SPTBN1

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Identifiers
Aliases
External IDs	GeneCards: [1]
Orthologs
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a
Wikidata
View/Edit Human

Spectrin beta chain, brain 1 is a protein that in humans is encoded by the SPTBN1 gene.

Function

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 that are involved in dimer formation. Multiple transcript variants encoding different isoforms have been found for this gene.

Interactions

SPTBN1 has been shown to interact with Merlin.

Model organisms

Spnb2 knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Abnormal
Recessive lethal study	Abnormal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Abnormal
Plasma immunoglobulins	Normal
Haematology	Normal
Peripheral blood lymphocytes	Normal
Micronucleus test	Normal
Heart weight	Normal
Tail epidermis wholemount	Normal
Skin Histopathology	Normal
Brain histopathology	Normal
MicroCT & Quantitative Faxitron	Abnormal
Salmonella infection	Normal
Citrobacter infection	Normal
All tests and analysis from

Model organisms have been used in the study of spectrin function. A conditional knockout mouse line, called Spnb2^{tm1a(EUCOMM)Wtsi} was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. Twenty seven tests were carried out on mutant mice and four significant abnormalities were observed. Few homozygous mutant embryos were identified during gestation and those that were present displayed oedema. None survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice. These animals had a decreased length of long bones, while males also displayed hypoalbuminemia .

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, Byers MG, Harris AS, Morrow JS, Watkins P, Shows TB, Forget BG (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, Ishibashi T, Ohkawara A (1996). "Calcium-dependent peripheral localization of 4.1-like proteins and fodrin in cultured human keratinocytes". Biol. Cell. 86 (1): 19–26. doi:10.1016/0248-4900(96)89520-7. PMID 8688828.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. 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. doi:10.1083/jcb.135.6.1815. PMC 2133946. PMID 8991093.
• Djinovic Carugo K, Bañuelos S, Saraste M (1997). "Crystal structure of a calponin homology domain". Nat. Struct. Biol. 4 (3): 175–9. doi:10.1038/nsb0397-175. PMID 9164454.
• Scoles DR, Huynh DP, Morcos PA, Coulsell ER, Robinson NG, Tamanoi F, Pulst SM (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. doi:10.1046/j.1471-4159.1998.71052220.x. 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. doi:10.1016/S0969-2126(98)00141-5. PMID 9817844.
• Löfvenberg L, Backman L (1999). "Calpain-induced proteolysis of beta-spectrins". FEBS Lett. 443 (2): 89–92. doi:10.1016/S0014-5793(98)01697-4. PMID 9989581.
• Hayes NV, Scott C, Heerkens E, Ohanian V, Maggs AM, Pinder JC, Kordeli E, Baines AJ (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 (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. doi:10.1042/0264-6021:3580727. PMC 1222106. PMID 11535133.
• Chen Y, Yu P, Lu D, Tagle DA, Cai T (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. doi:10.1385/JMN:17:1:59. 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. doi:10.1006/cbir.2002.0895. PMID 12119179.
• 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, Mishra B, Deng CX, Mishra L (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, Perry A, Mohandas N, Gutmann DH (2003). "Identification of a third Protein 4.1 tumor suppressor, Protein 4.1R, in meningioma pathogenesis". Neurobiol. Dis. 13 (3): 191–202. doi:10.1016/S0969-9961(03)00071-8. PMID 12901833.