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Spectrin (Sp), the most abundant of the erythrocyte membrane skeleton proteins, helps these cells maintain their characteristic biconcave shape while remaining flexible and elastic. Erythrocyte Sp is a heterodimer composed of a 280 kDa alpha subunit and a 246 kDa beta subunit which associate in a side-to-side, antiparallel configuration to form a 100 nm rod-like structure. Sp in other tissues may be composed of distinct but homologous alpha and beta subunits, sometimes referred to as fodrin. A newly introduced nomenclature designates the Sp subunits of the erythrocyte as alpha-1 and beta-1, and the fodrin subunits as alpha-2 and beta-2. Alternatively spliced forms of each are designated as epsilon-1, epsilon-2, etc. (e. g. beta-1 epsilon-1).
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: beta fodrin; beta-fodrin; beta-G spectrin; Beta-II spectrin; beta-spectrin 2; beta-spectrin 2, non-erythrocytic; beta-spectrin II; beta-spectrin non-erythrocytic 1; brain spectrin; embryonic liver beta-fodrin; Embryonic liver fodrin; embryonic liver fodrin beta chain; epididymis luminal protein 102; Fodrin beta chain; non-erythrocytic; spectrin beta 2; spectrin beta chain, brain 1; Spectrin beta chain, non-erythrocytic 1; spectrin G; spectrin, beta, non-erythrocytic 1; Spectrin, non-erythroid beta chain 1
Gene Aliases: 9930031C03Rik; AL033301; betaSpII; ELF; elf1; elf3; HEL102; mKIAA4049; Spnb-2; Spnb2; SPTB2; SPTBN1
UniProt ID: (Human) Q01082, (Mouse) Q62261
Entrez Gene ID: (Human) 6711, (Mouse) 20742
Molecular Function:
actin family cytoskeletal protein
cytoskeletal protein
non-motor actin binding protein
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