SPTBN4

Spectrin, beta, non-erythrocytic 4
Identifiers
Symbols	SPTBN4 ; QV; SPNB4; SPTBN3
External IDs	OMIM: 606214 MGI: 1890574 HomoloGene: 11879 GeneCards: SPTBN4 Gene
Gene ontology Molecular function • actin binding • structural constituent of cytoskeleton • protein binding • phospholipid binding • phosphatase binding • ankyrin binding • spectrin binding Cellular component • cytoplasm • cytosol • plasma membrane • adherens junction • spectrin • membrane • nuclear matrix • PML body • node of Ranvier • paranode region of axon • neuronal cell body • axon initial segment • axon hillock • extracellular exosome • cell body fiber Biological process • regulation of sodium ion transport • cytoskeletal anchoring at plasma membrane • axonogenesis • axon guidance • sensory perception of sound • adult walking behavior • fertilization • negative regulation of heart rate • vesicle-mediated transport • transmission of nerve impulse • central nervous system projection neuron axonogenesis • regulation of peptidyl-serine phosphorylation • positive regulation of multicellular organism growth • clustering of voltage-gated sodium channels • actin filament capping • cardiac conduction • establishment of protein localization to plasma membrane Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	57731	80297
Ensembl	ENSG00000160460	ENSMUSG00000011751
UniProt	Q9H254	D3YWH8
RefSeq (mRNA)	NM_020971	NM_001199234
RefSeq (protein)	NP_066022	NP_001186163
Location (UCSC)	Chr 19: 40.47 – 40.58 Mb	Chr 7: 27.36 – 27.45 Mb
PubMed search

Spectrin, beta, non-erythrocytic 4, also known as SPTBN4, is a protein that in humans is encoded by the SPTBN4 gene.^[1][2]

Spectrin is an actin crosslinking and molecular scaffold protein that links the cell 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 localizes to the nuclear matrix, PML nuclear bodies, and cytoplasmic vesicles. A highly similar gene in the mouse is required for localization of specific membrane proteins in polarized regions of neurons. Multiple transcript variants encoding different isoforms have been found for this gene.^[1]

Interactions

SPTBN4 has been shown to interact with PTPRN^[2] and DISC1.^[3]

References

1. "Entrez Gene: SPTBN4 spectrin, beta, non-erythrocytic 4".
2. Berghs S, Aggujaro D, Dirkx R, Maksimova E, Stabach P, Hermel JM, Zhang JP, Philbrick W, Slepnev V, Ort T, Solimena M (November 2000). "betaIV spectrin, a new spectrin localized at axon initial segments and nodes of ranvier in the central and peripheral nervous system". J. Cell Biol. 151 (5): 985–1002. doi:10.1083/jcb.151.5.985. PMC 2174349. PMID 11086001.
3. Morris JA, Kandpal G, Ma L, Austin CP (Jul 2003). "DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation". Hum. Mol. Genet. 12 (13): 1591–608. doi:10.1093/hmg/ddg162. PMID 12812986.

Further reading

• Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O (2001). "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro.". DNA Res. 7 (4): 273–81. doi:10.1093/dnares/7.4.271. PMID 10997877.
• Berghs S, Aggujaro D, Dirkx R, Maksimova E, Stabach P, Hermel JM, Zhang JP, Philbrick W, Slepnev V, Ort T, Solimena M (2001). "betaIV spectrin, a new spectrin localized at axon initial segments and nodes of ranvier in the central and peripheral nervous system.". J. Cell Biol. 151 (5): 985–1002. doi:10.1083/jcb.151.5.985. PMC 2174349. PMID 11086001.
• Tse WT, Tang J, Jin O, Korsgren C, John KM, Kung AL, Gwynn B, Peters LL, Lux SE (2001). "A new spectrin, beta IV, has a major truncated isoform that associates with promyelocytic leukemia protein nuclear bodies and the nuclear matrix.". J. Biol. Chem. 276 (26): 23974–85. doi:10.1074/jbc.M009307200. PMID 11294830.
• Komada M, Soriano P (2002). "[Beta]IV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier.". J. Cell Biol. 156 (2): 337–48. doi:10.1083/jcb.200110003. PMC 2199236. PMID 11807096.
• 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.
• Ozeki Y, Tomoda T, Kleiderlein J, Kamiya A, Bord L, Fujii K, Okawa M, Yamada N, Hatten ME, Snyder SH, Ross CA, Sawa A (2003). "Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents binding to NudE-like (NUDEL) and inhibits neurite outgrowth.". Proc. Natl. Acad. Sci. U.S.A. 100 (1): 289–94. doi:10.1073/pnas.0136913100. PMC 140954. PMID 12506198.
• Morris JA, Kandpal G, Ma L, Austin CP (2004). "DISC1 (Disrupted-In-Schizophrenia 1) is a centrosome-associated protein that interacts with MAP1A, MIPT3, ATF4/5 and NUDEL: regulation and loss of interaction with mutation.". Hum. Mol. Genet. 12 (13): 1591–608. doi:10.1093/hmg/ddg162. PMID 12812986.
• 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.