Recombinant Human Spectrin beta chain, erythrocyte (SPTB), partial

1. two sex-specific loci(SPTB in females and IZUMO3 in males), yielding associations that were particularly strong at a specific skeletal site, were identified. PMID: 28181694
2. Using Next-Generation sequencing, we identified the causative genetic mutations in fifteen patients with clinically suspected hereditary elliptocytosis and hereditary pyropoikilocytosis and correlated the identified mutations with the clinical phenotype and ektacytometry profile. PMID: 27667160
3. Targeted next generation sequencing identifies a novel beta-spectrin gene mutation A2059P in two Omani children with hereditary pyropoikilocytosis PMID: 28699249
4. Mutational characteristics of ANK1 and SPTB genes in Korean hereditary spherocytosis have been described. PMID: 26830532
5. a new mutation in the SPTB gene (466insG) leading to a frameshift and a premature stop codon 29 codons downstream in the region encoding the C-terminal part of the dimerization domain; instability of mutant mRNA results in spectrin deficiency and clinically moderate to serious hereditary spherocytosis PMID: 27709257
6. A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration. PMID: 22360420
7. Data postulate that direct interactions between spectrin ankBDn and PE-rich domains play an important role in stabilizing the structure of the spectrin-based membrane skeleton. PMID: 21738695
8. through the use of an ATP-driven phospholipid translocase (flippase), erythrocytes have evolved a protective mechanism against spectrin glycation and thus maintain their optimal membrane function during their long circulatory life span PMID: 20724481
9. CD45 lateral mobility is regulated by the spectrin-ankyrin cytoskeleton of T cells PMID: 20164196
10. Important region in the beta-spectrin C-terminus for association with the alpha chain and for spectrin tetramer formation is defined. PMID: 12038451
11. The spectrin-ankyrin skeleton controls CD45 surface display and interleukin-2 production PMID: 12354383
12. the repeats of five human beta-spectrins have been analysed PMID: 12655374
13. This study identifies the precise sites of all significant phosphorylation events on beta-spectrin and has determined that these phosphorylation events apparently occur in a tightly regulated sequential order. PMID: 15065869
14. Binding sites for both protein 4.1R and actin are located in both of the beta I-spectrin calponin homology domains, (CH1 and CH2). PMID: 16060676
15. analysis of conformational stabilities of the structural repeats of erythroid spectrin PMID: 16476728
16. The results indicate that the whole ankyrin-sensitive lipid-binding site of beta-spectrin exhibits a helical conformation revealing a distinct 3(10)-helix contribution at its N-terminus. PMID: 17520478
17. The spectrin tetramer can be modeled as a soft polymer with a unique flat force-extension profile over the range of biologically important lengths. PMID: 18202182
18. The structure of the ankyrin ZU5 domain shows a novel structure containing a beta core. PMID: 19141864
19. The putative coupling of flexibility and ligand binding suggests a mechanism by which spectrin might participate in mechanosensory regulation. PMID: 19168783
20. DNA analysis of SPTB in hereditary spherocytosis subjects with decreased SPTB mRNA levels revealed the presence of 5 previously undescribed mutations: R1756X, 781delT and IVS22nt-4G>A, 1502insA & IVS20nt-2A>G PMID: 19538529

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HGNC: 11274

OMIM: 182870

KEGG: hsa:6710

STRING: 9606.ENSP00000374372

UniGene: Hs.417303