PRKCSH Gene

HGNC Family	EF-hand domain containing
Name	protein kinase C substrate 80K-H
Description	This gene encodes the beta-subunit of glucosidase II, an N-linked glycan-processing enzyme in the endoplasmic reticulum. The encoded protein is an acidic phosphoprotein known to be a substrate for protein kinase C. Mutations in this gene have been associated with the autosomal dominant polycystic liver disease. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPRKCSH encodes hepatocystin, a protein whose dysfunction is intimately linked to autosomal dominant polycystic liver disease (PCLD). Genetic studies have revealed that mutations in this gene disrupt its normal function in the endoplasmic reticulum, compromising its role in the processing and quality control of nascent glycoproteins. Hepatocystin, which is also known as protein kinase C substrate 80K‑H or the noncatalytic β‑subunit of glucosidase II, is predominantly localized within the ER and appears to be crucial for the proper development and maintenance of bile ducts. These findings, derived from extensive mutational analyses and expression studies in various patient cohorts, underscore a loss‑of‑function mechanism and even a potential two‑hit phenomenon contributing to cystogenesis in the liver."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n \n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in maintaining hepatic architecture, PRKCSH exerts multifaceted functions in the endoplasmic reticulum by engaging in critical protein–protein interactions. Hepatocystin functions as a chaperone‑like molecule by binding to targets such as TRPP2, thereby preventing their premature degradation, and it can modulate Ca²⁺ release through its interaction with the COOH‑terminal domain of IP3 receptors. Moreover, through its association with PKCζ and subsequent complex formation with proteins like munc18c, PRKCSH participates in the regulation of insulin‐stimulated GLUT4 vesicle trafficking. These molecular interactions highlight a conserved role for PRKCSH in ensuring proper folding, processing, and signaling of glycoproteins in diverse cellular contexts."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "14"}]}, {"type": "t", "text": "\n \n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its established role in hepatobiliary disease, accumulating evidence implicates PRKCSH in broader cellular processes including autophagy regulation, cell cycle control, and tumorigenesis. Hepatocystin deficiency can trigger mTOR‑dependent autophagy without perturbing unfolded protein response pathways, highlighting its role in cellular homeostasis. Aberrant expression of PRKCSH is also associated with enhanced tumor progression and altered immune cell infiltration in several cancers, and its interplay with proteins involved in Wnt/β‑catenin signaling and ciliogenesis may further widen its impact on disease pathogenesis. Moreover, emerging data suggest that dysregulation of PRKCSH may influence diabetic complications through its function as an AGE receptor, underscoring the pleiotropic nature of this protein."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "19"}]}, {"type": "t", "text": ""}]}]}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Joost P H Drenth, Rene H M te Morsche, Renate Smink, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Germline mutations in PRKCSH are associated with autosomal dominant polycystic liver disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nat Genet (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/ng1104"}], "href": "https://doi.org/10.1038/ng1104"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12577059"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12577059"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Airong Li, Sonia Davila, Laszlo Furu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mutations in PRKCSH cause isolated autosomal dominant polycystic liver disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Hum Genet (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1086/368295"}], "href": "https://doi.org/10.1086/368295"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12529853"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12529853"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Joost P H Drenth, Jose A Martina, Rene H M Te Morsche, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Molecular characterization of hepatocystin, the protein that is defective in autosomal dominant polycystic liver disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Gastroenterology (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1053/j.gastro.2004.02.023"}], "href": "https://doi.org/10.1053/j.gastro.2004.02.023"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15188177"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15188177"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Manoe J Janssen, Esmé Waanders, René H M Te Morsche, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Secondary, somatic mutations might promote cyst formation in patients with autosomal dominant polycystic liver disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Gastroenterology (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1053/j.gastro.2011.08.004"}], "href": "https://doi.org/10.1053/j.gastro.2011.08.004"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21856269"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21856269"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "E Waanders, H Venselaar, R H M te Morsche, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Secondary and tertiary structure modeling reveals effects of novel mutations in polycystic liver disease genes PRKCSH and SEC63."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Clin Genet (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/j.1399-0004.2009.01353.x"}], "href": "https://doi.org/10.1111/j.1399-0004.2009.01353.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20095989"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20095989"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Joost P H Drenth, Esa Tahvanainen, Rene H M te Morsche, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Abnormal hepatocystin caused by truncating PRKCSH mutations leads to autosomal dominant polycystic liver disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hepatology (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/hep.20141"}], "href": "https://doi.org/10.1002/hep.20141"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15057895"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15057895"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Esmé Waanders, Huib J E Croes, Cathy N Maass, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cysts of PRKCSH mutated polycystic liver disease patients lack hepatocystin but express Sec63p."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Histochem Cell Biol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00418-008-0381-3"}], "href": "https://doi.org/10.1007/s00418-008-0381-3"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18224332"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18224332"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Esmé Waanders, Anke L L Lameris, Huub J M Op den Camp, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hepatocystin is not secreted in cyst fluid of hepatocystin mutant polycystic liver patients."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Proteome Res (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/pr8000282"}], "href": "https://doi.org/10.1021/pr8000282"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18419150"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18419150"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "An-Ming Yang, Shou-Chuan Shih, Cheng-Hsin Chu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PRKCSH genetic mutation was not found in Taiwanese patients with polycystic liver disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Dig Dis Sci (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s10620-009-0776-6"}], "href": "https://doi.org/10.1007/s10620-009-0776-6"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19308730"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19308730"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Wybrich R Cnossen, Jake S F Maurits, Jody Salomon, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Severe Polycystic Liver Disease Is Not Caused by Large Deletions of the PRKCSH Gene."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Clin Lab Anal (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/jcla.21875"}], "href": "https://doi.org/10.1002/jcla.21875"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26365003"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26365003"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Hongyu Gao, Yan Wang, Tomasz Wegierski, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PRKCSH/80K-H, the protein mutated in polycystic liver disease, protects polycystin-2/TRPP2 against HERP-mediated degradation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddp463"}], "href": "https://doi.org/10.1093/hmg/ddp463"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19801576"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19801576"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Conrad P Hodgkinson, Ann Mander, Graham J Sale "}, {"type": "b", "children": [{"type": "t", "text": "Identification of 80K-H as a protein involved in GLUT4 vesicle trafficking."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem J (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1042/BJ20041845"}], "href": "https://doi.org/10.1042/BJ20041845"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15707389"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15707389"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Katsuhiro Kawaai, Chihiro Hisatsune, Yukiko Kuroda, et al. "}, {"type": "b", "children": [{"type": "t", "text": "80K-H interacts with inositol 1,4,5-trisphosphate (IP3) receptors and regulates IP3-induced calcium release activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M805828200"}], "href": "https://doi.org/10.1074/jbc.M805828200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18990696"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18990696"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Natalie P Smithers, Conrad P Hodgkinson, Matt Cuttle, et al. "}, {"type": "b", "children": [{"type": "t", "text": "80K-H acts as a signaling bridge in intact living cells between PKCzeta and the GLUT4 translocation regulator Munc18c."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Recept Signal Transduct Res (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/10799890802598571"}], "href": "https://doi.org/10.1080/10799890802598571"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19061073"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19061073"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Jing Yang, Ying Zhao, Ke Ma, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Deficiency of hepatocystin induces autophagy through an mTOR-dependent pathway."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Autophagy (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4161/auto.7.7.15822"}], "href": "https://doi.org/10.4161/auto.7.7.15822"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21681021"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21681021"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Edgar S Wills, René H M Te Morsche, Jeroen van Reeuwijk, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Liver cyst gene knockout in cholangiocytes inhibits cilium formation and Wnt signaling."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddx308"}], "href": "https://doi.org/10.1093/hmg/ddx308"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28973524"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28973524"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "A Hoverfelt, R Sallinen, J M Söderlund, et al. "}, {"type": "b", "children": [{"type": "t", "text": "DDOST, PRKCSH and LGALS3, which encode AGE-receptors 1, 2 and 3, respectively, are not associated with diabetic nephropathy in type 1 diabetes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Diabetologia (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00125-010-1771-3"}], "href": "https://doi.org/10.1007/s00125-010-1771-3"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20490454"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20490454"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Ridan Lei, Meiling Zhou, Shusheng Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Potential role of PRKCSH in lung cancer: bioinformatics analysis and a case study of Nano ZnO."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nanoscale (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1039/d1nr08133k"}], "href": "https://doi.org/10.1039/d1nr08133k"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35254362"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35254362"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Qiankun Wang, Xiong Wang, Jiaoyuan Li, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PRKCSH serves as a potential immunological and prognostic biomarker in pan-cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-024-52153-w"}], "href": "https://doi.org/10.1038/s41598-024-52153-w"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38245572"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38245572"}]}]}]}
Synonyms	G19P1, AGE-R2, VASAP-60, PCLD, PKCSH, PCLD1, PLD1, GIIB
Proteins	GLU2B_HUMAN
NCBI Gene ID	5589
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PRKCSH has 8,021 functional associations with biological entities spanning 9 categories (molecular profile, organism, disease, phenotype or trait, chemical, functional term, phrase or reference, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 120 datasets.

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

If available, associations are ranked by standardized value

Harmonizome 3.0

PRKCSH 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 PRKCSH 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 PRKCSH 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 PRKCSH gene relative to other tissues from the Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles dataset.
	Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray	tissue samples with high or low expression of PRKCSH 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 PRKCSH 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 PRKCSH 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 PRKCSH 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 PRKCSH 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 PRKCSH gene relative to other cell types and tissues from the BioGPS Mouse Cell Type and Tissue Gene Expression Profiles dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of PRKCSH 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 PRKCSH gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PRKCSH protein from the CCLE Cell Line Proteomics dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of PRKCSH gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PRKCSH 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 PRKCSH gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	ClinVar Gene-Phenotype Associations	phenotypes associated with PRKCSH gene from the curated ClinVar Gene-Phenotype Associations dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of PRKCSH gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing PRKCSH protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing PRKCSH protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing PRKCSH 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 PRKCSH 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 PRKCSH 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 PRKCSH 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 PRKCSH gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with PRKCSH gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with PRKCSH gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with PRKCSH gene/protein from the curated CTD Gene-Disease Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of PRKCSH 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 PRKCSH gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores 2025	diseases associated with PRKCSH 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 PRKCSH 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 PRKCSH 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 PRKCSH gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with PRKCSH 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 PRKCSH 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 PRKCSH gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of PRKCSH 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 PRKCSH from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.
	GAD Gene-Disease Associations	diseases associated with PRKCSH gene in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.
	GAD High Level Gene-Disease Associations	diseases associated with PRKCSH gene in GWAS and other genetic association datasets from the GAD High Level Gene-Disease Associations dataset.