2VAF

Crystal structure of Human Cardiac Calsequestrin

Replaces:  2V0Q

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002027	biological_process	regulation of heart rate
A	0005509	molecular_function	calcium ion binding
A	0005513	biological_process	detection of calcium ion
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0006874	biological_process	intracellular calcium ion homeostasis
A	0006941	biological_process	striated muscle contraction
A	0010649	biological_process	regulation of cell communication by electrical coupling
A	0010880	biological_process	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A	0010881	biological_process	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
A	0014701	cellular_component	junctional sarcoplasmic reticulum membrane
A	0016529	cellular_component	sarcoplasmic reticulum
A	0030018	cellular_component	Z disc
A	0033017	cellular_component	sarcoplasmic reticulum membrane
A	0033018	cellular_component	sarcoplasmic reticulum lumen
A	0034704	cellular_component	calcium channel complex
A	0042803	molecular_function	protein homodimerization activity
A	0043267	biological_process	negative regulation of potassium ion transport
A	0046872	molecular_function	metal ion binding
A	0048306	molecular_function	calcium-dependent protein binding
A	0051258	biological_process	protein polymerization
A	0051279	biological_process	regulation of release of sequestered calcium ion into cytosol
A	0060048	biological_process	cardiac muscle contraction
A	0060306	biological_process	regulation of membrane repolarization
A	0071313	biological_process	cellular response to caffeine
A	0086029	biological_process	Purkinje myocyte to ventricular cardiac muscle cell signaling
A	0140314	molecular_function	calcium ion sequestering activity
A	1905024	biological_process	regulation of membrane repolarization during ventricular cardiac muscle cell action potential

Functional Information from PROSITE/UniProt

site_id	PS00864
Number of Residues	20
Details	CALSEQUESTRIN_2 Calsequestrin signature 2. ELEDWIEDVLsGkINTEDDD

Chain	Residue	Details
A	GLU1338-ASP1357

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O09161","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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