SPTB

Spectrin, beta, erythrocytic

PDB rendering based on 1s35.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
SymbolsSPTB ; EL3; HS2; HSPTB1; SPH2
External IDsOMIM: 182870 MGI: 98387 HomoloGene: 295 GeneCards: SPTB Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez671020741
EnsemblENSG00000070182ENSMUSG00000021061
UniProtP11277P15508
RefSeq (mRNA)NM_000347NM_013675
RefSeq (protein)NP_000338NP_038703
Location (UCSC)Chr 14:
65.21 – 65.35 Mb		Chr 12:
76.58 – 76.71 Mb
PubMed search

Spectrin beta chain, erythrocyte is a protein that in humans is encoded by the SPTB gene.[1][2]

References

  1. ↑ Fukushima Y, Byers MG, Watkins PC, Winkelmann JC, Forget BG, Shows TB (Nov 1990). "Assignment of the gene for beta-spectrin (SPTB) to chromosome 14q23----q24.2 by in situ hybridization". Cytogenet Cell Genet 53 (4): 232–3. doi:10.1159/000132939. PMID 2209094.
  2. ↑ "Entrez Gene: SPTB spectrin, beta, erythrocytic (includes spherocytosis, clinical type I)".

Further reading

  • Bennett V, Baines AJ (2001). "Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues.". Physiol. Rev. 81 (3): 1353–92. PMID 11427698.
  • Kanzaki A; Rabodonirina M; Yawata Y et al. (1992). "A deletional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin Tokyo (beta 220/216)". Blood 80 (8): 2115–21. PMID 1391962.
  • Speicher DW, Weglarz L, DeSilva TM (1992). "Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site". J. Biol. Chem. 267 (21): 14775–82. PMID 1634521.
  • Gallagher PG; Tse WT; Costa F et al. (1991). "A splice site mutation of the beta-spectrin gene causing exon skipping in hereditary elliptocytosis associated with a truncated beta-spectrin chain". J. Biol. Chem. 266 (23): 15154–9. PMID 1840591.
  • Tse WT; Lecomte MC; Costa FF et al. (1990). "Point mutation in the beta-spectrin gene associated with alpha I/74 hereditary elliptocytosis. Implications for the mechanism of spectrin dimer self-association". J. Clin. Invest. 86 (3): 909–16. doi:10.1172/JCI114792. PMC 296810. PMID 1975598.
  • Yoon SH, Kentros CG, Prchal JT (1990). "Identification of an unusual deletion within homologous repeats of human reticulocyte beta-spectrin and probable peptide polymorphism". Gene 91 (2): 297–302. doi:10.1016/0378-1119(90)90104-Y. PMID 1976574.
  • Garbarz M; Tse WT; Gallagher PG et al. (1991). "Spectrin Rouen (beta 220-218), a novel shortened beta-chain variant in a kindred with hereditary elliptocytosis. Characterization of the molecular defect as exon skipping due to a splice site mutation". J. Clin. Invest. 88 (1): 76–81. doi:10.1172/JCI115307. PMC 296005. PMID 2056132.
  • Tse WT; Gallagher PG; Pothier B et al. (1991). "An insertional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin nice (beta 220/216)". Blood 78 (2): 517–23. PMID 2070088.
  • Winkelmann JC; Chang JG; Tse WT et al. (1990). "Full-length sequence of the cDNA for human erythroid beta-spectrin". J. Biol. Chem. 265 (20): 11827–32. PMID 2195026.
  • Winkelmann JC, Costa FF, Linzie BL, Forget BG (1990). "Beta spectrin in human skeletal muscle. Tissue-specific differential processing of 3' beta spectrin pre-mRNA generates a beta spectrin isoform with a unique carboxyl terminus". J. Biol. Chem. 265 (33): 20449–54. PMID 2243099.
  • Coetzer T; Palek J; Lawler J et al. (1990). "Structural and functional heterogeneity of alpha spectrin mutations involving the spectrin heterodimer self-association site: relationships to hematologic expression of homozygous hereditary elliptocytosis and hereditary pyropoikilocytosis". Blood 75 (11): 2235–44. PMID 2346784.
  • Winkelmann JC; Leto TL; Watkins PC et al. (1988). "Molecular cloning of the cDNA for human erythrocyte beta-spectrin". Blood 72 (1): 328–34. PMID 3390609.
  • Prchal JT; Morley BJ; Yoon SH et al. (1987). "Isolation and characterization of cDNA clones for human erythrocyte beta-spectrin". Proc. Natl. Acad. Sci. U.S.A. 84 (21): 7468–72. doi:10.1073/pnas.84.21.7468. PMC 299317. PMID 3478706.
  • Pothier B; Morlé L; Alloisio N et al. (1987). "Spectrin Nice (beta 220/216): a shortened beta-chain variant associated with an increase of the alpha I/74 fragment in a case of elliptocytosis". Blood 69 (6): 1759–65. PMID 3580577.
  • Wolfe LC; John KM; Falcone JC et al. (1982). "A genetic defect in the binding of protein 4.1 to spectrin in a kindred with hereditary spherocytosis". N. Engl. J. Med. 307 (22): 1367–74. doi:10.1056/NEJM198211253072203. PMID 6215583.
  • Speicher DW, Marchesi VT (1984). "Erythrocyte spectrin is composed of many homologous triple helical segments". Nature 311 (5982): 177–80. doi:10.1038/311177a0. PMID 6472478.
  • Carlier MF, Simon C, Cassoly R, Pradel LA (1984). "Interaction between microtubule-associated protein tau and spectrin". Biochimie 66 (4): 305–11. doi:10.1016/0300-9084(84)90007-5. PMID 6743699.
  • Goodman SR, Shiffer KA, Casoria LA, Eyster ME (1982). "Identification of the molecular defect in the erythrocyte membrane skeleton of some kindreds with hereditary spherocytosis". Blood 60 (3): 772–84. PMID 7104494.
  • Schischmanoff PO; Winardi R; Discher DE et al. (1995). "Defining of the minimal domain of protein 4.1 involved in spectrin-actin binding". J. Biol. Chem. 270 (36): 21243–50. doi:10.1074/jbc.270.36.21243. PMID 7673158.