2FOT

Crystal structure of the complex between calmodulin and alphaII-spectrin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000922	cellular_component	spindle pole
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005819	cellular_component	spindle
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0010880	biological_process	regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A	0019904	molecular_function	protein domain specific binding
A	0030234	molecular_function	enzyme regulator activity
A	0032991	cellular_component	protein-containing complex
A	0046872	molecular_function	metal ion binding
A	0060315	biological_process	negative regulation of ryanodine-sensitive calcium-release channel activity
A	0060316	biological_process	positive regulation of ryanodine-sensitive calcium-release channel activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 201

Chain	Residue
A	ASP20
A	ASP22
A	ASP24
A	THR26
A	GLU31
A	HOH508

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 202

Chain	Residue
A	THR62
A	GLU67
A	HOH551
A	ASP56
A	ASP58
A	ASN60

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 203

Chain	Residue
A	ASP93
A	ASP95
A	ASN97
A	TYR99
A	GLU104
A	HOH515

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 204

Chain	Residue
A	ASP129
A	ASP131
A	ASP133
A	GLN135
A	GLU140

---

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL

Chain	Residue	Details
A	ASP20-LEU32
A	ASP56-PHE68
A	ASP93-LEU105
A	ASP129-PHE141

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	SITE: Cleavage; by mu-calpain

Chain	Residue	Details
A	GLY23
A	GLY25
A	ILE27
A	LEU32
C	TYR1174
A	ALA57
A	GLY59
A	GLY61
A	ILE63
A	PHE68
A	LYS94
A	GLY96
A	GLY98
A	ILE100
A	LEU105
A	ILE130
A	GLY132
A	GLY134
A	VAL136
A	PHE141

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332

Chain	Residue	Details
C	TYR1174

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P16546

Chain	Residue	Details
C	SER1188

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
C	SER1207

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23

Chain	Residue	Details
A	ALA102
A	GLU82

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23

Chain	Residue	Details
A	ASP95

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23

Chain	Residue	Details
A	GLU139
A	ILE100

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23

Chain	Residue	Details
A	ASN111

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23

Chain	Residue	Details
A	LEU116

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:9716384

Chain	Residue	Details
A	ASP22

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