Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0005509 | molecular_function | calcium ion binding |
A | 0005739 | cellular_component | mitochondrion |
A | 0005759 | cellular_component | mitochondrial matrix |
A | 0014809 | biological_process | regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion |
A | 0016020 | cellular_component | membrane |
A | 0016529 | cellular_component | sarcoplasmic reticulum |
A | 0030018 | cellular_component | Z disc |
A | 0030955 | molecular_function | potassium ion binding |
A | 0033017 | cellular_component | sarcoplasmic reticulum membrane |
A | 0033018 | cellular_component | sarcoplasmic reticulum lumen |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0045214 | biological_process | sarcomere organization |
A | 0046872 | molecular_function | metal ion binding |
A | 0051258 | biological_process | protein polymerization |
A | 0051281 | biological_process | positive regulation of release of sequestered calcium ion into cytosol |
A | 1901341 | biological_process | positive regulation of store-operated calcium channel activity |
A | 2001256 | biological_process | regulation of store-operated calcium entry |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MPD A 368 |
Chain | Residue |
A | PHE6 |
A | PRO7 |
A | TRP242 |
A | TYR298 |
A | TRP299 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MRD A 369 |
Chain | Residue |
A | HOH493 |
A | GLN63 |
A | LEU294 |
A | LEU295 |
A | HOH462 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE MPD A 370 |
Chain | Residue |
A | ASN279 |
A | GLU344 |
A | HOH413 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MPD A 371 |
Chain | Residue |
A | VAL314 |
A | ASN316 |
A | ASP321 |
A | VAL346 |
A | GLY349 |
A | GLU350 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 372 |
Chain | Residue |
A | ASN17 |
A | VAL18 |
A | LEU74 |
A | ASP80 |
A | HOH490 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 373 |
Chain | Residue |
A | GLU199 |
A | THR229 |
A | THR277 |
A | HOH756 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA A 374 |
Chain | Residue |
A | ASP210 |
A | PRO212 |
A | GLU217 |
A | HOH391 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CA A 375 |
Chain | Residue |
A | THR189 |
A | HOH474 |
A | HOH565 |
A | HOH684 |
A | HOH801 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA A 376 |
Chain | Residue |
A | PRO172 |
A | HOH629 |
A | HOH771 |
Functional Information from PROSITE/UniProt
site_id | PS00863 |
Number of Residues | 15 |
Details | CALSEQUESTRIN_1 Calsequestrin signature 1. EEGLDFPeYDGvDRV |
Chain | Residue | Details |
A | GLU1-VAL15 | |
site_id | PS00864 |
Number of Residues | 20 |
Details | CALSEQUESTRIN_2 Calsequestrin signature 2. ELEDWLEDVLeGeINTEDDD |
Chain | Residue | Details |
A | GLU338-ASP357 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | SER47 | |
A | SER182 | |
Chain | Residue | Details |
A | THR90 | |
Chain | Residue | Details |
A | ASN316 | |