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Q15878

- CAC1E_HUMAN

UniProt

Q15878 - CAC1E_HUMAN

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Protein

Voltage-dependent R-type calcium channel subunit alpha-1E

Gene

CACNA1E

Organism
Homo sapiens (Human)
Status
Reviewed - 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-1E gives rise to R-type calcium currents. R-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by nickel, and partially by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to dihydropyridines (DHP), omega-conotoxin-GVIA (omega-CTx-GVIA), and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing alpha-1E subunit could be involved in the modulation of firing patterns of neurons which is important for information processing.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei309 – 3091Calcium ion selectivity and permeabilityBy similarity
Sitei657 – 6571Calcium ion selectivity and permeabilityBy similarity
Sitei1372 – 13721Calcium ion selectivity and permeabilityBy similarity
Sitei1663 – 16631Calcium ion selectivity and permeabilityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi426 – 43712PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi1752 – 176312PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. high voltage-gated calcium channel activity Source: RefGenome
  3. voltage-gated calcium channel activity Source: MGI

GO - Biological processi

  1. calcium ion import Source: RefGenome
  2. energy reserve metabolic process Source: Reactome
  3. membrane depolarization Source: Reactome
  4. membrane depolarization during action potential Source: RefGenome
  5. regulation of insulin secretion Source: Reactome
  6. small molecule metabolic process Source: Reactome
  7. synaptic transmission Source: RefGenome
  8. transport Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Calcium channel, Ion channel, Voltage-gated channel

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_13606. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
REACT_18325. Regulation of insulin secretion.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-dependent R-type calcium channel subunit alpha-1E
Alternative name(s):
Brain calcium channel II
Short name:
BII
Calcium channel, L type, alpha-1 polypeptide, isoform 6
Voltage-gated calcium channel subunit alpha Cav2.3
Gene namesi
Name:CACNA1E
Synonyms:CACH6, CACNL1A6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:1392. CACNA1E.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8989CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei90 – 10819Helical; Name=S1 of repeat IAdd
BLAST
Topological domaini109 – 12719ExtracellularSequence AnalysisAdd
BLAST
Transmembranei128 – 14619Helical; Name=S2 of repeat IAdd
BLAST
Topological domaini147 – 15812CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei159 – 17315Helical; Name=S3 of repeat IAdd
BLAST
Topological domaini174 – 18512ExtracellularSequence AnalysisAdd
BLAST
Transmembranei186 – 20520Helical; Name=S4 of repeat IAdd
BLAST
Topological domaini206 – 22318CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei224 – 24421Helical; Name=S5 of repeat IAdd
BLAST
Topological domaini245 – 32682ExtracellularSequence AnalysisAdd
BLAST
Transmembranei327 – 35024Helical; Name=S6 of repeat IAdd
BLAST
Topological domaini351 – 476126CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei477 – 49620Helical; Name=S1 of repeat IIAdd
BLAST
Topological domaini497 – 50913ExtracellularSequence AnalysisAdd
BLAST
Transmembranei510 – 52920Helical; Name=S2 of repeat IIAdd
BLAST
Topological domaini530 – 5389CytoplasmicSequence Analysis
Transmembranei539 – 55719Helical; Name=S3 of repeat IIAdd
BLAST
Topological domaini558 – 56710ExtracellularSequence Analysis
Transmembranei568 – 58619Helical; Name=S4 of repeat IIAdd
BLAST
Topological domaini587 – 60519CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei606 – 62520Helical; Name=S5 of repeat IIAdd
BLAST
Topological domaini626 – 67853ExtracellularSequence AnalysisAdd
BLAST
Transmembranei679 – 70325Helical; Name=S6 of repeat IIAdd
BLAST
Topological domaini704 – 1148445CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1149 – 116517Helical; Name=S1 of repeat IIIAdd
BLAST
Topological domaini1166 – 118924ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1190 – 120920Helical; Name=S2 of repeat IIIAdd
BLAST
Topological domaini1210 – 12178CytoplasmicSequence Analysis
Transmembranei1218 – 124023Helical; Name=S3 of repeat IIIAdd
BLAST
Topological domaini1241 – 125414ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1255 – 127218Helical; Name=S4 of repeat IIIAdd
BLAST
Topological domaini1273 – 129119CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1292 – 131120Helical; Name=S5 of repeat IIIAdd
BLAST
Topological domaini1312 – 139887ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1399 – 142224Helical; Name=S6 of repeat IIIAdd
BLAST
Topological domaini1423 – 147957CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1480 – 149819Helical; Name=S1 of repeat IVAdd
BLAST
Topological domaini1499 – 151315ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1514 – 153320Helical; Name=S2 of repeat IVAdd
BLAST
Topological domaini1534 – 15418CytoplasmicSequence Analysis
Transmembranei1542 – 156019Helical; Name=S3 of repeat IVAdd
BLAST
Topological domaini1561 – 157111ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1572 – 159019Helical; Name=S4 of repeat IVAdd
BLAST
Topological domaini1591 – 160919CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei1610 – 162920Helical; Name=S5 of repeat IVAdd
BLAST
Topological domaini1630 – 169869ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1699 – 172426Helical; Name=S6 of repeat IVAdd
BLAST
Topological domaini1725 – 2313589CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. plasma membrane Source: RefGenome
  2. voltage-gated calcium channel complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26009.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23132313Voltage-dependent R-type calcium channel subunit alpha-1EPRO_0000053938Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1566 – 15661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1571 – 15711N-linked (GlcNAc...)Sequence Analysis
Modified residuei1734 – 17341Phosphoserine; by PKASequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ15878.
PRIDEiQ15878.

PTM databases

PhosphoSiteiQ15878.

Expressioni

Tissue specificityi

Expressed in neuronal tissues and in kidney.

Gene expression databases

BgeeiQ15878.
CleanExiHS_CACNA1E.
ExpressionAtlasiQ15878. baseline and differential.
GenevestigatoriQ15878.

Organism-specific databases

HPAiHPA042515.

Interactioni

Subunit structurei

Interacts with EFHC1. Voltage-dependent calcium channels are multisubunit complexes, 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.1 Publication

Protein-protein interaction databases

BioGridi107231. 3 interactions.
STRINGi9606.ENSP00000356545.

Structurei

Secondary structure

1
2313
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1868 – 188215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BXLX-ray2.30B1867-1887[»]
ProteinModelPortaliQ15878.
SMRiQ15878. Positions 358-402, 1249-1276.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15878.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati76 – 354279IAdd
BLAST
Repeati462 – 706245IIAdd
BLAST
Repeati1140 – 1426287IIIAdd
BLAST
Repeati1463 – 1726264IVAdd
BLAST
Domaini1739 – 177436EF-handPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni374 – 39118Binding to the beta subunitBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi716 – 7216Poly-Glu
Compositional biasi748 – 7536Poly-Arg
Compositional biasi767 – 7726Poly-Arg
Compositional biasi1228 – 12314Poly-Val
Compositional biasi2284 – 22885Poly-Arg

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

eggNOGiCOG1226.
GeneTreeiENSGT00760000118827.
HOGENOMiHOG000231530.
HOVERGENiHBG050763.
InParanoidiQ15878.
KOiK04852.
OMAiHMQMSSQ.
OrthoDBiEOG7T1RBQ.
PhylomeDBiQ15878.
TreeFamiTF312805.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005449. VDCC_R_a1su.
IPR002077. VDCCAlpha1.
[Graphical view]
PANTHERiPTHR10037:SF57. PTHR10037:SF57. 1 hit.
PfamiPF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view]
PRINTSiPR00167. CACHANNEL.
PR01633. RVDCCALPHA1.
SMARTiSM01062. Ca_chan_IQ. 1 hit.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q15878-1) [UniParc]FASTAAdd to Basket

Also known as: Alpha-1E

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
MARFGEAVVA RPGSGDGDSD QSRNRQGTPV PASGQAAAYK QTKAQRARTM
60 70 80 90 100
ALYNPIPVRQ NCFTVNRSLF IFGEDNIVRK YAKKLIDWPP FEYMILATII
110 120 130 140 150
ANCIVLALEQ HLPEDDKTPM SRRLEKTEPY FIGIFCFEAG IKIVALGFIF
160 170 180 190 200
HKGSYLRNGW NVMDFIVVLS GILATAGTHF NTHVDLRTLR AVRVLRPLKL
210 220 230 240 250
VSGIPSLQIV LKSIMKAMVP LLQIGLLLFF AILMFAIIGL EFYSGKLHRA
260 270 280 290 300
CFMNNSGILE GFDPPHPCGV QGCPAGYECK DWIGPNDGIT QFDNILFAVL
310 320 330 340 350
TVFQCITMEG WTTVLYNTND ALGATWNWLY FIPLIIIGSF FVLNLVLGVL
360 370 380 390 400
SGEFAKERER VENRRAFMKL RRQQQIEREL NGYRAWIDKA EEVMLAEENK
410 420 430 440 450
NAGTSALEVL RRATIKRSRT EAMTRDSSDE HCVDISSVGT PLARASIKSA
460 470 480 490 500
KVDGVSYFRH KERLLRISIR HMVKSQVFYW IVLSLVALNT ACVAIVHHNQ
510 520 530 540 550
PQWLTHLLYY AEFLFLGLFL LEMSLKMYGM GPRLYFHSSF NCFDFGVTVG
560 570 580 590 600
SIFEVVWAIF RPGTSFGISV LRALRLLRIF KITKYWASLR NLVVSLMSSM
610 620 630 640 650
KSIISLLFLL FLFIVVFALL GMQLFGGRFN FNDGTPSANF DTFPAAIMTV
660 670 680 690 700
FQILTGEDWN EVMYNGIRSQ GGVSSGMWSA IYFIVLTLFG NYTLLNVFLA
710 720 730 740 750
IAVDNLANAQ ELTKDEQEEE EAFNQKHALQ KAKEVSPMSA PNMPSIERDR
760 770 780 790 800
RRRHHMSMWE PRSSHLRERR RRHHMSVWEQ RTSQLRKHMQ MSSQEALNRE
810 820 830 840 850
EAPTMNPLNP LNPLSSLNPL NAHPSLYRRP RAIEGLALGL ALEKFEEERI
860 870 880 890 900
SRGGSLKGDG GDRSSALDNQ RTPLSLGQRE PPWLARPCHG NCDPTQQEAG
910 920 930 940 950
GGEAVVTFED RARHRQSQRR SRHRRVRTEG KESSSASRSR SASQERSLDE
960 970 980 990 1000
AMPTEGEKDH ELRGNHGAKE PTIQEERAQD LRRTNSLMVS RGSGLAGGLD
1010 1020 1030 1040 1050
EADTPLVLPH PELEVGKHVV LTEQEPEGSS EQALLGNVQL DMGRVISQSE
1060 1070 1080 1090 1100
PDLSCITANT DKATTESTSV TVAIPDVDPL VDSTVVHISN KTDGEASPLK
1110 1120 1130 1140 1150
EAEIREDEEE VEKKKQKKEK RETGKAMVPH SSMFIFSTTN PIRRACHYIV
1160 1170 1180 1190 1200
NLRYFEMCIL LVIAASSIAL AAEDPVLTNS ERNKVLRYFD YVFTGVFTFE
1210 1220 1230 1240 1250
MVIKMIDQGL ILQDGSYFRD LWNILDFVVV VGALVAFALA NALGTNKGRD
1260 1270 1280 1290 1300
IKTIKSLRVL RVLRPLKTIK RLPKLKAVFD CVVTSLKNVF NILIVYKLFM
1310 1320 1330 1340 1350
FIFAVIAVQL FKGKFFYCTD SSKDTEKECI GNYVDHEKNK MEVKGREWKR
1360 1370 1380 1390 1400
HEFHYDNIIW ALLTLFTVST GEGWPQVLQH SVDVTEEDRG PSRSNRMEMS
1410 1420 1430 1440 1450
IFYVVYFVVF PFFFVNIFVA LIIITFQEQG DKMMEECSLE KNERACIDFA
1460 1470 1480 1490 1500
ISAKPLTRYM PQNRHTFQYR VWHFVVSPSF EYTIMAMIAL NTVVLMMKYY
1510 1520 1530 1540 1550
SAPCTYELAL KYLNIAFTMV FSLECVLKVI AFGFLNYFRD TWNIFDFITV
1560 1570 1580 1590 1600
IGSITEIILT DSKLVNTSGF NMSFLKLFRA ARLIKLLRQG YTIRILLWTF
1610 1620 1630 1640 1650
VQSFKALPYV CLLIAMLFFI YAIIGMQVFG NIKLDEESHI NRHNNFRSFF
1660 1670 1680 1690 1700
GSLMLLFRSA TGEAWQEIML SCLGEKGCEP DTTAPSGQNE NERCGTDLAY
1710 1720 1730 1740 1750
VYFVSFIFFC SFLMLNLFVA VIMDNFEYLT RDSSILGPHH LDEFVRVWAE
1760 1770 1780 1790 1800
YDRAACGRIH YTEMYEMLTL MSPPLGLGKR CPSKVAYKRL VLMNMPVAED
1810 1820 1830 1840 1850
MTVHFTSTLM ALIRTALDIK IAKGGADRQQ LDSELQKETL AIWPHLSQKM
1860 1870 1880 1890 1900
LDLLVPMPKA SDLTVGKIYA AMMIMDYYKQ SKVKKQRQQL EEQKNAPMFQ
1910 1920 1930 1940 1950
RMEPSSLPQE IIANAKALPY LQQDPVSGLS GRSGYPSMSP LSPQDIFQLA
1960 1970 1980 1990 2000
CMDPADDGQF QERQSLEPEV SELKSVQPSN HGIYLPSDTQ EHAGSGRASS
2010 2020 2030 2040 2050
MPRLTVDPQV VTDPSSMRRS FSTIRDKRSN SSWLEEFSME RSSENTYKSR
2060 2070 2080 2090 2100
RRSYHSSLRL SAHRLNSDSG HKSDTHRSGG RERGRSKERK HLLSPDVSRC
2110 2120 2130 2140 2150
NSEERGTQAD WESPERRQSR SPSEGRSQTP NRQGTGSLSE SSIPSVSDTS
2160 2170 2180 2190 2200
TPRRSRRQLP PVPPKPRPLL SYSSLIRHAG SISPPADGSE EGSPLTSQAL
2210 2220 2230 2240 2250
ESNNACLTES SNSPHPQQSQ HASPQRYISE PYLALHEDSH ASDCGEEETL
2260 2270 2280 2290 2300
TFEAAVATSL GRSNTIGSAP PLRHSWQMPN GHYRRRRRGG PGPGMMCGAV
2310
NNLLSDTEED DKC
Length:2,313
Mass (Da):261,731
Last modified:October 14, 2008 - v3
Checksum:iCCC7F309C27C42F1
GO
Isoform 2 (identifier: Q15878-2) [UniParc]FASTAAdd to Basket

Also known as: Alpha-1E-1

The sequence of this isoform differs from the canonical sequence as follows:
     748-766: Missing.
     1967-2009: Missing.

Show »
Length:2,251
Mass (Da):254,604
Checksum:i73640AD59C386BB2
GO
Isoform 3 (identifier: Q15878-3) [UniParc]FASTAAdd to Basket

Also known as: Alpha-1E-3

The sequence of this isoform differs from the canonical sequence as follows:
     1967-2009: Missing.

Show »
Length:2,270
Mass (Da):257,116
Checksum:iD424C3592C9BD5F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti648 – 6481M → I in AAA72125. (PubMed:7536609)Curated
Sequence conflicti836 – 8383LAL → WP in AAA72125. (PubMed:7536609)Curated
Sequence conflicti2077 – 20771R → P in AAA59204. (PubMed:8071363)Curated
Sequence conflicti2077 – 20771R → P in AAA59205. (PubMed:8071363)Curated
Sequence conflicti2084 – 20841G → R in AAA59204. (PubMed:8071363)Curated
Sequence conflicti2084 – 20841G → R in AAA59205. (PubMed:8071363)Curated
Sequence conflicti2206 – 22061C → W in AAA59204. (PubMed:8071363)Curated
Sequence conflicti2206 – 22061C → W in AAA59205. (PubMed:8071363)Curated
Sequence conflicti2219 – 22191S → R in AAA59204. (PubMed:8071363)Curated
Sequence conflicti2219 – 22191S → R in AAA59205. (PubMed:8071363)Curated
Sequence conflicti2245 – 22451G → V in AAA59204. (PubMed:8071363)Curated
Sequence conflicti2245 – 22451G → V in AAA59205. (PubMed:8071363)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti859 – 8591D → E.
Corresponds to variant rs35737760 [ dbSNP | Ensembl ].
VAR_031912
Natural varianti1955 – 19551A → T.1 Publication
Corresponds to variant rs704326 [ dbSNP | Ensembl ].
VAR_046996

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei748 – 76619Missing in isoform 2. 1 PublicationVSP_000937Add
BLAST
Alternative sequencei1967 – 200943Missing in isoform 2 and isoform 3. 1 PublicationVSP_024817Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27745 mRNA. Translation: AAA72125.1.
L29384 mRNA. Translation: AAA59204.1.
L29385 mRNA. Translation: AAA59205.1.
AL161734
, AL160059, AL359270, AL590998 Genomic DNA. Translation: CAH72675.1.
AL161734
, AL160059, AL359270, AL590998 Genomic DNA. Translation: CAH72676.1.
AL161734
, AL160059, AL359270, AL590998 Genomic DNA. Translation: CAH72677.1.
AL359270
, AL160059, AL161734, AL590998 Genomic DNA. Translation: CAI14653.1.
AL359270
, AL160059, AL161734, AL590998 Genomic DNA. Translation: CAI14654.1.
AL359270
, AL160059, AL161734, AL590998 Genomic DNA. Translation: CAI14655.1.
AL160059
, AL161734, AL359270, AL590998 Genomic DNA. Translation: CAI17081.1.
AL160059
, AL161734, AL359270, AL590998 Genomic DNA. Translation: CAI17082.1.
AL160059
, AL161734, AL359270, AL590998 Genomic DNA. Translation: CAI17083.1.
AL590998
, AL160059, AL161734, AL359270 Genomic DNA. Translation: CAI22327.1.
AL590998
, AL160059, AL161734, AL359270 Genomic DNA. Translation: CAI22328.1.
AL590998
, AL160059, AL161734, AL359270 Genomic DNA. Translation: CAI22329.1.
CCDSiCCDS53443.1. [Q15878-3]
CCDS55664.1. [Q15878-1]
CCDS55665.1. [Q15878-2]
PIRiA54972.
B54972.
RefSeqiNP_000712.2. NM_000721.3. [Q15878-3]
NP_001192222.1. NM_001205293.1. [Q15878-1]
NP_001192223.1. NM_001205294.1. [Q15878-2]
UniGeneiHs.437444.

Genome annotation databases

EnsembliENST00000358338; ENSP00000351101; ENSG00000198216. [Q15878-2]
ENST00000367567; ENSP00000356539; ENSG00000198216. [Q15878-3]
ENST00000367570; ENSP00000356542; ENSG00000198216. [Q15878-3]
ENST00000367573; ENSP00000356545; ENSG00000198216. [Q15878-1]
ENST00000621551; ENSP00000483914; ENSG00000198216. [Q15878-1]
ENST00000621791; ENSP00000481619; ENSG00000198216. [Q15878-2]
GeneIDi777.
KEGGihsa:777.
UCSCiuc001gow.3. human. [Q15878-3]
uc009wxs.3. human. [Q15878-2]
uc009wxt.3. human. [Q15878-1]

Polymorphism databases

DMDMi209572758.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27745 mRNA. Translation: AAA72125.1 .
L29384 mRNA. Translation: AAA59204.1 .
L29385 mRNA. Translation: AAA59205.1 .
AL161734
, AL160059 , AL359270 , AL590998 Genomic DNA. Translation: CAH72675.1 .
AL161734
, AL160059 , AL359270 , AL590998 Genomic DNA. Translation: CAH72676.1 .
AL161734
, AL160059 , AL359270 , AL590998 Genomic DNA. Translation: CAH72677.1 .
AL359270
, AL160059 , AL161734 , AL590998 Genomic DNA. Translation: CAI14653.1 .
AL359270
, AL160059 , AL161734 , AL590998 Genomic DNA. Translation: CAI14654.1 .
AL359270
, AL160059 , AL161734 , AL590998 Genomic DNA. Translation: CAI14655.1 .
AL160059
, AL161734 , AL359270 , AL590998 Genomic DNA. Translation: CAI17081.1 .
AL160059
, AL161734 , AL359270 , AL590998 Genomic DNA. Translation: CAI17082.1 .
AL160059
, AL161734 , AL359270 , AL590998 Genomic DNA. Translation: CAI17083.1 .
AL590998
, AL160059 , AL161734 , AL359270 Genomic DNA. Translation: CAI22327.1 .
AL590998
, AL160059 , AL161734 , AL359270 Genomic DNA. Translation: CAI22328.1 .
AL590998
, AL160059 , AL161734 , AL359270 Genomic DNA. Translation: CAI22329.1 .
CCDSi CCDS53443.1. [Q15878-3 ]
CCDS55664.1. [Q15878-1 ]
CCDS55665.1. [Q15878-2 ]
PIRi A54972.
B54972.
RefSeqi NP_000712.2. NM_000721.3. [Q15878-3 ]
NP_001192222.1. NM_001205293.1. [Q15878-1 ]
NP_001192223.1. NM_001205294.1. [Q15878-2 ]
UniGenei Hs.437444.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BXL X-ray 2.30 B 1867-1887 [» ]
ProteinModelPortali Q15878.
SMRi Q15878. Positions 358-402, 1249-1276.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107231. 3 interactions.
STRINGi 9606.ENSP00000356545.

Chemistry

BindingDBi Q15878.
ChEMBLi CHEMBL2363032.
GuidetoPHARMACOLOGYi 534.

PTM databases

PhosphoSitei Q15878.

Polymorphism databases

DMDMi 209572758.

Proteomic databases

PaxDbi Q15878.
PRIDEi Q15878.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000358338 ; ENSP00000351101 ; ENSG00000198216 . [Q15878-2 ]
ENST00000367567 ; ENSP00000356539 ; ENSG00000198216 . [Q15878-3 ]
ENST00000367570 ; ENSP00000356542 ; ENSG00000198216 . [Q15878-3 ]
ENST00000367573 ; ENSP00000356545 ; ENSG00000198216 . [Q15878-1 ]
ENST00000621551 ; ENSP00000483914 ; ENSG00000198216 . [Q15878-1 ]
ENST00000621791 ; ENSP00000481619 ; ENSG00000198216 . [Q15878-2 ]
GeneIDi 777.
KEGGi hsa:777.
UCSCi uc001gow.3. human. [Q15878-3 ]
uc009wxs.3. human. [Q15878-2 ]
uc009wxt.3. human. [Q15878-1 ]

Organism-specific databases

CTDi 777.
GeneCardsi GC01P181382.
HGNCi HGNC:1392. CACNA1E.
HPAi HPA042515.
MIMi 601013. gene.
neXtProti NX_Q15878.
PharmGKBi PA26009.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1226.
GeneTreei ENSGT00760000118827.
HOGENOMi HOG000231530.
HOVERGENi HBG050763.
InParanoidi Q15878.
KOi K04852.
OMAi HMQMSSQ.
OrthoDBi EOG7T1RBQ.
PhylomeDBi Q15878.
TreeFami TF312805.

Enzyme and pathway databases

Reactomei REACT_13606. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.
REACT_18325. Regulation of insulin secretion.

Miscellaneous databases

ChiTaRSi CACNA1E. human.
EvolutionaryTracei Q15878.
GeneWikii R-type_calcium_channel.
GenomeRNAii 777.
NextBioi 3140.
PROi Q15878.
SOURCEi Search...

Gene expression databases

Bgeei Q15878.
CleanExi HS_CACNA1E.
ExpressionAtlasi Q15878. baseline and differential.
Genevestigatori Q15878.

Family and domain databases

Gene3Di 1.20.120.350. 4 hits.
InterProi IPR027359. Channel_four-helix_dom.
IPR002048. EF_hand_dom.
IPR005821. Ion_trans_dom.
IPR014873. VDCC_a1su_IQ.
IPR005449. VDCC_R_a1su.
IPR002077. VDCCAlpha1.
[Graphical view ]
PANTHERi PTHR10037:SF57. PTHR10037:SF57. 1 hit.
Pfami PF08763. Ca_chan_IQ. 1 hit.
PF00520. Ion_trans. 4 hits.
[Graphical view ]
PRINTSi PR00167. CACHANNEL.
PR01633. RVDCCALPHA1.
SMARTi SM01062. Ca_chan_IQ. 1 hit.
[Graphical view ]
PROSITEi PS50222. EF_HAND_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular analysis and functional expression of the human type E neuronal Ca2+ channel alpha 1 subunit."
    Schneider T., Wei X., Olcese R., Costantin J.L., Neely A., Palade P., Perez-Reyes E., Qin N., Zhou J., Crawford G.D., Smith R.G., Appel S.H., Stefani E., Birnbaumer M.
    Recept. Channels 2:255-270(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-1955.
    Tissue: Brain.
  2. "Structure and functional characterization of neuronal alpha 1E calcium channel subtypes."
    Williams M.E., Marubio L.M., Deal C.R., Hans M., Brust P.F., Philipson L.H., Miller R.J., Johnson E.C., Harpold M.M., Ellis S.B.
    J. Biol. Chem. 269:22347-22357(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
    Tissue: Hippocampus.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: INTERACTION WITH CACNA1E.
  5. "Crystal structure of the CaV2 IQ domain in complex with Ca2+/calmodulin: high-resolution mechanistic implications for channel regulation by Ca2+."
    Mori M.X., Vander Kooi C.W., Leahy D.J., Yue D.T.
    Structure 16:607-620(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1867-1885.

Entry informationi

Entry nameiCAC1E_HUMAN
AccessioniPrimary (citable) accession number: Q15878
Secondary accession number(s): B1AM12
, B1AM13, B1AM14, Q14580, Q14581
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: October 14, 2008
Last modified: November 26, 2014
This is version 145 of the entry and version 3 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 1
    Human chromosome 1: 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

External Data

Dasty 3