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2VAF

Crystal structure of Human Cardiac Calsequestrin

Replaces:  2V0Q
Functional Information from GO Data
ChainGOidnamespacecontents
A0002027biological_processregulation of heart rate
A0005509molecular_functioncalcium ion binding
A0005513biological_processdetection of calcium ion
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006874biological_processintracellular calcium ion homeostasis
A0006941biological_processstriated muscle contraction
A0010649biological_processregulation of cell communication by electrical coupling
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
A0014701cellular_componentjunctional sarcoplasmic reticulum membrane
A0016529cellular_componentsarcoplasmic reticulum
A0030018cellular_componentZ disc
A0033017cellular_componentsarcoplasmic reticulum membrane
A0033018cellular_componentsarcoplasmic reticulum lumen
A0034704cellular_componentcalcium channel complex
A0042803molecular_functionprotein homodimerization activity
A0043267biological_processnegative regulation of potassium ion transport
A0046872molecular_functionmetal ion binding
A0048306molecular_functioncalcium-dependent protein binding
A0051208biological_processsequestering of calcium ion
A0051258biological_processprotein polymerization
A0060048biological_processcardiac muscle contraction
A0060306biological_processregulation of membrane repolarization
A0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
A0071313biological_processcellular response to caffeine
A0086029biological_processPurkinje myocyte to ventricular cardiac muscle cell signaling
A0140314molecular_functioncalcium ion sequestering activity
A1901017biological_processnegative regulation of potassium ion transmembrane transporter activity
Functional Information from PROSITE/UniProt
site_idPS00864
Number of Residues20
DetailsCALSEQUESTRIN_2 Calsequestrin signature 2. ELEDWIEDVLsGkINTEDDD
ChainResidueDetails
AGLU1338-ASP1357

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:O09161
ChainResidueDetails
ATYR1263

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:21416293
ChainResidueDetails
ASER1366
ASER1374

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN1316

222624

PDB entries from 2024-07-17

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