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0CACB1_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCACNB1
DescriptionVoltage-dependent l-type calcium channel beta-1 subunit (cab1) (calcium channel, voltage-dependent, beta 1 subunit).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005891 voltage-gated calcium channel complex (TAS)
0005245 voltage-gated calcium channel activity (TAS)
0006810 transport (TAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by depolarizing stimuli.uch as action potentials.llows Ca2+ ions to enter neurons down a steep electrochemical gradient.roducing transient intracellular Ca2+ signals. Many of the processes that occur in neurons.ncluding transmitter release.ene transcription and metabolism are controlled by Ca2+ influx occurring simultaneously at different cellular locales. The activity of this pore is modulated by 4 tightly-coupled subunits: an intracellular beta subunit; a transmembrane gammasubunit; and a disulphide-linked complex of alpha-2 and delta subunits.hich are proteolytically cleaved from the same gene product. Voltage-gated calcium channels are classified as T.... and R.nd are distinguished by their sensitivity to pharmacological blocks.ingle-channel conductance kinetics.nd voltage-dependence. On the basis of their voltage activation properties.he voltage-gated calcium classes can be further divided into two broad groups: the low (T-type) and high (L... and R-type) threshold-activated channels .L-type calcium channnels are formed from different alpha-1 subunit isoforms that determine the pharmacological properties of the channel.ince they form the drug binding domain. Other properties.uch as gating voltage-dependence. protein modulation and kinase susceptibility.re influenced by alpha-2.elta and beta subunits. There are four distinct beta subunits: beta-1.eta-2.eta-3 and beta-4; and the magnitude of the shift in the voltage-dependence of activation of change to membrane potentials varies with the particular subtype .
  IPR000584:Dihydropyridine sensitive L-type calcium channel, beta subunit
This entry represents a domain found in guanylate kinase () and in L-type calcium channel.Guanylate kinase () (GK) catalyzes the ATP-dependent phosphorylation of GMP into GDP.It is essential for recycling GMP and indirectly.GMP. In prokaryotes (such as Escherichia coli).ower eukaryotes(such as yeast) and in vertebrates.K is a highly conserved monomeric protein of about 200 amino acids. GKhas been shown to be structurally similar to protein A57R (or SalG2R)from various strains of Vaccinia virus. L-type calcium channnels are formed from different alpha-1 subunit isoforms that determine the pharmacological properties of the channel.ince they form the drug binding domain. Other properties.uch as gating voltage-dependence. protein modulation and kinase susceptibility.re influenced by alpha-2.elta and beta subunits.
  IPR008145:Guanylate kinase/L-type calcium channel region
SH3 (src Homology-3) domains are small protein modules containing approximately 50 amino acid residues . They are found in a great variety of intracellular or membrane-associated proteins for example.n a variety of proteins with enzymatic activity.n adaptor proteins that lack catalytic sequences and in cytoskeletal proteins.uch as fodrin and yeast actin binding protein ABP-1. The SH3 domain has a characteristic fold which consists of five or six beta-strands arranged as two tightly packed anti-parallel beta sheets. The linker regions may contain short helices . The surface of the SH2-domain bears a flat.ydrophobic ligand-binding pocket which consists of three shallow grooves defined by conservative aromatic residues in which the ligand adopts an extended left-handed helical arrangement. The ligand binds with low affinity but this may be enhanced by multiple interactions.The region bound by the SH3 domain is in all cases proline-rich and contains PXXP as a core-conserved binding motif. The function of the SH3 domain is not well understood but they may mediate many diverse processes such as increasing local concentration of proteins.ltering their subcellular location and mediating the assembly of large multiprotein complexes .
  IPR001452:Src homology-3
Ca2+ ions are unique in that they not only carry charge but they are also the most widely used of diffusible second messengers. Voltage-dependent Ca2+ channels (VDCC) are a family of molecules that allow cells to couple electrical activity to intracellular Ca2+ signalling. The opening and closing of these channels by depolarizing stimuli.uch as action potentials.llows Ca2+ ions to enter neurons down a steep electrochemical gradient.roducing transient intracellular Ca2+ signals. Many of the processes that occur in neurons.ncluding transmitter release.ene transcription and metabolism are controlled by Ca2+ influx occurring simultaneously at different cellular locales. The activity of this pore is modulated by 4 tightly-coupled subunits: an intracellular beta subunit; a transmembrane gammasubunit; and a disulphide-linked complex of alpha-2 and delta subunits.hich are proteolytically cleaved from the same gene product. Voltage-gated calcium channels are classified as T.... and R.nd are distinguished by their sensitivity to pharmacological blocks.ingle-channel conductance kinetics.nd voltage-dependence. On the basis of their voltage activation properties.he voltage-gated calcium classes can be further divided into two broad groups: the low (T-type) and high (L... and R-type) threshold-activated channels . L-type calcium channnels are formed from different alpha-1 subunit isoforms that determine the pharmacological properties of the channel.ince they form the drug binding domain. Other properties.uch as gating voltage- dependence. protein modulation and kinase susceptibility.re influenced by alpha-2.elta and beta subunits . Co-expression of beta subunit mRNA with alpha-1 subunit mRNA in xenopus oocytes produces increased calcium currents.hich are accompanied by a shift in the voltage-dependence of activation to more negative membrane potentials. Conversely.icroinjection of antisense oligonucleotides to beta subunit mRNA produces decreased calcium currents and shifts voltage- dependent activation to more positive membrane potentials. There are four distinct beta subunits: beta-1.eta-2.eta-3 and beta-4; and the magnitude of these effects varies with the particular subtype.
  IPR005443:L-type calcium channel beta 1 subunit
IPR000584:Ca_channel_B 
Evalue:-171.920822143555 
Location:225-450IPR001452:SH3 
Evalue:-1.52287874528034 
Location:103-167IPR005443:LCACHANNELB1 
Evalue:0 
Location:171-188IPR005443:LCACHANNELB1 
Evalue:0 
Location:17-32IPR005443:LCACHANNELB1 
Evalue:0 
Location:1-16
SequencesProtein: CACB1_HUMAN (598 aa)
mRNA: NM_000723
Local Annotation
Synapse Ontology
?
sdb:0265 cAMP mediated STP  (Evidence:keywords)
KO assignmentK04862
  Level 3 annotation:
    calcium channel, voltage-dependent, beta 1 subunit
  Level 2 annotation:
    Ion channels
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 735 residues, 34583234-34585436Exon2: 64 residues, 34587128-34587314Exon3: 34 residues, 34587762-34587858Exon4: 52 residues, 34593491-34593643Exon5: 38 residues, 34593809-34593919Exon6: 21 residues, 34594103-34594162Exon7: 29 residues, 34594562-34594643Exon8: 8 residues, 34594909-34594929Exon9: 27 residues, 34596274-34596351Exon10: 47 residues, 34596571-34596708Exon11: 43 residues, 34597257-34597380Exon12: 42 residues, 34601252-34601372Exon13: 31 residues, 34604662-34604749Exon14: 81 residues, 34607190-34607427Exon15: 2 residues, -Jump to CACB1_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 3000 35036704-35046401 ~-10K 15710(PPP1R1B)(+)Loci: 3001 35046937-35073248 ~-26K 15714(STARD3)(+)Loci: 4284 34583234-34607427 ~-24K 15696(CACNB1)(-)Link out to UCSC