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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
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
A0016529cellular_componentsarcoplasmic reticulum
A0030018cellular_componentZ disc
A0033018cellular_componentsarcoplasmic reticulum lumen
A0046872molecular_functionmetal ion binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
B0016529cellular_componentsarcoplasmic reticulum
B0030018cellular_componentZ disc
B0033018cellular_componentsarcoplasmic reticulum lumen
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues42
DetailsRegion: {"description":"Calcium regulated hydrophobic site"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"O09161","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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