ATP2A1 Gene

HGNC Family	ATPases
Name	ATPase, Ca++ transporting, cardiac muscle, fast twitch 1
Description	This gene encodes one of the SERCA Ca(2+)-ATPases, which are intracellular pumps located in the sarcoplasmic or endoplasmic reticula of muscle cells. This enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen, and is involved in muscular excitation and contraction. Mutations in this gene cause some autosomal recessive forms of Brody disease, characterized by increasing impairment of muscular relaxation during exercise. Alternative splicing results in three transcript variants encoding different isoforms. [provided by RefSeq, Oct 2013]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nATP2A1 encodes the skeletal‐muscle–specific sarcoplasmic/endoplasmic reticulum Ca²⁺‐ATPase (SERCA1), which plays a pivotal role in muscle physiology by actively transporting Ca²⁺ from the cytosol into the sarcoplasmic reticulum. This Ca²⁺ reuptake is essential for muscle relaxation and for maintaining low resting cytosolic Ca²⁺ levels following contraction. Several studies demonstrate that ATP2A1 function is intricately regulated at the levels of alternative mRNA splicing and protein interactions. For example, aberrant splicing patterns of SERCA1 mRNA—resulting in altered expression of certain isoforms—have been implicated in diseases such as myotonic dystrophy, while regulatory interactions with partners like phospholamban contribute to modulation of the pump’s activity under varying intracellular conditions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFurthermore, ATP2A1 expression is developmentally regulated through the production of distinct splice isoforms—most notably SERCA1a (adult) and SERCA1b (neonatal/regenerating muscle). The neonatal SERCA1b isoform, which differs only at its C‐terminal tail, is predominantly expressed during early muscle formation or after injury, while the mature SERCA1a becomes the dominant species in fully differentiated muscle. Alterations in this tightly controlled splicing process have been associated not only with the pathogenesis of myotonic dystrophy but also with conditions such as Brody disease, where ATP2A1 mutations lead to reduced protein levels and impaired Ca²⁺ handling. In addition, studies in various muscle types—from limb muscles to extraocular fibers—show that ATP2A1 expression and function adapt both to physiologic exercise and to disease‐related changes that ultimately impact muscle contractility."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its core transport function, ATP2A1/SERCA1 activity is subject to modulation by a network of protein regulators and post‐translational modifications that fine‐tune Ca²⁺ homeostasis in muscle fibers. Interactions with small regulatory proteins—such as sAnk1, which can relieve inhibition by other modulators, and inhibitory partners like phospholamban and sarcolipin—affect enzyme conformation and kinetics, thereby dictating the efficiency of Ca²⁺ uptake. Moreover, exposure to factors such as pharmacologic agents or changes in the lipid environment can alter SERCA1’s affinity for Ca²⁺ and its catalytic turnover, with implications for muscle performance and disease phenotypes. Overall, the proper function of ATP2A1 is essential not only for timely muscle relaxation but also for adapting Ca²⁺ transport in response to developmental cues, exercise training, and pathophysiological stress, ensuring optimized muscle contractility and energy utilization."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Takashi Kimura, Masayuki Nakamori, John D Lueck, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Altered mRNA splicing of the skeletal muscle ryanodine receptor and sarcoplasmic/endoplasmic reticulum Ca2+-ATPase in myotonic dystrophy type 1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddi223"}], "href": "https://doi.org/10.1093/hmg/ddi223"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15972723"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15972723"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Mounia Chami, Bénédicte Oulès, György Szabadkai, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Role of SERCA1 truncated isoform in the proapoptotic calcium transfer from ER to mitochondria during ER stress."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2008.11.014"}], "href": "https://doi.org/10.1016/j.molcel.2008.11.014"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19061639"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19061639"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Chikashi Toyoshima, Michio Asahi, Yuji Sugita, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Modeling of the inhibitory interaction of phospholamban with the Ca2+ ATPase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0237326100"}], "href": "https://doi.org/10.1073/pnas.0237326100"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12525698"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12525698"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Michio Asahi, Yuji Sugita, Kazimierz Kurzydlowski, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Dissection of the functional differences between sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) 1 and 2 isoforms and characterization of Darier disease (SERCA2) mutants by steady-state and transient kinetic analyses."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2003)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M306784200"}], "href": "https://doi.org/10.1074/jbc.M306784200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12975374"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12975374"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Shin-Ichiro Hino, Shinichi Kondo, Hiroshi Sekiya, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Molecular mechanisms responsible for aberrant splicing of SERCA1 in myotonic dystrophy type 1."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddm239"}], "href": "https://doi.org/10.1093/hmg/ddm239"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17728322"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17728322"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Laura L Wootton, Francesco Michelangeli "}, {"type": "b", "children": [{"type": "t", "text": "The effects of the phenylalanine 256 to valine mutation on the sensitivity of sarcoplasmic/endoplasmic reticulum Ca2+ ATPase (SERCA) Ca2+ pump isoforms 1, 2, and 3 to thapsigargin and other inhibitors."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M510978200"}], "href": "https://doi.org/10.1074/jbc.M510978200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16410239"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16410239"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Ivan Toral-Ojeda, Garazi Aldanondo, Jaione Lasa-Elgarresta, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "SERCA1 protein expression in muscle of patients with Brody disease and Brody syndrome and in cultured human muscle fibers."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Genet Metab (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ymgme.2013.07.015"}], "href": "https://doi.org/10.1016/j.ymgme.2013.07.015"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23911890"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23911890"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Michele Salanova, Gudrun Schiffl, Dieter Blottner "}, {"type": "b", "children": [{"type": "t", "text": "Atypical fast SERCA1a protein expression in slow myofibers and differential S-nitrosylation prevented by exercise during long term bed rest."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Histochem Cell Biol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00418-009-0624-y"}], "href": "https://doi.org/10.1007/s00418-009-0624-y"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19644701"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19644701"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Taitan Nguyen, Neal A Rubinstein, Camasamudram Vijayasarathy, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "The neonatal sarcoplasmic reticulum Ca2+-ATPase gives a clue to development and pathology in human muscles."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Muscle Res Cell Motil (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s10974-014-9403-z"}], "href": "https://doi.org/10.1007/s10974-014-9403-z"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25487304"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25487304"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Tomasz Boczek, Marta Sobolczyk, Joanna Mackiewicz, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Sphingosine inhibits the sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA) activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2016.03.123"}], "href": "https://doi.org/10.1016/j.bbrc.2016.03.123"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27033604"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27033604"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "V Guglielmi, A Oosterhof, N C Voermans, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Calcium uptake and release through sarcoplasmic reticulum in the inferior oblique muscles of patients with inferior oblique overaction."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Yonsei Med J (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3349/ymj.2006.47.2.207"}], "href": "https://doi.org/10.3349/ymj.2006.47.2.207"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16642550"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16642550"}]}]}]}
Synonyms	SERCA1, ATP2A
Proteins	AT2A1_HUMAN
NCBI Gene ID	487
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Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

ATP2A1 has 6,264 functional associations with biological entities spanning 8 categories (molecular profile, organism, functional term, phrase or reference, chemical, disease, phenotype or trait, structural feature, cell line, cell type or tissue, gene, protein or microRNA) extracted from 137 datasets.

Click the + buttons to view associations for ATP2A1 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

ATP2A1 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 ATP2A1 gene relative to other tissues from the Allen Brain Atlas Adult Human 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 ATP2A1 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 ATP2A1 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 ATP2A1 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 ATP2A1 gene relative to other tissues from the Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles dataset.
	Biocarta Pathways	pathways involving ATP2A1 protein from the Biocarta Pathways dataset.
	BioGPS Cell Line Gene Expression Profiles	cell lines with high or low expression of ATP2A1 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 ATP2A1 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 ATP2A1 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 ATP2A1 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of ATP2A1 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 ATP2A1 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	CellMarker Gene-Cell Type Associations	cell types associated with ATP2A1 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 ATP2A1 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of ATP2A1 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 ATP2A1 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 ATP2A1 gene from the curated ClinVar Gene-Phenotype Associations dataset.
	ClinVar Gene-Phenotype Associations 2025	phenotypes associated with ATP2A1 gene from the curated ClinVar Gene-Phenotype Associations 2025 dataset.
	CM4AI KOLF21J CRISPRi Gene Perturbation Atlas	gene perturbations changing expression of ATP2A1 gene from the CM4AI KOLF21J CRISPRi Gene Perturbation Atlas dataset.
	CM4AI U2OS Cell Map Protein Localization Assemblies	assemblies containing ATP2A1 protein from integrated AP-MS and IF data from the CM4AI U2OS Cell Map Protein Localization Assemblies dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of ATP2A1 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing ATP2A1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing ATP2A1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Experimental Protein Localization Evidence Scores	cellular components containing ATP2A1 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 ATP2A1 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 ATP2A1 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 ATP2A1 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 ATP2A1 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with ATP2A1 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with ATP2A1 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with ATP2A1 gene/protein from the curated CTD Gene-Disease Associations dataset.
	DeepCoverMOA Drug Mechanisms of Action	small molecule perturbations with high or low expression of ATP2A1 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 ATP2A1 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DGIdb Drug Targets 2026	interacting drugs for ATP2A1 protein from the DGIdb Drug Targets 2026 dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores	diseases involving ATP2A1 gene from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores 2025	diseases involving ATP2A1 gene from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores	diseases associated with ATP2A1 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 ATP2A1 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 ATP2A1 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 ATP2A1 gene in abstracts of biomedical publications from the DISEASES Text-mining Gene-Disease Assocation Evidence Scores 2025 dataset.