SPTBN2

Spectrin, beta, non-erythrocytic 2

PDB rendering based on 1wjm.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1WJM, 1WYQ

Identifiers

Symbols

SPTBN2 ; GTRAP41; SCA5; SCAR14

External IDs

OMIM: 604985 MGI: 1313261 HomoloGene: 48482 GeneCards: SPTBN2 Gene

Gene ontology
Molecular function	• actin binding • structural constituent of cytoskeleton • phospholipid binding
Cellular component	• extracellular space • cytosol • spectrin • neuronal cell body
Biological process	• axon guidance • synapse assembly • cell death • vesicle-mediated transport • antigen processing and presentation of exogenous peptide antigen via MHC class II • cerebellar Purkinje cell layer morphogenesis • adult behavior • multicellular organism growth • actin filament capping
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 11:
66.45 – 66.5 Mb

Chr 19:
4.71 – 4.75 Mb

PubMed search

Spectrin beta chain, brain 2 is a protein that in humans is encoded by the SPTBN2 gene.^[1]^[2]^[3]

Clinical significance

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

Interactions

SPTBN2 has been shown to interact with:

References

↑ Stankewich MC, Tse WT, Peters LL, Ch'ng Y, John KM, Stabach PR et al. (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.
↑ Ikeda Y, Dick KA, Weatherspoon MR, Gincel D, Armbrust KR, Dalton JC et al. (January 2006). "Spectrin mutations cause spinocerebellar ataxia type 5". Nat Genet 38 (2): 184–90. doi:10.1038/ng1728. PMID 16429157.
↑ "Entrez Gene: SPTBN2 spectrin, beta, non-erythrocytic 2".
↑ 4.0 4.1 Mao B, Wu W, Li Y, Hoppe D, Stannek P, Glinka A et al. (May 2001). "LDL-receptor-related protein 6 is a receptor for Dickkopf proteins". Nature 411 (6835): 321–5. doi:10.1038/35077108. PMID 11357136.
↑ 5.0 5.1 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.
↑ Sakaguchi G, Orita S, Naito A, Maeda M, Igarashi H, Sasaki T et al. (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.

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 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. 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 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.
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 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.

PDB gallery

1wjm: Solution structure of pleckstrin homology domain of human beta III spectrin.

1wyq: Solution structure of the second CH domain of human spectrin beta chain, brain 2

Proteins of the cytoskeleton

Human

Microfilaments
(ABPs)

Myofilament

Actins	A1 A2 B C1 G1 G2

Myosins	I MYO1A MYO1B MYO1C MYO1D MYO1E MYO1F MYO1G MYO1H) II MYH1 MYH2 MYH3 MYH4 MYH6 MYH7 MYH7B MYH8 MYH9 MYH10 MYH11 MYH13 MYH14 MYH15 MYH16 III MYO3A MYO3B V MYO5A MYO5B MYO5C VI MYO6 VII MYO7A MYO7B IX MYO9A MYO9B X MYO10 XV MYO15A XVIII MYO18A MYO18B LC MYL1 MYL2 MYL3 MYL4 MYL5 MYL6 MYL6B MYL7 MYL9 MYLIP MYLK MYLK2 MYLL1

Other	Tropomodulin 1 2 3 4 Troponin T 1 2 3 C 1 2 I 1 2 3 Tropomyosin 1 2 3 4 Actinin 1 2 3 4 Arp2/3 complex actin depolymerizing factors Cofilin 1 2 Destrin Gelsolin Profilin 1 2 Titin

Other

Wiskott-Aldrich syndrome protein
Fibrillin
Filamin
- FLNA
- FLNB
- FLNC
Espin
TRIOBP

IFs

Type 1/2
(Keratin,
Cytokeratin)

Epithelial keratins (soft alpha-keratins)	type I/chromosome 17 10 12 13 14 15 16 17 19 20 chromosome 12 18 none 21 type II/chromosome 12 1 2A 3 4 5 6A 6B 7 8 9

Hair keratins (hard alpha-keratins)	type I/chromosome 17 31 32 33A 33B 34 35 36 37 38 type II/chromosome 12 81 82 83 84 85 86

Ungrouped alpha	chromosome 17 23 24 25 26 27 28 39 40 chromosome 12 71 72 73 74 75 76 77 78 79 80

Not alpha	Beta-keratin

Type 3

Type 4

Type 5

Lamin A
B

Microtubules/
MAPs

Kinesins	KIF1A KIF1B KIF2A KIF2C KIF3B KIF3C KIF4A KIF4B KIF5A KIF5B KIF5C KIF6 KIF7 KIF9 KIF11 KIF12 KIF13A KIF13B KIF14 KIF15 KIF16B KIF17 KIF18A KIF18B KIF19 KIF20A KIF20B KIF21A KIF21B KIF22 KIF23 KIF24 KIF25 KIF26A KIF26B KIF27 KIFC1 KIFC2 KIFC3

Dyneins	axonemal: DNAH1 DNAH2 DNAH3 DNAH5 DNAH6 DNAH7 DNAH8 DNAH9 DNAH10 DNAH11 DNAH12 DNAH13 DNAH14 DNAH17 DNAI1 DNAI2 DNALI1 DNAL1 DNAL4 cytoplasmic: DYNC1H1 DYNC2H1 DYNC1I1 DYNC1I2 DYNC1LI1 DYNC1LI2 DYNC2LI1 DYNLL1 DYNLL2 DYNLRB1 DYNLRB2 DYNLT1 DYNLT3

Other	Tau protein Dynactin DCTN1 Tubulins TUBA1A TUBA1B TUBA1C TUBA3C TUBA3D TUBA3E TUBA4A TUBA8 Stathmin Tektin TEKT1 TEKT2 TEKT3 TEKT4 TEKT5 Dynamin DNM1 DNM2 DNM3

Catenins

Membrane

Dystrophin
- Dystroglycan
Utrophin
Ankyrin
- ANK1
- ANK2
- ANK3
Spectrin
- SPTA1
- SPTAN1
- SPTB
- SPTBN1
- SPTBN2
- SPTBN4
- SPTBN5

Other

Nonhuman

See also: cytoskeletal defects

Index of cells

Description	Structure nucleus chromosome genetics Organelles peroxisome cytoskeleton centrosome epithelia cilia mitochondria Membranes proteins cell adhesions Membrane transport ion channels vesicular transport solute carrier ABC transporters ATPase oxidoreduction-driven

Disease	Structural peroxisome cytoskeleton cilia mitochondria nucleus scleroprotein Membrane channelopathy solute carrier ATPase ABC transporters other extracellular ligands cell surface receptors intracellular signalling Vesicular transport Pore-forming toxins

SPTBN2

Clinical significance

Interactions

References

Further reading