G2Cdb::Gene report

Gene id
G00001331
Gene symbol
CACNB1 (HGNC)
Species
Homo sapiens
Description
calcium channel, voltage-dependent, beta 1 subunit
Orthologue
G00000082 (Mus musculus)

Databases (7)

Gene
ENSG00000067191 (Ensembl human gene)
782 (Entrez Gene)
422 (G2Cdb plasticity & disease)
CACNB1 (GeneCards)
Literature
114207 (OMIM)
Marker Symbol
HGNC:1401 (HGNC)
Protein Sequence
Q02641 (UniProt)

Literature (18)

Pubmed - other

  • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

    Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P and Mann M

    Center for Experimental BioInformatics, Department of Biochemistry and Molecular Biology, University of Southern Denmark, DK-5230 Odense, Denmark.

    Cell signaling mechanisms often transmit information via posttranslational protein modifications, most importantly reversible protein phosphorylation. Here we develop and apply a general mass spectrometric technology for identification and quantitation of phosphorylation sites as a function of stimulus, time, and subcellular location. We have detected 6,600 phosphorylation sites on 2,244 proteins and have determined their temporal dynamics after stimulating HeLa cells with epidermal growth factor (EGF) and recorded them in the Phosida database. Fourteen percent of phosphorylation sites are modulated at least 2-fold by EGF, and these were classified by their temporal profiles. Surprisingly, a majority of proteins contain multiple phosphorylation sites showing different kinetics, suggesting that they serve as platforms for integrating signals. In addition to protein kinase cascades, the targets of reversible phosphorylation include ubiquitin ligases, guanine nucleotide exchange factors, and at least 46 different transcriptional regulators. The dynamic phosphoproteome provides a missing link in a global, integrative view of cellular regulation.

    Cell 2006;127;3;635-48

  • A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration.

    Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M and Zoghbi HY

    Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA.

    Many human inherited neurodegenerative disorders are characterized by loss of balance due to cerebellar Purkinje cell (PC) degeneration. Although the disease-causing mutations have been identified for a number of these disorders, the normal functions of the proteins involved remain, in many cases, unknown. To gain insight into the function of proteins involved in PC degeneration, we developed an interaction network for 54 proteins involved in 23 inherited ataxias and expanded the network by incorporating literature-curated and evolutionarily conserved interactions. We identified 770 mostly novel protein-protein interactions using a stringent yeast two-hybrid screen; of 75 pairs tested, 83% of the interactions were verified in mammalian cells. Many ataxia-causing proteins share interacting partners, a subset of which have been found to modify neurodegeneration in animal models. This interactome thus provides a tool for understanding pathogenic mechanisms common for this class of neurodegenerative disorders and for identifying candidate genes for inherited ataxias.

    Funded by: NICHD NIH HHS: HD24064; NINDS NIH HHS: NS27699

    Cell 2006;125;4;801-14

  • Molecular heterogeneity of calcium channel beta-subunits in canine and human heart: evidence for differential subcellular localization.

    Foell JD, Balijepalli RC, Delisle BP, Yunker AM, Robia SL, Walker JW, McEnery MW, January CT and Kamp TJ

    Department of Medicine, University of Wisconsin, Madison 53792, USA.

    Multiple Ca2+ channel beta-subunit (Ca(v)beta) isoforms are known to differentially regulate the functional properties and membrane trafficking of high-voltage-activated Ca2+ channels, but the precise isoform expression pattern of Ca(v)beta subunits in ventricular muscle has not been fully characterized. Using sequence data from the Human Genome Project to define the intron/exon structure of the four known Ca(v)beta genes, we designed a systematic RT-PCR strategy to screen human and canine left ventricular myocardial samples for all known Ca(v)beta isoforms. A total of 18 different Ca(v)beta isoforms were detected in both canine and human ventricles including splice variants from all four Ca(v)beta genes. Six of these isoforms have not previously been described. Western blots of ventricular membrane fractions and immunocytochemistry demonstrated that all four Ca(v)beta subunit genes are expressed at the protein level, and the Ca(v)beta subunits show differential subcellular localization with Ca(v)beta1b, Ca(v)beta2, and Ca(v)beta3 predominantly localized to the T-tubule sarcolemma, whereas Ca(v)beta1a and Ca(v)beta4 are more prevalent in the surface sarcolemma. Coexpression of the novel Ca(v)beta2c subunits (Ca(v)beta(2cN1), Ca(v)beta(2cN2), Ca(v)beta(2cN4)) with the pore-forming alpha1C (Ca(v)1.2) and Ca(v)alpha2delta subunits in HEK 293 cells resulted in a marked increase in ionic current and Ca(v)beta2c isoform-specific modulation of voltage-dependent activation. These results demonstrate a previously unappreciated heterogeneity of Ca(v)beta subunit isoforms in ventricular myocytes and suggest the presence of different subcellular populations of Ca2+ channels with distinct functional properties.

    Funded by: NHLBI NIH HHS: F32-HL-071476, P01-HL-47053, R01-HL-60723, R01-HL-61537

    Physiological genomics 2004;17;2;183-200

  • Proteomic identification of brain proteins that interact with dynein light chain LC8.

    Navarro-Lérida I, Martínez Moreno M, Roncal F, Gavilanes F, Albar JP and Rodríguez-Crespo I

    Departamento de Bioquímicay Biología Molecular, Facultad de Ciencias Químicas, Universidad Complutense de Madrid, Madrid, Spain. nacho@bbml.ucm.es

    Cytoplasmic dynein is a large minus end-directed microtubule motor that translocates cargos towards the minus end of microtubules. Light chain 8 of the dynein machinery (LC8) has been reported to interact with a large variety of proteins that possess K/RSTQT or GIQVD motifs in their sequence, hence permitting their transport in a retrograde manner. Yeast two-hybrid analysis has revealed that in brain, LC8 associates directly with several proteins such as neuronal nitric oxide synthase, guanylate kinase domain-associated protein and gephyrin. In this work, we report the identification of over 40 polypeptides, by means of a proteomic approach, that interact with LC8 either directly or indirectly. Many of the neuronal proteins that we identified cluster at the post-synaptic terminal, and some of them such as phosphofructokinase, lactate dehydrogenase or aldolase are directly involved in glutamate metabolism. Other pool of proteins identified displayed the LC8 consensus binding motif. Finally, recombinant LC8 was produced and a library of overlapping dodecapeptides (pepscan) was employed to map the LC8 binding site of some of the proteins that were previously identified using the proteomic approach, hence confirming binding to the consensus binding sites.

    Proteomics 2004;4;2;339-46

  • Regulation of voltage-gated calcium channel activity by the Rem and Rad GTPases.

    Finlin BS, Crump SM, Satin J and Andres DA

    Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, Lexington, KY 40536-0298, USA.

    Rem, Rem2, Rad, and Gem/Kir (RGK) represent a distinct GTPase family with largely unknown physiological functions. We report here that both Rem and Rad bind directly to Ca2+ channel beta-subunits (CaV beta) in vivo. No calcium currents are recorded from human embryonic kidney 293 cells coexpressing the L type Ca2+ channel subunits CaV1.2, CaV beta 2a, and Rem or Rad, but CaV1.2 and CaV beta 2a transfected cells elicit Ca2+ channel currents in the absence of these small G proteins. Importantly, CaV3 (T type) Ca2+ channels, which do not require accessory subunits for ionic current expression, are not inhibited by expression of Rem. Rem is expressed in primary skeletal myoblasts and, when overexpressed in C2C12 myoblasts, wild-type Rem inhibits L type Ca2+ channel activity. Deletion analysis demonstrates a critical role for the Rem C terminus in both regulation of functional Ca2+ channel expression and beta-subunit association. These results suggest that all members of the RGK GTPase family, via direct interaction with auxiliary beta-subunits, serve as regulators of L type Ca2+ channel activity. Thus, the RGK GTPase family may provide a mechanism for achieving cross talk between Ras-related GTPases and electrical signaling pathways.

    Funded by: NHLBI NIH HHS: HL072936, HL63416, HL74091, R01 HL063416, R01 HL072936, R01 HL074091, R56 HL074091

    Proceedings of the National Academy of Sciences of the United States of America 2003;100;24;14469-74

  • Structure and alternative splicing of the gene encoding the human beta1 subunit of voltage dependent calcium channels.

    Hogan K, Greg RG and Powers PA

    Department of Anesthesiology, University of Wisconsin, Madison 53792, USA. khogan@facstaff.wisc.edu

    The structure of the gene encoding the human brain beta1 subunit of voltage dependent calcium channels (CACNB1) was determined by comparison of its genomic sequence with beta1 cDNA sequence. CACNB1 is distributed over 25 kb and contains 13 exons. Alternative splicing of CACNB1 RNA occurs within the central domain at exon 7, and the 3' domain at exon 13, producing the variably expressed beta1a, beta1b and beta1c isoforms. Exon/intron boundaries and exon lengths are conserved for the nine exons shared by the beta1 and related brain beta3 and beta4 genes.

    Neuroscience letters 1999;277;2;111-4

  • Differential plasma membrane targeting of voltage-dependent calcium channel subunits expressed in a polarized epithelial cell line.

    Brice NL and Dolphin AC

    Department of Pharmacology, University College London, Gower Street, London WC1E 6BT, UK.

    1. Voltage-dependent calcium channels (VDCCs) show a highly non-uniform distribution in many cell types, including neurons and other polarized secretory cells. We have examined whether this can be mimicked in a polarized epithelial cell line (Madin-Darby canine kidney), which has been used extensively to study the targeting of proteins. 2. We expressed the VDCC alpha1A, alpha1B or alpha1C subunits either alone or in combination with accessory subunits alpha2-delta and the different beta subunits, and examined their localization immunocytochemically. An alpha1 subunit was only targeted to the plasma membrane if co-expressed with the accessory subunits. 3. The combination alpha1C/alpha2-delta and all beta subunits was always localized predominantly to the basolateral membrane. It has been suggested that this is equivalent to somatodendritic targeting in neurons. 4. In contrast, the alpha1B subunit was expressed at the apical membrane with all the accessory subunit combinations, by 24 h after microinjection. This membrane destination shows some parallels with axonal targeting in neurons. 5. The alpha1A subunit was consistently observed at the apical membrane in the combinations alpha1A/alpha2-delta/beta1b or beta4. In contrast, when co-expressed with alpha2-delta/beta2a, alpha1A was clearly targeted to the basolateral membrane. 6. In conclusion, the VDCC alpha1 subunit appears to be the primary determinant for targeting the VDCC complex, but the beta subunit can modify this destination, particularly for alpha1A.

    Funded by: Wellcome Trust

    The Journal of physiology 1999;515 ( Pt 3);685-94

  • Distribution of voltage-dependent calcium channel beta subunits in the hippocampus of patients with temporal lobe epilepsy.

    Lie AA, Blümcke I, Volsen SG, Wiestler OD, Elger CE and Beck H

    Department of Epileptology, University of Bonn Medical Center, Germany.

    Voltage-dependent Ca2+ channels constitute a major class of plasma membrane channels through which a significant amount of extracellular Ca2+ enters neuronal cells. Their pore-forming alpha1 subunits are associated with cytoplasmic regulatory beta subunits, which modify the distinct biophysical and pharmacological properties of the alpha1 subunits. Studies in animal models indicate altered expression of alpha1 and/or beta subunits in epilepsy. We have focused on the regulatory beta subunits and have analysed the immunoreactivity patterns of the beta1, beta2, beta3 and beta4 subunits in the hippocampus of patients with temporal lobe epilepsy (n = 18) compared to control specimens (n = 2). Temporal lobe epilepsy specimens were classified as Ammon's horn sclerosis (n = 9) or focal lesions without alteration of hippocampal cytoarchitecture (n = 9). Immunoreactivity for the beta subunits was observed in neuronal cell bodies, dendrites and neuropil. The beta1, beta2 and beta3 subunits were found mainly in cell bodies while the beta4 subunit was primarily localized to dendrites. Compared to the control specimens, epilepsy specimens of the Ammon's horn sclerosis and of the lesion group showed a similar beta subunit distribution, except for beta1 and beta2 staining in the Ammon's horn sclerosis group: in the severely sclerotic hippocampal subfields of these specimens, beta1 and beta2 immunoreactivity was enhanced in some of the remaining neuronal cell bodies and, in addition, strongly marked dendrites. Thus, hippocampal neurons apparently express multiple classes of beta subunits which segregate into particular subcellular domains. In addition, the enhancement of beta1 and beta2 immunoreactivity in neuronal cell bodies and the additional shift of the beta1 and beta2 subunits into the dendritic compartment in severely sclerotic hippocampal regions indicate specific changes in Ammon's horn sclerosis. Altered expression of these beta subunits may lead to increased currents carried by voltage-dependent calcium channels and to enhanced synaptic excitability.

    Neuroscience 1999;93;2;449-56

  • Absence of the beta subunit (cchb1) of the skeletal muscle dihydropyridine receptor alters expression of the alpha 1 subunit and eliminates excitation-contraction coupling.

    Gregg RG, Messing A, Strube C, Beurg M, Moss R, Behan M, Sukhareva M, Haynes S, Powell JA, Coronado R and Powers PA

    Waisman Center, University of Wisconsin, Madison 53705, USA. gregg@waisman.wisc.edu

    The multisubunit (alpha 1s, alpha 2/delta, beta 1, and gamma) skeletal muscle dihydropyridine receptor transduces transverse tubule membrane depolarization into release of Ca2+ from the sarcoplasmic reticulum, and also acts as an L-type Ca2+ channel. The alpha 1s subunit contains the voltage sensor and channel pore, the kinetics of which are modified by the other subunits. To determine the role of the beta 1 subunit in channel activity and excitation-contraction coupling we have used gene targeting to inactivate the beta 1 gene. beta 1-null mice die at birth from asphyxia. Electrical stimulation of beta 1-null muscle fails to induce twitches, however, contractures are induced by caffeine. In isolated beta 1-null myotubes, action potentials are normal, but fail to elicit a Ca2+ transient. L-type Ca2+ current is decreased 10- to 20-fold in the beta 1-null cells compared with littermate controls. Immunohistochemistry of cultured myotubes shows that not only is the beta 1 subunit absent, but the amount of alpha 1s in the membrane also is undetectable. In contrast, the beta 1 subunit is localized appropriately in dysgenic, mdg/mdg, (alpha 1s-null) cells. Therefore, the beta 1 subunit may not only play an important role in the transport/insertion of the alpha 1s subunit into the membrane, but may be vital for the targeting of the muscle dihydropyridine receptor complex to the transverse tubule/sarcoplasmic reticulum junction.

    Proceedings of the National Academy of Sciences of the United States of America 1996;93;24;13961-6

  • Cyclic AMP-dependent modulation of N- and Q-type Ca2+ channels expressed in Xenopus oocytes.

    Fukuda K, Kaneko S, Yada N, Kikuwaka M, Akaike A and Satoh M

    Department of Pharmacology, Faculty of Pharmaceutical Sciences, Kyoto University, Japan.

    Xenopus oocytes were used for investigating the cAMP-dependent modulation of N- and Q-type Ca2+ channels. Treatments to increase intracellular cAMP concentration with forskolin (FK) and 3-isobutyl-1-methylxanthine (IBMX) markedly potentiated Q-type Ca2+ channel current in oocytes coexpressing alpha 1A and beta subunits, and the enhancement was reversed by protein kinase A inhibitors. Moderate enhancement was observed by FK+IBMX in N-type channel current, of which potentiation was equivalent to that of endogenous Ca2+ channel current being activated by exogenously-expressed beta subunits. No potentiation was observed in the oocyte-native Ca2+ channel current. These results suggest that Q-type Ca2+ channels are more susceptible to the protein kinase A-mediated facilitation than N-type channels. A significant role of Ca2+ channel beta subunits for the cAMP-dependent positive modulation was also suggested.

    Neuroscience letters 1996;217;1;13-6

  • Genetic mapping of the beta 1- and gamma-subunits of the human skeletal muscle L-type voltage-dependent calcium channel on chromosome 17q and exclusion as candidate genes for malignant hyperthermia susceptibility.

    Iles DE, Segers B, Sengers RC, Monsieurs K, Heytens L, Halsall PJ, Hopkins PM, Ellis FR, Hall-Curran JL, Stewart AD et al.

    Department of Cell Biology and Histology, Faculty of Medical Sciences, Catholic University of Nijmegen, The Netherlands.

    Malignant hyperthermia susceptibility (MHS) is an autosomal dominant disorder of skeletal muscle which manifests as a life-threatening hypermetabolic crisis triggered by commonly-used inhalation anaesthetics and depolarizing muscle relaxants. Defects in the ryanodine receptor (RYR1) protein have been proposed to underly MHS, but significant genetic heterogeneity in MHS has recently been demonstrated. In order to investigate the potential roles played by other skeletal muscle calcium channels in MHS, we isolated cosmids containing the gene encoding the beta 1-subunit of skeletal muscle L-type voltage-dependent calcium channel (CACNLB1). We identified a new, highly polymorphic dinucleotide repeat motif close to this gene, and linkage analysis placed the marker proximal to the HOX2B locus, previously localized to chromosome segment 17q21-q22. We recently identified a novel marker within the gamma-subunit locus (CACNLG) at band 17q24, and since both markers are within the 17q11.2-q24 region reported to contain the MHS2 locus, we tested them for linkage in MHS families whose disease trait has been shown not to co-segregate with markers for the RYR1 region on chromosome 19q13.1. Our results exclude CACNLB1 and CACNLG as candidate genes for MHS2, and do not support the reported chromosome 17q localization for the MHS2 locus in our families.

    Human molecular genetics 1993;2;7;863-8

  • Molecular cloning of three isoforms of the L-type voltage-dependent calcium channel beta subunit from normal human heart.

    Collin T, Wang JJ, Nargeot J and Schwartz A

    Department of Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine, OH 45267-0575.

    We have cloned and sequenced cDNAs for three isoforms of the L-type voltage-dependent calcium channel beta subunit isolated from a normal human heart cDNA library. One of these subunits, designated beta a, hybridized with a 3.4-kb message, and the other two, designated beta b and beta c, hybridized with a message of approximately 1.9 kb. The presence of both of these latter two messages in human heart was confirmed by polymerase chain reaction methodology. Considering the differences between beta a and beta b/beta c, we find it likely that these messages may be encoded by two different gene sequences, beta a and beta b/beta c, and that the beta b/beta c sequence can be alternatively spliced in the 209-260 region. The data suggest that the human heart presents a different pattern of beta subunit expression from that found in the rat and rabbit heart.

    Funded by: NHLBI NIH HHS: 5R37 HL-43231-03, P01 HL-22619-15, T32 HL-07382-16

    Circulation research 1993;72;6;1337-44

  • Assignment of the human gene for the beta subunit of the voltage-dependent calcium channel (CACNLB1) to chromosome 17 using somatic cell hybrids and linkage mapping.

    Gregg RG, Powers PA and Hogan K

    Department of Pediatrics, University of Wisconsin, Madison 53705.

    A human clone containing a portion of the gene encoding several isoforms of the beta 1 subunit of voltage-dependent calcium channels was isolated and partially sequenced. The gene was mapped to chromosome 17 using the polymerase chain reaction with oligonucleotides that allowed the specific amplification of the human sequence in the human-rodent hybrids. A polymorphic dinucleotide repeat was identified within the gene and typed on a subset of the CEPH families. Using multipoint linkage analysis the most likely location of the beta 1 subunit gene is between D17S36 and NGFR on chromosome 17q11.2-q22.

    Genomics 1993;15;1;185-7

  • Skeletal muscle and brain isoforms of a beta-subunit of human voltage-dependent calcium channels are encoded by a single gene.

    Powers PA, Liu S, Hogan K and Gregg RG

    Department of Anesthesiology, University of Wisconsin, Madison 53705.

    Clones of the beta 1-subunit of the voltage-dependent calcium channel (VDCC) from human skeletal muscle and hippocampus cDNA libraries, and from human genomic libraries, were isolated using a human skeletal muscle beta 1 cDNA probe generated by polymerase chain reaction. The skeletal muscle beta 1 cDNA (beta 1M) encodes a protein of 523 amino acids that is 97% identical to the rabbit skeletal muscle beta-subunit. Two different cDNAs, beta 1B1 and beta 1B2, were obtained from the human hippocampus library. The beta 1B1 transcript encodes a protein of 478 amino acids that is identical to the skeletal muscle beta-subunit (beta 1M), except for an internal region of 52 amino acids. The beta 1B2 transcript encodes a protein of 596 amino acids. The beta 1B2 polypeptide is identical to the beta 1B1 polypeptide at amino acids 1-444; however, it has a unique 152 amino acid carboxyl terminus. Like beta 1B1, it differs from beta 1M at the internal 52 amino acids. Analysis of the beta 1 gene structure demonstrates that these three cDNAs represent transcripts encoded by a single beta 1 gene. Transcripts from the beta 1 gene were detected in RNA from skeletal muscle, heart, spleen, and brain, but not in RNA from liver, stomach, or kidney.

    The Journal of biological chemistry 1992;267;32;22967-72

  • Cloning and expression of a cardiac/brain beta subunit of the L-type calcium channel.

    Perez-Reyes E, Castellano A, Kim HS, Bertrand P, Baggstrom E, Lacerda AE, Wei XY and Birnbaumer L

    Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, Texas 77030.

    The skeletal muscle dihydropyridine receptor/Ca2+ channel is composed of five protein components (alpha 1, alpha 2 delta, beta, and gamma). Only two such components, alpha 1 and alpha 2, have been identified in heart. The present study reports the cloning and expression of a novel beta gene that is expressed in heart, lung, and brain. Coexpression of this beta with a cardiac alpha 1 in Xenopus oocytes causes the following changes in Ca2+ channel activity: it increases peak currents, accelerates activation kinetics, and shifts the current-voltage relationship toward more hyperpolarized potentials. It also increases dihydropyridine binding to alpha 1 in COS cells. These results indicate that the cardiac L-type Ca2+ channel has a similar subunit structure as in skeletal muscle, and provides evidence for the modulatory role of the beta subunit.

    Funded by: NHLBI NIH HHS: HL-37044

    The Journal of biological chemistry 1992;267;3;1792-7

  • Structure and functional expression of alpha 1, alpha 2, and beta subunits of a novel human neuronal calcium channel subtype.

    Williams ME, Feldman DH, McCue AF, Brenner R, Velicelebi G, Ellis SB and Harpold MM

    Salk Institute Biotechnology/Industrial Associates, Inc., La Jolla, California 92037.

    The primary structures of human neuronal alpha 1, alpha 2, and beta subunits of a voltage-dependent Ca2+ channel were deduced by characterizing cDNAs. The alpha 1 subunit (alpha 1D) directs the recombinant expression of a dihydropyridine-sensitive L-type Ca2+ channel when coexpressed with the beta (beta 2) and the alpha 2 (alpha 2b) subunits in Xenopus oocytes. The recombinant channel is also reversibly blocked by 10-15 microM omega-conotoxin. Expression of the alpha 1D subunit alone, or coexpression with the alpha 2b subunit, did not elicit functional Ca2+ channel activity. Thus, the beta 2 subunit appears to serve an obligatory function, whereas the alpha 2b subunit appears to play an accessory role that potentiates expression of the channel. The primary transcripts encoding the alpha 1D, alpha 2, and beta subunits are differentially processed. At least two forms of neuronal alpha 1D were identified. Different forms of alpha 2 and beta transcripts were also identified in CNS, skeletal muscle, and aorta tissues.

    Neuron 1992;8;1;71-84

  • Cloning and tissue-specific expression of the brain calcium channel beta-subunit.

    Pragnell M, Sakamoto J, Jay SD and Campbell KP

    Howard Hughes Medical Institute, Program in Neuroscience, University of Iowa College of Medicine, Iowa City 52242.

    A cDNA clone encoding a protein with high homology to the beta-subunit of the rabbit skeletal muscle dihydropyridine-sensitive calcium channel was isolated from a rat brain cDNA library. This rat brain beta-subunit cDNA hybridizes to a 3.4 kb message that is expressed in high levels in the cerebral hemispheres and hippocampus but is significantly reduced in cerebellum. The open reading frame encodes 597 amino acids with a predicted mass of 65 679 Da which is 82% homologous with the skeletal muscle beta-subunit. The brain cDNA encodes a unique 153 amino acid C-terminus and predicts the absence of a muscle-specific 50 amino acid internal segment. It also encodes numerous consensus phosphorylation sites suggesting a role in calcium channel regulation. The corresponding human beta-subunit gene was localized to chromosome 17. Hence the encoded brain beta-subunit, which has a primary structure highly similar to its isoform in skeletal muscle, may have a comparable role as an integral regulatory component of a neuronal calcium channel.

    FEBS letters 1991;291;2;253-8

Gene lists (5)

Gene List Source Species Name Description Gene count
L00000009 G2C Homo sapiens Human PSD Human orthologues of mouse PSD adapted from Collins et al (2006) 1080
L00000016 G2C Homo sapiens Human PSP Human orthologues of mouse PSP adapted from Collins et al (2006) 1121
L00000061 G2C Homo sapiens BAYES-COLLINS-MOUSE-PSD-CONSENSUS Mouse cortex PSD consensus (ortho) 984
L00000069 G2C Homo sapiens BAYES-COLLINS-HUMAN-PSD-FULL Human cortex biopsy PSD full list 1461
L00000071 G2C Homo sapiens BAYES-COLLINS-MOUSE-PSD-FULL Mouse cortex PSD full list (ortho) 1556
© 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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