PAFAH1B2 Gene

Name	platelet-activating factor acetylhydrolase 1b, catalytic subunit 2 (30kDa)
Description	Platelet-activating factor acetylhydrolase (PAFAH) inactivates platelet-activating factor (PAF) into acetate and LYSO-PAF. This gene encodes the beta subunit of PAFAH, the other subunits are alpha and gamma. Multiple alternatively spliced transcript variants have been described for this gene. [provided by RefSeq, Jan 2014]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nRecent studies have shown that PAFAH1B2, a catalytic subunit of type I platelet‐activating factor acetylhydrolase, plays a multifaceted role in cellular lipid metabolism that influences cancer pathogenicity. Activity‐based protein profiling revealed that PAFAH1B2 is consistently upregulated by a variety of oncogenes, and pharmacological inhibition of this enzyme impairs the viability and invasive behaviors of multiple cancer cell types—including breast, ovarian, melanoma, prostate, and pancreatic ductal adenocarcinoma. In breast and pancreatic cancers, PAFAH1B2 elevation is linked to enhanced epithelial–mesenchymal transition, cell migration, and metastasis, in part via modulation of PAF levels that govern key signaling events. These findings indicate that aberrant PAFAH1B2 activity promotes tumor progression by altering lipid mediator balances critical for oncogenic signaling."}, {"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 addition to its role in cancer biology, PAFAH1B2 is a key enzyme in aspirin metabolism. Purification studies from human erythrocytes and plasma have identified that the intracellular type I PAF acetylhydrolase complex—comprising PAFAH1B2 and its closely related subunit PAFAH1B3—effectively hydrolyzes the acetyl moiety of circulating aspirin. This enzymatic activity modulates aspirin’s bioavailability and its ability to inhibit platelet aggregation, with competitive interactions between exogenous PAF and aspirin contributing to inter-individual variability in aspirin response. Notably, aspirin hydrolysis in blood occurs via distinct mechanisms in erythrocytes versus plasma, with PAFAH1B2 playing a prominent role alongside butyrylcholinesterase."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond cancer and drug metabolism, PAFAH1B2 is implicated in diverse physiological processes. Overexpression studies have demonstrated that increased levels of PAFAH1B2 can disrupt dynein motor function by competing with Ndel1 for Lis1 binding, thereby affecting neuronal migration and mitotic progression—a finding that underscores its importance in neurodevelopment."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": " In the context of Alzheimer’s disease, RNA interference screens have revealed that knockdown of PAFAH1B2 enhances the degradation of amyloid precursor protein C-terminal fragments, leading to a marked reduction in Aβ production and suggesting a potential neuroprotective effect."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "7"}]}, {"type": "t", "text": " Complementary studies have identified splice variants of PAFAH1B2—with tissue-specific expression patterns such as in the testis—that may further diversify its cellular functions."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "8"}]}, {"type": "t", "text": " Conversely, in genetic investigations of thrombotic risk, alterations in PAFAH1B2 were not conclusively linked to inherited prothrombotic states"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "9"}]}, {"type": "t", "text": ", even as dysregulated PAF metabolism is observed in cardiovascular conditions"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "10"}]}, {"type": "t", "text": ", and alterations in serum PAF levels have been noted in ocular vascular disorders."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nTogether, these studies also hint at broader regulatory networks in which PAFAH1B2 operates. Although PAFAH1B2 is primarily known for its roles in lipid mediator turnover and downstream signaling in cancer, inflammation, and neurobiology, emerging evidence suggests that interconnected systems—including those modulated by enzymes such as RNF39, which governs ubiquitination events in innate immune pathways—may indirectly influence the functional landscape in which PAFAH1B2 acts."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "12"}]}, {"type": "t", "text": " This integrative perspective reinforces the view that targeting PAFAH1B2 represents a promising avenue for therapeutic intervention across a spectrum of human diseases.\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Rebecca A Kohnz, Melinda M Mulvihill, Jae Won Chang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Activity-Based Protein Profiling of Oncogene-Driven Changes in Metabolism Reveals Broad Dysregulation of PAFAH1B2 and 1B3 in Cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "ACS Chem Biol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1021/acschembio.5b00053"}], "href": "https://doi.org/10.1021/acschembio.5b00053"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25945974"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25945974"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Can Ma, Yan Guo, Yan Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PAFAH1B2 is a HIF1a target gene and promotes metastasis in pancreatic cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2018.05.039"}], "href": "https://doi.org/10.1016/j.bbrc.2018.05.039"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29758199"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29758199"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Kazunari Tanigawa, Mitsuo Kiriya, Yasuhiro Hayashi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cathepsin G-induced malignant progression of MCF-7 cells involves suppression of PAF signaling through induced expression of PAFAH1B2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta Mol Cell Biol Lipids (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbalip.2022.159164"}], "href": "https://doi.org/10.1016/j.bbalip.2022.159164"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35462067"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35462067"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Gang Zhou, Gopal K Marathe, Belinda Willard, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Intracellular erythrocyte platelet-activating factor acetylhydrolase I inactivates aspirin in blood."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M111.267161"}], "href": "https://doi.org/10.1074/jbc.M111.267161"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21844189"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21844189"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Gang Zhou, Gopal K Marathe, Jaana Hartiala, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Aspirin hydrolysis in plasma is a variable function of butyrylcholinesterase and platelet-activating factor acetylhydrolase 1b2 (PAFAH1b2)."}]}, {"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.M112.427674"}], "href": "https://doi.org/10.1074/jbc.M112.427674"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23508960"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23508960"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Chong Ding, Xujun Liang, Li Ma, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Opposing effects of Ndel1 and alpha1 or alpha2 on cytoplasmic dynein through competitive binding to Lis1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.048777"}], "href": "https://doi.org/10.1242/jcs.048777"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19622634"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19622634"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Richard M Page, Anna Münch, Thomas Horn, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Loss of PAFAH1B2 reduces amyloid-β generation by promoting the degradation of amyloid precursor protein C-terminal fragments."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Neurosci (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1523/JNEUROSCI.2681-12.2012"}], "href": "https://doi.org/10.1523/JNEUROSCI.2681-12.2012"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23238734"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23238734"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Bruce T Scott, Nels Olson, George L Long, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Novel isoforms of intracellular platelet activating factor acetylhydrolase (PAFAH1b2) in human testis; encoded by alternatively spliced mRNAs."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Prostaglandins Other Lipid Mediat (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.prostaglandins.2007.10.005"}], "href": "https://doi.org/10.1016/j.prostaglandins.2007.10.005"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18155631"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18155631"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Sandra J Hasstedt, Bruce T Scott, Frits R Rosendaal, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Exclusion of the alpha2 subunit of platelet-activating factor acetylhydrolase 1b (PAFAH1B2) as a prothrombotic gene in a protein C-deficient kindred and population-based case-control sample."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Thromb Haemost (2007)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17849047"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17849047"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Guo-Hua Zheng, Shang-Quan Xiong, Hai-Ying Chen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Associations of platelet-activating factor acetylhydrolase (PAF-AH) gene polymorphisms with circulating PAF-AH levels and risk of coronary heart disease or blood stasis syndrome in the Chinese Han population."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Biol Rep (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s11033-014-3597-4"}], "href": "https://doi.org/10.1007/s11033-014-3597-4"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25034894"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25034894"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Miaoling Li, Xiongze Zhang, Nanying Liao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Analysis of the Serum Lipid Profile in Polypoidal Choroidal Vasculopathy."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/srep38342"}], "href": "https://doi.org/10.1038/srep38342"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27910906"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27910906"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Wenwen Wang, Qi Li, Mutian Jia, et al. "}, {"type": "b", "children": [{"type": "t", "text": "RNF39 facilitates antiviral immune responses by promoting K63-linked ubiquitination of STING."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int Immunopharmacol (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.intimp.2024.113091"}], "href": "https://doi.org/10.1016/j.intimp.2024.113091"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "39255680"}], "href": "https://pubmed.ncbi.nlm.nih.gov/39255680"}]}]}]}
Synonyms	HEL-S-303
Proteins	PA1B2_HUMAN
NCBI Gene ID	5049
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

PAFAH1B2 has 6,250 functional associations with biological entities spanning 8 categories (molecular profile, organism, chemical, functional term, phrase or reference, disease, phenotype or trait, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 122 datasets.

Click the + buttons to view associations for PAFAH1B2 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Gene Mutation Profiles	cell lines with PAFAH1B2 gene mutations from the CCLE Cell Line Gene Mutation Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with PAFAH1B2 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with PAFAH1B2 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 PAFAH1B2 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing PAFAH1B2 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing PAFAH1B2 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with PAFAH1B2 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with PAFAH1B2 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with PAFAH1B2 gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with PAFAH1B2 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 PAFAH1B2 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 PAFAH1B2 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of PAFAH1B2 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 PAFAH1B2 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.
	GAD Gene-Disease Associations	diseases associated with PAFAH1B2 gene in GWAS and other genetic association datasets from the GAD Gene-Disease Associations dataset.