SPTA1 Gene

HGNC Family	EF-hand domain containing
Name	spectrin, alpha, erythrocytic 1
Description	This gene encodes a member of a family of molecular scaffold proteins that link the plasma membrane to the actin cytoskeleton and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. The encoded protein is primarily composed of 22 spectrin repeats which are involved in dimer formation. It forms a component of the erythrocyte plasma membrane. Mutations in this gene result in a variety of hereditary red blood cell disorders, including elliptocytosis-2, pyropoikilocytosis, and spherocytosis, type 3. [provided by RefSeq, Aug 2017]
Summary	{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nThe SPTA1 gene encodes the erythroid α‐spectrin protein, a vital constituent of the spectrin‐based membrane skeleton that underlies red blood cell (RBC) membranes. By interacting with β‐spectrin, α‐spectrin forms heterodimers that further associate into tetramers through specific self‐association domains. This network is essential for conferring elasticity, mechanical stability, and the proper biconcave shape necessary for RBC deformability. In addition, the expression of SPTA1 is tightly controlled by erythroid‐specific promoter elements—such as regions containing GATA‐1 binding sites—that ensure spatial and temporal regulation during erythropoiesis. These coordinated structural and regulatory functions underscore SPTA1’s central role in maintaining red cell membrane architecture."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMutations in SPTA1 are known to lead to a spectrum of hemolytic anemias—including hereditary spherocytosis, hereditary elliptocytosis, and hereditary pyropoikilocytosis—by disrupting the normal assembly and function of the spectrin network. Several studies have identified missense mutations and splicing defects (for example, H54P, L49F, and p.L155dup) that impair α‐spectrin self‐association, compromise tetramer formation, and reduce overall protein levels. Such defects weaken membrane integrity, lead to abnormal cell morphology and increased RBC fragility, and are often detected in patients with complex or overlapping red cell membrane disorders."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its classical role as a structural protein, α‐spectrin exhibits additional functionalities. Its modular domains harbor surface‐exposed hydrophobic patches that not only promote self‐association but can also mediate chaperone‐like activities by stabilizing target proteins and preventing their aggregation. Moreover, studies indicate that α‐spectrin may participate in regulated ubiquitination processes without affecting heterodimer formation, hinting at a role in protein turnover and quality control. These ancillary functions contribute to the dynamic modulation of the RBC membrane’s organization and its interactions with actin, lipid domains, and other cytoskeletal elements."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Ellice Y Wong, Jolinta Lin, Bernard G Forget, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Sequences downstream of the erythroid promoter are required for high level expression of the human alpha-spectrin gene."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M408886200"}], "href": "https://doi.org/10.1074/jbc.M408886200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15456760"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15456760"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Massimiliano Gaetani, Sara Mootien, Sandra Harper, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural and functional effects of hereditary hemolytic anemia-associated point mutations in the alpha spectrin tetramer site."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2007-11-122457"}], "href": "https://doi.org/10.1182/blood-2007-11-122457"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18218854"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18218854"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Patrick G Gallagher, Douglas G Nilson, Laurie A Steiner, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Association studies of erythroid alpha-spectrin at the tetramerization site."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Br J Haematol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1111/j.1365-2141.2009.07876.x"}], "href": "https://doi.org/10.1111/j.1365-2141.2009.07876.x"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19747366"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19747366"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Santhi K Ganesh, Neil A Zakai, Frank J A van Rooij, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "A novel splicing mutation of the alpha-spectrin gene in the original hereditary pyropoikilocytosis kindred."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Blood (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1182/blood-2005-05-1813"}], "href": "https://doi.org/10.1182/blood-2005-05-1813"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16150946"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16150946"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "Roberto H Nussenzveig, Robert D Christensen, Josef T Prchal, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Novel α-spectrin mutation in trans with α-spectrin causing severe neonatal jaundice from hereditary spherocytosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neonatology (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1159/000365586"}], "href": "https://doi.org/10.1159/000365586"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25277063"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25277063"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Yunyan He, Siyuan Jia, Roma Kajal Dewan, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Novel mutations in patients with hereditary red blood cell membrane disorders using next-generation sequencing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Gene (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.gene.2017.07.009"}], "href": "https://doi.org/10.1016/j.gene.2017.07.009"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28694211"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28694211"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Shiyue Ma, Jinqiu Qin, Aiqiu Wei, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Novel compound heterozygous SPTA1 mutations in a patient with hereditary elliptocytosis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Med Rep (2018)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3892/mmr.2018.8632"}], "href": "https://doi.org/10.3892/mmr.2018.8632"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "29484404"}], "href": "https://pubmed.ncbi.nlm.nih.gov/29484404"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "Mary Risinger, Georgios E Christakopoulos, Corinna L Schultz, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hereditary elliptocytosis-associated alpha-spectrin mutation p.L155dup as a modifier of sickle cell disease severity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Pediatr Blood Cancer (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/pbc.27531"}], "href": "https://doi.org/10.1002/pbc.27531"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30393954"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30393954"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Xiong Wang, Aiguo Liu, Yanjun Lu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Novel compound heterozygous mutations in the SPTA1 gene, causing hereditary spherocytosis in a neonate with Coombs‑negative hemolytic jaundice."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Med Rep (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3892/mmr.2019.9947"}], "href": "https://doi.org/10.3892/mmr.2019.9947"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30816434"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30816434"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Min Chen, Yu-Ping Ye, Lin Liao, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hereditary spherocytosis overlooked for 7 years in a pediatric patient with β-thalassemia trait and novel compound heterozygous mutations of SPTA1 gene."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hematology (2020)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1080/16078454.2020.1846874"}], "href": "https://doi.org/10.1080/16078454.2020.1846874"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "33210974"}], "href": "https://pubmed.ncbi.nlm.nih.gov/33210974"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Tejashree Anil More, Prabhakar Kedar "}, {"type": "b", "children": [{"type": "t", "text": "Unravelling the genetic and phenotypic heterogeneity of SPTA1 gene variants in Hereditary Elliptocytosis and Hereditary Pyropoikilocytosis patients using next-generation sequencing."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Gene (2022)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.gene.2022.146796"}], "href": "https://doi.org/10.1016/j.gene.2022.146796"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "35961434"}], "href": "https://pubmed.ncbi.nlm.nih.gov/35961434"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "G A Alekperova, A G Orudzhev, S A Javadov "}, {"type": "b", "children": [{"type": "t", "text": "Analysis of erythrocyte and platelet membrane proteins in various forms of beta-thalassemia."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochemistry (Mosc) (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1023/b:biry.0000040198.62939.56"}], "href": "https://doi.org/10.1023/b:biry.0000040198.62939.56"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15310273"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15310273"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Mahnoush H Riahi, David G Kakhniashvili, Steven R Goodman "}, {"type": "b", "children": [{"type": "t", "text": "Ubiquitination of red blood cell alpha-spectrin does not affect heterodimer formation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Hematol (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/ajh.20282"}], "href": "https://doi.org/10.1002/ajh.20282"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15795915"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15795915"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "Y J Hsu, W E Zimmer, S R Goodman "}, {"type": "b", "children": [{"type": "t", "text": "Erythrocyte spectrin's chimeric E2/E3 ubiquitin conjugating/ligating activity."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Mol Biol (Noisy-le-grand) (2005)"}]}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16171554"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16171554"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Dipayan Bose, Abhijit Chakrabarti "}, {"type": "b", "children": [{"type": "t", "text": "Localizing the chaperone activity of erythroid spectrin."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cytoskeleton (Hoboken) (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/cm.21556"}], "href": "https://doi.org/10.1002/cm.21556"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "31397976"}], "href": "https://pubmed.ncbi.nlm.nih.gov/31397976"}]}]}]}
Synonyms	SPTA, HPP, EL2, HS3, SPH3
Proteins	SPTA1_HUMAN
NCBI Gene ID	6708
API
Download Associations
Predicted Functions
Co-expressed Genes
Expression in Tissues and Cell Lines

Functional Associations

SPTA1 has 6,142 functional associations with biological entities spanning 9 categories (molecular profile, organism, chemical, disease, phenotype or trait, functional term, phrase or reference, structural feature, cell line, cell type or tissue, gene, protein or microRNA, sequence feature) extracted from 123 datasets.

Click the + buttons to view associations for SPTA1 from the datasets below.

If available, associations are ranked by standardized value

Harmonizome 3.0

SPTA1 Gene

Functional Associations

Please acknowledge the Harmonizome in your publications by citing the following reference(s):

	Dataset	Summary
	Allen Brain Atlas Adult Mouse Brain Tissue Gene Expression Profiles	tissues with high or low expression of SPTA1 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 SPTA1 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 SPTA1 gene relative to other tissue samples from the Allen Brain Atlas Developing Human Brain Tissue Gene Expression Profiles by Microarray dataset.
	Allen Brain Atlas Prenatal Human Brain Tissue Gene Expression Profiles	tissues with high or low expression of SPTA1 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 SPTA1 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 SPTA1 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 SPTA1 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 SPTA1 gene from the Carcinogenome Chemical Perturbation Carcinogenicity Signatures dataset.
	CCLE Cell Line Gene CNV Profiles	cell lines with high or low copy number of SPTA1 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 SPTA1 gene relative to other cell lines from the CCLE Cell Line Gene Expression Profiles dataset.
	ChEA Transcription Factor Binding Site Profiles	transcription factor binding site profiles with transcription factor binding evidence at the promoter of SPTA1 gene from the CHEA Transcription Factor Binding Site Profiles dataset.
	ChEA Transcription Factor Targets	transcription factors binding the promoter of SPTA1 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 SPTA1 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 SPTA1 gene from the curated ClinVar Gene-Phenotype Associations dataset.
	ClinVar Gene-Phenotype Associations 2025	phenotypes associated with SPTA1 gene from the curated ClinVar Gene-Phenotype Associations 2025 dataset.
	CM4AI KOLF21J CRISPRi Gene Perturbation Atlas	gene perturbations changing expression of SPTA1 gene from the CM4AI KOLF21J CRISPRi Gene Perturbation Atlas dataset.
	CMAP Signatures of Differentially Expressed Genes for Small Molecules	small molecule perturbations changing expression of SPTA1 gene from the CMAP Signatures of Differentially Expressed Genes for Small Molecules dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores	cellular components containing SPTA1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.
	COMPARTMENTS Curated Protein Localization Evidence Scores 2025	cellular components containing SPTA1 protein from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.
	COMPARTMENTS Text-mining Protein Localization Evidence Scores	cellular components co-occuring with SPTA1 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 SPTA1 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 SPTA1 gene relative to other cell lines from the COSMIC Cell Line Gene CNV Profiles dataset.
	COSMIC Cell Line Gene Mutation Profiles	cell lines with SPTA1 gene mutations from the COSMIC Cell Line Gene Mutation Profiles dataset.
	CTD Gene-Chemical Interactions	chemicals interacting with SPTA1 gene/protein from the curated CTD Gene-Chemical Interactions dataset.
	CTD Gene-Disease Associations	diseases associated with SPTA1 gene/protein from the curated CTD Gene-Disease Associations dataset.
	dbGAP Gene-Trait Associations	traits associated with SPTA1 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 SPTA1 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 SPTA1 gene knockdown relative to other cell lines from the DepMap CRISPR Gene Dependency dataset.
	DGIdb Drug Targets 2026	interacting drugs for SPTA1 protein from the DGIdb Drug Targets 2026 dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores	diseases involving SPTA1 gene from the DISEASES Curated Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Curated Gene-Disease Association Evidence Scores 2025	diseases involving SPTA1 gene from the DISEASES Curated Gene-Disease Association Evidence Scores 2025 dataset.
	DISEASES Experimental Gene-Disease Association Evidence Scores	diseases associated with SPTA1 gene in GWAS datasets from the DISEASES Experimental Gene-Disease Assocation Evidence Scores dataset.
	DISEASES Text-mining Gene-Disease Association Evidence Scores	diseases co-occuring with SPTA1 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 SPTA1 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 SPTA1 gene in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.
	DisGeNET Gene-Phenotype Associations	phenotypes associated with SPTA1 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 SPTA1 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 SPTA1 gene from the ENCODE Transcription Factor Binding Site Profiles dataset.
	ENCODE Transcription Factor Targets	transcription factors binding the promoter of SPTA1 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 SPTA1 from the ESCAPE Omics Signatures of Genes and Proteins for Stem Cells dataset.