CACB2_HUMAN
ID CACB2_HUMAN Reviewed; 660 AA.
AC Q08289; A6PVM5; A6PVM7; A6PVM8; O00304; Q5QJ99; Q5QJA0; Q5VVG9; Q5VVH0;
AC Q5VWV6; Q6TME1; Q6TME2; Q6TME3; Q8WX81; Q96NZ3; Q96NZ4; Q96NZ5; Q9BWU2;
AC Q9HD32; Q9Y340; Q9Y341;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Voltage-dependent L-type calcium channel subunit beta-2;
DE Short=CAB2;
DE AltName: Full=Calcium channel voltage-dependent subunit beta 2;
DE AltName: Full=Lambert-Eaton myasthenic syndrome antigen B;
DE Short=MYSB;
GN Name=CACNB2; Synonyms=CACNLB2, MYSB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2A; 2G AND 2H).
RC TISSUE=Fetal brain;
RX PubMed=8494331; DOI=10.1002/ana.410330126;
RA Rosenfeld M.R., Wong E., Dalmau J., Manley G., Posner J.B., Sher E.,
RA Furneaux H.M.;
RT "Cloning and characterization of a Lambert-Eaton myasthenic syndrome
RT antigen.";
RL Ann. Neurol. 33:113-120(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2A).
RC TISSUE=Brain;
RX PubMed=9254841; DOI=10.1007/pl00008704;
RA Taviaux S., Williams M.E., Harpold M.M., Nargeot J., Lory P.;
RT "Assignment of human genes for beta 2 and beta 4 subunits of voltage-
RT dependent Ca2+ channels to chromosomes 10p12 and 2q22-q23.";
RL Hum. Genet. 100:151-154(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2A; 2B; 2C; 2D AND 2E).
RX PubMed=12042350; DOI=10.1113/jphysiol.2002.018515;
RA Colecraft H.M., Alseikhan B., Takahashi S.X., Chaudhuri D., Mittman S.,
RA Yegnasubramanian V., Alvania R.S., Johns D.C., Marban E., Yue D.T.;
RT "Novel functional properties of Ca(2+) channel beta subunits revealed by
RT their expression in adult rat heart cells.";
RL J. Physiol. (Lond.) 541:435-452(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2B; 2C; 2H; 2CN2 AND 2CN4),
RP ALTERNATIVE SPLICING, AND SUBCELLULAR LOCATION.
RC TISSUE=Heart;
RX PubMed=14762176; DOI=10.1152/physiolgenomics.00207.2003;
RA Foell J.D., Balijepalli R.C., Delisle B.P., Yunker A.M.R., Robia S.L.,
RA Walker J.W., McEnery M.W., January C.T., Kamp T.J.;
RT "Molecular heterogeneity of calcium channel beta-subunits in canine and
RT human heart: evidence for differential subcellular localization.";
RL Physiol. Genomics 17:183-200(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2A AND 2D).
RA Mikala G., Yamaguchi H., Schwartz A.;
RT "Cooperative effects of alpha2delta and beta2a subunits on surface
RT expression of calcium channel alpha1c subunits.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2A).
RA Li D., Roberts R.;
RT "The beta 2 subunit of the voltage-dependent calcium channel (CACNB2):
RT genomic structure and mutational analysis as a candidate gene for ARVD6.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2F).
RC TISSUE=Jejunum;
RA Lyford G.L., Strege P., Shepard A., Miller S., Rae J., Gibbons S.,
RA Szurszewski J., Farrugia G.;
RT "Human jejunum voltage-gated calcium channel subunits.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP INTERACTION WITH RRAD.
RX PubMed=17525370; DOI=10.1161/circresaha.106.146399;
RA Yada H., Murata M., Shimoda K., Yuasa S., Kawaguchi H., Ieda M., Adachi T.,
RA Murata M., Ogawa S., Fukuda K.;
RT "Dominant negative suppression of Rad leads to QT prolongation and causes
RT ventricular arrhythmias via modulation of L-type Ca2+ channels in the
RT heart.";
RL Circ. Res. 101:69-77(2007).
RN [12]
RP INTERACTION WITH TMIGD2.
RX PubMed=22419821; DOI=10.1091/mbc.e11-11-0934;
RA Rahimi N., Rezazadeh K., Mahoney J.E., Hartsough E., Meyer R.D.;
RT "Identification of IGPR-1 as a novel adhesion molecule involved in
RT angiogenesis.";
RL Mol. Biol. Cell 23:1646-1656(2012).
RN [13]
RP INTERACTION WITH CAMK2A.
RX PubMed=28130356; DOI=10.1523/jneurosci.2068-16.2017;
RA Stephenson J.R., Wang X., Perfitt T.L., Parrish W.P., Shonesy B.C.,
RA Marks C.R., Mortlock D.P., Nakagawa T., Sutcliffe J.S., Colbran R.J.;
RT "Mutation Disrupts Dendritic Morphology and Synaptic Transmission, and
RT Causes ASD-Related Behaviors.";
RL J. Neurosci. 37:2216-2233(2017).
RN [14]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-99.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [15]
RP VARIANT BRGDA4 LEU-535, AND CHARACTERIZATION OF VARIANT BRGDA4 LEU-535.
RX PubMed=17224476; DOI=10.1161/circulationaha.106.668392;
RA Antzelevitch C., Pollevick G.D., Cordeiro J.M., Casis O., Sanguinetti M.C.,
RA Aizawa Y., Guerchicoff A., Pfeiffer R., Oliva A., Wollnik B., Gelber P.,
RA Bonaros E.P. Jr., Burashnikov E., Wu Y., Sargent J.D., Schickel S.,
RA Oberheiden R., Bhatia A., Hsu L.F., Haissaguerre M., Schimpf R.,
RA Borggrefe M., Wolpert C.;
RT "Loss-of-function mutations in the cardiac calcium channel underlie a new
RT clinical entity characterized by ST-segment elevation, short QT intervals,
RT and sudden cardiac death.";
RL Circulation 115:442-449(2007).
CC -!- FUNCTION: The beta subunit of voltage-dependent calcium channels
CC contributes to the function of the calcium channel by increasing peak
CC calcium current, shifting the voltage dependencies of activation and
CC inactivation, modulating G protein inhibition and controlling the
CC alpha-1 subunit membrane targeting.
CC -!- SUBUNIT: Component of a calcium channel complex consisting of a pore-
CC forming alpha subunit (CACNA1S) and the ancillary subunits CACNB1 or
CC CACNB2, CACNG1 and CACNA2D1. The channel complex contains alpha, beta,
CC gamma and delta subunits in a 1:1:1:1 ratio, i.e. it contains either
CC CACNB1 or CACNB2. Interacts with CACNA1C (By similarity). Interacts
CC with RRAD. Interaction with RRAD regulates the trafficking of CACNA1C
CC to the cell membrane (PubMed:17525370). Interacts with TMIGD2
CC (PubMed:22419821). Interacts with CAMK2D. Interacts with CBARP (By
CC similarity). Interacts with CAMK2A (PubMed:28130356).
CC {ECO:0000250|UniProtKB:Q8VGC3, ECO:0000269|PubMed:17525370,
CC ECO:0000269|PubMed:22419821, ECO:0000269|PubMed:28130356}.
CC -!- INTERACTION:
CC Q08289; P56545-3: CTBP2; NbExp=5; IntAct=EBI-2874501, EBI-10171902;
CC Q08289; Q96MH2: HEXIM2; NbExp=3; IntAct=EBI-2874501, EBI-5460660;
CC Q08289; O14744: PRMT5; NbExp=3; IntAct=EBI-2874501, EBI-351098;
CC Q08289; Q8WUU8: TMEM174; NbExp=3; IntAct=EBI-2874501, EBI-10276729;
CC Q08289-1; Q13936: CACNA1C; NbExp=4; IntAct=EBI-15707999, EBI-1038838;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=2d; Synonyms=CACNB2d;
CC IsoId=Q08289-1; Sequence=Displayed;
CC Name=2a; Synonyms=CACNB2a;
CC IsoId=Q08289-2; Sequence=VSP_000627;
CC Name=2b; Synonyms=CACNB2b, 2aN4;
CC IsoId=Q08289-3; Sequence=VSP_000628;
CC Name=2c; Synonyms=CACNB2c, 2aN2;
CC IsoId=Q08289-4; Sequence=VSP_000626;
CC Name=2e; Synonyms=CACNB2e;
CC IsoId=Q08289-5; Sequence=VSP_000629;
CC Name=2f;
CC IsoId=Q08289-6; Sequence=VSP_000627, VSP_000630;
CC Name=2g;
CC IsoId=Q08289-7; Sequence=VSP_000630;
CC Name=2h; Synonyms=2cN1;
CC IsoId=Q08289-8; Sequence=VSP_000631;
CC Name=2cN2;
CC IsoId=Q08289-9; Sequence=VSP_000626, VSP_000631;
CC Name=2cN4;
CC IsoId=Q08289-10; Sequence=VSP_000628, VSP_000631;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues.
CC -!- PTM: Regulated through phosphorylation at Thr-554 by CaMK2D.
CC {ECO:0000250}.
CC -!- DISEASE: Brugada syndrome 4 (BRGDA4) [MIM:611876]: A heart disease
CC characterized by the association of Brugada syndrome with shortened QT
CC intervals. Brugada syndrome is a tachyarrhythmia characterized by right
CC bundle branch block and ST segment elevation on an electrocardiogram
CC (ECG). It can cause the ventricles to beat so fast that the blood is
CC prevented from circulating efficiently in the body. When this situation
CC occurs, the individual will faint and may die in a few minutes if the
CC heart is not reset. {ECO:0000269|PubMed:17224476}. Note=The gene
CC represented in this entry may be involved in disease pathogenesis.
CC -!- SIMILARITY: Belongs to the calcium channel beta subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51370.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; S60415; AAB51370.1; ALT_FRAME; mRNA.
DR EMBL; U95019; AAB53332.1; -; mRNA.
DR EMBL; AF423189; AAL16948.1; -; mRNA.
DR EMBL; AF423190; AAL16949.1; -; mRNA.
DR EMBL; AF423191; AAL16950.1; -; mRNA.
DR EMBL; AF423192; AAL16951.1; -; mRNA.
DR EMBL; AF285239; AAG01473.2; -; mRNA.
DR EMBL; AY393858; AAQ97606.1; -; mRNA.
DR EMBL; AY393859; AAQ97607.1; -; mRNA.
DR EMBL; AY393860; AAQ97608.1; -; mRNA.
DR EMBL; AY393861; AAQ97609.1; -; mRNA.
DR EMBL; AY393862; AAQ97610.1; -; mRNA.
DR EMBL; AF137376; AAD33729.1; -; mRNA.
DR EMBL; AF137377; AAD33730.1; -; mRNA.
DR EMBL; AY027898; AAK16994.1; -; Genomic_DNA.
DR EMBL; AY027893; AAK16994.1; JOINED; Genomic_DNA.
DR EMBL; AY027894; AAK16994.1; JOINED; Genomic_DNA.
DR EMBL; AY027895; AAK16994.1; JOINED; Genomic_DNA.
DR EMBL; AY027896; AAK16994.1; JOINED; Genomic_DNA.
DR EMBL; AY027897; AAK16994.1; JOINED; Genomic_DNA.
DR EMBL; AF465485; AAL73495.1; -; mRNA.
DR EMBL; AL139814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL360231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450364; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL450384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86196.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86197.1; -; Genomic_DNA.
DR EMBL; BC136409; AAI36410.1; -; mRNA.
DR CCDS; CCDS41493.1; -. [Q08289-9]
DR CCDS; CCDS41494.1; -. [Q08289-3]
DR CCDS; CCDS7125.1; -. [Q08289-1]
DR CCDS; CCDS7126.1; -. [Q08289-8]
DR CCDS; CCDS7127.1; -. [Q08289-4]
DR CCDS; CCDS7128.1; -. [Q08289-2]
DR CCDS; CCDS7129.1; -. [Q08289-5]
DR CCDS; CCDS81442.1; -. [Q08289-6]
DR PIR; A48895; A48895.
DR RefSeq; NP_000715.2; NM_000724.3. [Q08289-2]
DR RefSeq; NP_001316989.1; NM_001330060.1. [Q08289-6]
DR RefSeq; NP_963864.1; NM_201570.2. [Q08289-5]
DR RefSeq; NP_963865.2; NM_201571.3. [Q08289-4]
DR RefSeq; NP_963866.2; NM_201572.3. [Q08289-9]
DR RefSeq; NP_963884.2; NM_201590.2. [Q08289-3]
DR RefSeq; NP_963887.2; NM_201593.2. [Q08289-7]
DR RefSeq; NP_963890.2; NM_201596.2. [Q08289-1]
DR RefSeq; NP_963891.1; NM_201597.2. [Q08289-8]
DR RefSeq; XP_011517961.1; XM_011519659.2. [Q08289-10]
DR AlphaFoldDB; Q08289; -.
DR SMR; Q08289; -.
DR BioGRID; 107237; 9.
DR ComplexPortal; CPX-3195; Cardiac muscle voltage-gated calcium channel complex.
DR IntAct; Q08289; 9.
DR MINT; Q08289; -.
DR STRING; 9606.ENSP00000320025; -.
DR BindingDB; Q08289; -.
DR ChEMBL; CHEMBL3317336; -.
DR DrugBank; DB01118; Amiodarone.
DR DrugBank; DB09231; Benidipine.
DR DrugBank; DB13746; Bioallethrin.
DR DrugBank; DB11148; Butamben.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR DrugBank; DB09232; Cilnidipine.
DR DrugBank; DB04855; Dronedarone.
DR DrugBank; DB06751; Drotaverine.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB00153; Ergocalciferol.
DR DrugBank; DB01023; Felodipine.
DR DrugBank; DB13961; Fish oil.
DR DrugBank; DB00270; Isradipine.
DR DrugBank; DB09236; Lacidipine.
DR DrugBank; DB00825; Levomenthol.
DR DrugBank; DB00653; Magnesium sulfate.
DR DrugBank; DB09238; Manidipine.
DR DrugBank; DB01388; Mibefradil.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB00622; Nicardipine.
DR DrugBank; DB01115; Nifedipine.
DR DrugBank; DB06712; Nilvadipine.
DR DrugBank; DB00393; Nimodipine.
DR DrugBank; DB00401; Nisoldipine.
DR DrugBank; DB01054; Nitrendipine.
DR DrugBank; DB00252; Phenytoin.
DR DrugBank; DB00243; Ranolazine.
DR DrugBank; DB00421; Spironolactone.
DR DrugBank; DB00273; Topiramate.
DR DrugBank; DB09089; Trimebutine.
DR TCDB; 8.A.22.1.2; the ca(2+) channel auxiliary subunit Beta types 1-4 (cca-Beta) family.
DR iPTMnet; Q08289; -.
DR PhosphoSitePlus; Q08289; -.
DR BioMuta; CACNB2; -.
DR DMDM; 145559447; -.
DR EPD; Q08289; -.
DR jPOST; Q08289; -.
DR MassIVE; Q08289; -.
DR MaxQB; Q08289; -.
DR PaxDb; Q08289; -.
DR PeptideAtlas; Q08289; -.
DR PRIDE; Q08289; -.
DR ProteomicsDB; 1694; -.
DR ProteomicsDB; 58586; -. [Q08289-1]
DR ProteomicsDB; 58587; -. [Q08289-2]
DR ProteomicsDB; 58588; -. [Q08289-3]
DR ProteomicsDB; 58589; -. [Q08289-4]
DR ProteomicsDB; 58590; -. [Q08289-5]
DR ProteomicsDB; 58591; -. [Q08289-6]
DR ProteomicsDB; 58592; -. [Q08289-7]
DR ProteomicsDB; 58593; -. [Q08289-8]
DR ABCD; Q08289; 1 sequenced antibody.
DR Antibodypedia; 12067; 579 antibodies from 35 providers.
DR DNASU; 783; -.
DR Ensembl; ENST00000282343.13; ENSP00000282343.8; ENSG00000165995.23. [Q08289-4]
DR Ensembl; ENST00000324631.13; ENSP00000320025.8; ENSG00000165995.23. [Q08289-1]
DR Ensembl; ENST00000352115.10; ENSP00000344474.6; ENSG00000165995.23. [Q08289-8]
DR Ensembl; ENST00000377315.5; ENSP00000366532.4; ENSG00000165995.23. [Q08289-5]
DR Ensembl; ENST00000377319.8; ENSP00000366536.3; ENSG00000165995.23. [Q08289-6]
DR Ensembl; ENST00000377329.10; ENSP00000366546.4; ENSG00000165995.23. [Q08289-3]
DR Ensembl; ENST00000396576.6; ENSP00000379821.2; ENSG00000165995.23. [Q08289-2]
DR Ensembl; ENST00000645287.1; ENSP00000496203.1; ENSG00000165995.23. [Q08289-9]
DR GeneID; 783; -.
DR KEGG; hsa:783; -.
DR MANE-Select; ENST00000324631.13; ENSP00000320025.8; NM_201596.3; NP_963890.2.
DR UCSC; uc001ipr.3; human. [Q08289-1]
DR CTD; 783; -.
DR DisGeNET; 783; -.
DR GeneCards; CACNB2; -.
DR GeneReviews; CACNB2; -.
DR HGNC; HGNC:1402; CACNB2.
DR HPA; ENSG00000165995; Tissue enhanced (retina).
DR MalaCards; CACNB2; -.
DR MIM; 600003; gene.
DR MIM; 611876; phenotype.
DR neXtProt; NX_Q08289; -.
DR OpenTargets; ENSG00000165995; -.
DR Orphanet; 130; Brugada syndrome.
DR PharmGKB; PA88; -.
DR VEuPathDB; HostDB:ENSG00000165995; -.
DR eggNOG; KOG3812; Eukaryota.
DR GeneTree; ENSGT00950000182837; -.
DR HOGENOM; CLU_021995_3_0_1; -.
DR InParanoid; Q08289; -.
DR OMA; IVVYVKI; -.
DR OrthoDB; 926074at2759; -.
DR PhylomeDB; Q08289; -.
DR TreeFam; TF316195; -.
DR PathwayCommons; Q08289; -.
DR Reactome; R-HSA-112308; Presynaptic depolarization and calcium channel opening.
DR Reactome; R-HSA-400042; Adrenaline,noradrenaline inhibits insulin secretion.
DR Reactome; R-HSA-419037; NCAM1 interactions.
DR Reactome; R-HSA-422356; Regulation of insulin secretion.
DR Reactome; R-HSA-5576892; Phase 0 - rapid depolarisation.
DR Reactome; R-HSA-5576893; Phase 2 - plateau phase.
DR Reactome; R-HSA-9662360; Sensory processing of sound by inner hair cells of the cochlea.
DR SignaLink; Q08289; -.
DR SIGNOR; Q08289; -.
DR BioGRID-ORCS; 783; 10 hits in 1070 CRISPR screens.
DR ChiTaRS; CACNB2; human.
DR GeneWiki; CACNB2; -.
DR GenomeRNAi; 783; -.
DR Pharos; Q08289; Tbio.
DR PRO; PR:Q08289; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q08289; protein.
DR Bgee; ENSG00000165995; Expressed in adrenal tissue and 157 other tissues.
DR ExpressionAtlas; Q08289; baseline and differential.
DR Genevisible; Q08289; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:1990454; C:L-type voltage-gated calcium channel complex; IDA:BHF-UCL.
DR GO; GO:0098684; C:photoreceptor ribbon synapse; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005891; C:voltage-gated calcium channel complex; IDA:BHF-UCL.
DR GO; GO:0051015; F:actin filament binding; ISS:BHF-UCL.
DR GO; GO:0005262; F:calcium channel activity; NAS:UniProtKB.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IDA:BHF-UCL.
DR GO; GO:0099635; F:voltage-gated calcium channel activity involved in positive regulation of presynaptic cytosolic calcium levels; IEA:Ensembl.
DR GO; GO:0070509; P:calcium ion import; IDA:BHF-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0098912; P:membrane depolarization during atrial cardiac muscle cell action potential; IMP:BHF-UCL.
DR GO; GO:0086045; P:membrane depolarization during AV node cell action potential; IMP:BHF-UCL.
DR GO; GO:0007528; P:neuromuscular junction development; IBA:GO_Central.
DR GO; GO:1904879; P:positive regulation of calcium ion transmembrane transport via high voltage-gated calcium channel; ISS:BHF-UCL.
DR GO; GO:0051928; P:positive regulation of calcium ion transport; IDA:BHF-UCL.
DR GO; GO:1901843; P:positive regulation of high voltage-gated calcium channel activity; ISS:BHF-UCL.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:BHF-UCL.
DR GO; GO:1901385; P:regulation of voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:Ensembl.
DR CDD; cd12040; SH3_CACNB2; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR035605; CACNB2_SH3.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR005444; VDCC_L_b2su.
DR InterPro; IPR000584; VDCC_L_bsu.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF12052; VGCC_beta4Aa_N; 1.
DR PRINTS; PR01626; LCACHANNELB.
DR PRINTS; PR01628; LCACHANNELB2.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Brugada syndrome; Calcium; Calcium channel;
KW Calcium transport; Cell membrane; Disease variant; Ion channel;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; SH3 domain;
KW Transport; Voltage-gated channel.
FT CHAIN 1..660
FT /note="Voltage-dependent L-type calcium channel subunit
FT beta-2"
FT /id="PRO_0000144051"
FT DOMAIN 114..183
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 39..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..261
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 549
FT /note="Required for CaMK2D-binding"
FT /evidence="ECO:0000250"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VGC3"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC27"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC27"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CC27"
FT MOD_RES 554
FT /note="Phosphothreonine; by CaMK2D"
FT /evidence="ECO:0000250|UniProtKB:Q8VGC3"
FT VAR_SEQ 1..71
FT /note="MVQRDMSKSPPTAAAAVAQEIQMELLENVAPAGALGAAAQSYGKGARRKNRF
FT KGSDGSTSSDTTSNSFVRQ -> MQCCGLVHRRRVRVSY (in isoform 2a and
FT isoform 2f)"
FT /evidence="ECO:0000303|PubMed:12042350,
FT ECO:0000303|PubMed:8494331, ECO:0000303|PubMed:9254841,
FT ECO:0000303|Ref.5, ECO:0000303|Ref.7"
FT /id="VSP_000627"
FT VAR_SEQ 1..71
FT /note="MVQRDMSKSPPTAAAAVAQEIQMELLENVAPAGALGAAAQSYGKGARRKNRF
FT KGSDGSTSSDTTSNSFVRQ -> MLDRRLIAPQTKYIIPG (in isoform 2b and
FT isoform 2cN4)"
FT /evidence="ECO:0000303|PubMed:12042350,
FT ECO:0000303|PubMed:14762176"
FT /id="VSP_000628"
FT VAR_SEQ 1..71
FT /note="MVQRDMSKSPPTAAAAVAQEIQMELLENVAPAGALGAAAQSYGKGARRKNRF
FT KGSDGSTSSDTTSNSFVRQ -> MKATWIRLLKRAKGGRLKNSDIC (in isoform
FT 2e)"
FT /evidence="ECO:0000303|PubMed:12042350"
FT /id="VSP_000629"
FT VAR_SEQ 1..40
FT /note="MVQRDMSKSPPTAAAAVAQEIQMELLENVAPAGALGAAAQ -> MNQGSGLD
FT LLKI (in isoform 2c and isoform 2cN2)"
FT /evidence="ECO:0000303|PubMed:12042350,
FT ECO:0000303|PubMed:14762176"
FT /id="VSP_000626"
FT VAR_SEQ 224..268
FT /note="AIDIDATGLDAEENDIPANHRSPKPSANSVTSPHSKEKRMPFFKK -> AKQ
FT KQKS (in isoform 2f and isoform 2g)"
FT /evidence="ECO:0000303|PubMed:8494331, ECO:0000303|Ref.7"
FT /id="VSP_000630"
FT VAR_SEQ 224..268
FT /note="AIDIDATGLDAEENDIPANHRSPKPSANSVTSPHSKEKRMPFFKK -> GAK
FT SADEQDQWKTAGLFWRFT (in isoform 2h, isoform 2cN2 and isoform
FT 2cN4)"
FT /evidence="ECO:0000303|PubMed:14762176,
FT ECO:0000303|PubMed:8494331"
FT /id="VSP_000631"
FT VARIANT 99
FT /note="A -> G (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs745502425)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036350"
FT VARIANT 535
FT /note="S -> L (in BRGDA4; unknown pathological
FT significance; affects channel activity; dbSNP:rs121917812)"
FT /evidence="ECO:0000269|PubMed:17224476"
FT /id="VAR_044041"
FT CONFLICT 56
FT /note="D -> N (in Ref. 4; AAQ97608)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="V -> L (in Ref. 5; AAD33729)"
FT /evidence="ECO:0000305"
FT CONFLICT 100..101
FT /note="ER -> Q (in Ref. 5; AAD33729)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="N -> D (in Ref. 5; AAD33729)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="L -> V (in Ref. 5; AAD33729/AAD33730)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="R -> T (in Ref. 5; AAD33729/AAD33730)"
FT /evidence="ECO:0000305"
FT CONFLICT 501
FT /note="D -> H (in Ref. 5; AAD33729/AAD33730)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="P -> G (in Ref. 5; AAD33729/AAD33730)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="Q -> QQ (in Ref. 5; AAD33729/AAD33730)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="R -> P (in Ref. 2; AAB53332, 3; AAG01473/AAL16948/
FT AAL16951/AAL16950, 4; AAQ97606/AAQ97607/AAQ97608/AAQ97609/
FT AAQ97610 and 6; AAL73495)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 73581 MW; 4A08B141EE66404E CRC64;
MVQRDMSKSP PTAAAAVAQE IQMELLENVA PAGALGAAAQ SYGKGARRKN RFKGSDGSTS
SDTTSNSFVR QGSADSYTSR PSDSDVSLEE DREAVRREAE RQAQAQLEKA KTKPVAFAVR
TNVSYSAAHE DDVPVPGMAI SFEAKDFLHV KEKFNNDWWI GRLVKEGCEI GFIPSPVKLE
NMRLQHEQRA KQGKFYSSKS GGNSSSSLGD IVPSSRKSTP PSSAIDIDAT GLDAEENDIP
ANHRSPKPSA NSVTSPHSKE KRMPFFKKTE HTPPYDVVPS MRPVVLVGPS LKGYEVTDMM
QKALFDFLKH RFEGRISITR VTADISLAKR SVLNNPSKHA IIERSNTRSS LAEVQSEIER
IFELARTLQL VVLDADTINH PAQLSKTSLA PIIVYVKISS PKVLQRLIKS RGKSQAKHLN
VQMVAADKLA QCPPELFDVI LDENQLEDAC EHLADYLEAY WKATHPPSSS LPNPLLSRTL
ATSSLPLSPT LASNSQGSQG DQRTDRSAPI RSASQAEEEP SVEPVKKSQH RSSSSAPHHN
HRSGTSRGLS RQETFDSETQ ESRDSAYVEP KEDYSHDHVD HYASHRDHNH RDETHGSSDH
RHRESRHRSR DVDREQDHNE CNKQRSRHKS KDRYCEKDGE VISKKRNEAG EWNRDVYIRQ
