Spectrin, alpha 1

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Spectrin, alpha, erythrocytic 1
Protein SPTA1 PDB 1owa.png
PDB rendering based on 1owa.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols SPTA1 ; EL2; HPP; HS3; SPH3; SPTA
External IDs OMIM182860 MGI98385 HomoloGene74460 GeneCards: SPTA1 Gene
RNA expression pattern
PBB GE SPTA1 206937 at tn.png
More reference expression data
Species Human Mouse
Entrez 6708 20739
Ensembl ENSG00000163554 ENSMUSG00000026532
UniProt P02549 P08032
RefSeq (mRNA) NM_003126 NM_011465
RefSeq (protein) NP_003117 NP_035595
Location (UCSC) Chr 1:
158.58 – 158.66 Mb
Chr 1:
174.17 – 174.25 Mb
PubMed search [1] [2]

Spectrin alpha chain, erythrocyte is a protein that in humans is encoded by the SPTA1 gene.[1]

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.[1]


Spectrin, alpha 1 has been shown to interact with Abl gene.[2]


  1. ^ a b "Entrez Gene: SPTA1 spectrin, alpha, erythrocytic 1 (elliptocytosis 2)". 
  2. ^ 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. 

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