G2Cdb::Gene report

Gene id
Gene symbol
Stom (MGI)
Mus musculus
G00006804 (Homo sapiens)

Databases (3)

ENSMUSG00000026880 (Ensembl mouse gene)
13830 (Entrez Gene)
Marker Symbol
MGI:95403 (MGI)

Synonyms (3)

  • Epb7.2
  • protein 7.2b
  • stomatin

Literature (17)

Pubmed - other

  • A high-resolution anatomical atlas of the transcriptome in the mouse embryo.

    Diez-Roux G, Banfi S, Sultan M, Geffers L, Anand S, Rozado D, Magen A, Canidio E, Pagani M, Peluso I, Lin-Marq N, Koch M, Bilio M, Cantiello I, Verde R, De Masi C, Bianchi SA, Cicchini J, Perroud E, Mehmeti S, Dagand E, Schrinner S, Nürnberger A, Schmidt K, Metz K, Zwingmann C, Brieske N, Springer C, Hernandez AM, Herzog S, Grabbe F, Sieverding C, Fischer B, Schrader K, Brockmeyer M, Dettmer S, Helbig C, Alunni V, Battaini MA, Mura C, Henrichsen CN, Garcia-Lopez R, Echevarria D, Puelles E, Garcia-Calero E, Kruse S, Uhr M, Kauck C, Feng G, Milyaev N, Ong CK, Kumar L, Lam M, Semple CA, Gyenesei A, Mundlos S, Radelof U, Lehrach H, Sarmientos P, Reymond A, Davidson DR, Dollé P, Antonarakis SE, Yaspo ML, Martinez S, Baldock RA, Eichele G and Ballabio A

    Telethon Institute of Genetics and Medicine, Naples, Italy.

    Ascertaining when and where genes are expressed is of crucial importance to understanding or predicting the physiological role of genes and proteins and how they interact to form the complex networks that underlie organ development and function. It is, therefore, crucial to determine on a genome-wide level, the spatio-temporal gene expression profiles at cellular resolution. This information is provided by colorimetric RNA in situ hybridization that can elucidate expression of genes in their native context and does so at cellular resolution. We generated what is to our knowledge the first genome-wide transcriptome atlas by RNA in situ hybridization of an entire mammalian organism, the developing mouse at embryonic day 14.5. This digital transcriptome atlas, the Eurexpress atlas (http://www.eurexpress.org), consists of a searchable database of annotated images that can be interactively viewed. We generated anatomy-based expression profiles for over 18,000 coding genes and over 400 microRNAs. We identified 1,002 tissue-specific genes that are a source of novel tissue-specific markers for 37 different anatomical structures. The quality and the resolution of the data revealed novel molecular domains for several developing structures, such as the telencephalon, a novel organization for the hypothalamus, and insight on the Wnt network involved in renal epithelial differentiation during kidney development. The digital transcriptome atlas is a powerful resource to determine co-expression of genes, to identify cell populations and lineages, and to identify functional associations between genes relevant to development and disease.

    Funded by: Medical Research Council: MC_U127527203; Telethon: TGM11S03

    PLoS biology 2011;9;1;e1000582

  • A single conserved proline residue determines the membrane topology of stomatin.

    Kadurin I, Huber S and Gründer S

    Institute of Physiology II, University of Würzburg, Röntgenring 9, Würzburg, Germany.

    Stomatin is an integral membrane protein which is widely expressed in many cell types. It is accepted that stomatin has a unique hairpin-loop topology: it is anchored to the membrane with an N-terminal hydrophobic domain and the N- and C-termini are cytoplasmically localized. Stomatin is a prototype for a family of related proteins, containing among others MEC-2 (mechanosensory protein 2) from Caenorhabditis elegans, SLP (stomatin-like protein)-3 and podocin, all of which interact with ion channels to regulate their activity. Members of the stomatin family partly localize in DRMs (detergent-resistant membrane domains) enriched in cholesterol and sphingolipids. It has been proposed that a highly conserved proline residue in the middle of the hydrophobic domain directly binds cholesterol and that cholesterol binding is necessary for the regulation of ion channels. In the present study we show that a small part of the stomatin pool exists as a single-pass transmembrane protein rather than a hairpin-loop protein. The highly conserved proline residue is crucial for adopting the hairpin-loop topology: substitution of this proline residue by serine transfers the whole stomatin pool to the single-pass transmembrane form, which no longer localizes to DRMs. These results suggest that formation of the hairpin loop is inefficient and that the conserved proline residue is indispensable for formation of the hairpin loop. The single-pass transmembrane form exists also for SLP-3 and it should be considered that it mediates part of the physiological functions of stomatin and related proteins.

    The Biochemical journal 2009;418;3;587-94

  • Stomatin and sensory neuron mechanotransduction.

    Martinez-Salgado C, Benckendorff AG, Chiang LY, Wang R, Milenkovic N, Wetzel C, Hu J, Stucky CL, Parra MG, Mohandas N and Lewin GR

    Department of Neuroscience, Max-Delbrück Center for Molecular Medicine and Charité Universitätsmedizin Berlin, Robert-Rössle Str, Berlin-Buch, Germany.

    Somatic sensory neurons of the dorsal root ganglia are necessary for a large part of our mechanosensory experience. However, we only have a good knowledge of the molecules required for mechanotransduction in simple invertebrates such as the nematode Caenorhabiditis elegans. In C. elegans, a number of so-called mec genes have been isolated that are required for the transduction of body touch. One such gene, mec-2 codes for an integral membrane protein of the stomatin family, a large group of genes with a stomatin homology domain. Using stomatin null mutant mice, we have tested the hypothesis that the founding member of this family, stomatin might play a role in the transduction of mechanical stimuli by primary sensory neurons. We used the in vitro mouse skin nerve preparation to record from a large population of low- and high-threshold mechanoreceptors with myelinated A-fiber (n = 553) and unmyelinated C-fiber (n = 157) axons. One subtype of mechanoreceptor, the d-hair receptor, which is a rapidly adapting mechanoreceptor, had reduced sensitivity to mechanical stimulation in the absence of stomatin. Other cutaneous mechanoreceptors, including nociceptive C-fibers were not affected by the absence of a functional stomatin protein. Patch-clamp analysis of presumptive D-hair receptor mechanoreceptive neurons, which were identified by a characteristic rosette morphology in culture, showed no change in membrane excitability in the absence of the stomatin protein. We conclude that stomatin is required for normal mechanotransduction in a subpopulation of vertebrate sensory neurons.

    Journal of neurophysiology 2007;98;6;3802-8

  • Fine mapping of collagen-induced arthritis quantitative trait loci in an advanced intercross line.

    Yu X, Bauer K, Wernhoff P, Koczan D, Möller S, Thiesen HJ and Ibrahim SM

    Immunogenetics Group, University of Rostock, Rostock, Germany.

    The generation of advanced intercross lines (AIL) is a powerful approach for high-resolution fine mapping of quantitative trait loci (QTLs), because they accumulate much more recombination events compared with conventional F2 intercross and N2 backcross. However, the application of this approach is severely hampered by the requirements of excessive resources to maintain such crosses, i.e., in terms of animal care, space, and time. Therefore, in this study, we produced an AIL to fine map collagen-induced arthritis (CIA) QTLs using comparatively limited resources. We used only 308 (DBA/1 x FVB/N)F11/12 AIL mice to refine QTLs controlling the severity and onset of arthritis as well as the Ab response and T cell subset in CIA, namely Cia2, Cia27, and Trmq3. These QTLs were originally identified in (DBA/1 x FVB/N)F2 progeny. The confidence intervals of the three QTLs were refined from 40, 43, and 48 Mb to 12, 4.1, and 12 Mb, respectively. The data were complemented by the use of another QTL fine-mapping approach, haplotype analysis, to further refine Cia2 into a 2-Mb genomic region. To aid in the search for candidate genes for the QTLs, genome-wide expression profiling was performed to identify strain-specific differentially expressed genes within the confidence intervals. Of the 1396 strain-specific differentially expressed genes, 3, 3, and 12 genes were within the support intervals of the Cia2, Cia27, and Trmq3, respectively. In addition, this study revealed that Cia27 and Trmq3 controlling anti-CII IgG2a Ab and CD4:CD8 T cell ratio, respectively, also regulated CIA clinical phenotypes.

    Journal of immunology (Baltimore, Md. : 1950) 2006;177;10;7042-9

  • BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system.

    Magdaleno S, Jensen P, Brumwell CL, Seal A, Lehman K, Asbury A, Cheung T, Cornelius T, Batten DM, Eden C, Norland SM, Rice DS, Dosooye N, Shakya S, Mehta P and Curran T

    Department of Developmental Neurobiology, St. Jude Children's Research Hospital, Memphis, Tennessee, United States.

    Funded by: NINDS NIH HHS: 5R37NS036558, N01-NS-0-2331, R37 NS036558

    PLoS biology 2006;4;4;e86

  • Stomatin modulates gating of acid-sensing ion channels.

    Price MP, Thompson RJ, Eshcol JO, Wemmie JA and Benson CJ

    Department of Internal Medicine, University of Iowa College of Medicine, 200 Hawkins Dr., Iowa City, IA 52242, USA.

    Acid-sensing ion channels (ASICs) are H(+)-gated members of the degenerin/epithelial Na(+) channel (DEG/ENaC) family in vertebrate neurons. Several ASICs are expressed in sensory neurons, where they play a role in responses to nociceptive, taste, and mechanical stimuli; others are expressed in central neurons, where they participate in synaptic plasticity and some forms of learning. Stomatin is an integral membrane protein found in lipid/protein-rich microdomains, and it is believed to regulate the function of ion channels and transporters. In Caenorhabditis elegans, stomatin homologs interact with DEG/ENaC channels, which together are necessary for normal mechanosensation in the worm. Therefore, we asked whether stomatin interacts with and modulates the function of ASICs. We found that stomatin co-immunoprecipitated and co-localized with ASIC proteins in heterologous cells. Moreover, stomatin altered the function of ASIC channels. Stomatin potently reduced acid-evoked currents generated by ASIC3 without changing steady state protein levels or the amount of ASIC3 expressed at the cell surface. In contrast, stomatin accelerated the desensitization rate of ASIC2 and heteromeric ASICs, whereas current amplitude was unaffected. These data suggest that stomatin binds to and alters the gating of ASICs. Our findings indicate that modulation of DEG/ENaC channels by stomatin-like proteins is evolutionarily conserved and may have important implications for mammalian nociception and mechanosensation.

    Funded by: NHLBI NIH HHS: HL04349

    The Journal of biological chemistry 2004;279;51;53886-91

  • Gene discovery by microarray: identification of novel genes induced during growth factor-mediated muscle cell survival and differentiation.

    Kuninger D, Kuzmickas R, Peng B, Pintar JE and Rotwein P

    Molecular Medicine Division, HRC 3, Department of Medicine, Oregon Health & Sciences University, Portland, OR 97239-3098, USA.

    Peptide growth factors regulate cell fate by activating distinct signal transduction pathways that ultimately influence gene expression. Insulin-like growth factors (IGFs) play central roles in controlling somatic growth and participate in skeletal muscle development and regeneration. In cultured muscle cells, IGF action is critical both for maintaining viability during the transition from proliferating to differentiating myoblasts and for facilitating differentiation. By contrast, platelet-derived growth factor (PDGF) can sustain cell survival but inhibits differentiation. Here we examine the genetic programs that accompany IGF and PDGF action in myoblasts. Through analysis of high-density oligonucleotide arrays containing approximately 36,000 mouse probe sets, we identify 90 transcripts differentially induced by IGF-I, including 28 muscle-specific genes and 33 previously unannotated mRNAs, and 55 transcripts specifically stimulated by PDGF, including 14 unknowns. Detailed study of one IGF-induced mRNA shows that it encodes a protein related to a recently characterized repulsive guidance molecule postulated to regulate neuronal targeting during development. Our results demonstrate the power of transcriptional profiling for gene discovery and provide opportunities for investigating new proteins potentially involved in different aspects of growth factor action in muscle.

    Funded by: NIDA NIH HHS: R01-DA15237; NIDDK NIH HHS: 5R01-DK42748, R01 DK042748, T32 DK007674; NINDS NIH HHS: R01-NS21970

    Genomics 2004;84;5;876-89

  • Stomatin immunoreactivity in ciliated cells of the human airway epithelium.

    Fricke B, Stewart GW, Treharne KJ, Mehta A, Knöpfle G, Friedrichs N, Müller KM and von Düring M

    Department of Neuroanatomy, Institute of Anatomy MA 6/152, Ruhr University, Universitaetsstrasse 150, 44801 Bochum, Germany. britta.fricke@ruhr-uni-bochum.de

    Stomatin is a widely distributed 32kD membrane protein of unknown function. In biochemical studies it is associated with cholesterol+sphingomyelin-rich 'rafts' in the cytomembrane. Genetic studies in C. elegans, supported by microscopic studies in mammalian tissue and co-expression studies in oocytes, suggest a functional link with the DEG/ENaC (degenerin/epithelial Na+ channel) superfamily of monovalent ion channels. Since ENaC channels play a prominent role in the physiology of the respiratory epithelium, we have studied the immunolocalization of stomatin in mature and developing human airway epithelium by means of Western blot analysis, immunocytochemistry, and immunoelectron microscopy. Stomatin immunoreactivity (stomatin-IR) was found in the ciliated cells of the conductive airway epithelium in a distinct distribution pattern with the strongest signal along the cilia. Immunogold labelling revealed immunogold particles at the basal bodies, along the cilia, and at the membrane of the microvilli. The presence of stomatin-IR paralleled the stages of ciliogenesis in airway development, and its appearance preceded the elongation of the axoneme and the cilial outgrowth. Due to its presence in the different cellular locations in the ciliated cell, we suggest that stomatin is involved in various cellular functions. From its ultrastructural position, stomatin could be a candidate for a membrane-associated mechanotransducer with a role in the control of ciliary motility. Stomatin as a raft protein might be a microtubule associated protein moving along the outer surface of the microtubules to its terminal site of action in the cilia. Stomatin-IR in microvilli supports the hypothesis of a co-localization with beta- and gamma- ENaC and, in conclusion, their potential functional interaction to control the composition of periciliary mucus electrolytes.

    Anatomy and embryology 2003;207;1;1-7

  • Overexpression of stomatin depresses GLUT-1 glucose transporter activity.

    Zhang JZ, Abbud W, Prohaska R and Ismail-Beigi F

    Department of Medicine, Case Western Reserve University, Cleveland, Ohio 44106-4951, USA.

    We showed previously that GLUT-1 glucose transporter is associated with stomatin (band 7.2b) in human red blood cell membranes and in Clone 9 cells. We show here that in a mixed population of stably transfected cells, overexpression of either murine or human stomatin resulted in 35-50% reduction in the basal rate of glucose transport. Moreover, there was a correlation between increased expression of stomatin and depression in the rate of glucose transport. In two clones chosen for further study, the ~10% and ~70% reduction in basal rate of glucose transport was associated with increases in stomatin mRNA and protein expression without a detectable change in GLUT-1 content in plasma membranes of either clone. In the clone overexpressing high levels of stomatin, immunoprecipitated GLUT-1 was associated with a large amount of stomatin as a coimmunoprecipitant. Employing extracts of cells overexpressing human stomatin, we found that stomatin bound to the glutathione-S-transferase (GST) fusion protein containing the COOH-terminal 42-amino acid segment of GLUT-1 but not to GST alone or a GST fusion protein containing the 66-amino acid central loop of GLUT-1. Rat stomatin cDNA was cloned by RT-PCR and found to be highly homologous to mouse (97%) and human (86%) stomatins. These results suggest that overexpression of stomatin results in a depression in the basal rate of glucose transport by decreasing the "intrinsic" activity of GLUT-1, probably through protein-protein interaction.

    Funded by: NIDDK NIH HHS: DK-45945

    American journal of physiology. Cell physiology 2001;280;5;C1277-83

  • Stomatin, a MEC-2 like protein, is expressed by mammalian sensory neurons.

    Mannsfeldt AG, Carroll P, Stucky CL and Lewin GR

    Growth Factor and Regeneration Group, Max Delbrück Center for Molecular Medicine, Berlin-Buch, 13122, Germany.

    The molecular mechanism whereby vertebrate primary sensory neurons convert mechanical energy at their receptive fields into action potentials is unknown. In recent years, genetic screens for touch insensitive mutants of the nematode worm Caenorhabditis elegans have led to the identification of several genes required for mechanical sensitivity. A model has been proposed in which a mechanically gated ion channel is connected both to the extracellular matrix and to the cytoskeleton. Displacement of the membrane is proposed to produce a shearing force that pulls the channel open. MEC-2 is thought to play an important role in this complex by linking the ion channel to the cytoskeleton. MEC-2 is highly homologous to a vertebrate protein called stomatin. Stomatin was first isolated from erythrocytes where it is a major integral membrane protein. To date, however, no data on neuronal expression of stomatin in the peripheral nervous system (PNS) or central nervous system (CNS) is available. Here, we have used RT-PCR, in situ hybridization, Northern blotting, and immunocytochemistry to demonstrate that stomatin is expressed by all sensory neurons in mouse dorsal root ganglia. Indirect immunofluorescence together with transfection of cultured adult sensory neurons with epitope-tagged stomatin show that stomatin is localized in spots on somatic and axonal membranes. During development, stomatin begins to be expressed by sensory neurons only as target innervation occurs. The onset of expression of stomatin thus coincides with the onset of functional mechanical sensitivity. Together, our data suggest that stomatin, like the C. elegans MEC-2 gene, is expressed in an appropriate temporal and spatial manner to participate in a putative vertebrate mechanotransduction complex.

    Molecular and cellular neurosciences 1999;13;6;391-404

  • Stomatocytosis is absent in "stomatin"-deficient murine red blood cells.

    Zhu Y, Paszty C, Turetsky T, Tsai S, Kuypers FA, Lee G, Cooper P, Gallagher PG, Stevens ME, Rubin E, Mohandas N and Mentzer WC

    Department of Pediatrics, University of California San Francisco, San Francisco, CA, USA.

    To examine the relationship between erythrocyte membrane protein 7. 2b deficiency and the hemolytic anemia of human hereditary stomatocytosis, we created 7.2b knock-out mice by standard gene targeting approaches. Immunoblots showed that homozygous knock-out mice completely lacked erythrocyte protein 7.2b. Despite the absence of protein 7.2b, there was no hemolytic anemia and mouse red blood cells (RBCs) were normal in morphology, cell indices, hydration status, monovalent cation content, and ability to translocate lipids. The absence of the phenotype of hereditary stomatocytosis implies that protein 7.2b deficiency plays no direct role in the etiology of this disorder and casts doubt on the previously proposed role of this protein as a mediator of cation transport in RBC.

    Funded by: NHLBI NIH HHS: HL 31579; NIDDK NIH HHS: DK 26263, DK 32094; ...

    Blood 1999;93;7;2404-10

  • Cloning and analysis of a cDNA encoding the BALB/c murine erythrocyte band 7 integral membrane protein.

    Schlegel W, Unfried I and Prohaska R

    Institute of Biochemistry, University of Vienna, Austria.

    cDNA clones encoding the BALB/c murine erythrocyte band 7 integral membrane protein (also termed protein 7.2b, or 'stomatin') were isolated by the screening of a corresponding bone-marrow lambda gt11 cDNA library with a human cDNA probe, and by 5'-RACE PCR cloning. Comparison of the murine, human and Caenorhabditis elegans protein 7.2b amino acid (aa) sequences revealed overall identities of 88% (human) and 61% (C. elegans), with the N-terminal domains showing only little similarity. The 7.2b protein sequences of the two mouse strains, BALB/c and C57BL/6J (B6), showed six rather conservative aa substitutions, three of them in the hydrophobic domain. The BALB/c murine mRNA, about 3.5 kb in size, is widely expressed in various tissues, most notably in spleen, lung and testis.

    Gene 1996;178;1-2;115-8

  • Genomic organization and 5'-flanking DNA sequence of the murine stomatin gene (Epb72).

    Gallagher PG, Turetsky T and Mentzer WC

    Department of Pediatrics, Yale University School of Medicine, New Haven, Connecticut, 06520-8064, USA.

    Stomatin is a poorly understood integral membrane protein that is absent from the erythrocyte membranes of many patients with hereditary stomatocytosis. This report describes the cloning of the murine stomatin chromosomal gene, determination of its genomic structure, and characterization of the 5'-flanking genomic DNA sequences. The stomatin gene is encoded by seven exons spread over approximately 25 kb of genomic DNA. There is no concordance between the exon structure of the stomatin gene and the locations of three domains predicted on the basis of protein structure. Inspection of the 5'-flanking DNA sequences reveals features of a TATA-less housekeeping gene promoter and consensus sequences for a number of potential DNA-binding proteins.

    Genomics 1996;34;3;410-2

  • cDNA structure, tissue-specific expression, and chromosomal localization of the murine band 7.2b gene.

    Gallagher PG, Romana M, Lieman JH and Ward DC

    Department of Pediatrics, Yale University School of Medicine, New Haven, CT 06510, USA.

    Band 7.2b is an integral phosphoprotein absent from the erythrocyte membranes of patients with hydrocytosis, an autosomal, dominantly inherited, hemolytic anemia characterized by stomatocytic red blood cells with abnormal permeability to Na+ and K+. The role of this protein in the erythrocyte membrane is not well understood. To gain additional insight into the structure and function of this protein, we have cloned the murine band 7.2b cDNA and studied its tissue-specific expression. 2,873 bp of cDNA with an open reading frame of 852 bp were isolated. This fragment encodes a protein of 284 amino acids with a predicted molecular weight of 31 kD. The band 7.2b gene had a wide pattern of expression, with high levels of mRNA in heart, liver, skeletal muscle, and testis and low levels in lung, brain, and spleen. Using fluorescent in situ hybridization, the murine band 7.2b gene was mapped to chromosome 2, at the border of the distal region of 2B and proximal region of C1, syntenic to 9q33-q34, the location of the human homologue. Models of the predicted protein structure showed a short NH2-terminal head, a strongly hydrophobic 28-amino acid stretch presumably encoding a single membrane-spanning domain, and a large domain composed of beta sheet and alpha helix. Database searching showed no significant homology of other known proteins to murine or human band 7.2b.

    Blood 1995;86;1;359-65

  • Comparative mapping of 50 human chromosome 9 loci in the laboratory mouse.

    Pilz A, Woodward K, Povey S and Abbott C

    Department of Genetics and Biometry, University College London, United Kingdom.

    We have set out to produce a comprehensive comparative map between human chromosome 9 (HSA9) and the laboratory mouse. The mouse homologues of 50 loci that were known to map to HSA9 were mapped by interspecific backcross linkage analysis. Ten loci from the short arm of HSA9 were mapped, and 40 from HSA9q, with 24 markers coming from the HSA9q33-q34 region--a part of the chromosome known to be very gene rich. Fifteen new assignments have been made--Ak3, Ctsl, Cntfr, C8g, D2H9S46E, Eng, Gcnt1, Irebp, Pappa, Ptgds, Snf212, Tal2, Tmod, Vav2, and Vldlr, the human homologues of which all map to HSA9. In addition, the assignment of Snf212 and Vldlr to MMU19 has defined a new region of synteny between the proximal portion of the short arm of HSA9 and the mouse.

    Genomics 1995;25;1;139-49

  • Genetic linkage analysis of the Ak1, Col5a1, Epb7.2, Fpgs, Grp78, Pbx3, and Notch1 genes in the region of mouse chromosome 2 homologous to human chromosome 9q.

    Pilz A, Prohaska R, Peters J and Abbott C

    Department of Genetics and Biometry, University College London, United Kingdom.

    The genes for adenylate kinase-1 (AK1), folyl polyglutamate synthetase (FPGS), the collagen pro alpha 1(V) chain (COL5A1), erythrocyte protein band 7.2b (EPB72), and a proto-oncogene homeobox (PBX3) all map to the distal portion of human chromosome 9q (HSA9q) but have not previously been mapped by linking analysis in the mouse. In this study, we have used two interspecific backcrosses to map the mouse homologues of each of these genes to mouse chromosome 2 (MMU2). The Ak1, Col5a1, Epb7.2, Fpgs, and Pbx3 genes were mapped with respect to the genes for Grp78, Rxra, Notch1 (the mouse homologue of TAN1), Spna2, Abl, and Hc (the mouse homologue of C5), all of which have previously been mapped by linkage analysis on MMU2 and have human homologues that map to HSA9q. Two of the reference loci for MMU2, D2Mit1 and Acra, were also mapped in the same cross to facilitate comparisons with existing maps. The consensus gene order deduced by combining data from both crosses is D2Mit1-(Dbh,Notch1)-(Col5a1,Rxra)-Spna2-Ab l-(Ak1,Fpgs)- (Grp78,Pbx3)-(Epb7.2,Hc,Gsn)-Acra. These loci therefore form part of the conserved synteny between HSA9q and MMU2.

    Funded by: NCRR NIH HHS: 2S07RR056545

    Genomics 1994;21;1;104-9

  • Maps from two interspecific backcross DNA panels available as a community genetic mapping resource.

    Rowe LB, Nadeau JH, Turner R, Frankel WN, Letts VA, Eppig JT, Ko MS, Thurston SJ and Birkenmeier EH

    Jackson Laboratory, Bar Harbor, Maine 04609.

    We established two mouse interspecific backcross DNA panels, one containing 94 N2 animals from the cross (C57BL/6J x Mus spretus)F1 x C57BL/6J, and another from 94 N2 animals from the reciprocal backcross (C57BL/6J x SPRET/Ei)F1 x SPRET/Ei. We prepared large quantities of DNA from most tissues of each animal to create a community resource of interspecific backcross DNA for use by laboratories interested in mapping loci in the mouse. Initial characterization of the genetic maps of both panels has been completed. We used MIT SSLP markers, proviral loci, and several other sequence-defined genes to anchor our maps to other published maps. The BSB panel map (from the backcross to C57BL/6J) contains 215 loci and is anchored by 45 SSLP and 32 gene sequence loci. The BSS panel map (from the backcross to SPRET/Ei) contains 451 loci and is anchored by 49 SSLP loci, 43 proviral loci, and 60 gene sequence loci. To obtain a high density of markers, we used motif-primed PCR to "fingerprint" the panel DNAs. We constructed two maps, each representing one of the two panels. All new loci can be located with a high degree of certainty on the maps at current marker density. Segregation patterns in these data reveal several examples of transmission ratio distortion and permit analysis of the distribution of crossovers on individual chromosomes.

    Funded by: NCRR NIH HHS: 2S07RR056545; NHGRI NIH HHS: HG00189, HG00941

    Mammalian genome : official journal of the International Mammalian Genome Society 1994;5;5;253-74

Gene lists (2)

Gene List Source Species Name Description Gene count
L00000060 G2C Mus musculus BAYES-COLLINS-HUMAN-PSD-CONSENSUS Human cortex PSD consensus (ortho) 748
L00000070 G2C Mus musculus BAYES-COLLINS-HUMAN-PSD-FULL Human cortex biopsy PSD full list (ortho) 1461
© G2C 2014. The Genes to Cognition Programme received funding from The Wellcome Trust and the EU FP7 Framework Programmes:
EUROSPIN (FP7-HEALTH-241498), SynSys (FP7-HEALTH-242167) and GENCODYS (FP7-HEALTH-241995).

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