CACNA1B

Available structures

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

External IDs

OMIM: 601012 MGI: 88296 HomoloGene: 20184 GeneCards: CACNA1B

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
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 • transport
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: 24.6 – 24.76 Mb

PubMed search

^[1]

^[2]

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.^[3]^[4]^[5]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ "Entrez Gene: CACNA1B calcium channel, voltage-dependent, N type, alpha 1B subunit".
↑ Diriong S, Lory P, Williams ME, Ellis SB, Harpold MM, Taviaux S (Dec 1995). "Chromosomal localization of the human genes for alpha 1A, alpha 1B, and alpha 1E voltage-dependent Ca2+ channel subunits". Genomics. 30 (3): 605–9. PMID 8825650. doi:10.1006/geno.1995.1284.
↑ Catterall WA, Perez-Reyes E, Snutch TP, Striessnig J (Dec 2005). "International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels". Pharmacological Reviews. 57 (4): 411–25. PMID 16382099. doi:10.1124/pr.57.4.5.

Mould J, Yasuda T, Schroeder CI, Beedle AM, Doering CJ, Zamponi GW, Adams DJ, Lewis RJ (Aug 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): 34705–14. PMID 15166237. doi:10.1074/jbc.M310848200.
Park SY, Park YT, Kim KE, Rhee MC, Cho HJ, Kim DS (Apr 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): 341–6. PMID 12018859.
Calabrese B, Tabarean IV, Juranka P, Morris CE (Nov 2002). "Mechanosensitivity of N-type calcium channel currents". Biophysical Journal. 83 (5): 2560–74. Bibcode:2002BpJ....83.2560C. PMC 1302342 . PMID 12414690. doi:10.1016/S0006-3495(02)75267-3.
Moskvina V, Craddock N, Holmans P, Nikolov I, Pahwa JS, Green E, Owen MJ, O'Donovan MC (Mar 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): 252–60. PMID 19065143. doi:10.1038/mp.2008.133.
Castiglioni AJ, Raingo J, Lipscombe D (Oct 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): 119–34. PMC 1995641 . PMID 16857708. doi:10.1113/jphysiol.2006.115030.
Catterall WA, Perez-Reyes E, Snutch TP, Striessnig J (Dec 2005). "International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels". Pharmacological Reviews. 57 (4): 411–25. PMID 16382099. doi:10.1124/pr.57.4.5.
Yokoyama CT, Myers SJ, Fu J, Mockus SM, Scheuer T, Catterall WA (Jan 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. PMID 15607937. doi:10.1016/j.mcn.2004.08.019.
Maeno-Hikichi Y, Chang S, Matsumura K, Lai M, Lin H, Nakagawa N, Kuroda S, Zhang JF (May 2003). "A PKC epsilon-ENH-channel complex specifically modulates N-type Ca2+ channels". Nature Neuroscience. 6 (5): 468–75. PMID 12665800. doi:10.1038/nn1041.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. PMID 17081983. doi:10.1016/j.cell.2006.09.026.
Li D, Wang F, Lai M, Chen Y, Zhang JF (Feb 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): 1914–23. PMID 15728831. doi:10.1523/JNEUROSCI.4790-04.2005.
Butcher AJ, Leroy J, Richards MW, Pratt WS, Dolphin AC (Jul 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): 387–98. PMC 1817768 . PMID 16627564. doi:10.1113/jphysiol.2006.109744.
Stotz SC, Barr W, McRory JE, Chen L, Jarvis SE, Zamponi GW (Jan 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): 3793–800. PMID 14602720. doi:10.1074/jbc.M308991200.
Maximov A, Bezprozvanny I (Aug 2002). "Synaptic targeting of N-type calcium channels in hippocampal neurons". The Journal of Neuroscience. 22 (16): 6939–52. PMC 3307533 . PMID 12177192.
Peng S, Hajela RK, Atchison WD (Dec 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): 1418–30. PMID 12435810. doi:10.1124/mol.62.6.1418.
Murakami M, Fleischmann B, De Felipe C, Freichel M, Trost C, Ludwig A, Wissenbach U, Schwegler H, Hofmann F, Hescheler J, Flockerzi V, Cavalié A (Oct 2002). "Pain perception in mice lacking the beta3 subunit of voltage-activated calcium channels". The Journal of Biological Chemistry. 277 (43): 40342–51. PMID 12161429. doi:10.1074/jbc.M203425200.
Vitko I, Shcheglovitov A, Baumgart JP, Arias-Olguín II, Murbartián J, Arias JM, Perez-Reyes E (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. PMC 2570331 . PMID 18958281. doi:10.1371/journal.pone.0003560.
Coppola T, Magnin-Luthi S, Perret-Menoud V, Gattesco S, Schiavo G, Regazzi R (Aug 2001). "Direct interaction of the Rab3 effector RIM with Ca2+ channels, SNAP-25, and synaptotagmin". The Journal of Biological Chemistry. 276 (35): 32756–62. PMID 11438518. doi:10.1074/jbc.M100929200.
Johnson JM, Castle J, Garrett-Engele P, Kan Z, Loerch PM, Armour CD, Santos R, Schadt EE, Stoughton R, Shoemaker DD (Dec 2003). "Genome-wide survey of human alternative pre-mRNA splicing with exon junction microarrays". Science. 302 (5653): 2141–4. Bibcode:2003Sci...302.2141J. PMID 14684825. doi:10.1126/science.1090100.
Agler HL, Evans J, Tay LH, Anderson MJ, Colecraft HM, Yue DT (Jun 2005). "G protein-gated inhibitory module of N-type (ca(v)2.2) ca2+ channels". Neuron. 46 (6): 891–904. PMID 15953418. doi:10.1016/j.neuron.2005.05.011.

External links

CACNA1B protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)

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CACNA1B

References

Further reading

External links