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Protein

Voltage-dependent N-type calcium channel subunit alpha-1B

Gene

CACNA1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1B gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei314Calcium ion selectivity and permeabilityBy similarity1
Sitei663Calcium ion selectivity and permeabilityBy similarity1
Sitei1365Calcium ion selectivity and permeabilityBy similarity1
Sitei1655Calcium ion selectivity and permeabilityBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi451 – 458ATPSequence analysis8
Calcium bindingi1737 – 1748PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium channel activity Source: Reactome
  • calcium ion binding Source: InterPro
  • high voltage-gated calcium channel activity Source: GO_Central
  • protein C-terminus binding Source: UniProtKB
  • voltage-gated calcium channel activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Voltage-gated channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000148408-MONOMER.
ReactomeiR-HSA-112308. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
SIGNORiQ00975.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent N-type calcium channel subunit alpha-1B
Alternative name(s):
Brain calcium channel III
Short name:
BIII
Calcium channel, L type, alpha-1 polypeptide isoform 5
Voltage-gated calcium channel subunit alpha Cav2.2
Gene namesi
Name:CACNA1B
Synonyms:CACH5, CACNL1A5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:1389. CACNA1B.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 95CytoplasmicSequence analysisAdd BLAST95
Transmembranei96 – 114Helical; Name=S1 of repeat ISequence analysisAdd BLAST19
Topological domaini115 – 132ExtracellularSequence analysisAdd BLAST18
Transmembranei133 – 152Helical; Name=S2 of repeat ISequence analysisAdd BLAST20
Topological domaini153 – 163CytoplasmicSequence analysisAdd BLAST11
Transmembranei164 – 183Helical; Name=S3 of repeat ISequence analysisAdd BLAST20
Topological domaini184 – 187ExtracellularSequence analysis4
Transmembranei188 – 206Helical; Name=S4 of repeat ISequence analysisAdd BLAST19
Topological domaini207 – 225CytoplasmicSequence analysisAdd BLAST19
Transmembranei226 – 245Helical; Name=S5 of repeat ISequence analysisAdd BLAST20
Topological domaini246 – 331ExtracellularSequence analysisAdd BLAST86
Transmembranei332 – 356Helical; Name=S6 of repeat ISequence analysisAdd BLAST25
Topological domaini357 – 482CytoplasmicSequence analysisAdd BLAST126
Transmembranei483 – 501Helical; Name=S1 of repeat IISequence analysisAdd BLAST19
Topological domaini502 – 516ExtracellularSequence analysisAdd BLAST15
Transmembranei517 – 536Helical; Name=S2 of repeat IISequence analysisAdd BLAST20
Topological domaini537 – 544CytoplasmicSequence analysis8
Transmembranei545 – 562Helical; Name=S3 of repeat IISequence analysisAdd BLAST18
Topological domaini563 – 573ExtracellularSequence analysisAdd BLAST11
Transmembranei574 – 592Helical; Name=S4 of repeat IISequence analysisAdd BLAST19
Topological domaini593 – 611CytoplasmicSequence analysisAdd BLAST19
Transmembranei612 – 631Helical; Name=S5 of repeat IISequence analysisAdd BLAST20
Topological domaini632 – 684ExtracellularSequence analysisAdd BLAST53
Transmembranei685 – 709Helical; Name=S6 of repeat IISequence analysisAdd BLAST25
Topological domaini710 – 1151CytoplasmicSequence analysisAdd BLAST442
Transmembranei1152 – 1169Helical; Name=S1 of repeat IIISequence analysisAdd BLAST18
Topological domaini1170 – 1185ExtracellularSequence analysisAdd BLAST16
Transmembranei1186 – 1205Helical; Name=S2 of repeat IIISequence analysisAdd BLAST20
Topological domaini1206 – 1217CytoplasmicSequence analysisAdd BLAST12
Transmembranei1218 – 1236Helical; Name=S3 of repeat IIISequence analysisAdd BLAST19
Topological domaini1237 – 1246ExtracellularSequence analysis10
Transmembranei1247 – 1265Helical; Name=S4 of repeat IIISequence analysisAdd BLAST19
Topological domaini1266 – 1284CytoplasmicSequence analysisAdd BLAST19
Transmembranei1285 – 1304Helical; Name=S5 of repeat IIISequence analysisAdd BLAST20
Topological domaini1305 – 1391ExtracellularSequence analysisAdd BLAST87
Transmembranei1392 – 1416Helical; Name=S6 of repeat IIISequence analysisAdd BLAST25
Topological domaini1417 – 1471CytoplasmicSequence analysisAdd BLAST55
Transmembranei1472 – 1490Helical; Name=S1 of repeat IVSequence analysisAdd BLAST19
Topological domaini1491 – 1505ExtracellularSequence analysisAdd BLAST15
Transmembranei1506 – 1525Helical; Name=S2 of repeat IVSequence analysisAdd BLAST20
Topological domaini1526 – 1533CytoplasmicSequence analysis8
Transmembranei1534 – 1552Helical; Name=S3 of repeat IVSequence analysisAdd BLAST19
Topological domaini1553 – 1563ExtracellularSequence analysisAdd BLAST11
Transmembranei1564 – 1582Helical; Name=S4 of repeat IVSequence analysisAdd BLAST19
Topological domaini1583 – 1601CytoplasmicSequence analysisAdd BLAST19
Transmembranei1602 – 1621Helical; Name=S5 of repeat IVSequence analysisAdd BLAST20
Topological domaini1622 – 1683ExtracellularSequence analysisAdd BLAST62
Transmembranei1684 – 1708Helical; Name=S6 of repeat IVSequence analysisAdd BLAST25
Topological domaini1709 – 2339CytoplasmicSequence analysisAdd BLAST631

GO - Cellular componenti

  • dendrite Source: Ensembl
  • neuronal cell body Source: Ensembl
  • plasma membrane Source: Reactome
  • presynapse Source: GOC
  • voltage-gated calcium channel complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Involvement in diseasei

Dystonia 23 (DYT23)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of dystonia, a disorder defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. DYT23 is an autosomal dominant dystonia affecting the face, neck, limbs. Some DYT23 patients manifest generalized myoclonus in addition to progressive action-induced multifocal dystonia.
See also OMIM:614860
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0734321389R → H in DYT23; gain of function mutation. 1 PublicationCorresponds to variant rs184841813dbSNPEnsembl.1

Keywords - Diseasei

Congenital generalized lipodystrophy, Disease mutation, Dystonia, Mental retardation

Organism-specific databases

DisGeNETi774.
MIMi614860. phenotype.
OpenTargetsiENSG00000148408.
PharmGKBiPA26008.

Chemistry databases

ChEMBLiCHEMBL4478.
DrugBankiDB00381. Amlodipine.
DB00996. Gabapentin.
DB01202. Levetiracetam.
DB00421. Spironolactone.
DB00661. Verapamil.
GuidetoPHARMACOLOGYi533.

Polymorphism and mutation databases

BioMutaiCACNA1B.
DMDMi1705854.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000539211 – 2339Voltage-dependent N-type calcium channel subunit alpha-1BAdd BLAST2339

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei22Omega-N-methylarginineBy similarity1
Glycosylationi256N-linked (GlcNAc...)Sequence analysis1
Modified residuei411PhosphoserineBy similarity1
Modified residuei745PhosphoserineBy similarity1
Modified residuei748PhosphoserineBy similarity1
Modified residuei783PhosphoserineBy similarity1
Modified residuei1069PhosphoserineBy similarity1
Glycosylationi1563N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1675N-linked (GlcNAc...)Sequence analysis1
Modified residuei1719Phosphoserine; by PKASequence analysis1
Modified residuei2066PhosphoserineBy similarity1
Modified residuei2224PhosphoserineBy similarity1
Modified residuei2233PhosphoserineBy similarity1
Modified residuei2256PhosphoserineBy similarity1

Post-translational modificationi

Phosphorylated in vitro by CaM-kinase II, PKA, PKC and CGPK.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

EPDiQ00975.
PaxDbiQ00975.
PeptideAtlasiQ00975.
PRIDEiQ00975.

PTM databases

iPTMnetiQ00975.
PhosphoSitePlusiQ00975.

Expressioni

Tissue specificityi

Isoform Alpha-1b-1 and isoform Alpha-1b-2 are expressed in the central nervous system, but not in skeletal muscle or aorta.

Gene expression databases

BgeeiENSG00000148408.
CleanExiHS_CACNA1B.
ExpressionAtlasiQ00975. baseline and differential.
GenevisibleiQ00975. HS.

Organism-specific databases

HPAiHPA044347.

Interactioni

Subunit structurei

Multisubunit complex consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity. Interacts with RIMS1. Interacts with FMR1 (via C-terminus); this interaction induces a deacrease in the number of presynaptic functional CACNA1B channels at the cell surface.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Ppm1aP206503EBI-1055161,EBI-7491743From a different organism.
RXRBP287023EBI-1055161,EBI-748576

GO - Molecular functioni

  • protein C-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107228. 7 interactors.
IntActiQ00975. 7 interactors.
MINTiMINT-102376.
STRINGi9606.ENSP00000360406.

Chemistry databases

BindingDBiQ00975.

Structurei

Secondary structure

12339
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1244 – 1263Combined sources20
Turni1264 – 1266Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LCMNMR-A1242-1269[»]
ProteinModelPortaliQ00975.
SMRiQ00975.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati82 – 359IAdd BLAST278
Repeati468 – 712IIAdd BLAST245
Repeati1137 – 1419IIIAdd BLAST283
Repeati1456 – 1711IVAdd BLAST256
Domaini1724 – 1759EF-handPROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni379 – 396Binding to the beta subunitBy similarityAdd BLAST18

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi2050 – 2054Poly-His5
Compositional biasi2118 – 2122Poly-Ser5

Domaini

Each of the four internal repeats contains five hydrophobic transmembrane segments (S1, S2, S3, S5, S6) and one positively charged transmembrane segment (S4). S4 segments probably represent the voltage-sensor and are characterized by a series of positively charged amino acids at every third position.

Sequence similaritiesi

Contains 1 EF-hand domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
GeneTreeiENSGT00830000128247.
HOGENOMiHOG000231530.
HOVERGENiHBG050763.
InParanoidiQ00975.
KOiK04849.
PhylomeDBiQ00975.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005447. VDCC_N_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF161. PTHR10037:SF161. 3 hits.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16905. GPHH. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01631. NVDCCALPHA1.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Alpha-1B-1 (identifier: Q00975-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVRFGDELGG RYGGPGGGER ARGGGAGGAG GPGPGGLQPG QRVLYKQSIA
60 70 80 90 100
QRARTMALYN PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM
110 120 130 140 150
ILATIIANCI VLALEQHLPD GDKTPMSERL DDTEPYFIGI FCFEAGIKII
160 170 180 190 200
ALGFVFHKGS YLRNGWNVMD FVVVLTGILA TAGTDFDLRT LRAVRVLRPL
210 220 230 240 250
KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII GLEFYMGKFH
260 270 280 290 300
KACFPNSTDA EPVGDFPCGK EAPARLCEGD TECREYWPGP NFGITNFDNI
310 320 330 340 350
LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL
360 370 380 390 400
VLGVLSGEFA KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML
410 420 430 440 450
AEEDRNAEEK SPLDVLKRAA TKKSRNDLIH AEEGEDRFAD LCAVGSPFAR
460 470 480 490 500
ASLKSGKTES SSYFRRKEKM FRFFIRRMVK AQSFYWVVLC VVALNTLCVA
510 520 530 540 550
MVHYNQPRRL TTTLYFAEFV FLGLFLTEMS LKMYGLGPRS YFRSSFNCFD
560 570 580 590 600
FGVIVGSVFE VVWAAIKPGS SFGISVLRAL RLLRIFKVTK YWSSLRNLVV
610 620 630 640 650
SLLNSMKSII SLLFLLFLFI VVFALLGMQL FGGQFNFQDE TPTTNFDTFP
660 670 680 690 700
AAILTVFQIL TGEDWNAVMY HGIESQGGVS KGMFSSFYFI VLTLFGNYTL
710 720 730 740 750
LNVFLAIAVD NLANAQELTK DEEEMEEAAN QKLALQKAKE VAEVSPMSAA
760 770 780 790 800
NISIAARQQN SAKARSVWEQ RASQLRLQNL RASCEALYSE MDPEERLRFA
810 820 830 840 850
TTRHLRPDMK THLDRPLVVE LGRDGARGPV GGKARPEAAE APEGVDPPRR
860 870 880 890 900
HHRHRDKDKT PAAGDQDRAE APKAESGEPG AREERPRPHR SHSKEAAGPP
910 920 930 940 950
EARSERGRGP GPEGGRRHHR RGSPEEAAER EPRRHRAHRH QDPSKECAGA
960 970 980 990 1000
KGERRARHRG GPRAGPREAE SGEEPARRHR ARHKAQPAHE AVEKETTEKE
1010 1020 1030 1040 1050
ATEKEAEIVE ADKEKELRNH QPREPHCDLE TSGTVTVGPM HTLPSTCLQK
1060 1070 1080 1090 1100
VEEQPEDADN QRNVTRMGSQ PPDPNTIVHI PVMLTGPLGE ATVVPSGNVD
1110 1120 1130 1140 1150
LESQAEGKKE VEADDVMRSG PRPIVPYSSM FCLSPTNLLR RFCHYIVTMR
1160 1170 1180 1190 1200
YFEVVILVVI ALSSIALAAE DPVRTDSPRN NALKYLDYIF TGVFTFEMVI
1210 1220 1230 1240 1250
KMIDLGLLLH PGAYFRDLWN ILDFIVVSGA LVAFAFSGSK GKDINTIKSL
1260 1270 1280 1290 1300
RVLRVLRPLK TIKRLPKLKA VFDCVVNSLK NVLNILIVYM LFMFIFAVIA
1310 1320 1330 1340 1350
VQLFKGKFFY CTDESKELER DCRGQYLDYE KEEVEAQPRQ WKKYDFHYDN
1360 1370 1380 1390 1400
VLWALLTLFT VSTGEGWPMV LKHSVDATYE EQGPSPGYRM ELSIFYVVYF
1410 1420 1430 1440 1450
VVFPFFFVNI FVALIIITFQ EQGDKVMSEC SLEKNERACI DFAISAKPLT
1460 1470 1480 1490 1500
RYMPQNRQSF QYKTWTFVVS PPFEYFIMAM IALNTVVLMM KFYDAPYEYE
1510 1520 1530 1540 1550
LMLKCLNIVF TSMFSMECVL KIIAFGVLNY FRDAWNVFDF VTVLGSITDI
1560 1570 1580 1590 1600
LVTEIAETNN FINLSFLRLF RAARLIKLLR QGYTIRILLW TFVQSFKALP
1610 1620 1630 1640 1650
YVCLLIAMLF FIYAIIGMQV FGNIALDDDT SINRHNNFRT FLQALMLLFR
1660 1670 1680 1690 1700
SATGEAWHEI MLSCLSNQAC DEQANATECG SDFAYFYFVS FIFLCSFLML
1710 1720 1730 1740 1750
NLFVAVIMDN FEYLTRDSSI LGPHHLDEFI RVWAEYDPAA CGRISYNDMF
1760 1770 1780 1790 1800
EMLKHMSPPL GLGKKCPARV AYKRLVRMNM PISNEDMTVH FTSTLMALIR
1810 1820 1830 1840 1850
TALEIKLAPA GTKQHQCDAE LRKEISVVWA NLPQKTLDLL VPPHKPDEMT
1860 1870 1880 1890 1900
VGKVYAALMI FDFYKQNKTT RDQMQQAPGG LSQMGPVSLF HPLKATLEQT
1910 1920 1930 1940 1950
QPAVLRGARV FLRQKSSTSL SNGGAIQNQE SGIKESVSWG TQRTQDAPHE
1960 1970 1980 1990 2000
ARPPLERGHS TEIPVGRSGA LAVDVQMQSI TRRGPDGEPQ PGLESQGRAA
2010 2020 2030 2040 2050
SMPRLAAETQ PVTDASPMKR SISTLAQRPR GTHLCSTTPD RPPPSQASSH
2060 2070 2080 2090 2100
HHHHRCHRRR DRKQRSLEKG PSLSADMDGA PSSAVGPGLP PGEGPTGCRR
2110 2120 2130 2140 2150
ERERRQERGR SQERRQPSSS SSEKQRFYSC DRFGGREPPK PKPSLSSHPT
2160 2170 2180 2190 2200
SPTAGQEPGP HPQGSGSVNG SPLLSTSGAS TPGRGGRRQL PQTPLTPRPS
2210 2220 2230 2240 2250
ITYKTANSSP IHFAGAQTSL PAFSPGRLSR GLSEHNALLQ RDPLSQPLAP
2260 2270 2280 2290 2300
GSRIGSDPYL GQRLDSEASV HALPEDTLTF EEAVATNSGR SSRTSYVSSL
2310 2320 2330
TSQSHPLRRV PNGYHCTLGL SSGGRARHSY HHPDQDHWC
Length:2,339
Mass (Da):262,496
Last modified:October 1, 1996 - v1
Checksum:i17A45C6D1E76B39D
GO
Isoform Alpha-1B-2 (identifier: Q00975-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2164-2339: GSGSVNGSPL...YHHPDQDHWC → AGSAVGFPNT...APPGLPTCPP

Show »
Length:2,237
Mass (Da):251,716
Checksum:i28804E510F1E7747
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform Alpha-1B-2 (identifier: Q00975-2)
Sequence conflicti2215L → R in AAA51898 (PubMed:1321501).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_048741167N → K.Corresponds to variant rs4422842dbSNPEnsembl.1
Natural variantiVAR_061100862A → S.Corresponds to variant rs7873074dbSNPEnsembl.1
Natural variantiVAR_061101996T → A.Corresponds to variant rs11137342dbSNPEnsembl.1
Natural variantiVAR_0734321389R → H in DYT23; gain of function mutation. 1 PublicationCorresponds to variant rs184841813dbSNPEnsembl.1
Natural variantiVAR_0487421436E → K.Corresponds to variant rs12377346dbSNPEnsembl.1
Natural variantiVAR_0487431500E → K.Corresponds to variant rs12377346dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0008822164 – 2339GSGSV…QDHWC → AGSAVGFPNTTPCCRETPSA SPWPLALELALTLTWGSVWT VRPLSTPCLRTLSLSRRLWP PTRAAPPGLPTCPP in isoform Alpha-1B-2. 1 PublicationAdd BLAST176

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94172 mRNA. Translation: AAA51897.1.
M94173 mRNA. Translation: AAA51898.1.
AL591424, AL772363 Genomic DNA. Translation: CAI40687.1.
AL772363, AL591424 Genomic DNA. Translation: CAI17144.1.
U76666 Genomic DNA. Translation: AAC51138.1.
CCDSiCCDS59522.1. [Q00975-1]
CCDS59523.1. [Q00975-2]
PIRiA42566.
T45115.
RefSeqiNP_000709.1. NM_000718.3. [Q00975-1]
NP_001230741.1. NM_001243812.1. [Q00975-2]
UniGeneiHs.495522.

Genome annotation databases

EnsembliENST00000277551; ENSP00000277551; ENSG00000148408. [Q00975-2]
ENST00000371372; ENSP00000360423; ENSG00000148408. [Q00975-1]
GeneIDi774.
KEGGihsa:774.
UCSCiuc064xny.1. human. [Q00975-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94172 mRNA. Translation: AAA51897.1.
M94173 mRNA. Translation: AAA51898.1.
AL591424, AL772363 Genomic DNA. Translation: CAI40687.1.
AL772363, AL591424 Genomic DNA. Translation: CAI17144.1.
U76666 Genomic DNA. Translation: AAC51138.1.
CCDSiCCDS59522.1. [Q00975-1]
CCDS59523.1. [Q00975-2]
PIRiA42566.
T45115.
RefSeqiNP_000709.1. NM_000718.3. [Q00975-1]
NP_001230741.1. NM_001243812.1. [Q00975-2]
UniGeneiHs.495522.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2LCMNMR-A1242-1269[»]
ProteinModelPortaliQ00975.
SMRiQ00975.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107228. 7 interactors.
IntActiQ00975. 7 interactors.
MINTiMINT-102376.
STRINGi9606.ENSP00000360406.

Chemistry databases

BindingDBiQ00975.
ChEMBLiCHEMBL4478.
DrugBankiDB00381. Amlodipine.
DB00996. Gabapentin.
DB01202. Levetiracetam.
DB00421. Spironolactone.
DB00661. Verapamil.
GuidetoPHARMACOLOGYi533.

PTM databases

iPTMnetiQ00975.
PhosphoSitePlusiQ00975.

Polymorphism and mutation databases

BioMutaiCACNA1B.
DMDMi1705854.

Proteomic databases

EPDiQ00975.
PaxDbiQ00975.
PeptideAtlasiQ00975.
PRIDEiQ00975.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000277551; ENSP00000277551; ENSG00000148408. [Q00975-2]
ENST00000371372; ENSP00000360423; ENSG00000148408. [Q00975-1]
GeneIDi774.
KEGGihsa:774.
UCSCiuc064xny.1. human. [Q00975-1]

Organism-specific databases

CTDi774.
DisGeNETi774.
GeneCardsiCACNA1B.
HGNCiHGNC:1389. CACNA1B.
HPAiHPA044347.
MIMi601012. gene.
614860. phenotype.
neXtProtiNX_Q00975.
OpenTargetsiENSG00000148408.
PharmGKBiPA26008.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2301. Eukaryota.
ENOG410XNP6. LUCA.
GeneTreeiENSGT00830000128247.
HOGENOMiHOG000231530.
HOVERGENiHBG050763.
InParanoidiQ00975.
KOiK04849.
PhylomeDBiQ00975.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000148408-MONOMER.
ReactomeiR-HSA-112308. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
SIGNORiQ00975.

Miscellaneous databases

ChiTaRSiCACNA1B. human.
GeneWikiiN-type_calcium_channel.
GenomeRNAii774.
PROiQ00975.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000148408.
CleanExiHS_CACNA1B.
ExpressionAtlasiQ00975. baseline and differential.
GenevisibleiQ00975. HS.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR031649. GPHH_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005447. VDCC_N_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF161. PTHR10037:SF161. 3 hits.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF16905. GPHH. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01631. NVDCCALPHA1.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAC1B_HUMAN
AccessioniPrimary (citable) accession number: Q00975
Secondary accession number(s): B1AQK5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.