Spectrin, alpha 1

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Protein SPTA1 PDB 1owa.png
Available structures
PDBOrtholog search: PDBe RCSB
AliasesSPTA1, EL2, HPP, HS3, SPH3, SPTA, Spectrin, alpha 1, spectrin alpha, erythrocytic 1
External IDsMGI: 98385 HomoloGene: 74460 GeneCards: SPTA1
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for SPTA1
Genomic location for SPTA1
Band1q23.1Start158,610,706 bp[1]
End158,686,715 bp[1]
RNA expression pattern
PBB GE SPTA1 206937 at fs.png
More reference expression data
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC)Chr 1: 158.61 – 158.69 MbChr 1: 174.17 – 174.25 Mb
PubMed search[3][4]
View/Edit HumanView/Edit Mouse

Spectrin alpha chain, erythrocyte is a protein that in humans is encoded by the SPTA1 gene.[5]

Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is a tetramer made up of alpha-beta dimers linked in a head-to-head arrangement. This gene is one member of a family of alpha-spectrin genes. The encoded protein is primarily composed of 22 spectrin repeats which are involved in dimer formation. It forms weaker tetramer interactions than non-erythrocytic alpha spectrin, which may increase the plasma membrane elasticity and deformability of red blood cells. Mutations in this gene result in a variety of hereditary red blood cell disorders, including elliptocytosis type 2, pyropoikilocytosis, and spherocytic hemolytic anemia.[5]


Spectrin, alpha 1 has been shown to interact with Abl gene.[6]


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000163554 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026532 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:".
  4. ^ "Mouse PubMed Reference:".
  5. ^ a b "Entrez Gene: SPTA1 spectrin, alpha, erythrocytic 1 (elliptocytosis 2)".
  6. ^ Ziemnicka-Kotula, D; Xu J; Gu H; Potempska A; Kim K S; Jenkins E C; Trenkner E; Kotula L (May 1998). "Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association of tyrosine kinases with the spectrin-based membrane skeleton". J. Biol. Chem. UNITED STATES. 273 (22): 13681–92. doi:10.1074/jbc.273.22.13681. ISSN 0021-9258. PMID 9593709.

Further reading[edit]