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O14958

- CASQ2_HUMAN

UniProt

O14958 - CASQ2_HUMAN

Protein

Calsequestrin-2

Gene

CASQ2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (19 Sep 2002)
      Previous versions | rss
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    Functioni

    Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. The release of calcium bound to calsequestrin through a calcium release channel triggers muscle contraction. The skeletal muscle isoform (CASQ1) binds around 80 Ca2+ ions, while the cardiac isoform (CASQ2) binds approximately 60 Ca2+ ions.1 Publication

    GO - Molecular functioni

    1. calcium ion binding Source: BHF-UCL
    2. protein binding Source: BHF-UCL
    3. protein homodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. cardiac muscle contraction Source: BHF-UCL
    2. cellular response to caffeine Source: BHF-UCL
    3. detection of calcium ion Source: BHF-UCL
    4. ion transmembrane transport Source: Reactome
    5. negative regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
    6. negative regulation of potassium ion transport Source: BHF-UCL
    7. negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
    8. protein polymerization Source: BHF-UCL
    9. Purkinje myocyte to ventricular cardiac muscle cell signaling Source: BHF-UCL
    10. regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
    11. regulation of cell communication by electrical coupling Source: BHF-UCL
    12. regulation of heart rate Source: BHF-UCL
    13. regulation of membrane repolarization Source: BHF-UCL
    14. regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
    15. sequestering of calcium ion Source: BHF-UCL
    16. striated muscle contraction Source: ProtInc
    17. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Muscle protein

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_160189. Stimuli-sensing channels.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calsequestrin-2
    Alternative name(s):
    Calsequestrin, cardiac muscle isoform
    Gene namesi
    Name:CASQ2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1513. CASQ2.

    Subcellular locationi

    Sarcoplasmic reticulum lumen
    Note: This isoform of calsequestrin occurs in the sarcoplasmic reticulum's terminal cisternae luminal spaces of cardiac and slow skeletal muscle cells.

    GO - Cellular componenti

    1. calcium channel complex Source: BHF-UCL
    2. cytoplasm Source: BHF-UCL
    3. intracellular Source: BHF-UCL
    4. junctional sarcoplasmic reticulum membrane Source: BHF-UCL
    5. sarcoplasmic reticulum Source: BHF-UCL
    6. sarcoplasmic reticulum lumen Source: BHF-UCL
    7. sarcoplasmic reticulum membrane Source: Reactome
    8. Z disc Source: BHF-UCL

    Keywords - Cellular componenti

    Sarcoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331R → Q in CPVT2; reduces calcium-dependent dimerization. 1 Publication
    VAR_055234
    Natural varianti167 – 1671L → 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. 2 Publications
    VAR_044118
    Natural varianti307 – 3071D → H in CPVT2; reduces calcium-binding; causes 50% decrease in calcium-dependent binding to TRDN; causes 50% decrease in calcium-dependent binding to ASPH. 1 Publication
    VAR_016075

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi611938. phenotype.
    Orphaneti3286. Catecholaminergic polymorphic ventricular tachycardia.
    PharmGKBiPA26096.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Chaini20 – 399380Calsequestrin-2PRO_0000004218Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi335 – 3351N-linked (GlcNAc...)Sequence Analysis
    Modified residuei385 – 3851Phosphoserine1 Publication
    Modified residuei393 – 3931Phosphoserine1 Publication

    Post-translational modificationi

    Phosphorylation in the C-terminus, probably by CK2, moderately increases calcium buffering capacity.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiO14958.
    PRIDEiO14958.

    PTM databases

    PhosphoSiteiO14958.

    Expressioni

    Gene expression databases

    ArrayExpressiO14958.
    BgeeiO14958.
    CleanExiHS_CASQ2.
    GenevestigatoriO14958.

    Organism-specific databases

    HPAiCAB037203.
    HPA027285.
    HPA055298.

    Interactioni

    Subunit structurei

    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.2 Publications

    Protein-protein interaction databases

    BioGridi107295. 1 interaction.
    STRINGi9606.ENSP00000261448.

    Structurei

    Secondary structure

    1
    399
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 3816
    Helixi39 – 4810
    Beta strandi49 – 6618
    Helixi67 – 8418
    Beta strandi85 – 9713
    Helixi98 – 1036
    Beta strandi104 – 13027
    Helixi131 – 14111
    Beta strandi142 – 15211
    Helixi153 – 1586
    Beta strandi159 – 17618
    Helixi177 – 18812
    Beta strandi189 – 20012
    Helixi201 – 2077
    Beta strandi208 – 21710
    Beta strandi219 – 2235
    Beta strandi229 – 2335
    Helixi234 – 24310
    Beta strandi248 – 2525
    Helixi256 – 2616
    Beta strandi262 – 27817
    Helixi279 – 29416
    Beta strandi295 – 2984
    Beta strandi300 – 3078
    Helixi312 – 3209
    Beta strandi321 – 3288
    Beta strandi330 – 35122
    Helixi356 – 3616
    Beta strandi362 – 3698

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2VAFX-ray3.80A22-399[»]
    ProteinModelPortaliO14958.
    SMRiO14958. Positions 22-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14958.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi356 – 39944Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Belongs to the calsequestrin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG77804.
    HOGENOMiHOG000049047.
    HOVERGENiHBG050805.
    InParanoidiO14958.
    OMAiAIPNKPY.
    OrthoDBiEOG725DHM.
    PhylomeDBiO14958.
    TreeFamiTF313796.

    Family and domain databases

    Gene3Di3.40.30.10. 3 hits.
    InterProiIPR001393. Calsequestrin.
    IPR018233. Calsequestrin_CS.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF01216. Calsequestrin. 1 hit.
    [Graphical view]
    PRINTSiPR00312. CALSEQUESTRN.
    SUPFAMiSSF52833. SSF52833. 3 hits.
    PROSITEiPS00863. CALSEQUESTRIN_1. 1 hit.
    PS00864. CALSEQUESTRIN_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14958-1) [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

    MKRTHLFIVG IYFLSSCRAE EGLNFPTYDG KDRVVSLSEK NFKQVLKKYD    50
    LLCLYYHEPV SSDKVTQKQF QLKEIVLELV AQVLEHKAIG FVMVDAKKEA 100
    KLAKKLGFDE EGSLYILKGD RTIEFDGEFA ADVLVEFLLD LIEDPVEIIS 150
    SKLEVQAFER IEDYIKLIGF FKSEDSEYYK AFEEAAEHFQ PYIKFFATFD 200
    KGVAKKLSLK MNEVDFYEPF MDEPIAIPNK PYTEEELVEF VKEHQRPTLR 250
    RLRPEEMFET WEDDLNGIHI VAFAEKSDPD GYEFLEILKQ VARDNTDNPD 300
    LSILWIDPDD FPLLVAYWEK TFKIDLFRPQ IGVVNVTDAD SVWMEIPDDD 350
    DLPTAEELED WIEDVLSGKI NTEDDDEDDD DDDNSDEEDN DDSDDDDDE 399
    Length:399
    Mass (Da):46,436
    Last modified:September 19, 2002 - v2
    Checksum:i7794DC2FF7E4B064
    GO
    Isoform 2 (identifier: O14958-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         107-178: GFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDYIKLIGFFKSEDSEY → D

    Note: No experimental confirmation available.

    Show »
    Length:328
    Mass (Da):38,269
    Checksum:i42E722133CA1BCB0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti67 – 671Q → P in BAA23494. 1 PublicationCurated
    Sequence conflicti175 – 1751D → G in BAG35873. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331R → Q in CPVT2; reduces calcium-dependent dimerization. 1 Publication
    VAR_055234
    Natural varianti66 – 661T → A.1 Publication
    Corresponds to variant rs4074536 [ dbSNP | Ensembl ].
    VAR_023692
    Natural varianti76 – 761V → M.1 Publication
    Corresponds to variant rs10801999 [ dbSNP | Ensembl ].
    VAR_023693
    Natural varianti167 – 1671L → 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. 2 Publications
    VAR_044118
    Natural varianti244 – 2441H → R.
    Corresponds to variant rs28730716 [ dbSNP | Ensembl ].
    VAR_067036
    Natural varianti307 – 3071D → H in CPVT2; reduces calcium-binding; causes 50% decrease in calcium-dependent binding to TRDN; causes 50% decrease in calcium-dependent binding to ASPH. 1 Publication
    VAR_016075
    Natural varianti335 – 3351N → K.
    Corresponds to variant rs28730712 [ dbSNP | Ensembl ].
    VAR_067037

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei107 – 17872GFDEE…EDSEY → D in isoform 2. 1 PublicationVSP_056477Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D55655 mRNA. Translation: BAA23494.1.
    AK295502 mRNA. Translation: BAG58422.1.
    AK313041 mRNA. Translation: BAG35873.1.
    AL449264, AL450389 Genomic DNA. Translation: CAI14532.1.
    AL450389, AL449264 Genomic DNA. Translation: CAI23373.1.
    CH471122 Genomic DNA. Translation: EAW56635.1.
    BC022288 mRNA. Translation: AAH22288.1.
    CCDSiCCDS884.1.
    RefSeqiNP_001223.2. NM_001232.3.
    UniGeneiHs.57975.

    Genome annotation databases

    EnsembliENST00000261448; ENSP00000261448; ENSG00000118729.
    ENST00000456138; ENSP00000403858; ENSG00000118729.
    GeneIDi845.
    KEGGihsa:845.
    UCSCiuc001efx.4. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Calsequestrin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D55655 mRNA. Translation: BAA23494.1 .
    AK295502 mRNA. Translation: BAG58422.1 .
    AK313041 mRNA. Translation: BAG35873.1 .
    AL449264 , AL450389 Genomic DNA. Translation: CAI14532.1 .
    AL450389 , AL449264 Genomic DNA. Translation: CAI23373.1 .
    CH471122 Genomic DNA. Translation: EAW56635.1 .
    BC022288 mRNA. Translation: AAH22288.1 .
    CCDSi CCDS884.1.
    RefSeqi NP_001223.2. NM_001232.3.
    UniGenei Hs.57975.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2VAF X-ray 3.80 A 22-399 [» ]
    ProteinModelPortali O14958.
    SMRi O14958. Positions 22-370.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107295. 1 interaction.
    STRINGi 9606.ENSP00000261448.

    PTM databases

    PhosphoSitei O14958.

    Proteomic databases

    PaxDbi O14958.
    PRIDEi O14958.

    Protocols and materials databases

    DNASUi 845.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261448 ; ENSP00000261448 ; ENSG00000118729 .
    ENST00000456138 ; ENSP00000403858 ; ENSG00000118729 .
    GeneIDi 845.
    KEGGi hsa:845.
    UCSCi uc001efx.4. human.

    Organism-specific databases

    CTDi 845.
    GeneCardsi GC01M116242.
    GeneReviewsi CASQ2.
    HGNCi HGNC:1513. CASQ2.
    HPAi CAB037203.
    HPA027285.
    HPA055298.
    MIMi 114251. gene.
    611938. phenotype.
    neXtProti NX_O14958.
    Orphaneti 3286. Catecholaminergic polymorphic ventricular tachycardia.
    PharmGKBi PA26096.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG77804.
    HOGENOMi HOG000049047.
    HOVERGENi HBG050805.
    InParanoidi O14958.
    OMAi AIPNKPY.
    OrthoDBi EOG725DHM.
    PhylomeDBi O14958.
    TreeFami TF313796.

    Enzyme and pathway databases

    Reactomei REACT_160189. Stimuli-sensing channels.

    Miscellaneous databases

    EvolutionaryTracei O14958.
    GenomeRNAii 845.
    NextBioi 3542.
    PROi O14958.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14958.
    Bgeei O14958.
    CleanExi HS_CASQ2.
    Genevestigatori O14958.

    Family and domain databases

    Gene3Di 3.40.30.10. 3 hits.
    InterProi IPR001393. Calsequestrin.
    IPR018233. Calsequestrin_CS.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF01216. Calsequestrin. 1 hit.
    [Graphical view ]
    PRINTSi PR00312. CALSEQUESTRN.
    SUPFAMi SSF52833. SSF52833. 3 hits.
    PROSITEi PS00863. CALSEQUESTRIN_1. 1 hit.
    PS00864. CALSEQUESTRIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a human cDNA for cardiac calsequestrin and its chromosomal assignment to 1p13.3 by fluorescence in situ hybridization."
      Tanaka T., Inazawa J., Nakamura Y.
      Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Heart.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain and 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: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Skeletal muscle.
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Phosphorylation of human calsequestrin: implications for calcium regulation."
      Sanchez E.J., Munske G.R., Criswell A., Milting H., Dunker A.K., Kang C.
      Mol. Cell. Biochem. 353:195-204(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-385 AND SER-393.
    8. "Characterization of human cardiac calsequestrin and its deleterious mutants."
      Kim E., Youn B., Kemper L., Campbell C., Milting H., Varsanyi M., Kang C.
      J. Mol. Biol. 373:1047-1057(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 22-399, SUBUNIT, FUNCTION, CHARACTERIZATION OF VARIANTS CPVT2 GLN-33; HIS-167 AND HIS-307, CHARACTERIZATION OF VARIANTS ALA-66 AND MET-76.
    9. "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."
      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.
      Am. J. Hum. Genet. 69:1378-1384(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CPVT2 HIS-307.
    10. "Molecular genetics of exercise-induced polymorphic ventricular tachycardia: identification of three novel cardiac ryanodine receptor mutations and two common calsequestrin 2 amino-acid polymorphisms."
      Laitinen P.J., Swan H., Kontula K.
      Eur. J. Hum. Genet. 11:888-891(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ALA-66 AND MET-76.
    11. "Calsequestrin mutant D307H exhibits depressed binding to its protein targets and a depressed response to calcium."
      Houle T.D., Ram M.L., Cala S.E.
      Cardiovasc. Res. 64:227-233(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANT CPVT2 HIS-307, INTERACTION WITH ASPH AND TRDN.
    12. "Clinical phenotype and functional characterization of CASQ2 mutations associated with catecholaminergic polymorphic ventricular tachycardia."
      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.
      Circulation 114:1012-1019(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CPVT2 HIS-167, CHARACTERIZATION OF VARIANT CPVT2 HIS-167.
    13. "Catecholaminergic polymorphic ventricular tachycardia-related mutations R33Q and L167H alter calcium sensitivity of human cardiac calsequestrin."
      Valle G., Galla D., Nori A., Priori S.G., Gyorke S., de Filippis V., Volpe P.
      Biochem. J. 413:291-303(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CPVT2 GLN-33 AND HIS-167, CHARACTERIZATION OF VARIANTS CPVT2 GLN-33 AND HIS-167.

    Entry informationi

    Entry nameiCASQ2_HUMAN
    AccessioniPrimary (citable) accession number: O14958
    Secondary accession number(s): B2R7M6
    , B4DIB0, Q5T1D2, Q8TBW8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: September 19, 2002
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 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