CACNA1B

Protein-coding gene in the species Homo sapiens

CACNA1B

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
2LCM

Identifiers

Aliases

CACNA1B, BIII, CACNL1A5, CACNN, Cav2.2, DYT23, calcium voltage-gated channel subunit alpha1 B, NEDNEH

External IDs

OMIM: 601012; MGI: 88296; HomoloGene: 20184; GeneCards: CACNA1B; OMA:CACNA1B - orthologs

Gene location (Human)

Chr.	Chromosome 9 (human)^[1]

Band	9q34.3	Start	137,877,782 bp^[1]
Band	9q34.3	End	138,124,624 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 2 (mouse)^[2]

Band	2 A3\|2 16.58 cM	Start	24,493,899 bp^[2]
Band	2 A3\|2 16.58 cM	End	24,653,164 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

middle temporal gyrus

Brodmann area 23

postcentral gyrus

endothelial cell

superior frontal gyrus

entorhinal cortex

right hemisphere of cerebellum

primary visual cortex

Brodmann area 46

cerebellar vermis

Top expressed in

supraoptic nucleus

ventromedial nucleus

dorsomedial hypothalamic nucleus

anterior amygdaloid area

trigeminal ganglion

gastrula

subiculum

arcuate nucleus

lumbar spinal ganglion

mammillary body

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	protein C-terminus binding metal ion binding nucleotide binding calcium ion binding voltage-gated calcium channel activity high voltage-gated calcium channel activity ion channel activity ATP binding voltage-gated ion channel activity protein binding calcium channel activity amyloid-beta binding
Cellular component	integral component of membrane presynapse membrane neuronal cell body dendrite voltage-gated calcium channel complex plasma membrane
Biological process	calcium ion transport chemical synaptic transmission transmembrane transport membrane depolarization during action potential locomotory behavior regulation of ion transmembrane transport regulation of blood pressure regulation of calcium ion transport ion transport regulation of heart contraction calcium ion transmembrane transport response to pain membrane depolarization neurotransmitter secretion calcium ion import modulation of chemical synaptic transmission response to amyloid-beta
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


774


12287

Ensembl


ENSG00000148408


ENSMUSG00000004113

UniProt


Q00975


O55017

RefSeq (mRNA)


NM_000718 NM_001243812


NM_001042528 NM_007579

RefSeq (protein)


NP_000709 NP_001230741


NP_001035993 NP_031605

Location (UCSC)

Chr 9: 137.88 – 138.12 Mb

Chr 2: 24.49 – 24.65 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

The voltage-dependent N-type calcium channel subunit alpha-1B is a protein that in humans is encoded by the CACNA1B gene.^[5]^[6]^[7] The α1B protein, together with β and α2δ subunits forms N-type calcium channel (Ca_v2.2 channel).^[8] It is a R-type calcium channel.^{[citation needed]}

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000148408 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000004113 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Entrez Gene: CACNA1B calcium channel, voltage-dependent, N type, alpha 1B subunit".
^ Diriong S, Lory P, Williams ME, Ellis SB, Harpold MM, Taviaux S (December 1995). "Chromosomal localization of the human genes for alpha 1A, alpha 1B, and alpha 1E voltage-dependent Ca2+ channel subunits". Genomics. 30 (3): 605–609. doi:10.1006/geno.1995.1284. PMID 8825650.
^ Catterall WA, Perez-Reyes E, Snutch TP, Striessnig J (December 2005). "International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels". Pharmacological Reviews. 57 (4): 411–425. doi:10.1124/pr.57.4.5. PMID 16382099. S2CID 10386627.
^ Heyes S, Pratt WS, Rees E, Dahimene S, Ferron L, Owen MJ, et al. (November 2015). "Genetic disruption of voltage-gated calcium channels in psychiatric and neurological disorders". Progress in Neurobiology. 134: 36–54. doi:10.1016/j.pneurobio.2015.09.002. PMC 4658333. PMID 26386135.

Mould J, Yasuda T, Schroeder CI, Beedle AM, Doering CJ, Zamponi GW, et al. (August 2004). "The alpha2delta auxiliary subunit reduces affinity of omega-conotoxins for recombinant N-type (Cav2.2) calcium channels". The Journal of Biological Chemistry. 279 (33): 34705–34714. doi:10.1074/jbc.M310848200. PMID 15166237.
Park SY, Park YT, Kim KE, Rhee MC, Cho HJ, Kim DS (April 2002). "A direct repeat of N-type Ca2+ channel alpha1B gene functions as a negative regulatory element in HeLa cells". Molecules and Cells. 13 (2): 341–346. doi:10.1016/S1016-8478(23)15043-6. PMID 12018859.
Calabrese B, Tabarean IV, Juranka P, Morris CE (November 2002). "Mechanosensitivity of N-type calcium channel currents". Biophysical Journal. 83 (5): 2560–2574. Bibcode:2002BpJ....83.2560C. doi:10.1016/S0006-3495(02)75267-3. PMC 1302342. PMID 12414690.
Moskvina V, Craddock N, Holmans P, Nikolov I, Pahwa JS, Green E, et al. (March 2009). "Gene-wide analyses of genome-wide association data sets: evidence for multiple common risk alleles for schizophrenia and bipolar disorder and for overlap in genetic risk". Molecular Psychiatry. 14 (3): 252–260. doi:10.1038/mp.2008.133. PMC 3970088. PMID 19065143.
Castiglioni AJ, Raingo J, Lipscombe D (October 2006). "Alternative splicing in the C-terminus of CaV2.2 controls expression and gating of N-type calcium channels". The Journal of Physiology. 576 (Pt 1): 119–134. doi:10.1113/jphysiol.2006.115030. PMC 1995641. PMID 16857708.
Catterall WA, Perez-Reyes E, Snutch TP, Striessnig J (December 2005). "International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels". Pharmacological Reviews. 57 (4): 411–425. doi:10.1124/pr.57.4.5. PMID 16382099. S2CID 10386627.
Yokoyama CT, Myers SJ, Fu J, Mockus SM, Scheuer T, Catterall WA (January 2005). "Mechanism of SNARE protein binding and regulation of Cav2 channels by phosphorylation of the synaptic protein interaction site". Molecular and Cellular Neurosciences. 28 (1): 1–17. doi:10.1016/j.mcn.2004.08.019. PMID 15607937. S2CID 38370138.
Maeno-Hikichi Y, Chang S, Matsumura K, Lai M, Lin H, Nakagawa N, et al. (May 2003). "A PKC epsilon-ENH-channel complex specifically modulates N-type Ca2+ channels". Nature Neuroscience. 6 (5): 468–475. doi:10.1038/nn1041. PMID 12665800. S2CID 19964052.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, et al. (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–648. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
Li D, Wang F, Lai M, Chen Y, Zhang JF (February 2005). "A protein phosphatase 2calpha-Ca2+ channel complex for dephosphorylation of neuronal Ca2+ channels phosphorylated by protein kinase C". The Journal of Neuroscience. 25 (8): 1914–1923. doi:10.1523/JNEUROSCI.4790-04.2005. PMC 6726054. PMID 15728831.
Butcher AJ, Leroy J, Richards MW, Pratt WS, Dolphin AC (July 2006). "The importance of occupancy rather than affinity of CaV(beta) subunits for the calcium channel I-II linker in relation to calcium channel function". The Journal of Physiology. 574 (Pt 2): 387–398. doi:10.1113/jphysiol.2006.109744. PMC 1817768. PMID 16627564.
Stotz SC, Barr W, McRory JE, Chen L, Jarvis SE, Zamponi GW (January 2004). "Several structural domains contribute to the regulation of N-type calcium channel inactivation by the beta 3 subunit". The Journal of Biological Chemistry. 279 (5): 3793–3800. doi:10.1074/jbc.M308991200. PMID 14602720.
Maximov A, Bezprozvanny I (August 2002). "Synaptic targeting of N-type calcium channels in hippocampal neurons". The Journal of Neuroscience. 22 (16): 6939–6952. doi:10.1523/JNEUROSCI.22-16-06939.2002. PMC 3307533. PMID 12177192.
Peng S, Hajela RK, Atchison WD (December 2002). "Characteristics of block by Pb2+ of function of human neuronal L-, N-, and R-type Ca2+ channels transiently expressed in human embryonic kidney 293 cells". Molecular Pharmacology. 62 (6): 1418–1430. doi:10.1124/mol.62.6.1418. PMID 12435810.
Murakami M, Fleischmann B, De Felipe C, Freichel M, Trost C, Ludwig A, et al. (October 2002). "Pain perception in mice lacking the beta3 subunit of voltage-activated calcium channels". The Journal of Biological Chemistry. 277 (43): 40342–40351. doi:10.1074/jbc.M203425200. hdl:10261/310195. PMID 12161429.
Vitko I, Shcheglovitov A, Baumgart JP, Arias-Olguín II, Murbartián J, Arias JM, et al. (2008). Schwartz A (ed.). "Orientation of the calcium channel beta relative to the alpha(1)2.2 subunit is critical for its regulation of channel activity". PLOS ONE. 3 (10): e3560. Bibcode:2008PLoSO...3.3560V. doi:10.1371/journal.pone.0003560. PMC 2570331. PMID 18958281.
Coppola T, Magnin-Luthi S, Perret-Menoud V, Gattesco S, Schiavo G, Regazzi R (August 2001). "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin". The Journal of Biological Chemistry. 276 (35): 32756–32762. doi:10.1074/jbc.M100929200. PMID 11438518.
Johnson JM, Castle J, Garrett-Engele P, Kan Z, Loerch PM, Armour CD, et al. (December 2003). "Genome-wide survey of human alternative pre-mRNA splicing with exon junction microarrays". Science. 302 (5653): 2141–2144. Bibcode:2003Sci...302.2141J. doi:10.1126/science.1090100. PMID 14684825. S2CID 10007258.
Agler HL, Evans J, Tay LH, Anderson MJ, Colecraft HM, Yue DT (June 2005). "G protein-gated inhibitory module of N-type (ca(v)2.2) ca2+ channels". Neuron. 46 (6): 891–904. doi:10.1016/j.neuron.2005.05.011. PMID 15953418. S2CID 16963916.