Spectrin, beta, non-erythrocytic 1, also known as SPTBN1, is a human gene.cite web | title = Entrez Gene: SPTBN1 spectrin, beta, non-erythrocytic 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6711| accessdate = ]

section_title =
summary_text = Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma 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 contains an N-terminal actin-binding domain, and 17 spectrin repeats which are involved in dimer formation. Multiple transcript variants encoding different isoforms have been found for this gene.cite web | title = Entrez Gene: SPTBN1 spectrin, beta, non-erythrocytic 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6711| accessdate = ]


Further reading

citations =
*cite journal | author=Hu RJ, Watanabe M, Bennett V |title=Characterization of human brain cDNA encoding the general isoform of beta-spectrin. |journal=J. Biol. Chem. |volume=267 |issue= 26 |pages= 18715–22 |year= 1992 |pmid= 1527002 |doi=
*cite journal | author=Yoon SH, Skalka H, Prchal JT |title=Presence of erythroid and nonerythroid spectrin transcripts in human lens and cerebellum. |journal=Invest. Ophthalmol. Vis. Sci. |volume=30 |issue= 8 |pages= 1860–6 |year= 1989 |pmid= 2474519 |doi=
*cite journal | author=Chang JG, Scarpa A, Eddy RL, "et al." |title=Cloning of a portion of the chromosomal gene and cDNA for human beta-fodrin, the nonerythroid form of beta-spectrin. |journal=Genomics |volume=17 |issue= 2 |pages= 287–93 |year= 1993 |pmid= 8406479 |doi= 10.1006/geno.1993.1323
*cite journal | author=Shimizu T, Takakuwa Y, Koizumi H, "et al." |title=Calcium-dependent peripheral localization of 4.1-like proteins and fodrin in cultured human keratinocytes. |journal=Biol. Cell |volume=86 |issue= 1 |pages= 19–26 |year= 1996 |pmid= 8688828 |doi=
*cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791–806 |year= 1997 |pmid= 8889548 |doi=
*cite journal | author=Holleran EA, Tokito MK, Karki S, Holzbaur EL |title=Centractin (ARP1) associates with spectrin revealing a potential mechanism to link dynactin to intracellular organelles. |journal=J. Cell Biol. |volume=135 |issue= 6 Pt 2 |pages= 1815–29 |year= 1997 |pmid= 8991093 |doi=
*cite journal | author=Djinovic Carugo K, Bañuelos S, Saraste M |title=Crystal structure of a calponin homology domain. |journal=Nat. Struct. Biol. |volume=4 |issue= 3 |pages= 175–9 |year= 1997 |pmid= 9164454 |doi=
*cite journal | author=Scoles DR, Huynh DP, Morcos PA, "et al." |title=Neurofibromatosis 2 tumour suppressor schwannomin interacts with betaII-spectrin. |journal=Nat. Genet. |volume=18 |issue= 4 |pages= 354–9 |year= 1998 |pmid= 9537418 |doi= 10.1038/ng0498-354
*cite journal | author=Sihag RK |title=Brain beta-spectrin phosphorylation: phosphate analysis and identification of threonine-347 as a heparin-sensitive protein kinase phosphorylation site. |journal=J. Neurochem. |volume=71 |issue= 5 |pages= 2220–8 |year= 1998 |pmid= 9798950 |doi=
*cite journal | author=Bañuelos S, Saraste M, Djinović Carugo K |title=Structural comparisons of calponin homology domains: implications for actin binding. |journal=Structure |volume=6 |issue= 11 |pages= 1419–31 |year= 1999 |pmid= 9817844 |doi=
*cite journal | author=Löfvenberg L, Backman L |title=Calpain-induced proteolysis of beta-spectrins. |journal=FEBS Lett. |volume=443 |issue= 2 |pages= 89–92 |year= 1999 |pmid= 9989581 |doi=
*cite journal | author=Hayes NV, Scott C, Heerkens E, "et al." |title=Identification of a novel C-terminal variant of beta II spectrin: two isoforms of beta II spectrin have distinct intracellular locations and activities. |journal=J. Cell. Sci. |volume=113 ( Pt 11) |issue= |pages= 2023–34 |year= 2000 |pmid= 10806113 |doi=
*cite journal | author=Kontrogianni-Konstantopoulos A, Frye CS, Benz EJ, Huang SC |title=The prototypical 4.1R-10-kDa domain and the 4.1g-10-kDa paralog mediate fodrin-actin complex formation. |journal=J. Biol. Chem. |volume=276 |issue= 23 |pages= 20679–87 |year= 2001 |pmid= 11274145 |doi= 10.1074/jbc.M010581200
*cite journal | author=Neill GW, Crompton MR |title=Binding of the merlin-I product of the neurofibromatosis type 2 tumour suppressor gene to a novel site in beta-fodrin is regulated by association between merlin domains. |journal=Biochem. J. |volume=358 |issue= Pt 3 |pages= 727–35 |year= 2001 |pmid= 11535133 |doi=
*cite journal | author=Chen Y, Yu P, Lu D, "et al." |title=A novel isoform of beta-spectrin II localizes to cerebellar Purkinje-cell bodies and interacts with neurofibromatosis type 2 gene product schwannomin. |journal=J. Mol. Neurosci. |volume=17 |issue= 1 |pages= 59–70 |year= 2002 |pmid= 11665863 |doi=
*cite journal | author=Shoeman RL, Hartig R, Hauses C, Traub P |title=Organization of focal adhesion plaques is disrupted by action of the HIV-1 protease. |journal=Cell Biol. Int. |volume=26 |issue= 6 |pages= 529–39 |year= 2003 |pmid= 12119179 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Tomsig JL, Snyder SL, Creutz CE |title=Identification of targets for calcium signaling through the copine family of proteins. Characterization of a coiled-coil copine-binding motif. |journal=J. Biol. Chem. |volume=278 |issue= 12 |pages= 10048–54 |year= 2003 |pmid= 12522145 |doi= 10.1074/jbc.M212632200
*cite journal | author=Tang Y, Katuri V, Dillner A, "et al." |title=Disruption of transforming growth factor-beta signaling in ELF beta-spectrin-deficient mice. |journal=Science |volume=299 |issue= 5606 |pages= 574–7 |year= 2003 |pmid= 12543979 |doi= 10.1126/science.1075994
*cite journal | author=Robb VA, Li W, Gascard P, "et al." |title=Identification of a third Protein 4.1 tumor suppressor, Protein 4.1R, in meningioma pathogenesis. |journal=Neurobiol. Dis. |volume=13 |issue= 3 |pages= 191–202 |year= 2003 |pmid= 12901833 |doi=

update_page = yes
require_manual_inspection = no
update_protein_box = yes
update_summary = yes
update_citations = yes

Wikimedia Foundation. 2010.

Look at other dictionaries:

  • Microtubule — Space filling model of a microtubule segment derived from cryo electron microscopy. The protofilaments are seen running along the axis of the segment. The microtubule (+) end is towards the top of the image.[1] Microtubules are a component of the …   Wikipedia

  • Keratin — Not to be confused with kerogen, carotene, chitin, or creatine. Microscopy of keratin filaments inside cells. Keratin refers to a family of fibrous structural proteins. Keratin is the key structural material making up the outer layer of human… …   Wikipedia

  • Cytoskeleton — The eukaryotic cytoskeleton. Actin filaments are shown in red, microtubules in green, and the nuclei are in blue. The cytoskeleton (also CSK) is a cellular scaffolding or skeleton contained within a cell s cytoplasm and is made out of protein.… …   Wikipedia

  • Microfilament — Actin cytoskeleton of mouse embryo fibroblasts, stained with Fluorescein isothiocyanate phalloidin Microfilaments ( or actin filaments) are the thinnest filaments of the cytoskeleton, a structure found in the cytoplasm of all eukaryotic cells.… …   Wikipedia

  • Actin — G Actin (PDB code: 1j6z). ADP and the divalent cation are highlighted …   Wikipedia

  • Myosin — Part of the myosin II structure. Atoms in the heavy chain are colored red on the left hand side, and atoms in the light chains are colored orange and yellow. Myosins comprise a family of ATP dependent motor proteins and are best known for their… …   Wikipedia

  • Lamin — Nuclear lamins, also known as Class V intermediate filaments, are fibrous proteins providing structural function and transcriptional regulation in the cell nucleus. Nuclear lamins interact with membrane associated proteins to form the nuclear… …   Wikipedia

  • MreB — Procaryotic MreB (PDB code: 1jce) in cartoon representation. The fold of the protein is similar to its eukaryotic counterpart actin. MreB is a protein found in bacteria that has been identified as a homologue of actin, as indicated by… …   Wikipedia

  • Kinesin — Animation of kinesin walking on a microtubule The kinesin dimer attaches to, and mo …   Wikipedia

  • Dynein — A dynein complex. Cytoplasmic dynein has two heavy chains with globular head …   Wikipedia