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Calsequestrin-2 (Calsequestrin, cardiac muscle isoform)

 CASQ2_HUMAN             Reviewed;         399 AA.
O14958; B2R7M6; B4DIB0; Q5T1D2; Q8TBW8;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 2.
25-OCT-2017, entry version 162.
RecName: Full=Calsequestrin-2;
AltName: Full=Calsequestrin, cardiac muscle isoform;
Flags: Precursor;
Name=CASQ2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart;
Tanaka T., Inazawa J., Nakamura Y.;
"Molecular cloning of a human cDNA for cardiac calsequestrin and its
chromosomal assignment to 1p13.3 by fluorescence in situ
hybridization.";
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skeletal muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
PHOSPHORYLATION AT SER-385 AND SER-393, FUNCTION, AND SUBUNIT.
PubMed=21416293; DOI=10.1007/s11010-011-0787-4;
Sanchez E.J., Munske G.R., Criswell A., Milting H., Dunker A.K.,
Kang C.;
"Phosphorylation of human calsequestrin: implications for calcium
regulation.";
Mol. Cell. Biochem. 353:195-204(2011).
[8]
X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 22-399, SUBUNIT, FUNCTION,
CHARACTERIZATION OF VARIANTS CPVT2 GLN-33; HIS-167 AND HIS-307, AND
CHARACTERIZATION OF VARIANTS ALA-66 AND MET-76.
PubMed=17881003; DOI=10.1016/j.jmb.2007.08.055;
Kim E., Youn B., Kemper L., Campbell C., Milting H., Varsanyi M.,
Kang C.;
"Characterization of human cardiac calsequestrin and its deleterious
mutants.";
J. Mol. Biol. 373:1047-1057(2007).
[9]
VARIANT CPVT2 HIS-307.
PubMed=11704930; DOI=10.1086/324565;
Lahat H., Pras E., Olender T., Avidan N., Ben-Asher E., Man O.,
Levy-Nissenbaum E., Khoury A., Lorber A., Goldman B., Lancet D.,
Eldar M.;
"A missense mutation in a highly conserved region of CASQ2 is
associated with autosomal recessive catecholamine-induced polymorphic
ventricular tachycardia in Bedouin families from Israel.";
Am. J. Hum. Genet. 69:1378-1384(2001).
[10]
VARIANTS ALA-66 AND MET-76.
PubMed=14571276; DOI=10.1038/sj.ejhg.5201061;
Laitinen P.J., Swan H., Kontula K.;
"Molecular genetics of exercise-induced polymorphic ventricular
tachycardia: identification of three novel cardiac ryanodine receptor
mutations and two common calsequestrin 2 amino-acid polymorphisms.";
Eur. J. Hum. Genet. 11:888-891(2003).
[11]
CHARACTERIZATION OF VARIANT CPVT2 HIS-307, INTERACTION WITH ASPH AND
TRDN, GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=15485681; DOI=10.1016/j.cardiores.2004.09.009;
Houle T.D., Ram M.L., Cala S.E.;
"Calsequestrin mutant D307H exhibits depressed binding to its protein
targets and a depressed response to calcium.";
Cardiovasc. Res. 64:227-233(2004).
[12]
VARIANT CPVT2 HIS-167, CHARACTERIZATION OF VARIANT CPVT2 HIS-167, AND
FUNCTION.
PubMed=16908766; DOI=10.1161/CIRCULATIONAHA.106.623793;
di Barletta M.R., Viatchenko-Karpinski S., Nori A., Memmi M.,
Terentyev D., Turcato F., Valle G., Rizzi N., Napolitano C.,
Gyorke S., Volpe P., Priori S.G.;
"Clinical phenotype and functional characterization of CASQ2 mutations
associated with catecholaminergic polymorphic ventricular
tachycardia.";
Circulation 114:1012-1019(2006).
[13]
VARIANTS CPVT2 GLN-33 AND HIS-167, CHARACTERIZATION OF VARIANTS CPVT2
GLN-33 AND HIS-167, AND FUNCTION.
PubMed=18399795; DOI=10.1042/BJ20080163;
Valle G., Galla D., Nori A., Priori S.G., Gyorke S., de Filippis V.,
Volpe P.;
"Catecholaminergic polymorphic ventricular tachycardia-related
mutations R33Q and L167H alter calcium sensitivity of human cardiac
calsequestrin.";
Biochem. J. 413:291-303(2008).
[14]
VARIANT CPVT2 ARG-180.
PubMed=27157848; DOI=10.1016/j.hrthm.2016.05.004;
Gray B., Bagnall R.D., Lam L., Ingles J., Turner C., Haan E.,
Davis A., Yang P.C., Clancy C.E., Sy R.W., Semsarian C.;
"A novel heterozygous mutation in cardiac calsequestrin causes
autosomal dominant catecholaminergic polymorphic ventricular
tachycardia.";
Heart Rhythm 13:1652-1660(2016).
-!- FUNCTION: Calsequestrin is a high-capacity, moderate affinity,
calcium-binding protein and thus acts as an internal calcium store
in muscle. Calcium ions are bound by clusters of acidic residues
at the protein surface, especially at the interface between
subunits. Can bind around 60 Ca(2+) ions. Regulates the release of
lumenal Ca(2+) via the calcium release channel RYR2; this plays an
important role in triggering muscle contraction. Plays a role in
excitation-contraction coupling in the heart and in regulating the
rate of heart beats. {ECO:0000269|PubMed:16908766,
ECO:0000269|PubMed:17881003, ECO:0000269|PubMed:18399795,
ECO:0000269|PubMed:21416293}.
-!- SUBUNIT: Monomer, homodimer and homooligomer. Mostly monomeric in
the absence of calcium. Forms higher oligomers in a calcium-
dependent manner. Dimers associate to form tetramers, that then
form linear homopolymer chains. Interacts with ASPH and TRDN.
{ECO:0000269|PubMed:15485681, ECO:0000269|PubMed:17881003,
ECO:0000269|PubMed:21416293}.
-!- SUBCELLULAR LOCATION: Sarcoplasmic reticulum lumen
{ECO:0000250|UniProtKB:O09161}. Note=This isoform of calsequestrin
occurs in the sarcoplasmic reticulum's terminal cisternae luminal
spaces of cardiac and slow skeletal muscle cells.
{ECO:0000250|UniProtKB:O09161}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O14958-1; Sequence=Displayed;
Name=2;
IsoId=O14958-2; Sequence=VSP_056477;
Note=No experimental confirmation available.;
-!- PTM: Phosphorylation in the C-terminus, probably by CK2,
moderately increases calcium buffering capacity.
{ECO:0000269|PubMed:21416293}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:15485681}.
-!- DISEASE: Ventricular tachycardia, catecholaminergic polymorphic, 2
(CPVT2) [MIM:611938]: An arrhythmogenic disorder characterized by
stress-induced, bidirectional ventricular tachycardia that may
degenerate into cardiac arrest and cause sudden death. Patients
present with recurrent syncope, seizures, or sudden death after
physical activity or emotional stress. CPVT2 inheritance is
autosomal recessive. {ECO:0000269|PubMed:11704930,
ECO:0000269|PubMed:15485681, ECO:0000269|PubMed:16908766,
ECO:0000269|PubMed:17881003, ECO:0000269|PubMed:18399795,
ECO:0000269|PubMed:27157848}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the calsequestrin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Calsequestrin entry;
URL="https://en.wikipedia.org/wiki/Calsequestrin";
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EMBL; D55655; BAA23494.1; -; mRNA.
EMBL; AK295502; BAG58422.1; -; mRNA.
EMBL; AK313041; BAG35873.1; -; mRNA.
EMBL; AL449264; CAI14532.1; -; Genomic_DNA.
EMBL; AL450389; CAI14532.1; JOINED; Genomic_DNA.
EMBL; AL450389; CAI23373.1; -; Genomic_DNA.
EMBL; AL449264; CAI23373.1; JOINED; Genomic_DNA.
EMBL; CH471122; EAW56635.1; -; Genomic_DNA.
EMBL; BC022288; AAH22288.1; -; mRNA.
CCDS; CCDS884.1; -. [O14958-1]
RefSeq; NP_001223.2; NM_001232.3. [O14958-1]
UniGene; Hs.57975; -.
PDB; 2VAF; X-ray; 3.80 A; A=22-399.
PDBsum; 2VAF; -.
ProteinModelPortal; O14958; -.
SMR; O14958; -.
BioGrid; 107295; 46.
STRING; 9606.ENSP00000261448; -.
iPTMnet; O14958; -.
PhosphoSitePlus; O14958; -.
BioMuta; CASQ2; -.
PaxDb; O14958; -.
PeptideAtlas; O14958; -.
PRIDE; O14958; -.
DNASU; 845; -.
Ensembl; ENST00000261448; ENSP00000261448; ENSG00000118729. [O14958-1]
GeneID; 845; -.
KEGG; hsa:845; -.
UCSC; uc001efx.5; human. [O14958-1]
CTD; 845; -.
DisGeNET; 845; -.
EuPathDB; HostDB:ENSG00000118729.11; -.
GeneCards; CASQ2; -.
GeneReviews; CASQ2; -.
HGNC; HGNC:1513; CASQ2.
HPA; HPA027285; -.
HPA; HPA055298; -.
MalaCards; CASQ2; -.
MIM; 114251; gene.
MIM; 611938; phenotype.
neXtProt; NX_O14958; -.
OpenTargets; ENSG00000118729; -.
Orphanet; 3286; Catecholaminergic polymorphic ventricular tachycardia.
PharmGKB; PA26096; -.
eggNOG; ENOG410IGY5; Eukaryota.
eggNOG; ENOG4111R2M; LUCA.
GeneTree; ENSGT00390000019377; -.
HOGENOM; HOG000049047; -.
HOVERGEN; HBG050805; -.
InParanoid; O14958; -.
OMA; TWEDDLN; -.
OrthoDB; EOG091G08VX; -.
PhylomeDB; O14958; -.
TreeFam; TF313796; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
Reactome; R-HSA-5578775; Ion homeostasis.
SIGNOR; O14958; -.
ChiTaRS; CASQ2; human.
EvolutionaryTrace; O14958; -.
GenomeRNAi; 845; -.
PRO; PR:O14958; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000118729; -.
CleanEx; HS_CASQ2; -.
Genevisible; O14958; HS.
GO; GO:0034704; C:calcium channel complex; TAS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005622; C:intracellular; IMP:BHF-UCL.
GO; GO:0030314; C:junctional membrane complex; IEA:Ensembl.
GO; GO:0014701; C:junctional sarcoplasmic reticulum membrane; TAS:BHF-UCL.
GO; GO:0016529; C:sarcoplasmic reticulum; ISS:BHF-UCL.
GO; GO:0033018; C:sarcoplasmic reticulum lumen; IC:BHF-UCL.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0030018; C:Z disc; ISS:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:BHF-UCL.
GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
GO; GO:0071313; P:cellular response to caffeine; IMP:BHF-UCL.
GO; GO:0005513; P:detection of calcium ion; TAS:BHF-UCL.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:1901017; P:negative regulation of potassium ion transmembrane transporter activity; ISS:BHF-UCL.
GO; GO:0043267; P:negative regulation of potassium ion transport; ISS:BHF-UCL.
GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO; GO:0051258; P:protein polymerization; IDA:UniProtKB.
GO; GO:0086029; P:Purkinje myocyte to ventricular cardiac muscle cell signaling; NAS:BHF-UCL.
GO; GO:1903779; P:regulation of cardiac conduction; TAS:Reactome.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IMP:BHF-UCL.
GO; GO:0010649; P:regulation of cell communication by electrical coupling; IMP:BHF-UCL.
GO; GO:0002027; P:regulation of heart rate; IMP:UniProtKB.
GO; GO:0060306; P:regulation of membrane repolarization; ISS:BHF-UCL.
GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISS:BHF-UCL.
GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
GO; GO:0051208; P:sequestering of calcium ion; IDA:BHF-UCL.
GO; GO:0006941; P:striated muscle contraction; TAS:ProtInc.
InterPro; IPR001393; Calsequestrin.
InterPro; IPR018233; Calsequestrin_CS.
InterPro; IPR036249; Thioredoxin-like_sf.
PANTHER; PTHR10033; PTHR10033; 1.
Pfam; PF01216; Calsequestrin; 1.
SUPFAM; SSF52833; SSF52833; 3.
PROSITE; PS00863; CALSEQUESTRIN_1; 1.
PROSITE; PS00864; CALSEQUESTRIN_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Complete proteome;
Disease mutation; Glycoprotein; Metal-binding; Muscle protein;
Phosphoprotein; Polymorphism; Reference proteome;
Sarcoplasmic reticulum; Signal.
SIGNAL 1 19 {ECO:0000250}.
CHAIN 20 399 Calsequestrin-2.
/FTId=PRO_0000004218.
COMPBIAS 356 399 Asp/Glu-rich (acidic).
MOD_RES 282 282 Phosphotyrosine.
{ECO:0000250|UniProtKB:O09161}.
MOD_RES 385 385 Phosphoserine.
{ECO:0000269|PubMed:21416293}.
MOD_RES 393 393 Phosphoserine.
{ECO:0000269|PubMed:21416293}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 107 178 GFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVE
IISSKLEVQAFERIEDYIKLIGFFKSEDSEY -> D (in
isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056477.
VARIANT 33 33 R -> Q (in CPVT2; reduces calcium-
dependent dimerization;
dbSNP:rs749547712).
{ECO:0000269|PubMed:17881003,
ECO:0000269|PubMed:18399795}.
/FTId=VAR_055234.
VARIANT 66 66 T -> A (no effect on calcium-binding and
calcium-dependent dimerization;
dbSNP:rs4074536).
{ECO:0000269|PubMed:14571276,
ECO:0000269|PubMed:17881003}.
/FTId=VAR_023692.
VARIANT 76 76 V -> M (increases dimerization in the
absence of calcium; dbSNP:rs10801999).
{ECO:0000269|PubMed:14571276,
ECO:0000269|PubMed:17881003}.
/FTId=VAR_023693.
VARIANT 167 167 L -> H (in CPVT2; alters protein folding;
reduces calcium-binding; reduces calcium-
dependent oligomerization; decreases
sarcoplasmic reticulum Ca(2+) storing
capacity; reduces the amplitude of I(Ca)-
induced Ca(2+) transients; reduces
spontaneous Ca(2+) sparks in
permeabilized myocytes;
dbSNP:rs121434550).
{ECO:0000269|PubMed:16908766,
ECO:0000269|PubMed:17881003,
ECO:0000269|PubMed:18399795}.
/FTId=VAR_044118.
VARIANT 180 180 K -> R (in CPVT2).
{ECO:0000269|PubMed:27157848}.
/FTId=VAR_076546.
VARIANT 244 244 H -> R (in dbSNP:rs28730716).
/FTId=VAR_067036.
VARIANT 307 307 D -> H (in CPVT2; reduces calcium-
binding; impairs calcium-dependent
oligomerization; causes 50% decrease in
calcium-dependent binding to TRDN; causes
50% decrease in calcium-dependent binding
to ASPH; dbSNP:rs121434549).
{ECO:0000269|PubMed:11704930,
ECO:0000269|PubMed:15485681,
ECO:0000269|PubMed:17881003}.
/FTId=VAR_016075.
VARIANT 335 335 N -> K (in dbSNP:rs28730712).
/FTId=VAR_067037.
CONFLICT 67 67 Q -> P (in Ref. 1; BAA23494).
{ECO:0000305}.
CONFLICT 175 175 D -> G (in Ref. 2; BAG35873).
{ECO:0000305}.
SEQUENCE 399 AA; 46436 MW; 7794DC2FF7E4B064 CRC64;
MKRTHLFIVG IYFLSSCRAE EGLNFPTYDG KDRVVSLSEK NFKQVLKKYD LLCLYYHEPV
SSDKVTQKQF QLKEIVLELV AQVLEHKAIG FVMVDAKKEA KLAKKLGFDE EGSLYILKGD
RTIEFDGEFA ADVLVEFLLD LIEDPVEIIS SKLEVQAFER IEDYIKLIGF FKSEDSEYYK
AFEEAAEHFQ PYIKFFATFD KGVAKKLSLK MNEVDFYEPF MDEPIAIPNK PYTEEELVEF
VKEHQRPTLR RLRPEEMFET WEDDLNGIHI VAFAEKSDPD GYEFLEILKQ VARDNTDNPD
LSILWIDPDD FPLLVAYWEK TFKIDLFRPQ IGVVNVTDAD SVWMEIPDDD DLPTAEELED
WIEDVLSGKI NTEDDDEDDD DDDNSDEEDN DDSDDDDDE


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EIAAB05406 Calsequestrin, cardiac muscle isoform,Calsequestrin-2,Casq2,Mouse,Mus musculus
EIAAB05402 Calsequestrin, cardiac muscle isoform,Calsequestrin-2,Casq2,Rat,Rattus norvegicus
EIAAB05405 Calsequestrin, cardiac muscle isoform,Calsequestrin-2,CASQ2,Pig,Sus scrofa
EIAAB05400 Calsequestrin, cardiac muscle isoform,Calsequestrin-2,CASQ2,Oryctolagus cuniculus,Rabbit
EIAAB05403 Calsequestrin, cardiac muscle isoform,Calsequestrin-2,CASQ2,Homo sapiens,Human
EIAAB05404 Calsequestrin, cardiac muscle isoform,Calsequestrin-2,Canis familiaris,Canis lupus familiaris,CASQ2,Dog
EIAAB05398 Calsequestrin, skeletal muscle isoform,Calsequestrin-1,Casq1,Mouse,Mus musculus
EIAAB05396 Calmitin,Calsequestrin, skeletal muscle isoform,Calsequestrin-1,CASQ,CASQ1,Homo sapiens,Human
EIAAB05395 Aspartactin,Calsequestrin, skeletal muscle isoform,Calsequestrin-1,Casq1,Laminin-binding protein,Rat,Rattus norvegicus
EIAAB05399 Aspartactin,Calsequestrin, skeletal muscle isoform,Calsequestrin-1,CASQ1,Laminin-binding protein,Oryctolagus cuniculus,Rabbit
EIAAB05397 Calsequestrin, skeletal muscle isoform,Calsequestrin-1,Canis familiaris,Canis lupus familiaris,CASQ1,Dog
orb80992 Dog Calsequestrin-2 protein Calsequestrin is the major calcium storage protein of the sarcoplasmic reticulum. Intraluminar Ca2+ binds to calsequestrin during diastole to prevent Ca2+ precipitation and 2
201-20-0833 CASQ2{calsequestrin 2 (cardiac muscle)}rabbit.pAb 0.1ml
CASS4 CASQ2 Gene calsequestrin 2 (cardiac muscle)
abx111338 Polyclonal Rabbit Calsequestrin 2 (Cardiac Muscle) Antibody 50 μl
GS-0287a calsequestrin 2 (cardiac muscle) primary antibody, Host: Rabbit 200ul
CASQ2-2035H Protein Recombinant Human Calsequestrin 2 (Cardiac Muscle), His-tagged 0.1mg
CASQ2-2035H Protein: Recombinant Human Calsequestrin 2 (Cardiac Muscle), His-tagged 0.1mg
CSB-EL004557DO Dog calsequestrin 2 (cardiac muscle) (CASQ2) ELISA kit, Species Dog, Sample Type serum, plasma 96T
CSB-EL004557PI Pig calsequestrin 2 (cardiac muscle) (CASQ2) ELISA kit, Species Pig, Sample Type serum, plasma 96T
CSB-EL004557RA Rat calsequestrin 2 (cardiac muscle) (CASQ2) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL004557CH Chicken calsequestrin 2 (cardiac muscle) (CASQ2) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
CSB-EL004557MO Mouse calsequestrin 2 (cardiac muscle) (CASQ2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL004557RB Rabbit calsequestrin 2 (cardiac muscle) (CASQ2) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T
CSB-EL004557HU Human calsequestrin 2 (cardiac muscle) (CASQ2) ELISA kit, Species Human, Sample Type serum, plasma 96T


 

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