OMA1 Gene

Name	OMA1 zinc metallopeptidase
Description	Enables metalloendopeptidase activity. Involved in several processes, including HRI-mediated signaling; proteolysis; and regulation of mitochondrion organization. Located in mitochondrial inner membrane. Is active in mitochondrial intermembrane space. [provided by Alliance of Genome Resources, Mar 2025]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nOMA1 is a stress‐activated, zinc‐dependent metalloprotease anchored in the mitochondrial inner membrane that plays a central role in regulating mitochondrial dynamics. Under normal conditions, specific OPA1 isoforms mediate mitochondrial inner membrane fusion, but upon mitochondrial stress—such as loss of membrane potential or ATP depletion—OMA1 becomes activated and cleaves these OPA1 isoforms. This inducible cleavage triggers remodeling of cristae structure, limits fusion competence, and facilitates apoptotic progression by promoting cytochrome c release. Several studies have delineated how alternative splicing of OPA1 and its subsequent proteolysis by OMA1—and in some cases by other proteases—dictate mitochondrial quality control and apoptotic sensitivity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "Neuroprotective and stress‐response signaling functions of OMA1 have also been uncovered. In addition to OPA1 processing, OMA1 cleaves the inner membrane protein DELE1, which then relocates to the cytosol and binds to the eIF2α kinase HRI, thereby linking mitochondrial dysfunction to the integrated stress response. Through this cascade, OMA1 modulates not only apoptosis but also broader cellular adaptations to metabolic and oxidative stress. These findings have been extended to show that OMA1-mediated remodeling of mitochondrial membranes is essential for the execution of cell death programs in response to both intrinsic apoptotic stimuli and chemotherapeutic agents."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "11"}]}, {"type": "t", "text": "Beyond its immediate role in mitochondrial dynamics and stress response, OMA1 has emerged as a key modulator in various disease settings. Reduced or dysregulated OMA1 activity alters mitochondrial proteostasis and bioenergetics, thereby contributing to pathologies such as neurodegeneration, cardiomyopathy, and cancer. For example, in cancer models, diminished OMA1 activity correlates with enhanced metastatic competence and chemoresistance, while in cardiac tissues, OMA1-dependent regulation of OPA1 cleavage influences recovery after stress-induced mitochondrial fragmentation. Moreover, alterations in OMA1 processing have been linked to dysregulated cellular metabolism and impaired clearance of misfolded mitochondrial proteins, highlighting its therapeutic potential as a target in diseases marked by mitochondrial dysfunction."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "22"}]}, {"type": "t", "text": ""}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Stéphane Duvezin-Caubet, Mirko Koppen, Johannes Wagener, et al. "}, {"type": "b", "children": [{"type": "t", "text": "OPA1 processing reconstituted in yeast depends on the subunit composition of the m-AAA protease in mitochondria."}]}, {"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.e07-02-0164"}], "href": "https://doi.org/10.1091/mbc.e07-02-0164"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17615298"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17615298"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Brian Head, Lorena Griparic, Mandana Amiri, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Inducible proteolytic inactivation of OPA1 mediated by the OMA1 protease in mammalian cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1083/jcb.200906083"}], "href": "https://doi.org/10.1083/jcb.200906083"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20038677"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20038677"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Thomas D B MacVicar, Jon D Lane "}, {"type": "b", "children": [{"type": "t", "text": "Impaired OMA1-dependent cleavage of OPA1 and reduced DRP1 fission activity combine to prevent mitophagy in cells that are dependent on oxidative phosphorylation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.144337"}], "href": "https://doi.org/10.1242/jcs.144337"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24634514"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24634514"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Kuan Zhang, Huihui Li, Zhiyin Song "}, {"type": "b", "children": [{"type": "t", "text": "Membrane depolarization activates the mitochondrial protease OMA1 by stimulating self-cleavage."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO Rep (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/embr.201338240"}], "href": "https://doi.org/10.1002/embr.201338240"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24719224"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24719224"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Bao Kong, Qi Wang, Ella Fung, et al. "}, {"type": "b", "children": [{"type": "t", "text": "p53 is required for cisplatin-induced processing of the mitochondrial fusion protein L-Opa1 that is mediated by the mitochondrial metallopeptidase Oma1 in gynecologic cancers."}]}, {"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.M114.594812"}], "href": "https://doi.org/10.1074/jbc.M114.594812"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25112877"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25112877"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Xian Jiang, Hui Jiang, Zhirong Shen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Activation of mitochondrial protease OMA1 by Bax and Bak promotes cytochrome c release during apoptosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.1417253111"}], "href": "https://doi.org/10.1073/pnas.1417253111"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25275009"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25275009"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "T Kelly Rainbolt, Justine Lebeau, Cristina Puchades, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Reciprocal Degradation of YME1L and OMA1 Adapts Mitochondrial Proteolytic Activity during Stress."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Rep (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.celrep.2016.02.011"}], "href": "https://doi.org/10.1016/j.celrep.2016.02.011"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26923599"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26923599"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Francesco Consolato, Francesca Maltecca, Susanna Tulli, et al. "}, {"type": "b", "children": [{"type": "t", "text": "m-AAA and i-AAA complexes coordinate to regulate OMA1, the stress-activated supervisor of mitochondrial dynamics."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Sci (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1242/jcs.213546"}], "href": "https://doi.org/10.1242/jcs.213546"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29545505"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29545505"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Marcel V Alavi "}, {"type": "b", "children": [{"type": "t", "text": "Targeted OMA1 therapies for cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Cancer (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/ijc.32177"}], "href": "https://doi.org/10.1002/ijc.32177"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30714136"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30714136"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Shiori Sekine, Chunxin Wang, Dionisia P Sideris, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Reciprocal Roles of Tom7 and OMA1 during Mitochondrial Import and Activation of PINK1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2019.01.002"}], "href": "https://doi.org/10.1016/j.molcel.2019.01.002"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30733118"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30733118"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Xiaoyan Guo, Giovanni Aviles, Yi Liu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mitochondrial stress is relayed to the cytosol by an OMA1-DELE1-HRI pathway."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Nature (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41586-020-2078-2"}], "href": "https://doi.org/10.1038/s41586-020-2078-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32132707"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32132707"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Amita Daverey, Roman M Levytskyy, Kimberly M Stanke, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Depletion of mitochondrial protease OMA1 alters proliferative properties and promotes metastatic growth of breast cancer cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Sci Rep (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/s41598-019-49327-2"}], "href": "https://doi.org/10.1038/s41598-019-49327-2"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31611601"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31611601"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Mohammad Amin Amini, Jamshid Karimi, Iraj Khodadadi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Overexpression of ROMO1 and OMA1 are Potentially Biomarkers and Predict Unfavorable Prognosis in Gastric Cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Gastrointest Cancer (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s12029-019-00330-w"}], "href": "https://doi.org/10.1007/s12029-019-00330-w"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31729644"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31729644"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Dong Hu, Shiyang Li, Senlin Hu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A Common Missense Variant in OMA1 Associated with the Prognosis of Heart Failure."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cardiovasc Drugs Ther (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s10557-020-06960-8"}], "href": "https://doi.org/10.1007/s10557-020-06960-8"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "32236861"}], "href": "https://pubmed.ncbi.nlm.nih.gov/32236861"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Daisuke Murata, Tatsuya Yamada, Takeshi Tokuyama, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mitochondrial Safeguard: a stress response that offsets extreme fusion and protects respiratory function via flickering-induced Oma1 activation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "EMBO J (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.15252/embj.2020105074"}], "href": "https://doi.org/10.15252/embj.2020105074"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33200421"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33200421"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Marcel V Alavi "}, {"type": "b", "children": [{"type": "t", "text": "Tau phosphorylation and OPA1 proteolysis are unrelated events: Implications for Alzheimer's Disease."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochim Biophys Acta Mol Cell Res (2021)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbamcr.2021.119116"}], "href": "https://doi.org/10.1016/j.bbamcr.2021.119116"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "34400172"}], "href": "https://pubmed.ncbi.nlm.nih.gov/34400172"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Jun Li, Yuanjin Zhang, Farui Sun, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Long Noncoding RNA PCGEM1 Facilitates Tumor Growth and Metastasis of Osteosarcoma by Sponging miR-433-3p and Targeting OMA1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Orthop Surg (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/os.13648"}], "href": "https://doi.org/10.1111/os.13648"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "36782343"}], "href": "https://pubmed.ncbi.nlm.nih.gov/36782343"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Pablo Rivera-Mejías, Álvaro Jesús Narbona-Pérez, Lidwina Hasberg, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The mitochondrial protease OMA1 acts as a metabolic safeguard upon nuclear DNA damage."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Rep (2023)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.celrep.2023.112332"}], "href": "https://doi.org/10.1016/j.celrep.2023.112332"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "37002921"}], "href": "https://pubmed.ncbi.nlm.nih.gov/37002921"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Magda Krakowczyk, Anna M Lenkiewicz, Tomasz Sitarz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "OMA1 protease eliminates arrested protein import intermediates upon mitochondrial depolarization."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Cell Biol (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1083/jcb.202306051"}], "href": "https://doi.org/10.1083/jcb.202306051"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38530280"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38530280"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Wen de Zhu, Jin Rao, Li Hua Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "OMA1 competitively binds to HSPA9 to promote mitophagy and activate the cGAS-STING pathway to mediate GBM immune escape."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Immunother Cancer (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1136/jitc-2023-008718"}], "href": "https://doi.org/10.1136/jitc-2023-008718"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "38604814"}], "href": "https://pubmed.ncbi.nlm.nih.gov/38604814"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Yuan-Yuan Wei, Jing-Jing Ye, Da-Wei Zhang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Melatonin Rescues Influenza A Virus-Induced Cellular Energy Exhaustion via OMA1-OPA1-S in Acute Exacerbation of COPD."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Pineal Res (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/jpi.12991"}], "href": "https://doi.org/10.1111/jpi.12991"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "39039850"}], "href": "https://pubmed.ncbi.nlm.nih.gov/39039850"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Gunjan Purohit, Polash Ghosh, Oleh Khalimonchuk "}, {"type": "b", "children": [{"type": "t", "text": "Mitochondrial metallopeptidase OMA1 in cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Adv Cancer Res (2024)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/bs.acr.2024.05.001"}], "href": "https://doi.org/10.1016/bs.acr.2024.05.001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "39069370"}], "href": "https://pubmed.ncbi.nlm.nih.gov/39069370"}]}]}]}
Synonyms	2010001O09RIK, MPRP-1, ZMPOMA1, DAB1, MPRP1, PEPTIDASE, YKR087C
Proteins	OMA1_HUMAN
NCBI Gene ID	115209
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

OMA1 has 5,003 functional associations with biological entities spanning 9 categories (molecular profile, organism, functional term, phrase or reference, disease, phenotype or trait, chemical, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 108 datasets.

Click the + buttons to view associations for OMA1 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

OMA1 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 OMA1 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 OMA1 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 OMA1 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 RNA-seq	tissue samples with high or low expression of OMA1 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 OMA1 gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	BioGPS Human Cell Type and Tissue Gene Expression Profiles	cell types and tissues with high or low expression of OMA1 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 OMA1 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 OMA1 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 OMA1 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CCLE Cell Line Proteomics	Cell lines associated with OMA1 protein from the CCLE Cell Line Proteomics dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with OMA1 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 OMA1 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of OMA1 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 OMA1 gene in low- or high-throughput transcription factor functional studies from the CHEA Transcription Factor Targets 2022 dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing OMA1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing OMA1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing OMA1 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 OMA1 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 OMA1 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 OMA1 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 OMA1 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with OMA1 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Disease Associations	diseases associated with OMA1 gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with OMA1 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 OMA1 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 OMA1 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores	diseases associated with OMA1 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores 2025	diseases associated with OMA1 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 OMA1 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 OMA1 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 OMA1 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with OMA1 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 OMA1 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 OMA1 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of OMA1 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 OMA1 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.
	GeneRIF Biological Term Annotations	biological terms co-occuring with OMA1 gene in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.
	GeneSigDB Published Gene Signatures	PubMedIDs of publications reporting gene signatures containing OMA1 from the GeneSigDB Published Gene Signatures dataset.
	GEO Signatures of Differentially Expressed Genes for Diseases	disease perturbations changing expression of OMA1 gene from the GEO Signatures of Differentially Expressed Genes for Diseases dataset.
	GEO Signatures of Differentially Expressed Genes for Gene Perturbations	gene perturbations changing expression of OMA1 gene from the GEO Signatures of Differentially Expressed Genes for Gene Perturbations dataset.