SPTBN2

From Wikipedia, the free encyclopedia

Spectrin, beta, non-erythrocytic 2

PDB rendering based on 1wjm.

Available structures: 1wjm, 1wyq

Identifiers

Symbol(s)

SPTBN2; SCA5

External IDs

OMIM: 604985 MGI: 1313261 HomoloGene: 48482

Gene ontology
Molecular Function:	• actin binding • structural constituent of cytoskeleton
Cellular Component:	• cytoskeleton • spectrin • membrane
Biological Process:	• cell death • vesicle-mediated transport • barbed-end actin filament capping

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_006946 (mRNA)
NP_008877 (protein)

NM_021287 (mRNA)
NP_067262 (protein)

Location

Chr 11: 66.21 - 66.25 Mb

Chr 19: 4.71 - 4.75 Mb

Pubmed search

[1]

[2]

Spectrin, beta, non-erythrocytic 2, also known as SPTBN2, is a human gene.^[1]

[edit] References

^ Entrez Gene: SPTBN2 spectrin, beta, non-erythrocytic 2.

[edit] Further reading

De Matteis MA, Morrow JS (2000). "Spectrin tethers and mesh in the biosynthetic pathway.". J. Cell. Sci. 113 ( Pt 13): 2331-43. PMID 10852813.
Ranum LP, Schut LJ, Lundgren JK, et al. (1995). "Spinocerebellar ataxia type 5 in a family descended from the grandparents of President Lincoln maps to chromosome 11.". Nat. Genet. 8 (3): 280-4. doi:10.1038/ng1194-280. PMID 7874171.
Nagase T, Ishikawa K, Nakajima D, et al. (1997). "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro.". DNA Res. 4 (2): 141-50. PMID 9205841.
Ohara O, Ohara R, Yamakawa H, et al. (1998). "Characterization of a new beta-spectrin gene which is predominantly expressed in brain.". Brain Res. Mol. Brain Res. 57 (2): 181-92. PMID 9675416.
Sakaguchi G, Orita S, Naito A, et al. (1998). "A novel brain-specific isoform of beta spectrin: isolation and its interaction with Munc13.". Biochem. Biophys. Res. Commun. 248 (3): 846-51. doi:10.1006/bbrc.1998.9067. PMID 9704016.
Stankewich MC, Tse WT, Peters LL, et al. (1998). "A widely expressed betaIII spectrin associated with Golgi and cytoplasmic vesicles.". Proc. Natl. Acad. Sci. U.S.A. 95 (24): 14158-63. PMID 9826670.
Holleran EA, Ligon LA, Tokito M, et al. (2001). "beta III spectrin binds to the Arp1 subunit of dynactin.". J. Biol. Chem. 276 (39): 36598-605. doi:10.1074/jbc.M104838200. PMID 11461920.
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.
Nakayama M, Kikuno R, Ohara O (2003). "Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs.". Genome Res. 12 (11): 1773-84. doi:10.1101/gr.406902. PMID 12421765.
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.
Bignone PA, Baines AJ (2003). "Spectrin alpha II and beta II isoforms interact with high affinity at the tetramerization site.". Biochem. J. 374 (Pt 3): 613-24. doi:10.1042/BJ20030507. PMID 12820899.
Ikeda Y, Dick KA, Weatherspoon MR, et al. (2006). "Spectrin mutations cause spinocerebellar ataxia type 5.". Nat. Genet. 38 (2): 184-90. doi:10.1038/ng1728. PMID 16429157.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635-48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.