yeast S. pombe, where it is encoded by genes cdc28 and cdc2, respectively. With its cyclin partners, Cdk1 forms complexes that phosphorylate a variety of target substrates ; phosphorylation of these proteins leads to cell cycle progression.

Mitogen-activated protein kinase 3, also known as p44MAPK and ERK1, is an enzyme that in humans is encoded by the MAPK3 gene.

Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform is an enzyme that is encoded by the PPP2CA gene.

M-phase inducer phosphatase 1 also known as dual specificity phosphatase Cdc25A is a protein that in humans is encoded by the cell division cycle 25 homolog A (CDC25A) gene.

M-phase inducer phosphatase 2 is an enzyme that in humans is encoded by the CDC25B gene.

CDK-activating kinase assembly factor MAT1 is an enzyme that in humans is encoded by the MNAT1 gene.

G1/S-specific cyclin-E1 is a protein that in humans is encoded by the CCNE1 gene.

Cell division control protein 6 homolog is a protein that in humans is encoded by the CDC6 gene.

Cyclin-A1 is a protein that in humans is encoded by the CCNA1 gene.

Alpha-actinin-1 is a protein that in humans is encoded by the ACTN1 gene.

Cyclin-dependent kinase 5 activator 1 is an enzyme that in humans is encoded by the CDK5R1 gene.

PITSLRE serine/threonine-protein kinase CDC2L1 is an enzyme that in humans is encoded by the CDC2L1 gene.

Protein phosphatase 1A is an enzyme that in humans is encoded by the PPM1A gene.

A kinase anchor protein 1, mitochondrial is an enzyme that in humans is encoded by the AKAP1 gene.

Cell division protein kinase 3 is an enzyme that in humans is encoded by the CDK3 gene.

Cyclin-dependent kinase inhibitor 3 is an enzyme that in humans is encoded by the CDKN3 gene.

CTD small phosphatase-like protein is an enzyme that in humans is encoded by the CTDSPL gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000138032 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000061130 - 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.
↑ 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.
1 2 "Entrez Gene: PPM1B protein phosphatase 1B (formerly 2C), magnesium-dependent, beta isoform".
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.
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.
↑ 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.
↑ 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.

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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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000138032 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid9684878-5] 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.

[entrez-6] 1 2 "Entrez Gene: PPM1B protein phosphatase 1B (formerly 2C), magnesium-dependent, beta isoform".

[pmid10934208-7] 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.

[pmid14585847-8] 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.

[pmid11104763-9] 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.

[pmid23320500-10] 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.

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PPM1B

Contents

Function

Interactions

Related Research Articles

References

Further reading