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O14958

- CASQ2_HUMAN

UniProt

O14958 - CASQ2_HUMAN

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Protein

Calsequestrin-2

Gene

CASQ2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 Ca2+ ions. Regulates the release of lumenal Ca2+ 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.4 Publications

GO - Molecular functioni

  1. calcium-dependent protein binding Source: UniProtKB
  2. calcium ion binding Source: UniProtKB
  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: UniProtKB
  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: UniProtKB
  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
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

Calcium, Metal-binding

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

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
Complete GO annotation...

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. 2 Publications
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. 3 Publications
VAR_044118
Natural varianti307 – 3071D → 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. 2 Publications
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
N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiO14958.
PRIDEiO14958.

PTM databases

PhosphoSiteiO14958.

Expressioni

Gene expression databases

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.3 Publications

Protein-protein interaction databases

BioGridi107295. 44 interactions.
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.
GeneTreeiENSGT00390000019377.
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

        10         20         30         40         50
MKRTHLFIVG IYFLSSCRAE EGLNFPTYDG KDRVVSLSEK NFKQVLKKYD
60 70 80 90 100
LLCLYYHEPV SSDKVTQKQF QLKEIVLELV AQVLEHKAIG FVMVDAKKEA
110 120 130 140 150
KLAKKLGFDE EGSLYILKGD RTIEFDGEFA ADVLVEFLLD LIEDPVEIIS
160 170 180 190 200
SKLEVQAFER IEDYIKLIGF FKSEDSEYYK AFEEAAEHFQ PYIKFFATFD
210 220 230 240 250
KGVAKKLSLK MNEVDFYEPF MDEPIAIPNK PYTEEELVEF VKEHQRPTLR
260 270 280 290 300
RLRPEEMFET WEDDLNGIHI VAFAEKSDPD GYEFLEILKQ VARDNTDNPD
310 320 330 340 350
LSILWIDPDD FPLLVAYWEK TFKIDLFRPQ IGVVNVTDAD SVWMEIPDDD
360 370 380 390
DLPTAEELED WIEDVLSGKI NTEDDDEDDD DDDNSDEEDN DDSDDDDDE
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. 2 Publications
VAR_055234
Natural varianti66 – 661T → A No effect on calcium-binding and calcium-dependent dimerization. 2 Publications
Corresponds to variant rs4074536 [ dbSNP | Ensembl ].
VAR_023692
Natural varianti76 – 761V → M Increases dimerization in the absence of calcium. 2 Publications
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. 3 Publications
VAR_044118
Natural varianti244 – 2441H → R.
Corresponds to variant rs28730716 [ dbSNP | Ensembl ].
VAR_067036
Natural varianti307 – 3071D → 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. 2 Publications
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. [O14958-1]
RefSeqiNP_001223.2. NM_001232.3.
UniGeneiHs.57975.

Genome annotation databases

EnsembliENST00000261448; ENSP00000261448; ENSG00000118729. [O14958-1]
GeneIDi845.
KEGGihsa:845.
UCSCiuc001efx.4. human. [O14958-1]

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. [O14958-1 ]
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. 44 interactions.
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 . [O14958-1 ]
GeneIDi 845.
KEGGi hsa:845.
UCSCi uc001efx.4. human. [O14958-1 ]

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.
GeneTreei ENSGT00390000019377.
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

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

« Hide 'large scale' publications
  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, FUNCTION, SUBUNIT.
  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, GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
  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, FUNCTION.
  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, FUNCTION.

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 29, 2014
This is version 135 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