SPTB

SPTB
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1S35, 3EDU, 3F57, 3KBT, 3KBU, 3LBX
Identifiers
Aliases	SPTB, EL3, HS2, HSPTB1, SPH2, spectrin beta, erythrocytic
External IDs	OMIM: 182870; MGI: 98387; HomoloGene: 295; GeneCards: SPTB; OMA:SPTB - orthologs
Gene location (Human) Chr. Chromosome 14 (human) Band 14q23.3 Start 64,746,283 bp End 64,879,907 bp
Gene location (Mouse) Chr. Chromosome 12 (mouse) Band 12 C3|12 33.73 cM Start 76,627,262 bp End 76,757,321 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gastrocnemius muscle muscle of thigh apex of heart Skeletal muscle tissue of rectus abdominis tibialis anterior muscle triceps brachii muscle cerebellar hemisphere right hemisphere of cerebellum glutes right auricle Top expressed in muscle of thigh fetal liver hematopoietic progenitor cell epithelium of lens dentate gyrus of hippocampal formation granule cell cerebellar cortex tibiofemoral joint ankle superior frontal gyrus skeletal muscle tissue pontine nuclei More reference expression data BioGPS More reference expression data
Gene ontology Molecular function actin filament binding structural constituent of cytoskeleton protein binding ankyrin binding actin binding Cellular component spectrin intrinsic component of the cytoplasmic side of the plasma membrane cell surface cell cortex actin cytoskeleton spectrin-associated cytoskeleton cytoskeleton cytoplasm Golgi apparatus cytosol protein-containing complex Biological process MAPK cascade axon guidance endoplasmic reticulum to Golgi vesicle-mediated transport actin filament capping cytoskeleton organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6710 20741 Ensembl ENSG00000070182 ENSMUSG00000021061 UniProt P11277 P15508 RefSeq (mRNA) NM_000347 NM_001024858 NM_001355436 NM_001355437 NM_013675 RefSeq (protein) NP_001020029 NP_001342365 NP_001342366 n/a Location (UCSC) Chr 14: 64.75 – 64.88 Mb Chr 12: 76.63 – 76.76 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

Further reading

• Bennett V, Baines AJ (July 2001). "Spectrin and ankyrin-based pathways: metazoan inventions for integrating cells into tissues". Physiological Reviews. 81 (3): 1353–92. doi:10.1152/physrev.2001.81.3.1353. PMID 11427698. S2CID 15307181.
• Kanzaki A, Rabodonirina M, Yawata Y, Wilmotte R, Wada H, Ata K, Yamada O, Akatsuka J, Iyori H, Horiguchi M (October 1992). "A deletional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin Tokyo (beta 220/216)". Blood. 80 (8): 2115–21. doi:10.1182/blood.V80.8.2115.2115. PMID 1391962.
• Speicher DW, Weglarz L, DeSilva TM (July 1992). "Properties of human red cell spectrin heterodimer (side-to-side) assembly and identification of an essential nucleation site". The Journal of Biological Chemistry. 267 (21): 14775–82. doi:10.1016/S0021-9258(18)42107-2. PMID 1634521.
• Gallagher PG, Tse WT, Costa F, Scarpa A, Boivin P, Delaunay J, Forget BG (August 1991). "A splice site mutation of the beta-spectrin gene causing exon skipping in hereditary elliptocytosis associated with a truncated beta-spectrin chain". The Journal of Biological Chemistry. 266 (23): 15154–9. doi:10.1016/S0021-9258(18)98598-4. PMID 1840591.
• Tse WT, Lecomte MC, Costa FF, Garbarz M, Feo C, Boivin P, Dhermy D, Forget BG (September 1990). "Point mutation in the beta-spectrin gene associated with alpha I/74 hereditary elliptocytosis. Implications for the mechanism of spectrin dimer self-association". The Journal of Clinical Investigation. 86 (3): 909–16. doi:10.1172/JCI114792. PMC 296810. PMID 1975598.
• Yoon SH, Kentros CG, Prchal JT (July 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, Picat C, Lecomte MC, Galibert F, Dhermy D, Forget BG (July 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". The Journal of Clinical Investigation. 88 (1): 76–81. doi:10.1172/JCI115307. PMC 296005. PMID 2056132.
• Tse WT, Gallagher PG, Pothier B, Costa FF, Scarpa A, Delaunay J, Forget BG (July 1991). "An insertional frameshift mutation of the beta-spectrin gene associated with elliptocytosis in spectrin nice (beta 220/216)". Blood. 78 (2): 517–23. doi:10.1182/blood.V78.2.517.517. PMID 2070088.
• Winkelmann JC, Chang JG, Tse WT, Scarpa AL, Marchesi VT, Forget BG (July 1990). "Full-length sequence of the cDNA for human erythroid beta-spectrin". The Journal of Biological Chemistry. 265 (20): 11827–32. doi:10.1016/S0021-9258(19)38473-X. PMID 2195026.
• Winkelmann JC, Costa FF, Linzie BL, Forget BG (November 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". The Journal of Biological Chemistry. 265 (33): 20449–54. doi:10.1016/S0021-9258(17)30525-2. PMID 2243099.
• Coetzer T, Palek J, Lawler J, Liu SC, Jarolim P, Lahav M, Prchal JT, Wang W, Alter BP, Schewitz G (June 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. doi:10.1182/blood.V75.11.2235.2235. PMID 2346784.
• Winkelmann JC, Leto TL, Watkins PC, Eddy R, Shows TB, Linnenbach AJ, Sahr KE, Kathuria N, Marchesi VT, Forget BG (July 1988). "Molecular cloning of the cDNA for human erythrocyte beta-spectrin". Blood. 72 (1): 328–34. doi:10.1182/blood.V72.1.328.328. PMID 3390609.
• Prchal JT, Morley BJ, Yoon SH, Coetzer TL, Palek J, Conboy JG, Kan YW (November 1987). "Isolation and characterization of cDNA clones for human erythrocyte beta-spectrin". Proceedings of the National Academy of Sciences of the United States of America. 84 (21): 7468–72. Bibcode:1987PNAS...84.7468P. doi:10.1073/pnas.84.21.7468. PMC 299317. PMID 3478706.
• Pothier B, Morlé L, Alloisio N, Ducluzeau MT, Caldani C, Féo C, Garbarz M, Chaveroche I, Dhermy D, Lecomte MC (June 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. doi:10.1182/blood.V69.6.1759.1759. PMID 3580577.
• Wolfe LC, John KM, Falcone JC, Byrne AM, Lux SE (November 1982). "A genetic defect in the binding of protein 4.1 to spectrin in a kindred with hereditary spherocytosis". The New England Journal of Medicine. 307 (22): 1367–74. doi:10.1056/NEJM198211253072203. PMID 6215583.
• Speicher DW, Marchesi VT (1984). "Erythrocyte spectrin is comprised of many homologous triple helical segments". Nature. 311 (5982): 177–80. doi:10.1038/311177a0. PMID 6472478. S2CID 4340715.
• Carlier MF, Simon C, Cassoly R, Pradel LA (April 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 (September 1982). "Identification of the molecular defect in the erythrocyte membrane skeleton of some kindreds with hereditary spherocytosis". Blood. 60 (3): 772–84. doi:10.1182/blood.V60.3.772.772. PMID 7104494.
• Schischmanoff PO, Winardi R, Discher DE, Parra MK, Bicknese SE, Witkowska HE, Conboy JG, Mohandas N (September 1995). "Defining of the minimal domain of protein 4.1 involved in spectrin-actin binding". The Journal of Biological Chemistry. 270 (36): 21243–50. doi:10.1074/jbc.270.36.21243. PMID 7673158.