PPP1R9B Gene

HGNC Family	Protein phosphatase 1 regulatory subunits (PPP1R)
Name	protein phosphatase 1, regulatory subunit 9B
Description	This gene encodes a scaffold protein that functions as a regulatory subunit of protein phosphatase 1a. Expression of this gene is particularly high in dendritic spines, suggesting that the encoded protein may play a role in receiving signals from the central nervous system. The encoded protein has putative tumor suppressor function and decreased expression has been observed in tumors. [provided by RefSeq, Feb 2014]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPPP1R9B, also known as spinophilin or neurabin‐II, is a multifunctional scaffold that couples the ubiquitous serine/threonine phosphatase PP1 to specific substrates, thereby imparting spatial and temporal specificity to dephosphorylation events. In neurons, PPP1R9B is highly enriched in dendritic spines where its actin‐binding properties facilitate the formation and stabilization of postsynaptic structures. By targeting PP1 to dendritic compartments, it regulates glutamate receptor activity and modulates downstream signaling cascades—including ERK, calcium, and Rac1 pathways—that underlie synaptic plasticity and neurotransmission. Moreover, PPP1R9B interacts with a variety of receptor systems (group I metabotropic glutamate receptors, opioid receptors, α₂‑adrenergic receptors, and adenosine receptors) and plays roles in neuroprotective as well as neuromodulatory processes; its altered expression has been linked to dysfunctions observed in Alzheimer’s disease, Parkinson’s disease, and even in the assembly and maturation of natural killer cell immunological synapses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond the nervous system, PPP1R9B exerts critical functions in regulating cellular growth, adhesion, and migration. Its downregulation is associated with enhanced tumorigenicity, increased cancer stem cell traits, and aggressive behavior in cancers such as those of the breast, colorectum, and head and neck. In these contexts, PPP1R9B influences cell cycle progression—partly through effects on retinoblastoma protein phosphorylation—and modulates cytoskeletal dynamics by interacting with Rac exchange factors and other signaling proteins. In platelets, it contributes to maintaining quiescence and fine‐tunes activation responses by orchestrating the assembly and disassembly of multi‐protein complexes, thereby balancing prothrombotic and antithrombotic signals."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nOverall, the dual roles of PPP1R9B—as a precise PP1-targeting module in neuronal signaling and as a regulator of cell adhesion, migration, and proliferation in peripheral tissues—highlight its importance as an integrator of cytoskeletal and cell cycle control. Its involvement in both synaptic modulation and tumor suppression not only provides insights into the molecular basis of neurodegenerative and psychiatric disorders but also suggests that modulation of PPP1R9B function could represent a promising therapeutic strategy for a range of diseases.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Stacie D Grossman, Linda C Hsieh-Wilson, Patrick B Allen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The actin-binding domain of spinophilin is necessary and sufficient for targeting to dendritic spines."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neuromolecular Med (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1385/NMM:2:1:61"}], "href": "https://doi.org/10.1385/NMM:2:1:61"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12230305"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12230305"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Xiaobo Meng, Namita Kanwar, Qiujiang Du, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PPP1R9B (Neurabin 2): involvement and dynamics in the NK immunological synapse."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Eur J Immunol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/eji.200838474"}], "href": "https://doi.org/10.1002/eji.200838474"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19130477"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19130477"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Wolfgang Peti, Angus C Nairn, Rebecca Page "}, {"type": "b", "children": [{"type": "t", "text": "Structural basis for protein phosphatase 1 regulation and specificity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "FEBS J (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/j.1742-4658.2012.08509.x"}], "href": "https://doi.org/10.1111/j.1742-4658.2012.08509.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22284538"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22284538"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Christopher Cottingham, Xiaohua Li, Qin Wang "}, {"type": "b", "children": [{"type": "t", "text": "Noradrenergic antidepressant responses to desipramine in vivo are reciprocally regulated by arrestin3 and spinophilin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neuropharmacology (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.neuropharm.2012.02.011"}], "href": "https://doi.org/10.1016/j.neuropharm.2012.02.011"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22369787"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22369787"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Danai-Dionysia Fourla, Maria-Pagona Papakonstantinou, Stavroula-Maria Vrana, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Selective interactions of spinophilin with the C-terminal domains of the δ- and μ-opioid receptors and G proteins differentially modulate opioid receptor signaling."}]}, {"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.2012.08.002"}], "href": "https://doi.org/10.1016/j.cellsig.2012.08.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22922354"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22922354"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Andrea R Di Sebastiano, Sandra Fahim, Henry A Dunn, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Role of Spinophilin in Group I Metabotropic Glutamate Receptor Endocytosis, Signaling, and Synaptic Plasticity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M116.722355"}], "href": "https://doi.org/10.1074/jbc.M116.722355"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27358397"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27358397"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Mujeeburahiman Cheerathodi, Naze G Avci, Paola A Guerrero, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The Cytoskeletal Adapter Protein Spinophilin Regulates Invadopodia Dynamics and Tumor Cell Invasion in Glioblastoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cancer Res (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/1541-7786.MCR-16-0251"}], "href": "https://doi.org/10.1158/1541-7786.MCR-16-0251"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27655131"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27655131"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Zhiping Mi, Eric E Abrahamson, Angela Y Ryu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Loss of precuneus dendritic spines immunopositive for spinophilin is related to cognitive impairment in early Alzheimer's disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neurobiol Aging (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.neurobiolaging.2017.01.022"}], "href": "https://doi.org/10.1016/j.neurobiolaging.2017.01.022"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28259365"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28259365"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Andrew C Hiday, Michael C Edler, Asma B Salek, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mechanisms and Consequences of Dopamine Depletion-Induced Attenuation of the Spinophilin/Neurofilament Medium Interaction."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neural Plast (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1155/2017/4153076"}], "href": "https://doi.org/10.1155/2017/4153076"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28634551"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28634551"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Yunjia Chen, Christopher Booth, Hongxia Wang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Effective Attenuation of Adenosine A1R Signaling by Neurabin Requires Oligomerization of Neurabin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Pharmacol (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1124/mol.117.109462"}], "href": "https://doi.org/10.1124/mol.117.109462"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28954816"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28954816"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "M Sagara, Y Kawasaki, S-i Iemura, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Asef2 and Neurabin2 cooperatively regulate actin cytoskeletal organization and are involved in HGF-induced cell migration."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/onc.2008.478"}], "href": "https://doi.org/10.1038/onc.2008.478"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19151759"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19151759"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Soumitra Rajagopal, Yuxin Ji, Kun Xu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Scaffold proteins IRSp53 and spinophilin regulate localized Rac activation by T-lymphocyte invasion and metastasis protein 1 (TIAM1)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M109.051490"}], "href": "https://doi.org/10.1074/jbc.M109.051490"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20360004"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20360004"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Peisong Ma, Aleksandra Cierniewska, Rachel Signarvic, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A newly identified complex of spinophilin and the tyrosine phosphatase, SHP-1, modulates platelet activation by regulating G protein-dependent signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2011-10-387910"}], "href": "https://doi.org/10.1182/blood-2011-10-387910"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22210881"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22210881"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "A Aigelsreiter, A L Ress, K Bettermann, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Low expression of the putative tumour suppressor spinophilin is associated with higher proliferative activity and poor prognosis in patients with hepatocellular carcinoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Br J Cancer (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/bjc.2013.165"}], "href": "https://doi.org/10.1038/bjc.2013.165"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23591196"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23591196"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Purificacion Estevez-Garcia, Iker Lopez-Calderero, Sonia Molina-Pinelo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Spinophilin loss correlates with poor patient prognosis in advanced stages of colon carcinoma."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Clin Cancer Res (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/1078-0432.CCR-13-0057"}], "href": "https://doi.org/10.1158/1078-0432.CCR-13-0057"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23729363"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23729363"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Alena Maria Aigelsreiter, Ariane Aigelsreiter, Martin Wehrschuetz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Loss of the putative tumor suppressor protein spinophilin is associated with poor prognosis in head and neck cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Pathol (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.humpath.2013.11.014"}], "href": "https://doi.org/10.1016/j.humpath.2013.11.014"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24565202"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24565202"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Anna Lena Ress, Verena Stiegelbauer, Daniela Schwarzenbacher, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Spinophilin expression determines cellular growth, cancer stemness and 5-flourouracil resistance in colorectal cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncotarget (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/oncotarget.2329"}], "href": "https://doi.org/10.18632/oncotarget.2329"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25261368"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25261368"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Daniela Schwarzenbacher, Verena Stiegelbauer, Alexander Deutsch, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Low spinophilin expression enhances aggressive biological behavior of breast cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncotarget (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/oncotarget.3586"}], "href": "https://doi.org/10.18632/oncotarget.3586"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25857299"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25857299"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "I Ferrer, E M Verdugo-Sivianes, M A Castilla, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Loss of the tumor suppressor spinophilin (PPP1R9B) increases the cancer stem cell population in breast tumors."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/onc.2015.341"}], "href": "https://doi.org/10.1038/onc.2015.341"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26387546"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26387546"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Eva M Verdugo-Sivianes, Ana M Rojas, Sandra Muñoz-Galván, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mutation of SPINOPHILIN (PPP1R9B) found in human tumors promotes the tumorigenic and stemness properties of cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Theranostics (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.7150/thno.53572"}], "href": "https://doi.org/10.7150/thno.53572"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33537097"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33537097"}]}]}]}
Synonyms	PPP1R9, SPINO
Proteins	NEB2_HUMAN
NCBI Gene ID	84687
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PPP1R9B has 9,326 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 114 datasets.

Click the + buttons to view associations for PPP1R9B from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

PPP1R9B 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 PPP1R9B 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 PPP1R9B 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 PPP1R9B 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 PPP1R9B gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray dataset.
	Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of PPP1R9B gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	BioGPS Human Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of PPP1R9B 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 PPP1R9B 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 PPP1R9B gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of PPP1R9B 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 PPP1R9B gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PPP1R9B protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with PPP1R9B 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 PPP1R9B gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PPP1R9B 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 PPP1R9B gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	CM4AI KOLF21J CRISPRi Gene Perturbation Atlas	gene perturbations changing expression of PPP1R9B gene from the CM4AI KOLF21J CRISPRi Gene Perturbation Atlas dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing PPP1R9B protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing PPP1R9B protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores 2025	cellular components containing PPP1R9B 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 PPP1R9B 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 PPP1R9B 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 PPP1R9B gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with PPP1R9B gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with PPP1R9B gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with PPP1R9B gene in GWAS and other genetic association datasets from the dbGAP Gene-Trait Associations dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with PPP1R9B 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 PPP1R9B 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 PPP1R9B gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with PPP1R9B 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 PPP1R9B 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 PPP1R9B gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of PPP1R9B 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 PPP1R9B from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.
	GAD Gene-Disease Associations	diseases associated with PPP1R9B gene in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.
	GAD High Level Gene-Disease Associations	diseases associated with PPP1R9B gene in GWAS and other genetic association datasets from the GAD High Level Gene-Disease Associations dataset.
	GeneRIF Biological Term Annotations	biological terms co-occuring with PPP1R9B gene in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.
	GeneSigDB Published Gene Signatures	PubMedIDs of publications reporting gene signatures containing PPP1R9B from the GeneSigDB Published Gene Signatures dataset.
	GEO Signatures of Differentially Expressed Genes for Diseases	disease perturbations changing expression of PPP1R9B gene from the GEO Signatures of Differentially Expressed Genes for Diseases dataset.
	GEO Signatures of Differentially Expressed Genes for Gene Perturbations	gene perturbations changing expression of PPP1R9B gene from the GEO Signatures of Differentially Expressed Genes for Gene Perturbations dataset.
	GEO Signatures of Differentially Expressed Genes for Kinase Perturbations	kinase perturbations changing expression of PPP1R9B gene from the GEO Signatures of Differentially Expressed Genes for Kinase Perturbations dataset.