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Q00975

- CAC1B_HUMAN

UniProt

Q00975 - CAC1B_HUMAN

Protein

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

Gene

CACNA1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Sitei314 – 3141Calcium ion selectivity and permeabilityBy similarity
    Sitei663 – 6631Calcium ion selectivity and permeabilityBy similarity
    Sitei1365 – 13651Calcium ion selectivity and permeabilityBy similarity
    Sitei1655 – 16551Calcium ion selectivity and permeabilityBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi451 – 4588ATPSequence Analysis
    Calcium bindingi1737 – 174812PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium ion binding Source: InterPro
    3. high voltage-gated calcium channel activity Source: RefGenome
    4. protein binding Source: UniProtKB
    5. protein C-terminus binding Source: UniProtKB
    6. voltage-gated calcium channel activity Source: ProtInc

    GO - Biological processi

    1. calcium ion import Source: RefGenome
    2. locomotory behavior Source: Ensembl
    3. membrane depolarization Source: Reactome
    4. membrane depolarization during action potential Source: RefGenome
    5. neurotransmitter secretion Source: Ensembl
    6. regulation of blood pressure Source: Ensembl
    7. regulation of calcium ion transport Source: Ensembl
    8. regulation of heart contraction Source: Ensembl
    9. response to pain Source: Ensembl
    10. synaptic transmission Source: RefGenome
    11. transport Source: ProtInc

    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

    ReactomeiREACT_13606. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.

    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
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:1389. CACNA1B.

    Subcellular locationi

    GO - Cellular componenti

    1. dendrite Source: Ensembl
    2. neuronal cell body Source: Ensembl
    3. plasma membrane Source: RefGenome
    4. voltage-gated calcium channel complex Source: ProtInc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26008.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 23392339Voltage-dependent N-type calcium channel subunit alpha-1BPRO_0000053921Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
    Modified residuei783 – 7831PhosphoserineBy similarity
    Glycosylationi1563 – 15631N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1675 – 16751N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1719 – 17191Phosphoserine; by PKASequence Analysis

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ00975.
    PRIDEiQ00975.

    PTM databases

    PhosphoSiteiQ00975.

    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

    ArrayExpressiQ00975.
    BgeeiQ00975.
    CleanExiHS_CACNA1B.
    GenevestigatoriQ00975.

    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 and RIMBP2 By similarity.By similarity

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi107228. 7 interactions.
    IntActiQ00975. 6 interactions.
    MINTiMINT-102376.
    STRINGi9606.ENSP00000277549.

    Structurei

    Secondary structure

    1
    2339
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1244 – 126320
    Turni1264 – 12663

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LCMNMR-A1242-1269[»]
    ProteinModelPortaliQ00975.
    SMRiQ00975. Positions 97-407, 475-710, 1146-1417, 1473-1709.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 9595CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini115 – 13218ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini153 – 16311CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini184 – 1874ExtracellularSequence Analysis
    Topological domaini207 – 22519CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini246 – 33186ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini357 – 482126CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini502 – 51615ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini537 – 5448CytoplasmicSequence Analysis
    Topological domaini563 – 57311ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini593 – 61119CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini632 – 68453ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini710 – 1151442CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1170 – 118516ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1206 – 121712CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1237 – 124610ExtracellularSequence Analysis
    Topological domaini1266 – 128419CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1305 – 139187ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1417 – 147155CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1491 – 150515ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1526 – 15338CytoplasmicSequence Analysis
    Topological domaini1553 – 156311ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1583 – 160119CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini1622 – 168362ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1709 – 2339631CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei96 – 11419Helical; Name=S1 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei133 – 15220Helical; Name=S2 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei164 – 18320Helical; Name=S3 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei188 – 20619Helical; Name=S4 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei226 – 24520Helical; Name=S5 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei332 – 35625Helical; Name=S6 of repeat ISequence AnalysisAdd
    BLAST
    Transmembranei483 – 50119Helical; Name=S1 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei517 – 53620Helical; Name=S2 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei545 – 56218Helical; Name=S3 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei574 – 59219Helical; Name=S4 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei612 – 63120Helical; Name=S5 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei685 – 70925Helical; Name=S6 of repeat IISequence AnalysisAdd
    BLAST
    Transmembranei1152 – 116918Helical; Name=S1 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1186 – 120520Helical; Name=S2 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1218 – 123619Helical; Name=S3 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1247 – 126519Helical; Name=S4 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1285 – 130420Helical; Name=S5 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1392 – 141625Helical; Name=S6 of repeat IIISequence AnalysisAdd
    BLAST
    Transmembranei1472 – 149019Helical; Name=S1 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1506 – 152520Helical; Name=S2 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1534 – 155219Helical; Name=S3 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1564 – 158219Helical; Name=S4 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1602 – 162120Helical; Name=S5 of repeat IVSequence AnalysisAdd
    BLAST
    Transmembranei1684 – 170825Helical; Name=S6 of repeat IVSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati82 – 359278IAdd
    BLAST
    Repeati468 – 712245IIAdd
    BLAST
    Repeati1137 – 1419283IIIAdd
    BLAST
    Repeati1456 – 1711256IVAdd
    BLAST
    Domaini1724 – 175936EF-handPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni379 – 39618Binding to the beta subunitBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi2050 – 20545Poly-His
    Compositional biasi2118 – 21225Poly-Ser

    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.
    HOGENOMiHOG000231530.
    HOVERGENiHBG050763.
    KOiK04849.
    PhylomeDBiQ00975.

    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.
    IPR005447. VDCC_N_a1su.
    IPR002077. VDCCAlpha1.
    [Graphical view]
    PfamiPF08763. Ca_chan_IQ. 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. Align

    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

    MVRFGDELGG RYGGPGGGER ARGGGAGGAG GPGPGGLQPG QRVLYKQSIA     50
    QRARTMALYN PIPVKQNCFT VNRSLFVFSE DNVVRKYAKR ITEWPPFEYM 100
    ILATIIANCI VLALEQHLPD GDKTPMSERL DDTEPYFIGI FCFEAGIKII 150
    ALGFVFHKGS YLRNGWNVMD FVVVLTGILA TAGTDFDLRT LRAVRVLRPL 200
    KLVSGIPSLQ VVLKSIMKAM VPLLQIGLLL FFAILMFAII GLEFYMGKFH 250
    KACFPNSTDA EPVGDFPCGK EAPARLCEGD TECREYWPGP NFGITNFDNI 300
    LFAILTVFQC ITMEGWTDIL YNTNDAAGNT WNWLYFIPLI IIGSFFMLNL 350
    VLGVLSGEFA KERERVENRR AFLKLRRQQQ IERELNGYLE WIFKAEEVML 400
    AEEDRNAEEK SPLDVLKRAA TKKSRNDLIH AEEGEDRFAD LCAVGSPFAR 450
    ASLKSGKTES SSYFRRKEKM FRFFIRRMVK AQSFYWVVLC VVALNTLCVA 500
    MVHYNQPRRL TTTLYFAEFV FLGLFLTEMS LKMYGLGPRS YFRSSFNCFD 550
    FGVIVGSVFE VVWAAIKPGS SFGISVLRAL RLLRIFKVTK YWSSLRNLVV 600
    SLLNSMKSII SLLFLLFLFI VVFALLGMQL FGGQFNFQDE TPTTNFDTFP 650
    AAILTVFQIL TGEDWNAVMY HGIESQGGVS KGMFSSFYFI VLTLFGNYTL 700
    LNVFLAIAVD NLANAQELTK DEEEMEEAAN QKLALQKAKE VAEVSPMSAA 750
    NISIAARQQN SAKARSVWEQ RASQLRLQNL RASCEALYSE MDPEERLRFA 800
    TTRHLRPDMK THLDRPLVVE LGRDGARGPV GGKARPEAAE APEGVDPPRR 850
    HHRHRDKDKT PAAGDQDRAE APKAESGEPG AREERPRPHR SHSKEAAGPP 900
    EARSERGRGP GPEGGRRHHR RGSPEEAAER EPRRHRAHRH QDPSKECAGA 950
    KGERRARHRG GPRAGPREAE SGEEPARRHR ARHKAQPAHE AVEKETTEKE 1000
    ATEKEAEIVE ADKEKELRNH QPREPHCDLE TSGTVTVGPM HTLPSTCLQK 1050
    VEEQPEDADN QRNVTRMGSQ PPDPNTIVHI PVMLTGPLGE ATVVPSGNVD 1100
    LESQAEGKKE VEADDVMRSG PRPIVPYSSM FCLSPTNLLR RFCHYIVTMR 1150
    YFEVVILVVI ALSSIALAAE DPVRTDSPRN NALKYLDYIF TGVFTFEMVI 1200
    KMIDLGLLLH PGAYFRDLWN ILDFIVVSGA LVAFAFSGSK GKDINTIKSL 1250
    RVLRVLRPLK TIKRLPKLKA VFDCVVNSLK NVLNILIVYM LFMFIFAVIA 1300
    VQLFKGKFFY CTDESKELER DCRGQYLDYE KEEVEAQPRQ WKKYDFHYDN 1350
    VLWALLTLFT VSTGEGWPMV LKHSVDATYE EQGPSPGYRM ELSIFYVVYF 1400
    VVFPFFFVNI FVALIIITFQ EQGDKVMSEC SLEKNERACI DFAISAKPLT 1450
    RYMPQNRQSF QYKTWTFVVS PPFEYFIMAM IALNTVVLMM KFYDAPYEYE 1500
    LMLKCLNIVF TSMFSMECVL KIIAFGVLNY FRDAWNVFDF VTVLGSITDI 1550
    LVTEIAETNN FINLSFLRLF RAARLIKLLR QGYTIRILLW TFVQSFKALP 1600
    YVCLLIAMLF FIYAIIGMQV FGNIALDDDT SINRHNNFRT FLQALMLLFR 1650
    SATGEAWHEI MLSCLSNQAC DEQANATECG SDFAYFYFVS FIFLCSFLML 1700
    NLFVAVIMDN FEYLTRDSSI LGPHHLDEFI RVWAEYDPAA CGRISYNDMF 1750
    EMLKHMSPPL GLGKKCPARV AYKRLVRMNM PISNEDMTVH FTSTLMALIR 1800
    TALEIKLAPA GTKQHQCDAE LRKEISVVWA NLPQKTLDLL VPPHKPDEMT 1850
    VGKVYAALMI FDFYKQNKTT RDQMQQAPGG LSQMGPVSLF HPLKATLEQT 1900
    QPAVLRGARV FLRQKSSTSL SNGGAIQNQE SGIKESVSWG TQRTQDAPHE 1950
    ARPPLERGHS TEIPVGRSGA LAVDVQMQSI TRRGPDGEPQ PGLESQGRAA 2000
    SMPRLAAETQ PVTDASPMKR SISTLAQRPR GTHLCSTTPD RPPPSQASSH 2050
    HHHHRCHRRR DRKQRSLEKG PSLSADMDGA PSSAVGPGLP PGEGPTGCRR 2100
    ERERRQERGR SQERRQPSSS SSEKQRFYSC DRFGGREPPK PKPSLSSHPT 2150
    SPTAGQEPGP HPQGSGSVNG SPLLSTSGAS TPGRGGRRQL PQTPLTPRPS 2200
    ITYKTANSSP IHFAGAQTSL PAFSPGRLSR GLSEHNALLQ RDPLSQPLAP 2250
    GSRIGSDPYL GQRLDSEASV HALPEDTLTF EEAVATNSGR SSRTSYVSSL 2300
    TSQSHPLRRV PNGYHCTLGL SSGGRARHSY HHPDQDHWC 2339
    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)LengthDescriptionGraphical viewFeature identifierActions
    Isoform Alpha-1B-2 (identifier: Q00975-2)
    Sequence conflicti2215 – 22151L → R in AAA51898. (PubMed:1321501)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti167 – 1671N → K.
    Corresponds to variant rs4422842 [ dbSNP | Ensembl ].
    VAR_048741
    Natural varianti862 – 8621A → S.
    Corresponds to variant rs7873074 [ dbSNP | Ensembl ].
    VAR_061100
    Natural varianti996 – 9961T → A.
    Corresponds to variant rs11137342 [ dbSNP | Ensembl ].
    VAR_061101
    Natural varianti1436 – 14361E → K.
    Corresponds to variant rs12377346 [ dbSNP | Ensembl ].
    VAR_048742
    Natural varianti1500 – 15001E → K.
    Corresponds to variant rs12377346 [ dbSNP | Ensembl ].
    VAR_048743

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2164 – 2339176GSGSV…QDHWC → AGSAVGFPNTTPCCRETPSA SPWPLALELALTLTWGSVWT VRPLSTPCLRTLSLSRRLWP PTRAAPPGLPTCPP in isoform Alpha-1B-2. 1 PublicationVSP_000882Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    UniGeneiHs.495522.

    Genome annotation databases

    EnsembliENST00000277551; ENSP00000277551; ENSG00000148408. [Q00975-2]
    ENST00000371372; ENSP00000360423; ENSG00000148408. [Q00975-1]
    GeneIDi774.
    KEGGihsa:774.
    UCSCiuc004cog.3. human. [Q00975-1]

    Polymorphism databases

    DMDMi1705854.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS59522.1. [Q00975-1 ]
    CCDS59523.1. [Q00975-2 ]
    PIRi A42566.
    T45115.
    RefSeqi NP_000709.1. NM_000718.3. [Q00975-1 ]
    NP_001230741.1. NM_001243812.1.
    UniGenei Hs.495522.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LCM NMR - A 1242-1269 [» ]
    ProteinModelPortali Q00975.
    SMRi Q00975. Positions 97-407, 475-710, 1146-1417, 1473-1709.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107228. 7 interactions.
    IntActi Q00975. 6 interactions.
    MINTi MINT-102376.
    STRINGi 9606.ENSP00000277549.

    Chemistry

    BindingDBi Q00975.
    ChEMBLi CHEMBL2363032.
    DrugBanki DB00381. Amlodipine.
    DB00996. Gabapentin.
    GuidetoPHARMACOLOGYi 533.

    PTM databases

    PhosphoSitei Q00975.

    Polymorphism databases

    DMDMi 1705854.

    Proteomic databases

    PaxDbi Q00975.
    PRIDEi Q00975.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000277551 ; ENSP00000277551 ; ENSG00000148408 . [Q00975-2 ]
    ENST00000371372 ; ENSP00000360423 ; ENSG00000148408 . [Q00975-1 ]
    GeneIDi 774.
    KEGGi hsa:774.
    UCSCi uc004cog.3. human. [Q00975-1 ]

    Organism-specific databases

    CTDi 774.
    GeneCardsi GC09P140772.
    HGNCi HGNC:1389. CACNA1B.
    HPAi HPA044347.
    MIMi 601012. gene.
    neXtProti NX_Q00975.
    PharmGKBi PA26008.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1226.
    HOGENOMi HOG000231530.
    HOVERGENi HBG050763.
    KOi K04849.
    PhylomeDBi Q00975.

    Enzyme and pathway databases

    Reactomei REACT_13606. Depolarization of the Presynaptic Terminal Triggers the Opening of Calcium Channels.

    Miscellaneous databases

    GeneWikii N-type_calcium_channel.
    GenomeRNAii 774.
    NextBioi 3128.
    PROi Q00975.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00975.
    Bgeei Q00975.
    CleanExi HS_CACNA1B.
    Genevestigatori Q00975.

    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.
    IPR005447. VDCC_N_a1su.
    IPR002077. VDCCAlpha1.
    [Graphical view ]
    Pfami PF08763. Ca_chan_IQ. 1 hit.
    PF00520. Ion_trans. 4 hits.
    [Graphical view ]
    PRINTSi PR00167. CACHANNEL.
    PR01631. NVDCCALPHA1.
    SMARTi SM01062. Ca_chan_IQ. 1 hit.
    [Graphical view ]
    PROSITEi PS50222. EF_HAND_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and functional expression of an omega-conotoxin-sensitive human N-type calcium channel."
      Williams M.E., Brust P.F., Feldman D.H., Patthi S., Simerson S., Maroufi A., McCue A.F., Velicelebi G., Ellis S.B., Harpold M.M.
      Science 257:389-395(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA-1B-1 AND ALPHA-1B-2).
      Tissue: Brain.
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Isolation and characterization of the 5'-upstream region of the human N-type calcium channel alpha1B subunit gene. Chromosomal localization and promoter analysis."
      Kim D.S., Jung H.-H., Park S.-H., Chin H.
      J. Biol. Chem. 272:5098-5104(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-94.
      Tissue: Lung fibroblast.

    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: October 1, 2014
    This is version 141 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

    External Data

    Dasty 3