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	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	0016529	cellular_component	sarcoplasmic reticulum
A	0030018	cellular_component	Z disc
A	0033018	cellular_component	sarcoplasmic reticulum lumen
A	0046872	molecular_function	metal ion binding
A	0060315	biological_process	negative regulation of ryanodine-sensitive calcium-release channel activity
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
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	0016529	cellular_component	sarcoplasmic reticulum
B	0030018	cellular_component	Z disc
B	0033018	cellular_component	sarcoplasmic reticulum lumen
B	0046872	molecular_function	metal ion binding
B	0060315	biological_process	negative regulation of ryanodine-sensitive calcium-release channel activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O09161

Chain	Residue	Details
A	TYR263
B	TYR263

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site_id	SWS_FT_FI2
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN316
B	ASN316

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