SPTBN4

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

SPTBN4
Identifiers
Aliases	SPTBN4, QV, SPNB4, SPTBN3, spectrin beta, non-erythrocytic 4, CMND, NEDHND
External IDs	OMIM: 606214; MGI: 1890574; HomoloGene: 11879; GeneCards: SPTBN4; OMA:SPTBN4 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19q13.2 Start 40,466,241 bp End 40,576,464 bp
Gene location (Mouse) Chr. Chromosome 7 (mouse) Band 7 A3|7 15.88 cM Start 27,055,808 bp End 27,147,111 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right hemisphere of cerebellum right frontal lobe Brodmann area 9 anterior cingulate cortex prefrontal cortex nucleus accumbens caudate nucleus putamen amygdala pituitary gland Top expressed in superior frontal gyrus primary visual cortex cerebellar cortex nucleus of stria terminalis central gray substance of midbrain dentate gyrus of hippocampal formation granule cell subiculum piriform cortex nucleus accumbens cerebellar vermis More reference expression data BioGPS More reference expression data
Gene ontology Molecular function phosphatase binding spectrin binding structural constituent of cytoskeleton protein binding ankyrin binding actin binding phospholipid binding Cellular component cytoplasm cytosol PML body spectrin membrane cell body fiber nuclear matrix adherens junction plasma membrane node of Ranvier axon soma cell cortex axon hillock axon initial segment paranode region of axon extracellular exosome cytoskeleton intercalated disc Biological process clustering of voltage-gated sodium channels axonogenesis regulation of sodium ion transport transmission of nerve impulse hearing negative regulation of heart rate MAPK cascade axon guidance endoplasmic reticulum to Golgi vesicle-mediated transport reproductive process adult behavior cardiac conduction regulation of peptidyl-serine phosphorylation actin filament capping positive regulation of multicellular organism growth fertilization central nervous system projection neuron axonogenesis vesicle-mediated transport adult walking behavior protein localization to plasma membrane regulation of molecular function cytoskeleton organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 57731 80297 Ensembl ENSG00000160460 ENSMUSG00000011751 UniProt Q9H254 n/a RefSeq (mRNA) NM_020971 NM_025213 NM_001199234 NM_001199235 NM_001199236 NM_032610 RefSeq (protein) NP_066022 NP_079489 n/a Location (UCSC) Chr 19: 40.47 – 40.58 Mb Chr 7: 27.06 – 27.15 Mb PubMed search
Wikidata
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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.

Interactions

SPTBN4 has been shown to interact with PTPRN and DISC1.

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. S2CID 39778155.
• 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. Bibcode:2003PNAS..100..289O. 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. S2CID 7827573.