SPTBN1: Difference between revisions

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{{Infobox gene}}
{{PBB_Controls
'''Spectrin beta chain, brain 1''' is a [[protein]] that in humans is encoded by the ''SPTBN1'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SPTBN1 spectrin, beta, non-erythrocytic 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6711| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
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 that are involved in dimer formation. Multiple transcript variants encoding different isoforms have been found for this gene.<ref name="entrez"/>
| image = PBB_Protein_SPTBN1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aa2.
| PDB = {{PDB2|1aa2}}, {{PDB2|1bkr}}, {{PDB2|1btn}}, {{PDB2|1mph}}
| Name = Spectrin, beta, non-erythrocytic 1
| HGNCid = 11275
| Symbol = SPTBN1
| AltSymbols =; ELF; SPTB2; betaSpII
| OMIM = 182790
| ECnumber = 
| Homologene = 2354
| MGIid = 98388
| GeneAtlas_image1 = PBB_GE_SPTBN1_215918_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SPTBN1_200671_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_SPTBN1_200672_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0008091 |text = spectrin}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0051016 |text = barbed-end actin filament capping}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6711
    | Hs_Ensembl = ENSG00000115306
    | Hs_RefseqProtein = NP_003119
    | Hs_RefseqmRNA = NM_003128
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 54537143
    | Hs_GenLoc_end = 54749366
    | Hs_Uniprot = Q01082
    | Mm_EntrezGene = 20742
    | Mm_Ensembl = ENSMUSG00000020315
    | Mm_RefseqmRNA = NM_009260
    | Mm_RefseqProtein = NP_033286
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 29999722
    | Mm_GenLoc_end = 30168144
    | Mm_Uniprot = Q3TEM7
  }}
}}
'''Spectrin, beta, non-erythrocytic 1''', also known as '''SPTBN1''', is a human [[gene]].<ref name="entrez">{{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 = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{PBB_Summary
SPTBN1 has been shown to [[Protein-protein interaction|interact]] with [[Merlin (protein)|Merlin]].<ref name=pmid11535133>{{cite journal | vauthors = 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 | date = September 2001 | pmid = 11535133 | pmc = 1222106 | doi = 10.1042/0264-6021:3580727 }}</ref>
| 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.<ref name="entrez">{{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 = }}</ref>
}}


==References==
==Model organisms==
{{reflist|2}}
{| class="wikitable sortable collapsible collapsed" border="1" cellpadding="2" style="float: right;" |
==Further reading==
|+ ''Spnb2'' knockout mouse phenotype
{{refbegin | 2}}
|-
{{PBB_Further_reading
! Characteristic!! Phenotype
| 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=  }}
}}
{{refend}}


{{protein-stub}}
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{{WikiDoc Sources}}
| [[Homozygote]] viability || bgcolor="#C40000"|Abnormal
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| [[Recessive]] lethal study || bgcolor="#C40000"|Abnormal
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| Body weight || bgcolor="#488ED3"|Normal
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| [[Open Field (animal test)|Anxiety]] || bgcolor="#488ED3"|Normal
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| Neurological assessment || bgcolor="#488ED3"|Normal
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| Grip strength || bgcolor="#488ED3"|Normal
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| [[Hot plate test|Hot plate]] || bgcolor="#488ED3"|Normal
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| [[Dysmorphology]] || bgcolor="#488ED3"|Normal
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| [[Indirect calorimetry]] || bgcolor="#488ED3"|Normal
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| [[Glucose tolerance test]] || bgcolor="#488ED3"|Normal
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| [[Auditory brainstem response]] || bgcolor="#488ED3"|Normal
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| [[Dual-energy X-ray absorptiometry|DEXA]] || bgcolor="#488ED3"|Normal
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| [[Radiography]] || bgcolor="#488ED3"|Normal
|-
| Body temperature || bgcolor="#488ED3"|Normal
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| Eye morphology || bgcolor="#488ED3"|Normal
|-
| [[Clinical chemistry]] || bgcolor="#C40000"|Abnormal<ref name="Clinical chemistry">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBAX/plasma-chemistry/ |title=Clinical chemistry data for Spnb2 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| [[Blood plasma|Plasma]] [[immunoglobulin]]s || bgcolor="#488ED3"|Normal
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| [[Haematology]] || bgcolor="#488ED3"|Normal
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| [[Peripheral blood lymphocyte]]s || bgcolor="#488ED3"|Normal
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| [[Micronucleus test]] || bgcolor="#488ED3"|Normal
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| Heart weight || bgcolor="#488ED3"|Normal
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| Tail epidermis wholemount || bgcolor="#488ED3"|Normal
|-
| Skin Histopathology || bgcolor="#488ED3"|Normal
|-
| Brain histopathology || bgcolor="#488ED3"|Normal
|-
| MicroCT & Quantitative Faxitron || bgcolor="#C40000"|Abnormal
|-
| ''[[Salmonella]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Salmonella'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBAX/salmonella-challenge/ |title=''Salmonella'' infection data for Spnb2 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| ''[[Citrobacter]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Citrobacter'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MBAX/citrobacter-challenge/ |title=''Citrobacter'' infection data for Spnb2 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| colspan=2; style="text-align: center;" | All tests and analysis from<ref name="mgp_reference">{{cite journal | doi = 10.1111/j.1755-3768.2010.4142.x | title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice | year = 2010 | author = Gerdin AK | journal = Acta Ophthalmologica | volume = 88 | pages =  925–7 }}</ref><ref>[http://www.sanger.ac.uk/mouseportal/ Mouse Resources Portal], Wellcome Trust Sanger Institute.</ref>
|}
[[Model organism]]s have been used in the study of spectrin function. A conditional [[knockout mouse]] line, called ''Spnb2<sup>tm1a(EUCOMM)Wtsi</sup>''<ref name="allele_ref">{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Spnb2 |title=International Knockout Mouse Consortium}}</ref><ref name="mgi_allele_ref">{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4432393 |title=Mouse Genome Informatics}}</ref> was generated as part of the [[International Knockout Mouse Consortium]] program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.<ref name="pmid21677750">{{cite journal |title=A conditional knockout resource for the genome-wide study of mouse gene function|vauthors=Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A|journal=[[Nature (journal)|Nature]]|pmid=21677750|date=15 June 2011|volume=474|issue=7351|pages=337–42|doi=10.1038/nature10163|pmc=3572410}}</ref><ref name="mouse_library">{{cite journal | vauthors = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | year = 2011 | pmid = 21677718 | doi = 10.1038/474262a }}</ref><ref name="mouse_for_all_reasons">{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A Mouse for All Reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | year = 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}</ref>
 
Male and female animals underwent a standardized [[phenotypic screen]] to determine the effects of deletion.<ref name="mgp_reference" /><ref name="pmid21722353">{{cite journal | vauthors = van der Weyden L, White JK, Adams DJ, Logan DW | title = The mouse genetics toolkit: revealing function and mechanism. | journal = Genome Biol | volume = 12 | issue = 6 | pages = 224 | year = 2011 | pmid = 21722353 | pmc = 3218837 | doi = 10.1186/gb-2011-12-6-224 }}</ref> Twenty seven tests were carried out on [[mutant]] mice and four significant abnormalities were observed.<ref name="mgp_reference" /> Few [[homozygous]] [[mutant]] embryos were identified during gestation and those that were present displayed oedema. None survived until [[weaning]]. The remaining tests were carried out on [[heterozygous]] mutant adult mice. These animals had a decreased length of long bones, while males also displayed [[hypoalbuminemia]] .<ref name="mgp_reference" />
 
== References ==
{{Reflist}}
 
== Further reading ==
{{Refbegin | 2}}
* {{cite journal | vauthors = 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 | vauthors = 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 | vauthors = Chang JG, Scarpa A, Eddy RL, Byers MG, Harris AS, Morrow JS, Watkins P, Shows TB, Forget BG | 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 | vauthors = Shimizu T, Takakuwa Y, Koizumi H, Ishibashi T, Ohkawara A | 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 = 10.1016/0248-4900(96)89520-7 }}
* {{cite journal | vauthors = 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 = 10.1101/gr.6.9.791 }}
* {{cite journal | vauthors = 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 | pmc = 2133946 | doi = 10.1083/jcb.135.6.1815 }}
* {{cite journal | vauthors = 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 = 10.1038/nsb0397-175 }}
* {{cite journal | vauthors = Scoles DR, Huynh DP, Morcos PA, Coulsell ER, Robinson NG, Tamanoi F, Pulst SM | 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 | vauthors = 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 = 10.1046/j.1471-4159.1998.71052220.x }}
* {{cite journal | vauthors = 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 = 10.1016/S0969-2126(98)00141-5 }}
* {{cite journal | vauthors = 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 = 10.1016/S0014-5793(98)01697-4 }}
* {{cite journal | vauthors = Hayes NV, Scott C, Heerkens E, Ohanian V, Maggs AM, Pinder JC, Kordeli E, Baines AJ | 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 | issue = 11 | pages = 2023–34 | year = 2000 | pmid = 10806113 | doi =  }}
* {{cite journal | vauthors = 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 | vauthors = 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 | pmc = 1222106 | doi = 10.1042/0264-6021:3580727 }}
* {{cite journal | vauthors = Chen Y, Yu P, Lu D, Tagle DA, Cai T | 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 = 10.1385/JMN:17:1:59 }}
* {{cite journal | vauthors = 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 = 10.1006/cbir.2002.0895 }}
* {{cite journal | vauthors = 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 | vauthors = Tang Y, Katuri V, Dillner A, Mishra B, Deng CX, Mishra L | 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 | vauthors = Robb VA, Li W, Gascard P, Perry A, Mohandas N, Gutmann DH | 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 = 10.1016/S0969-9961(03)00071-8 }}
{{Refend}}
 
{{PDB Gallery|geneid=6711}}
{{Cytoskeletal Proteins}}
{{Use dmy dates|date=April 2017}}
 
[[Category:Genes mutated in mice]]

Latest revision as of 20:53, 8 November 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Spectrin beta chain, brain 1 is a protein that in humans is encoded by the SPTBN1 gene.[1]

Function

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 that are involved in dimer formation. Multiple transcript variants encoding different isoforms have been found for this gene.[1]

Interactions

SPTBN1 has been shown to interact with Merlin.[2]

Model organisms

Model organisms have been used in the study of spectrin function. A conditional knockout mouse line, called Spnb2tm1a(EUCOMM)Wtsi[8][9] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[10][11][12]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[6][13] Twenty seven tests were carried out on mutant mice and four significant abnormalities were observed.[6] Few homozygous mutant embryos were identified during gestation and those that were present displayed oedema. None survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice. These animals had a decreased length of long bones, while males also displayed hypoalbuminemia .[6]

References

  1. ↑ 1.0 1.1 "Entrez Gene: SPTBN1 spectrin, beta, non-erythrocytic 1".
  2. ↑ Neill GW, Crompton MR (September 2001). "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". Biochem. J. 358 (Pt 3): 727–35. doi:10.1042/0264-6021:3580727. PMC 1222106. PMID 11535133.
  3. ↑ "Clinical chemistry data for Spnb2". Wellcome Trust Sanger Institute.
  4. ↑ "Salmonella infection data for Spnb2". Wellcome Trust Sanger Institute.
  5. ↑ "Citrobacter infection data for Spnb2". Wellcome Trust Sanger Institute.
  6. ↑ 6.0 6.1 6.2 6.3 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  7. ↑ Mouse Resources Portal, Wellcome Trust Sanger Institute.
  8. ↑ "International Knockout Mouse Consortium".
  9. ↑ "Mouse Genome Informatics".
  10. ↑ Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (15 June 2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  11. ↑ Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  12. ↑ Collins FS, Rossant J, Wurst W (2007). "A Mouse for All Reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  13. ↑ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.

Further reading

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