PRKACB Gene

Name	protein kinase, cAMP-dependent, catalytic, beta
Description	The protein encoded by this gene is a member of the serine/threonine protein kinase family. The encoded protein is a catalytic subunit of cAMP (cyclic AMP)-dependent protein kinase, which mediates signalling though cAMP. cAMP signaling is important to a number of processes, including cell proliferaton and differentiation. Multiple alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2014]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe PRKACB gene encodes the beta catalytic subunit of cyclic AMP‐dependent protein kinase (PKA) and plays a central role in transducing cAMP signals that regulate key cellular processes. For instance, c‐MYC directly induces PRKACB transcription to boost PKA activity and promote cellular transformation, while a specific variant of PKA‐Cβ has been shown to interact with the neurotrophin receptor p75(NTR), phosphorylating it at Ser304 to facilitate its lipid raft translocation and consequent neurite outgrowth. Moreover, PKA‐Cβ directly phosphorylates transcription factors such as p73, leading to an intramolecular interaction that ultimately suppresses p73’s pro‐apoptotic function, and it localizes to nuclear splicing factor compartments where it modulates alternative pre–mRNA splicing."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "4"}]}, {"type": "t", "text": "Disruption of PRKACB function is also implicated in various human diseases. In neuropsychiatric and mood disorders, for example, altered expression levels of PKA‐Cβ have been detected in the prefrontal cortex of depressed individuals. In prostate cancer, differential regulation of PRKACB splice variants has been observed during neuroendocrine differentiation, with some variants correlating with tumor progression. In airway epithelial cells, PKA‐Cβ is essential for phosphorylating the NF‐κB p65 subunit at Ser276, an event that underlies the synergistic induction of PDE4B2 and contributes to inflammatory signaling. Additionally, the human Cβ isoform expressed predominantly in the brain, as well as its promoter characteristics, suggest an important role in neuroprotection against toxic proteins such as tau and Aβ."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "5", "end_ref": "10"}]}, {"type": "t", "text": "Genetic alterations involving PRKACB further underscore its multifaceted roles in human development and disease. Germline mutations in PRKACB that increase the sensitivity of PKA holoenzymes to cAMP have been linked to congenital malformation syndromes characterized by cardiac defects, polydactyly, skeletal anomalies, and ectodermal defects. In disorders resembling primary pigmented nodular adrenocortical disease, rare PRKACB variants affect protein stability and lead to aberrant PKA signaling, thereby contributing to endocrine and skeletal abnormalities. In addition, studies in yeast and mammalian cells have revealed that PRKACB phosphorylates key factors required for non‐homologous end joining, highlighting a role in DNA double‐strand break repair. Tissue‐specific interaction mapping using advanced purification techniques has further identified numerous binding partners of PKA‐Cβ, and recurrent fusion events involving PRKACB—as seen in intraductal oncocytic papillary neoplasms—emphasize its impact on oncogenic signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "17"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Kou-Juey Wu, Michela Mattioli, Herbert C Morse, et al. "}, {"type": "b", "children": [{"type": "t", "text": "c-MYC activates protein kinase A (PKA) by direct transcriptional activation of the PKA catalytic subunit beta (PKA-Cbeta) gene."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.onc.1205986"}], "href": "https://doi.org/10.1038/sj.onc.1205986"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12420224"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12420224"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Haruhisa Higuchi, Toshihide Yamashita, Hideki Yoshikawa, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PKA phosphorylates the p75 receptor and regulates its localization to lipid rafts."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO J (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/emboj/cdg177"}], "href": "https://doi.org/10.1093/emboj/cdg177"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12682012"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12682012"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Takayuki Hanamoto, Toshinori Ozaki, Kazushige Furuya, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification of protein kinase A catalytic subunit beta as a novel binding partner of p73 and regulation of p73 function."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M414323200"}], "href": "https://doi.org/10.1074/jbc.M414323200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15723830"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15723830"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Anne-Katrine Kvissel, Sigurd Ørstavik, Sissel Eikvar, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Involvement of the catalytic subunit of protein kinase A and of HA95 in pre-mRNA splicing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Cell Res (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.yexcr.2007.05.014"}], "href": "https://doi.org/10.1016/j.yexcr.2007.05.014"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17594903"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17594903"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Ane Funderud, Heidi H Henanger, Tilahun T Hafte, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Identification, cloning and characterization of a novel 47 kDa murine PKA C subunit homologous to human and bovine Cbeta2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "BMC Biochem (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/1471-2091-7-20"}], "href": "https://doi.org/10.1186/1471-2091-7-20"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16889664"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16889664"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Anne-Katrine Kvissel, Håkon Ramberg, Turid Eide, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Androgen dependent regulation of protein kinase A subunits in prostate cancer cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Signal (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cellsig.2006.07.011"}], "href": "https://doi.org/10.1016/j.cellsig.2006.07.011"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16949795"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16949795"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Richard C Shelton, D Hal Manier, David A Lewis "}, {"type": "b", "children": [{"type": "t", "text": "Protein kinases A and C in post-mortem prefrontal cortex from persons with major depression and normal controls."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Neuropsychopharmacol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1017/S1461145709000285"}], "href": "https://doi.org/10.1017/S1461145709000285"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19573263"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19573263"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Seiko Susuki-Miyata, Masanori Miyata, Byung-Cheol Lee, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cross-talk between PKA-Cβ and p65 mediates synergistic induction of PDE4B by roflumilast and NTHi."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1418716112"}], "href": "https://doi.org/10.1073/pnas.1418716112"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25831493"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25831493"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Line Victoria Moen, Håkon Ramberg, Sen Zhao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Observed correlation between the expression levels of catalytic subunit, Cβ2, of cyclic adenosine monophosphate-dependent protein kinase and prostate cancer aggressiveness."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Urol Oncol (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.urolonc.2016.10.002"}], "href": "https://doi.org/10.1016/j.urolonc.2016.10.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27838142"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27838142"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Safoura Khamse, Zahra Jafarian, Ali Bozorgmehr, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Novel implications of a strictly monomorphic (GCC) repeat in the human PRKACB gene."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-021-99932-3"}], "href": "https://doi.org/10.1038/s41598-021-99932-3"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34667254"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34667254"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Andrea Erlbruch, Chien-Wen Hung, Joerg Seidler, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Uncoupling of bait-protein expression from the prey protein environment adds versatility for cell and tissue interaction proteomics and reveals a complex of CARP-1 and the PKA Cbeta1 subunit."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proteomics (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/pmic.200900593"}], "href": "https://doi.org/10.1002/pmic.200900593"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20564261"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20564261"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Adrian Palencia-Campos, Phillip C Aoto, Erik M F Machal, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Germline and Mosaic Variants in PRKACA and PRKACB Cause a Multiple Congenital Malformation Syndrome."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Hum Genet (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ajhg.2020.09.005"}], "href": "https://doi.org/10.1016/j.ajhg.2020.09.005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33058759"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33058759"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Stephanie Espiard, Ludivine Drougat, Nikolaos Settas, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PRKACB variants in skeletal disease or adrenocortical hyperplasia: effects on protein kinase A."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Endocr Relat Cancer (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1530/ERC-20-0309"}], "href": "https://doi.org/10.1530/ERC-20-0309"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33055300"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33055300"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Matthew Jessulat, Shahreen Amin, Mohsen Hooshyar, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The conserved Tpk1 regulates non-homologous end joining double-strand break repair by phosphorylation of Nej1, a homolog of the human XLF."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nucleic Acids Res (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/nar/gkab585"}], "href": "https://doi.org/10.1093/nar/gkab585"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34244791"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34244791"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Yifare Maimaitiaili, Yuki Fukumura, Kenichi Hirabayashi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Investigation of -PRKACA/-PRKACB fusion genes in oncocytic tumors of the pancreatobiliary and other systems."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Virchows Arch (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00428-022-03415-3"}], "href": "https://doi.org/10.1007/s00428-022-03415-3"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36152045"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36152045"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Taito Itoh, Yuko Omori, Mitsuru Seino, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Gene Rearrangement and Expression of PRKACA and PRKACB Govern Morphobiology of Pancreatobiliary Oncocytic Neoplasms."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mod Pathol (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.modpat.2023.100358"}], "href": "https://doi.org/10.1016/j.modpat.2023.100358"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37871652"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37871652"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Mariko Tanaka, Kimiko Takeshita, Akiko Kunita, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PRKACA/PRKACB Fusions in Pancreatobiliary Intraductal Oncocytic Papillary Neoplasms Including Those With Atypical Morphology: An Analysis of 22 Cases Expanding Morphologic Spectrum."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Surg Pathol (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1097/PAS.0000000000002259"}], "href": "https://doi.org/10.1097/PAS.0000000000002259"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38841868"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38841868"}]}]}]}
Synonyms	PKA C-BETA, PKACB
Proteins	KAPCB_HUMAN
NCBI Gene ID	5567
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PRKACB has 13,772 functional associations with biological entities spanning 9 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, sequence feature) extracted from 132 datasets.

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

If available, associations are ranked by standardized value

Harmonizome 3.0

PRKACB 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 PRKACB 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 PRKACB 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 PRKACB 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 PRKACB 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 PRKACB 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 PRKACB gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	Biocarta Pathways	pathways involving PRKACB protein from the Biocarta Pathways dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of PRKACB 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 PRKACB 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 PRKACB 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 PRKACB gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of PRKACB 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 PRKACB gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Gene Mutation Profiles	cell lines with PRKACB gene mutations from the CCLE Cell Line Gene Mutation Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PRKACB protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with PRKACB 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 PRKACB gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PRKACB 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 PRKACB gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of PRKACB gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing PRKACB protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing PRKACB protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with PRKACB 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 PRKACB protein in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.
	CORUM Protein Complexes	protein complexs containing PRKACB protein from the CORUM Protein Complexes dataset.
	COSMIC Cell Line Gene CNV Profiles	cell lines with high or low copy number of PRKACB gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with PRKACB gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with PRKACB gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with PRKACB gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with PRKACB gene in GWAS and other genetic association datasets from the dbGAP Gene-Trait Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of PRKACB protein relative to other small molecule perturbations from the DeepCoverMOA Drug Mechanisms of Action dataset.
	DepMap CRISPR Gene Dependency	cell lines with fitness changed by PRKACB gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with PRKACB 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 PRKACB 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 PRKACB gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with PRKACB gene in GWAS and other genetic association datasets from the DisGeNET Gene-Phenoptype Associations dataset.
	DrugBank Drug Targets	interacting drugs for PRKACB protein from the curated DrugBank Drug Targets dataset.
	ENCODE Histone Modification Site Profiles	histone modification site profiles with high histone modification abundance at PRKACB 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 PRKACB gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of PRKACB gene in ChIP-seq datasets from the ENCODE Transcription Factor Targets dataset.