5CRE

Human skeletal calsequestrin, D210G mutant low-calcium complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0005783	cellular_component	endoplasmic reticulum
A	0005790	cellular_component	smooth endoplasmic reticulum
A	0007519	biological_process	skeletal muscle tissue development
A	0014701	cellular_component	junctional sarcoplasmic reticulum membrane
A	0014802	cellular_component	terminal cisterna
A	0014804	cellular_component	terminal cisterna lumen
A	0014809	biological_process	regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
A	0014870	biological_process	response to muscle inactivity
A	0014894	biological_process	response to denervation involved in regulation of muscle adaptation
A	0016529	cellular_component	sarcoplasmic reticulum
A	0030016	cellular_component	myofibril
A	0030018	cellular_component	Z disc
A	0030315	cellular_component	T-tubule
A	0031674	cellular_component	I band
A	0033017	cellular_component	sarcoplasmic reticulum membrane
A	0033018	cellular_component	sarcoplasmic reticulum lumen
A	0042383	cellular_component	sarcolemma
A	0042802	molecular_function	identical protein binding
A	0045214	biological_process	sarcomere organization
A	0046872	molecular_function	metal ion binding
A	0051258	biological_process	protein polymerization
A	0051279	biological_process	regulation of release of sequestered calcium ion into cytosol
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	3
Details	binding site for residue CA A 401

Chain	Residue
A	ASN17
A	VAL18
A	ASP80

---

site_id	AC2
Number of Residues	3
Details	binding site for residue CA A 402

Chain	Residue
A	GLU199
A	THR229
A	THR277

---

site_id	AC3
Number of Residues	4
Details	binding site for residue MPD A 403

Chain	Residue
A	LEU295
A	PRO7
A	GLU8
A	TYR9

---

site_id	AC4
Number of Residues	5
Details	binding site for residue MPD A 404

Chain	Residue
A	LEU233
A	MET238
A	TRP242
A	TYR298
A	TRP299

---

Functional Information from PROSITE/UniProt

site_id	PS00863
Number of Residues	15
Details	CALSEQUESTRIN_1 Calsequestrin signature 1. QEGLDFPeYDGvDRV

Chain	Residue	Details
A	GLN1-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

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P19633","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P19633","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P19633","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---