PPM1B Gene

HGNC Family	Phosphatases
Name	protein phosphatase, Mg2+/Mn2+ dependent, 1B
Description	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. [provided by RefSeq, Jul 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPPM1B functions prominently as a negative regulator of pro‐inflammatory and antiviral signaling. It terminates cytokine‐induced NF‑κB activation by directly dephosphorylating IKKβ at key serine residues and, similarly, dephosphorylates TBK1 to dampen antiviral responses. In addition, biochemical studies revealed that a related PP2C isoform associates with the IKK complex, underscoring a broader role for PPM1B in turning off aberrant inflammatory signals."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond immune regulation, PPM1B is pivotal in fine‑tuning transcription and cell cycle pathways through dephosphorylation of key effectors. It modulates the activity of Cdk9, thus influencing RNA polymerase II elongation"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": ", and directly dephosphorylates PPARγ, enhancing its transcriptional output in adipocytes."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": " Moreover, PPM1B acts as an integral component of repressor complexes by dephosphorylating transcription factors such as Pax2—thereby switching it from an activator to a repressor"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": "—and by regulating the erythroid transcription factor EKLF."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": " Its ability to counteract toxic protein phosphorylation is further exemplified by the dephosphorylation of DYRK1A, resulting in reduced tau phosphorylation and oligomerization."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": " In addition, post-translational modification by PKA through phosphorylation of Ser-195 can destabilize PPM1B, and reduced levels of PPM1B have been linked to the induction of cellular senescence."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn cancer and cell migration contexts, PPM1B serves as a brake on oncogenic signaling cascades. It dephosphorylates RhoGDI1, thereby attenuating the activation of Rho GTPases that drive cell motility."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": " In bladder, nasopharyngeal, head and neck, and gastric cancers, alterations in PPM1B—either via direct targeting by oncogenic microRNAs (e.g. miR-186) or through protein degradation mediated by regulators such as TRIM59 and PLEK2—lead to enhanced proliferation, invasion, and metastasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "16"}]}, {"type": "t", "text": " Furthermore, depletion of PPM1B sensitizes cells to chemotherapeutic agents via alterations in the p38–RB1–E2F1 pathway"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": ", and studies of RBM10 complexes elucidate how loss of PPM1B function contributes to tumorigenicity."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "18"}]}, {"type": "t", "text": " Additionally, degradation of PPM1B by PLEK2 underscores its importance in sustaining NF‑κB–mediated metastatic signals."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPPM1B also partakes in metabolic and vascular regulation. It positively modulates hPXR activity, thereby enhancing CYP3A4 expression in liver cells by counteracting CDK2-mediated inhibition."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "20"}]}, {"type": "t", "text": " In the vasculature, a circRNA/miRNA axis involving circ_0090231 and miR-942-5p targets PPM1B, affecting vascular smooth muscle cell proliferation and invasion in the context of atherosclerosis."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Wenjing Sun, Yang Yu, Gianpietro Dotti, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PPM1A and PPM1B act as IKKbeta phosphatases to terminate TNFalpha-induced IKKbeta-NF-kappaB activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Signal (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cellsig.2008.09.012"}], "href": "https://doi.org/10.1016/j.cellsig.2008.09.012"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18930133"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18930133"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Shashi Prajapati, Udit Verma, Yumi Yamamoto, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein phosphatase 2Cbeta association with the IkappaB kinase complex is involved in regulating NF-kappaB activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M306273200"}], "href": "https://doi.org/10.1074/jbc.M306273200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14585847"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14585847"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Yanling Zhao, Li Liang, Yihui Fan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PPM1B negatively regulates antiviral response via dephosphorylating TBK1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Signal (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cellsig.2012.06.017"}], "href": "https://doi.org/10.1016/j.cellsig.2012.06.017"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22750291"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22750291"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Steven Pregizer, Artem Barski, Charles A Gersbach, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of novel Runx2 targets in osteoblasts: cell type-specific BMP-dependent regulation of Tram2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biochem (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/jcb.21366"}], "href": "https://doi.org/10.1002/jcb.21366"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17486635"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17486635"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Ismayil Tasdelen, Olivier van Beekum, Olena Gorbenko, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The serine/threonine phosphatase PPM1B (PP2Cβ) selectively modulates PPARγ activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BJ20121113"}], "href": "https://doi.org/10.1042/BJ20121113"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23320500"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23320500"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Saji Abraham, Raghavendra Paknikar, Samina Bhumbra, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The Groucho-associated phosphatase PPM1B displaces Pax transactivation domain interacting protein (PTIP) to switch the transcription factor Pax2 from a transcriptional activator to a repressor."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M114.607424"}], "href": "https://doi.org/10.1074/jbc.M114.607424"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25631048"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25631048"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Yvette Y Yien, James J Bieker "}, {"type": "b", "children": [{"type": "t", "text": "Functional interactions between erythroid Krüppel-like factor (EKLF/KLF1) and protein phosphatase PPM1B/PP2Cβ."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M112.350496"}], "href": "https://doi.org/10.1074/jbc.M112.350496"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22393050"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22393050"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Ye Hyung Lee, Eunju Im, Minju Hyun, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein phosphatase PPM1B inhibits DYRK1A kinase through dephosphorylation of pS258 and reduces toxic tau aggregation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.RA120.015574"}], "href": "https://doi.org/10.1074/jbc.RA120.015574"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33380426"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33380426"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Hyo-Kyung Choi, Soo-Yeon Park, Hye-Jeong Oh, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PKA negatively regulates PP2Cβ to activate NF-κB-mediated inflammatory signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2013.05.129"}], "href": "https://doi.org/10.1016/j.bbrc.2013.05.129"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23756813"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23756813"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Jeong Hyeon Park, Tracy K Hale, Rebecca Jane Smith, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PPM1B depletion induces premature senescence in human IMR-90 fibroblasts."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mech Ageing Dev (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.mad.2014.03.003"}], "href": "https://doi.org/10.1016/j.mad.2014.03.003"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24674756"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24674756"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Hee Jun Cho, Jong-Tae Kim, Seon-Jin Lee, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein phosphatase 1B dephosphorylates Rho guanine nucleotide dissociation inhibitor 1 and suppresses cancer cell migration and invasion."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Lett (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.canlet.2018.01.002"}], "href": "https://doi.org/10.1016/j.canlet.2018.01.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29307615"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29307615"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Jianan Yang, Daozhang Yuan, Jing Li, et al. "}, {"type": "b", "children": [{"type": "t", "text": "miR-186 downregulates protein phosphatase PPM1B in bladder cancer and mediates G1-S phase transition."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Tumour Biol (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s13277-015-4117-4"}], "href": "https://doi.org/10.1007/s13277-015-4117-4"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26494000"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26494000"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Hanning Ying, Lin Ji, Zhiyao Xu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "TRIM59 promotes tumor growth in hepatocellular carcinoma and regulates the cell cycle by degradation of protein phosphatase 1B."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Lett (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.canlet.2019.12.030"}], "href": "https://doi.org/10.1016/j.canlet.2019.12.030"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31875525"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31875525"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "W Wang, L Zhou, Z Sun, et al. "}, {"type": "b", "children": [{"type": "t", "text": "[TRIM59 regulates invasion and migration of nasopharyngeal carcinoma cells by targeted modulation of PPM1B]."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nan Fang Yi Ke Da Xue Xue Bao (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.12122/j.issn.1673-4254.2021.07.09"}], "href": "https://doi.org/10.12122/j.issn.1673-4254.2021.07.09"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34308852"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34308852"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "G V Kakurina, E S Kolegova, E E Shashova, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Relationship between the Levels of mRNA Expression for Protein Phosphatase 1B and Proteins Involved in Cytoskeleton Remodeling in Squamous Cell Carcinoma of the Larynx and Hypopharynx."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Bull Exp Biol Med (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s10517-020-04918-2"}], "href": "https://doi.org/10.1007/s10517-020-04918-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32915364"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32915364"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Riheng Li, Jian Dou, Tianliang Bai, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein Phosphatase PPM1B Inhibits Gastric Cancer Progression and Serves as a Favorable Prognostic Biomarker."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Appl Immunohistochem Mol Morphol (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1097/PAI.0000000000001012"}], "href": "https://doi.org/10.1097/PAI.0000000000001012"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35319516"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35319516"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Rachel Elizabeth Miller, Nathalie Uwamahoro, Jeong Hyeon Park "}, {"type": "b", "children": [{"type": "t", "text": "PPM1B depletion in U2OS cells supresses cell growth through RB1-E2F1 pathway and stimulates bleomycin-induced cell death."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2018.04.084"}], "href": "https://doi.org/10.1016/j.bbrc.2018.04.084"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29654756"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29654756"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Yueyang Li, Di Wei, Zixiang Chen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RBM10 regulates the tumorigenic potential of human cancer cells by modulating PPM1B and YBX1 activities."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Cell Res (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.yexcr.2024.113932"}], "href": "https://doi.org/10.1016/j.yexcr.2024.113932"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38246397"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38246397"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Liping Du, Junyan Li, Yonglu Tian, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Protein phosphatase 2Cbetal regulates human pregnane X receptor-mediated CYP3A4 gene expression in HepG2 liver carcinoma cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Drug Metab Dispos (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1124/dmd.110.032128"}], "href": "https://doi.org/10.1124/dmd.110.032128"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20538721"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20538721"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Jian Yang, Xiangyan Li, Yuming Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Circ_0090231 knockdown protects vascular smooth muscle cells from ox-LDL-induced proliferation, migration and invasion via miR-942-5p/PPM1B axis during atherosclerosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell Biochem (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s11010-023-04811-2"}], "href": "https://doi.org/10.1007/s11010-023-04811-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37515673"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37515673"}]}]}]}
Synonyms	PPC2BETAX, PP2C-BETA-X, PP2CBETA, PP2C-BETA, PP2CB
Proteins	PPM1B_HUMAN
NCBI Gene ID	5495
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PPM1B has 7,598 functional associations with biological entities spanning 8 categories (molecular profile, organism, chemical, functional term, phrase or reference, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA) extracted from 131 datasets.

Click the + buttons to view associations for PPM1B from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

PPM1B Gene

Functional Associations

Please acknowledge the Harmonizome in your publications by citing the following reference(s):

	Dataset	Summary
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of PPM1B gene relative to other tissues from the Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles	tissues with high or low expression of PPM1B gene relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles	tissue samples with high or low expression of PPM1B gene relative to other tissue samples from the Allen Brain Atlas Aging Dementia and Traumatic Brain Injury Tissue Sample Gene Expression Profiles dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray	tissue samples with high or low expression of PPM1B gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq	tissue samples with high or low expression of PPM1B gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by RNA-seq dataset.
	Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of PPM1B gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of PPM1B gene relative to other cell lines from the BioGPS Cell Line Gene Expression Profiles dataset.
	BioGPS Human Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of PPM1B gene relative to other cell types and tissues from the BioGPS Human Cell Type and Tissue Gene Expression Profiles dataset.
	BioGPS Mouse Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of PPM1B gene relative to other cell types and tissues from the BioGPS Mouse Cell Type and Tissue Gene Expression Profiles dataset.
	Carcinogenome Chemical Perturbation Carcinogenicity Signatures	small molecule perturbations changing expression of PPM1B gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of PPM1B gene relative to other cell lines from the CCLE Cell Line Gene CNV Profiles dataset.
	CCLE Cell Line Gene Expression Profiles	cell lines with high or low expression of PPM1B gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PPM1B protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with PPM1B gene from the CellMarker Gene-Cell Type Associations dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of PPM1B gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PPM1B gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets dataset.
	ChEA Transcription Factor Targets 2022	transcription factors binding the promoter of PPM1B gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing PPM1B protein from integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of PPM1B gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing PPM1B protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing PPM1B protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing PPM1B protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores 2025	cellular components containing PPM1B protein in low- or high-throughput protein localization assays from the COMPARTMENTS Experimental Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with PPM1B protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025	cellular components co-occuring with PPM1B protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of PPM1B gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with PPM1B gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Disease Associations	diseases associated with PPM1B gene/protein from the curated CTD Gene-Disease Associations dataset.
	DepMap CRISPR Gene Dependency	cell lines with fitness changed by PPM1B gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores	diseases associated with PPM1B gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with PPM1B gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores 2025	diseases co-occuring with PPM1B gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.
	DisGeNET Gene-Disease Associations	diseases associated with PPM1B gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with PPM1B gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at PPM1B gene from the ENCODE Histone Modification Site Profiles dataset.
	ENCODE Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of PPM1B gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of PPM1B gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.
	ESCAPE Omics Signatures of Genes and Proteins for Stem Cells	PubMedIDs of publications reporting gene signatures containing PPM1B from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.
	GAD Gene-Disease Associations	diseases associated with PPM1B gene in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.
	GAD High Level Gene-Disease Associations	diseases associated with PPM1B gene in GWAS and other genetic association datasets from the GAD High Level Gene-Disease Associations dataset.