PRKAR2A Gene

Name	protein kinase, cAMP-dependent, regulatory, type II, alpha
Description	cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase, which transduces the signal through phosphorylation of different target proteins. The inactive kinase holoenzyme is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits have been identified in humans. The protein encoded by this gene is one of the regulatory subunits. This subunit can be phosphorylated by the activated catalytic subunit. It may interact with various A-kinase anchoring proteins and determine the subcellular localization of cAMP-dependent protein kinase. This subunit has been shown to regulate protein transport from endosomes to the Golgi apparatus and further to the endoplasmic reticulum (ER). [provided by RefSeq, Jul 2008]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPRKAR2A encodes the regulatory subunit RIIα of cyclic AMP–dependent protein kinase (PKA), which plays a central role in targeting the kinase to discrete subcellular compartments. High‐resolution structural analyses have revealed that the dimerization/docking (D/D) domain of RIIα, by accommodating amphipathic helices from A-kinase anchoring proteins (AKAPs), ensures both high-affinity binding and isoform specificity, thereby mediating localized cAMP signaling events. This precise anchoring is critical for directing PKA activity within particular cellular microdomains."}, {"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": "\nIn polarized cells, the localization of RIIα is essential for the regulation of membrane trafficking and cellular architecture. In hepatocytes, for example, RIIα anchoring at the Golgi apparatus facilitates the direct apical targeting of proteins and glycosphingolipids required for bile canalicular lumen development, while in the human myometrium its expression increases during gestation to modulate the cytoskeletal elements underlying contractile quiescence."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "4", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPRKAR2A also contributes to the dynamic regulation of PKA holoenzyme activity through mechanisms such as autophosphorylation and cAMP-induced dissociation. Alterations in RIIα phosphorylation, as observed in conditions like heart failure where enhanced site-specific phosphorylation occurs, can modulate downstream signaling cascades and alter cellular responses."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "2"}, {"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its classical role in cAMP signaling, RIIα is capable of binding alternative cyclic nucleotides and engaging in non-canonical interactions. For instance, cCMP has been shown to activate RIIα, broadening the repertoire of its regulatory functions, while direct binding of transcriptional modulators such as Smad4 links TGFβ signaling to PKA activity and influences processes like epithelial–mesenchymal transition."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nThe balance between PKA regulatory isoforms is a crucial determinant of cellular proliferation and differentiation. Studies comparing the effects of modulating PKA-I and PKA-II levels indicate that an altered RI:RII ratio can tip the scales between malignant transformation and phenotypic reversion."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": " In certain malignancies, such as fibrolamellar carcinoma and other liver tumors, genetic inactivation or mutation of PRKAR2A has been implicated in cellular dedifferentiation and transdifferentiation, while therapeutic shRNA-mediated downregulation in glioblastoma models has been associated with reduced tumor cell viability."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "13"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, RIIα’s expression and function are context dependent. Its role is underscored by interactions with novel anchoring partners such as neurochondrin that display strong isoform selectivity, as well as by observations from developmental studies; for example, in human odontogenesis, PRKAR2A is expressed in tooth germ tissues—a pattern that contrasts with that observed in mice—and comprehensive analyses of PKA subunit balance further highlight the importance of PRKAR2A in fine-tuning intracellular signaling networks."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Matthew G Gold, Birgitte Lygren, Pawel Dokurno, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Molecular basis of AKAP specificity for PKA regulatory subunits."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2006.09.006"}], "href": "https://doi.org/10.1016/j.molcel.2006.09.006"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17081989"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17081989"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Brent R Martin, Thomas J Deerinck, Mark H Ellisman, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Isoform-specific PKA dynamics revealed by dye-triggered aggregation and DAKAP1alpha-mediated localization in living cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Chem Biol (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.chembiol.2007.07.017"}], "href": "https://doi.org/10.1016/j.chembiol.2007.07.017"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17884635"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17884635"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Jennifer S Hermann, Philipp Skroblin, Daniela Bertinetti, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Neurochondrin is an atypical RIIα-specific A-kinase anchoring protein."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbapap.2015.04.018"}], "href": "https://doi.org/10.1016/j.bbapap.2015.04.018"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25916936"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25916936"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Kacper A Wojtal, Erik de Vries, Dick Hoekstra, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Efficient trafficking of MDR1/P-glycoprotein to apical canalicular plasma membranes in HepG2 cells requires PKA-RIIalpha anchoring and glucosylceramide."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Cell (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1091/mbc.e06-03-0230"}], "href": "https://doi.org/10.1091/mbc.e06-03-0230"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16723498"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16723498"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Malcolm W J MacDougall, G Nicholas Europe-Finner, Stephen C Robson "}, {"type": "b", "children": [{"type": "t", "text": "Human myometrial quiescence and activation during gestation and parturition involve dramatic changes in expression and activity of particulate type II (RII alpha) protein kinase A holoenzyme."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Clin Endocrinol Metab (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1210/jc.2002-021862"}], "href": "https://doi.org/10.1210/jc.2002-021862"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12727975"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12727975"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Kacper A Wojtal, Dick Hoekstra, Sven C D van Ijzendoorn "}, {"type": "b", "children": [{"type": "t", "text": "Anchoring of protein kinase A-regulatory subunit IIalpha to subapically positioned centrosomes mediates apical bile canalicular lumen development in response to oncostatin M but not cAMP."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Cell (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1091/mbc.e06-08-0732"}], "href": "https://doi.org/10.1091/mbc.e06-08-0732"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17494870"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17494870"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Young Soo Han, Jennifer Arroyo, Ozgur Ogut "}, {"type": "b", "children": [{"type": "t", "text": "Human heart failure is accompanied by altered protein kinase A subunit expression and post-translational state."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Arch Biochem Biophys (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.abb.2013.08.002"}], "href": "https://doi.org/10.1016/j.abb.2013.08.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23942052"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23942052"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Andreas Hammerschmidt, Bijon Chatterji, Johannes Zeiser, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Binding of regulatory subunits of cyclic AMP-dependent protein kinase to cyclic CMP agarose."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0039848"}], "href": "https://doi.org/10.1371/journal.pone.0039848"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22808067"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22808067"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Huibin Yang, Gangyong Li, Jing-Jiang Wu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Protein kinase A modulates transforming growth factor-β signaling through a direct interaction with Smad4 protein."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M113.455675"}], "href": "https://doi.org/10.1074/jbc.M113.455675"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23362281"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23362281"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Yoon S Cho-Chung, Maria V Nesterova "}, {"type": "b", "children": [{"type": "t", "text": "Tumor reversion: protein kinase A isozyme switching."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Ann N Y Acad Sci (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1196/annals.1359.014"}], "href": "https://doi.org/10.1196/annals.1359.014"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16394127"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16394127"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Dan-Na Chen, Yan-Tao Ma, Huadie Liu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Functional rescue of Kallmann syndrome-associated prokineticin receptor 2 (PKR2) mutants deficient in trafficking."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M114.556381"}], "href": "https://doi.org/10.1074/jbc.M114.556381"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24753254"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24753254"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Laura Rüland, Francesco Andreatta, Simone Massalini, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Organoid models of fibrolamellar carcinoma mutations reveal hepatocyte transdifferentiation through cooperative BAP1 and PRKAR2A loss."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Commun (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41467-023-37951-6"}], "href": "https://doi.org/10.1038/s41467-023-37951-6"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37137901"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37137901"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Maira Zorzan, Claudia Del Vecchio, Stefania Vogiatzis, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Targeting the Regulatory Subunit R2Alpha of Protein Kinase A in Human Glioblastoma through shRNA-Expressing Lentiviral Vectors."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Viruses (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3390/v13071361"}], "href": "https://doi.org/10.3390/v13071361"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34372567"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34372567"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Sílvia Ferreira de Sousa, Katsushige Kawasaki, Maiko Kawasaki, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PKA regulatory subunit expression in tooth development."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Gene Expr Patterns (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.gep.2014.04.002"}], "href": "https://doi.org/10.1016/j.gep.2014.04.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24755349"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24755349"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Emmanouil Saloustros, Paraskevi Salpea, Chen-Feng Qi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hematopoietic neoplasms in Prkar2a-deficient mice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Exp Clin Cancer Res (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/s13046-015-0257-z"}], "href": "https://doi.org/10.1186/s13046-015-0257-z"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26608815"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26608815"}]}]}]}
Synonyms	PRKAR2, PKR2
Proteins	KAP2_HUMAN
NCBI Gene ID	5576
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PRKAR2A has 8,898 functional associations with biological entities spanning 8 categories (molecular profile, organism, functional term, phrase or reference, chemical, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA) extracted from 137 datasets.

Click the + buttons to view associations for PRKAR2A from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

PRKAR2A Gene

Functional Associations

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

	Dataset	Summary
	Achilles Cell Line Gene Essentiality Profiles	cell lines with fitness changed by PRKAR2A gene knockdown relative to other cell lines from the Achilles Cell Line Gene Essentiality Profiles dataset.
	Allen Brain Atlas Adult Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of PRKAR2A 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 PRKAR2A 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 PRKAR2A 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 PRKAR2A 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 PRKAR2A 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 PRKAR2A gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	Biocarta Pathways	pathways involving PRKAR2A protein from the Biocarta Pathways dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of PRKAR2A 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 PRKAR2A 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 PRKAR2A 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 PRKAR2A gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of PRKAR2A 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 PRKAR2A gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PRKAR2A protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with PRKAR2A 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 PRKAR2A gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PRKAR2A 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 PRKAR2A 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 PRKAR2A gene from the CM4AI KOLF21J CRISPRi Gene Perturbation Atlas dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of PRKAR2A gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing PRKAR2A protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing PRKAR2A protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores 2025	cellular components containing PRKAR2A 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 PRKAR2A 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 PRKAR2A protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	CORUM Protein Complexes	protein complexs containing PRKAR2A protein from the CORUM Protein Complexes dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of PRKAR2A gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with PRKAR2A gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with PRKAR2A gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with PRKAR2A gene/protein from the curated CTD Gene-Disease Associations dataset.
	DepMap CRISPR Gene Dependency	cell lines with fitness changed by PRKAR2A gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DEPOD Substrates of Phosphatases	phosphatases that dephosphorylate PRKAR2A protein from the curated DEPOD Substrates of Phosphatases dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores 2025	diseases associated with PRKAR2A gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores 2025 dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with PRKAR2A 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 PRKAR2A 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 PRKAR2A gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with PRKAR2A gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.
	DrugBank Drug Targets	interacting drugs for PRKAR2A protein from the curated DrugBank Drug Targets dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at PRKAR2A gene from the ENCODE Histone Modification Site Profiles dataset.