2Y83

Actin filament pointed end

Functional Information from GO Data

Chain	GOid	namespace	contents
O	0000166	molecular_function	nucleotide binding
O	0000287	molecular_function	magnesium ion binding
O	0001725	cellular_component	stress fiber
O	0003785	molecular_function	actin monomer binding
O	0005509	molecular_function	calcium ion binding
O	0005515	molecular_function	protein binding
O	0005523	molecular_function	tropomyosin binding
O	0005524	molecular_function	ATP binding
O	0005737	cellular_component	cytoplasm
O	0005856	cellular_component	cytoskeleton
O	0005865	cellular_component	striated muscle thin filament
O	0005884	cellular_component	actin filament
O	0010628	biological_process	positive regulation of gene expression
O	0016787	molecular_function	hydrolase activity
O	0019904	molecular_function	protein domain specific binding
O	0030027	cellular_component	lamellipodium
O	0030041	biological_process	actin filament polymerization
O	0030175	cellular_component	filopodium
O	0030240	biological_process	skeletal muscle thin filament assembly
O	0031013	molecular_function	troponin I binding
O	0031432	molecular_function	titin binding
O	0031941	cellular_component	filamentous actin
O	0032036	molecular_function	myosin heavy chain binding
O	0032432	cellular_component	actin filament bundle
O	0042802	molecular_function	identical protein binding
O	0044297	cellular_component	cell body
O	0048306	molecular_function	calcium-dependent protein binding
O	0048741	biological_process	skeletal muscle fiber development
O	0051017	biological_process	actin filament bundle assembly
O	0090131	biological_process	mesenchyme migration
O	0098723	cellular_component	skeletal muscle myofibril
O	0140660	molecular_function	cytoskeletal motor activator activity
P	0000166	molecular_function	nucleotide binding
P	0000287	molecular_function	magnesium ion binding
P	0001725	cellular_component	stress fiber
P	0003785	molecular_function	actin monomer binding
P	0005509	molecular_function	calcium ion binding
P	0005515	molecular_function	protein binding
P	0005523	molecular_function	tropomyosin binding
P	0005524	molecular_function	ATP binding
P	0005737	cellular_component	cytoplasm
P	0005856	cellular_component	cytoskeleton
P	0005865	cellular_component	striated muscle thin filament
P	0005884	cellular_component	actin filament
P	0010628	biological_process	positive regulation of gene expression
P	0016787	molecular_function	hydrolase activity
P	0019904	molecular_function	protein domain specific binding
P	0030027	cellular_component	lamellipodium
P	0030041	biological_process	actin filament polymerization
P	0030175	cellular_component	filopodium
P	0030240	biological_process	skeletal muscle thin filament assembly
P	0031013	molecular_function	troponin I binding
P	0031432	molecular_function	titin binding
P	0031941	cellular_component	filamentous actin
P	0032036	molecular_function	myosin heavy chain binding
P	0032432	cellular_component	actin filament bundle
P	0042802	molecular_function	identical protein binding
P	0044297	cellular_component	cell body
P	0048306	molecular_function	calcium-dependent protein binding
P	0048741	biological_process	skeletal muscle fiber development
P	0051017	biological_process	actin filament bundle assembly
P	0090131	biological_process	mesenchyme migration
P	0098723	cellular_component	skeletal muscle myofibril
P	0140660	molecular_function	cytoskeletal motor activator activity
Q	0000166	molecular_function	nucleotide binding
Q	0000287	molecular_function	magnesium ion binding
Q	0001725	cellular_component	stress fiber
Q	0003785	molecular_function	actin monomer binding
Q	0005509	molecular_function	calcium ion binding
Q	0005515	molecular_function	protein binding
Q	0005523	molecular_function	tropomyosin binding
Q	0005524	molecular_function	ATP binding
Q	0005737	cellular_component	cytoplasm
Q	0005856	cellular_component	cytoskeleton
Q	0005865	cellular_component	striated muscle thin filament
Q	0005884	cellular_component	actin filament
Q	0010628	biological_process	positive regulation of gene expression
Q	0016787	molecular_function	hydrolase activity
Q	0019904	molecular_function	protein domain specific binding
Q	0030027	cellular_component	lamellipodium
Q	0030041	biological_process	actin filament polymerization
Q	0030175	cellular_component	filopodium
Q	0030240	biological_process	skeletal muscle thin filament assembly
Q	0031013	molecular_function	troponin I binding
Q	0031432	molecular_function	titin binding
Q	0031941	cellular_component	filamentous actin
Q	0032036	molecular_function	myosin heavy chain binding
Q	0032432	cellular_component	actin filament bundle
Q	0042802	molecular_function	identical protein binding
Q	0044297	cellular_component	cell body
Q	0048306	molecular_function	calcium-dependent protein binding
Q	0048741	biological_process	skeletal muscle fiber development
Q	0051017	biological_process	actin filament bundle assembly
Q	0090131	biological_process	mesenchyme migration
Q	0098723	cellular_component	skeletal muscle myofibril
Q	0140660	molecular_function	cytoskeletal motor activator activity
R	0000166	molecular_function	nucleotide binding
R	0000287	molecular_function	magnesium ion binding
R	0001725	cellular_component	stress fiber
R	0003785	molecular_function	actin monomer binding
R	0005509	molecular_function	calcium ion binding
R	0005515	molecular_function	protein binding
R	0005523	molecular_function	tropomyosin binding
R	0005524	molecular_function	ATP binding
R	0005737	cellular_component	cytoplasm
R	0005856	cellular_component	cytoskeleton
R	0005865	cellular_component	striated muscle thin filament
R	0005884	cellular_component	actin filament
R	0010628	biological_process	positive regulation of gene expression
R	0016787	molecular_function	hydrolase activity
R	0019904	molecular_function	protein domain specific binding
R	0030027	cellular_component	lamellipodium
R	0030041	biological_process	actin filament polymerization
R	0030175	cellular_component	filopodium
R	0030240	biological_process	skeletal muscle thin filament assembly
R	0031013	molecular_function	troponin I binding
R	0031432	molecular_function	titin binding
R	0031941	cellular_component	filamentous actin
R	0032036	molecular_function	myosin heavy chain binding
R	0032432	cellular_component	actin filament bundle
R	0042802	molecular_function	identical protein binding
R	0044297	cellular_component	cell body
R	0048306	molecular_function	calcium-dependent protein binding
R	0048741	biological_process	skeletal muscle fiber development
R	0051017	biological_process	actin filament bundle assembly
R	0090131	biological_process	mesenchyme migration
R	0098723	cellular_component	skeletal muscle myofibril
R	0140660	molecular_function	cytoskeletal motor activator activity
S	0000166	molecular_function	nucleotide binding
S	0000287	molecular_function	magnesium ion binding
S	0001725	cellular_component	stress fiber
S	0003785	molecular_function	actin monomer binding
S	0005509	molecular_function	calcium ion binding
S	0005515	molecular_function	protein binding
S	0005523	molecular_function	tropomyosin binding
S	0005524	molecular_function	ATP binding
S	0005737	cellular_component	cytoplasm
S	0005856	cellular_component	cytoskeleton
S	0005865	cellular_component	striated muscle thin filament
S	0005884	cellular_component	actin filament
S	0010628	biological_process	positive regulation of gene expression
S	0016787	molecular_function	hydrolase activity
S	0019904	molecular_function	protein domain specific binding
S	0030027	cellular_component	lamellipodium
S	0030041	biological_process	actin filament polymerization
S	0030175	cellular_component	filopodium
S	0030240	biological_process	skeletal muscle thin filament assembly
S	0031013	molecular_function	troponin I binding
S	0031432	molecular_function	titin binding
S	0031941	cellular_component	filamentous actin
S	0032036	molecular_function	myosin heavy chain binding
S	0032432	cellular_component	actin filament bundle
S	0042802	molecular_function	identical protein binding
S	0044297	cellular_component	cell body
S	0048306	molecular_function	calcium-dependent protein binding
S	0048741	biological_process	skeletal muscle fiber development
S	0051017	biological_process	actin filament bundle assembly
S	0090131	biological_process	mesenchyme migration
S	0098723	cellular_component	skeletal muscle myofibril
S	0140660	molecular_function	cytoskeletal motor activator activity
T	0000166	molecular_function	nucleotide binding
T	0000287	molecular_function	magnesium ion binding
T	0001725	cellular_component	stress fiber
T	0003785	molecular_function	actin monomer binding
T	0005509	molecular_function	calcium ion binding
T	0005515	molecular_function	protein binding
T	0005523	molecular_function	tropomyosin binding
T	0005524	molecular_function	ATP binding
T	0005737	cellular_component	cytoplasm
T	0005856	cellular_component	cytoskeleton
T	0005865	cellular_component	striated muscle thin filament
T	0005884	cellular_component	actin filament
T	0010628	biological_process	positive regulation of gene expression
T	0016787	molecular_function	hydrolase activity
T	0019904	molecular_function	protein domain specific binding
T	0030027	cellular_component	lamellipodium
T	0030041	biological_process	actin filament polymerization
T	0030175	cellular_component	filopodium
T	0030240	biological_process	skeletal muscle thin filament assembly
T	0031013	molecular_function	troponin I binding
T	0031432	molecular_function	titin binding
T	0031941	cellular_component	filamentous actin
T	0032036	molecular_function	myosin heavy chain binding
T	0032432	cellular_component	actin filament bundle
T	0042802	molecular_function	identical protein binding
T	0044297	cellular_component	cell body
T	0048306	molecular_function	calcium-dependent protein binding
T	0048741	biological_process	skeletal muscle fiber development
T	0051017	biological_process	actin filament bundle assembly
T	0090131	biological_process	mesenchyme migration
T	0098723	cellular_component	skeletal muscle myofibril
T	0140660	molecular_function	cytoskeletal motor activator activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP O 400

Chain	Residue
O	ASP11
O	ASP157
O	GLY182
O	LYS213
O	GLU214
O	MET305
O	TYR306
O	LYS336
O	CA500
O	ASN12
O	GLY13
O	SER14
O	GLY15
O	LEU16
O	LYS18
O	GLN137
O	GLY156

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA O 500

Chain	Residue
O	ASP11
O	ASN12
O	GLN137
O	ADP400

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP P 400

Chain	Residue
P	ASP11
P	ASN12
P	GLY13
P	SER14
P	GLY15
P	LEU16
P	LYS18
P	GLN137
P	GLY156
P	ASP157
P	GLY182
P	LYS213
P	GLU214
P	MET305
P	TYR306
P	LYS336
P	CA500

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA P 500

Chain	Residue
P	ASP11
P	ASN12
P	GLN137
P	ADP400

---

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ADP Q 400

Chain	Residue
Q	ASP11
Q	GLY13
Q	SER14
Q	GLY15
Q	LEU16
Q	LYS18
Q	GLN137
Q	GLY156
Q	ASP157
Q	GLY158
Q	ARG210
Q	LYS213
Q	GLU214
Q	GLY302
Q	MET305
Q	TYR306
Q	LYS336
Q	CA500

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA Q 500

Chain	Residue
Q	ASP11
Q	GLN137
Q	ADP400

---

site_id	AC7
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP R 400

Chain	Residue
R	ASP11
R	GLY13
R	SER14
R	GLY15
R	LEU16
R	LYS18
R	GLN137
R	GLY156
R	ASP157
R	GLY158
R	ARG210
R	LYS213
R	GLU214
R	GLU334
R	LYS336
R	TYR337
R	CA500

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA R 500

Chain	Residue
R	ASP11
R	GLN137
R	ADP400

---

site_id	AC9
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ADP S 400

Chain	Residue
S	LYS336
S	CA500
S	ASP11
S	ASN12
S	GLY13
S	SER14
S	GLY15
S	LEU16
S	LYS18
S	GLN137
S	GLY156
S	ASP157
S	GLY158
S	LYS213
S	GLU214
S	GLY302
S	MET305
S	TYR306

---

site_id	BC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA S 500

Chain	Residue
S	ASP11
S	GLN137
S	ADP400

---

site_id	BC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ADP T 400

Chain	Residue
T	ASP11
T	ASN12
T	GLY13
T	SER14
T	GLY15
T	LEU16
T	LYS18
T	GLN137
T	GLY156
T	ASP157
T	GLY182
T	LYS213
T	GLU214
T	GLY302
T	MET305
T	TYR306
T	LYS336
T	CA500

---

site_id	BC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA T 500

Chain	Residue
T	ASP11
T	GLN137
T	ADP400

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
O	TYR53-GLY63

---

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

Chain	Residue	Details
O	TRP356-GLU364

---

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

Chain	Residue	Details
O	LEU104-ARG116

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	150
Details	Region: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	6
Details	Modified residue: {"description":"N-acetylaspartate; in Actin, alpha skeletal muscle","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P68134","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	6
Details	Modified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---