SPTBN2

SPTBN2
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 1WJM, 1WYQ
Identifiers
Aliases	SPTBN2, GTRAP41, SCA5, SCAR14, spectrin beta, non-erythrocytic 2
External IDs	MGI: 1313261 HomoloGene: 48482 GeneCards: SPTBN2
Gene ontology Molecular function • actin binding • phospholipid binding • structural constituent of cytoskeleton • cadherin binding involved in cell-cell adhesion • Ras guanyl-nucleotide exchange factor activity Cellular component • cytosol • extracellular fluid • cell junction • neuronal cell body • cell cortex • apical plasma membrane • cytoskeleton • cell-cell adherens junction • spectrin • cytoplasm Biological process • antigen processing and presentation of exogenous peptide antigen via MHC class II • multicellular organism growth • MAPK cascade • axon guidance • cerebellar Purkinje cell layer morphogenesis • ER to Golgi vesicle-mediated transport • adult behavior • actin filament capping • synapse assembly • vesicle-mediated transport • cytoskeleton organization • cell-cell adhesion • positive regulation of GTPase activity Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6712	20743
Ensembl	ENSG00000173898	ENSMUSG00000067889
UniProt	O15020	n/a
RefSeq (mRNA)	NM_006946	NM_021287
RefSeq (protein)	NP_008877.1	n/a
Location (UCSC)	Chr 11: 66.69 – 66.73 Mb	Chr 19: 4.71 – 4.75 Mb
PubMed search	[1]	[2]
Wikidata

View/Edit Human

View/Edit Mouse

Spectrin beta chain, brain 2 is a protein that in humans is encoded by the SPTBN2 gene.^[3][4][5]

Clinical significance

Mutations in this gene is associated with Spinocerebellar ataxia type 5.

Interactions

SPTBN2 has been shown to interact with:

• ACTR1A,^[6][7]
• Beta-actin,^[6][7] and
• UNC13B.^[8]

References

1. "Human PubMed Reference:".
2. "Mouse PubMed Reference:".
3. Stankewich MC, Tse WT, Peters LL, Ch'ng Y, John KM, Stabach PR, Devarajan P, Morrow JS, Lux SE (Dec 1998). "A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles". Proc Natl Acad Sci U S A. 95 (24): 14158–63. doi:10.1073/pnas.95.24.14158. PMC 24343. PMID 9826670.
4. Ikeda Y, Dick KA, Weatherspoon MR, Gincel D, Armbrust KR, Dalton JC, Stevanin G, Dürr A, Zühlke C, Bürk K, Clark HB, Brice A, Rothstein JD, Schut LJ, Day JW, Ranum LP (January 2006). "Spectrin mutations cause spinocerebellar ataxia type 5". Nat Genet. 38 (2): 184–90. doi:10.1038/ng1728. PMID 16429157.
5. "Entrez Gene: SPTBN2 spectrin, beta, non-erythrocytic 2".
6. Mao B, Wu W, Li Y, Hoppe D, Stannek P, Glinka A, Niehrs C (May 2001). "LDL-receptor-related protein 6 is a receptor for Dickkopf proteins". Nature. 411 (6835): 321–5. doi:10.1038/35077108. PMID 11357136.
7. Holleran EA, Ligon LA, Tokito M, Stankewich MC, Morrow JS, Holzbaur EL (September 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.
8. Sakaguchi G, Orita S, Naito A, Maeda M, Igarashi H, Sasaki T, Takai Y (July 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.

Further reading

• De Matteis MA, Morrow JS (2000). "Spectrin tethers and mesh in the biosynthetic pathway". J. Cell. Sci. 113 (13): 2331–43. PMID 10852813.
• Ranum LP, Schut LJ, Lundgren JK, Orr HT, Livingston DM (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, Ohira M, Seki N, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (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. doi:10.1093/dnares/4.2.141. PMID 9205841.
• Ohara O, Ohara R, Yamakawa H, Nakajima D, Nakayama M (1998). "Characterization of a new beta-spectrin gene which is predominantly expressed in brain". Brain Res. Mol. Brain Res. 57 (2): 181–92. doi:10.1016/S0169-328X(98)00068-0. PMID 9675416.
• Sakaguchi G, Orita S, Naito A, Maeda M, Igarashi H, Sasaki T, Takai Y (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.
• Holleran EA, Ligon LA, Tokito M, Stankewich MC, Morrow JS, Holzbaur EL (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. doi:10.1006/cbir.2002.0895. 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. PMC 187542. PMID 12421765.
• 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. PMC 1223645. PMID 12820899.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (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.