SPTB

Spectrin, beta, erythrocytic

PDB rendering based on 1s35.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols SPTB ; EL3; HS2; HSPTB1; SPH2
External IDs OMIM: 182870 MGI: 98387 HomoloGene: 295 GeneCards: SPTB Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 6710 20741
Ensembl ENSG00000070182 ENSMUSG00000021061
UniProt P11277 P15508
RefSeq (mRNA) NM_000347 NM_013675
RefSeq (protein) NP_000338 NP_038703
Location (UCSC) Chr 14:
64.75 – 64.88 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. 
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