1SJI

Comparing skeletal and cardiac calsequestrin structures and their calcium binding: a proposed mechanism for coupled calcium binding and protein polymerization

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005783	cellular_component	endoplasmic reticulum
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	0014802	cellular_component	terminal cisterna
A	0016529	cellular_component	sarcoplasmic reticulum
A	0030018	cellular_component	Z disc
A	0033018	cellular_component	sarcoplasmic reticulum lumen
A	0051279	biological_process	regulation of release of sequestered calcium ion into cytosol
A	0140314	molecular_function	calcium ion sequestering activity
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005783	cellular_component	endoplasmic reticulum
B	0010880	biological_process	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B	0010881	biological_process	regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
B	0014802	cellular_component	terminal cisterna
B	0016529	cellular_component	sarcoplasmic reticulum
B	0030018	cellular_component	Z disc
B	0033018	cellular_component	sarcoplasmic reticulum lumen
B	0051279	biological_process	regulation of release of sequestered calcium ion into cytosol
B	0140314	molecular_function	calcium ion sequestering activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	42
Details	Region: {"description":"Calcium regulated hydrophobic site"}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O09161","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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