SPTBN1

From Wikipedia, the free encyclopedia

Spectrin, beta, non-erythrocytic 1

PDB rendering based on 1aa2.

Available structures: 1aa2, 1bkr, 1btn, 1mph

Identifiers

Symbol(s)

SPTBN1; ELF; SPTB2; betaSpII

External IDs

OMIM: 182790 MGI: 98388 HomoloGene: 2354

Gene ontology
Molecular Function:	• actin binding • structural constituent of cytoskeleton • calmodulin binding
Cellular Component:	• cytoskeleton • spectrin • membrane
Biological Process:	• barbed-end actin filament capping

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003128 (mRNA)
NP_003119 (protein)

NM_009260 (mRNA)
NP_033286 (protein)

Location

Chr 2: 54.54 - 54.75 Mb

Chr 11: 30 - 30.17 Mb

Pubmed search

[1]

[2]

Spectrin, beta, non-erythrocytic 1, also known as SPTBN1, is a human gene.^[1]

Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. This gene is one member of a family of beta-spectrin genes. The encoded protein contains an N-terminal actin-binding domain, and 17 spectrin repeats which are involved in dimer formation. Multiple transcript variants encoding different isoforms have been found for this gene.^[1]

[edit] References

^ ^a ^b Entrez Gene: SPTBN1 spectrin, beta, non-erythrocytic 1.

[edit] Further reading

Hu RJ, Watanabe M, Bennett V (1992). "Characterization of human brain cDNA encoding the general isoform of beta-spectrin.". J. Biol. Chem. 267 (26): 18715–22. PMID 1527002.
Yoon SH, Skalka H, Prchal JT (1989). "Presence of erythroid and nonerythroid spectrin transcripts in human lens and cerebellum.". Invest. Ophthalmol. Vis. Sci. 30 (8): 1860–6. PMID 2474519.
Chang JG, Scarpa A, Eddy RL, et al. (1993). "Cloning of a portion of the chromosomal gene and cDNA for human beta-fodrin, the nonerythroid form of beta-spectrin.". Genomics 17 (2): 287–93. doi:10.1006/geno.1993.1323. PMID 8406479.
Shimizu T, Takakuwa Y, Koizumi H, et al. (1996). "Calcium-dependent peripheral localization of 4.1-like proteins and fodrin in cultured human keratinocytes.". Biol. Cell 86 (1): 19–26. PMID 8688828.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Holleran EA, Tokito MK, Karki S, Holzbaur EL (1997). "Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles.". J. Cell Biol. 135 (6 Pt 2): 1815–29. PMID 8991093.
Djinovic Carugo K, Bañuelos S, Saraste M (1997). "Crystal structure of a calponin homology domain.". Nat. Struct. Biol. 4 (3): 175–9. PMID 9164454.
Scoles DR, Huynh DP, Morcos PA, et al. (1998). "Neurofibromatosis 2 tumour suppressor schwannomin interacts with betaII-spectrin.". Nat. Genet. 18 (4): 354–9. doi:10.1038/ng0498-354. PMID 9537418.
Sihag RK (1998). "Brain beta-spectrin phosphorylation: phosphate analysis and identification of threonine-347 as a heparin-sensitive protein kinase phosphorylation site.". J. Neurochem. 71 (5): 2220–8. PMID 9798950.
Bañuelos S, Saraste M, Djinović Carugo K (1999). "Structural comparisons of calponin homology domains: implications for actin binding.". Structure 6 (11): 1419–31. PMID 9817844.
Löfvenberg L, Backman L (1999). "Calpain-induced proteolysis of beta-spectrins.". FEBS Lett. 443 (2): 89–92. PMID 9989581.
Hayes NV, Scott C, Heerkens E, et al. (2000). "Identification of a novel C-terminal variant of beta II spectrin: two isoforms of beta II spectrin have distinct intracellular locations and activities.". J. Cell. Sci. 113 ( Pt 11): 2023–34. PMID 10806113.
Kontrogianni-Konstantopoulos A, Frye CS, Benz EJ, Huang SC (2001). "The prototypical 4.1R-10-kDa domain and the 4.1g-10-kDa paralog mediate fodrin-actin complex formation.". J. Biol. Chem. 276 (23): 20679–87. doi:10.1074/jbc.M010581200. PMID 11274145.
Neill GW, Crompton MR (2001). "Binding of the merlin-I product of the neurofibromatosis type 2 tumour suppressor gene to a novel site in beta-fodrin is regulated by association between merlin domains.". Biochem. J. 358 (Pt 3): 727–35. PMID 11535133.
Chen Y, Yu P, Lu D, et al. (2002). "A novel isoform of beta-spectrin II localizes to cerebellar Purkinje-cell bodies and interacts with neurofibromatosis type 2 gene product schwannomin.". J. Mol. Neurosci. 17 (1): 59–70. PMID 11665863.
Shoeman RL, Hartig R, Hauses C, Traub P (2003). "Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease.". Cell Biol. Int. 26 (6): 529–39. PMID 12119179.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Tomsig JL, Snyder SL, Creutz CE (2003). "Identification of targets for calcium signaling through the copine family of proteins. Characterization of a coiled-coil copine-binding motif.". J. Biol. Chem. 278 (12): 10048–54. doi:10.1074/jbc.M212632200. PMID 12522145.
Tang Y, Katuri V, Dillner A, et al. (2003). "Disruption of transforming growth factor-beta signaling in ELF beta-spectrin-deficient mice.". Science 299 (5606): 574–7. doi:10.1126/science.1075994. PMID 12543979.
Robb VA, Li W, Gascard P, et al. (2003). "Identification of a third Protein 4.1 tumor suppressor, Protein 4.1R, in meningioma pathogenesis.". Neurobiol. Dis. 13 (3): 191–202. PMID 12901833.