9JUS

Structure of villin bound to an actin trimer

Functional Information from GO Data

Chain	GOid	namespace	contents
f	0001725	cellular_component	stress fiber
f	0005200	molecular_function	structural constituent of cytoskeleton
f	0005515	molecular_function	protein binding
f	0005856	cellular_component	cytoskeleton
f	0005865	cellular_component	striated muscle thin filament
f	0005884	cellular_component	actin filament
f	0015629	cellular_component	actin cytoskeleton
f	0016887	molecular_function	ATP hydrolysis activity
f	0030240	biological_process	skeletal muscle thin filament assembly
f	0048741	biological_process	skeletal muscle fiber development
F	0001725	cellular_component	stress fiber
F	0005200	molecular_function	structural constituent of cytoskeleton
F	0005515	molecular_function	protein binding
F	0005856	cellular_component	cytoskeleton
F	0005865	cellular_component	striated muscle thin filament
F	0005884	cellular_component	actin filament
F	0015629	cellular_component	actin cytoskeleton
F	0016887	molecular_function	ATP hydrolysis activity
F	0030240	biological_process	skeletal muscle thin filament assembly
F	0048741	biological_process	skeletal muscle fiber development
g	0001725	cellular_component	stress fiber
g	0005200	molecular_function	structural constituent of cytoskeleton
g	0005515	molecular_function	protein binding
g	0005856	cellular_component	cytoskeleton
g	0005865	cellular_component	striated muscle thin filament
g	0005884	cellular_component	actin filament
g	0015629	cellular_component	actin cytoskeleton
g	0016887	molecular_function	ATP hydrolysis activity
g	0030240	biological_process	skeletal muscle thin filament assembly
g	0048741	biological_process	skeletal muscle fiber development
G	0001725	cellular_component	stress fiber
G	0005200	molecular_function	structural constituent of cytoskeleton
G	0005515	molecular_function	protein binding
G	0005856	cellular_component	cytoskeleton
G	0005865	cellular_component	striated muscle thin filament
G	0005884	cellular_component	actin filament
G	0015629	cellular_component	actin cytoskeleton
G	0016887	molecular_function	ATP hydrolysis activity
G	0030240	biological_process	skeletal muscle thin filament assembly
G	0048741	biological_process	skeletal muscle fiber development
p	0001725	cellular_component	stress fiber
p	0005200	molecular_function	structural constituent of cytoskeleton
p	0005515	molecular_function	protein binding
p	0005856	cellular_component	cytoskeleton
p	0005865	cellular_component	striated muscle thin filament
p	0005884	cellular_component	actin filament
p	0015629	cellular_component	actin cytoskeleton
p	0016887	molecular_function	ATP hydrolysis activity
p	0030240	biological_process	skeletal muscle thin filament assembly
p	0048741	biological_process	skeletal muscle fiber development
P	0001725	cellular_component	stress fiber
P	0005200	molecular_function	structural constituent of cytoskeleton
P	0005515	molecular_function	protein binding
P	0005856	cellular_component	cytoskeleton
P	0005865	cellular_component	striated muscle thin filament
P	0005884	cellular_component	actin filament
P	0015629	cellular_component	actin cytoskeleton
P	0016887	molecular_function	ATP hydrolysis activity
P	0030240	biological_process	skeletal muscle thin filament assembly
P	0048741	biological_process	skeletal muscle fiber development
v	0003779	molecular_function	actin binding
v	0007010	biological_process	cytoskeleton organization
v	0051015	molecular_function	actin filament binding
V	0003779	molecular_function	actin binding
V	0007010	biological_process	cytoskeleton organization
V	0051015	molecular_function	actin filament binding

Functional Information from PROSITE/UniProt

site_id	PS00406
Number of Residues	11
Details	ACTINS_1 Actins signature 1. YVGDEAQs.KRG

Chain	Residue	Details
p	TYR53-GLY63

---

site_id	PS00432
Number of Residues	9
Details	ACTINS_2 Actins signature 2. WITKqEYDE

Chain	Residue	Details
p	TRP356-GLU364

---

site_id	PS01132
Number of Residues	13
Details	ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR

Chain	Residue	Details
p	LEU104-ARG116

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"12356759","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MDU","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---