6UPV

Alpha-E-catenin ABD-F-actin complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0001725	cellular_component	stress fiber
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005856	cellular_component	cytoskeleton
A	0005865	cellular_component	striated muscle thin filament
A	0005884	cellular_component	actin filament
A	0015629	cellular_component	actin cytoskeleton
A	0016787	molecular_function	hydrolase activity
A	0030240	biological_process	skeletal muscle thin filament assembly
A	0048741	biological_process	skeletal muscle fiber development
B	0000166	molecular_function	nucleotide binding
B	0001725	cellular_component	stress fiber
B	0005200	molecular_function	structural constituent of cytoskeleton
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005856	cellular_component	cytoskeleton
B	0005865	cellular_component	striated muscle thin filament
B	0005884	cellular_component	actin filament
B	0015629	cellular_component	actin cytoskeleton
B	0016787	molecular_function	hydrolase activity
B	0030240	biological_process	skeletal muscle thin filament assembly
B	0048741	biological_process	skeletal muscle fiber development
C	0000166	molecular_function	nucleotide binding
C	0001725	cellular_component	stress fiber
C	0005200	molecular_function	structural constituent of cytoskeleton
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005856	cellular_component	cytoskeleton
C	0005865	cellular_component	striated muscle thin filament
C	0005884	cellular_component	actin filament
C	0015629	cellular_component	actin cytoskeleton
C	0016787	molecular_function	hydrolase activity
C	0030240	biological_process	skeletal muscle thin filament assembly
C	0048741	biological_process	skeletal muscle fiber development
D	0000166	molecular_function	nucleotide binding
D	0001725	cellular_component	stress fiber
D	0005200	molecular_function	structural constituent of cytoskeleton
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005856	cellular_component	cytoskeleton
D	0005865	cellular_component	striated muscle thin filament
D	0005884	cellular_component	actin filament
D	0015629	cellular_component	actin cytoskeleton
D	0016787	molecular_function	hydrolase activity
D	0030240	biological_process	skeletal muscle thin filament assembly
D	0048741	biological_process	skeletal muscle fiber development
E	0000166	molecular_function	nucleotide binding
E	0001725	cellular_component	stress fiber
E	0005200	molecular_function	structural constituent of cytoskeleton
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005856	cellular_component	cytoskeleton
E	0005865	cellular_component	striated muscle thin filament
E	0005884	cellular_component	actin filament
E	0015629	cellular_component	actin cytoskeleton
E	0016787	molecular_function	hydrolase activity
E	0030240	biological_process	skeletal muscle thin filament assembly
E	0048741	biological_process	skeletal muscle fiber development
L	0001541	biological_process	ovarian follicle development
L	0001669	cellular_component	acrosomal vesicle
L	0003723	molecular_function	RNA binding
L	0005198	molecular_function	structural molecule activity
L	0005515	molecular_function	protein binding
L	0005634	cellular_component	nucleus
L	0005737	cellular_component	cytoplasm
L	0005829	cellular_component	cytosol
L	0005856	cellular_component	cytoskeleton
L	0005886	cellular_component	plasma membrane
L	0005911	cellular_component	cell-cell junction
L	0005912	cellular_component	adherens junction
L	0005915	cellular_component	zonula adherens
L	0005925	cellular_component	focal adhesion
L	0007155	biological_process	cell adhesion
L	0008013	molecular_function	beta-catenin binding
L	0008092	molecular_function	cytoskeletal protein binding
L	0008584	biological_process	male gonad development
L	0014704	cellular_component	intercalated disc
L	0015629	cellular_component	actin cytoskeleton
L	0016264	biological_process	gap junction assembly
L	0016342	cellular_component	catenin complex
L	0016477	biological_process	cell migration
L	0016600	cellular_component	flotillin complex
L	0017166	molecular_function	vinculin binding
L	0030027	cellular_component	lamellipodium
L	0030054	cellular_component	cell junction
L	0031103	biological_process	axon regeneration
L	0042475	biological_process	odontogenesis of dentin-containing tooth
L	0042802	molecular_function	identical protein binding
L	0043297	biological_process	apical junction assembly
L	0043627	biological_process	response to estrogen
L	0044877	molecular_function	protein-containing complex binding
L	0045295	molecular_function	gamma-catenin binding
L	0045296	molecular_function	cadherin binding
L	0051015	molecular_function	actin filament binding
L	0070161	cellular_component	anchoring junction
L	0071681	biological_process	cellular response to indole-3-methanol
L	0098609	biological_process	cell-cell adhesion
L	0098797	cellular_component	plasma membrane protein complex
L	1900181	biological_process	negative regulation of protein localization to nucleus
M	0001541	biological_process	ovarian follicle development
M	0001669	cellular_component	acrosomal vesicle
M	0003723	molecular_function	RNA binding
M	0005198	molecular_function	structural molecule activity
M	0005515	molecular_function	protein binding
M	0005634	cellular_component	nucleus
M	0005737	cellular_component	cytoplasm
M	0005829	cellular_component	cytosol
M	0005856	cellular_component	cytoskeleton
M	0005886	cellular_component	plasma membrane
M	0005911	cellular_component	cell-cell junction
M	0005912	cellular_component	adherens junction
M	0005915	cellular_component	zonula adherens
M	0005925	cellular_component	focal adhesion
M	0007155	biological_process	cell adhesion
M	0008013	molecular_function	beta-catenin binding
M	0008092	molecular_function	cytoskeletal protein binding
M	0008584	biological_process	male gonad development
M	0014704	cellular_component	intercalated disc
M	0015629	cellular_component	actin cytoskeleton
M	0016264	biological_process	gap junction assembly
M	0016342	cellular_component	catenin complex
M	0016477	biological_process	cell migration
M	0016600	cellular_component	flotillin complex
M	0017166	molecular_function	vinculin binding
M	0030027	cellular_component	lamellipodium
M	0030054	cellular_component	cell junction
M	0031103	biological_process	axon regeneration
M	0042475	biological_process	odontogenesis of dentin-containing tooth
M	0042802	molecular_function	identical protein binding
M	0043297	biological_process	apical junction assembly
M	0043627	biological_process	response to estrogen
M	0044877	molecular_function	protein-containing complex binding
M	0045295	molecular_function	gamma-catenin binding
M	0045296	molecular_function	cadherin binding
M	0051015	molecular_function	actin filament binding
M	0070161	cellular_component	anchoring junction
M	0071681	biological_process	cellular response to indole-3-methanol
M	0098609	biological_process	cell-cell adhesion
M	0098797	cellular_component	plasma membrane protein complex
M	1900181	biological_process	negative regulation of protein localization to nucleus

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	binding site for residue ADP A 401

Chain	Residue
A	GLY13
A	TYR306
A	MG402
A	SER14
A	LEU16
A	LYS18
A	ASP157
A	GLY182
A	LYS213
A	GLY302
A	THR303

---

site_id	AC2
Number of Residues	2
Details	binding site for residue MG A 402

Chain	Residue
A	GLN137
A	ADP401

---

site_id	AC3
Number of Residues	13
Details	binding site for residue ADP B 401

Chain	Residue
B	GLY13
B	SER14
B	LEU16
B	LYS18
B	GLY156
B	ASP157
B	GLY182
B	LYS213
B	GLU214
B	GLY302
B	TYR306
B	LYS336
B	MG402

---

site_id	AC4
Number of Residues	2
Details	binding site for residue MG B 402

Chain	Residue
B	GLN137
B	ADP401

---

site_id	AC5
Number of Residues	13
Details	binding site for residue ADP C 401

Chain	Residue
C	GLY13
C	SER14
C	GLY15
C	LEU16
C	LYS18
C	GLY156
C	ASP157
C	LYS213
C	GLU214
C	GLY302
C	TYR306
C	LYS336
C	MG402

---

site_id	AC6
Number of Residues	2
Details	binding site for residue MG C 402

Chain	Residue
C	GLN137
C	ADP401

---

site_id	AC7
Number of Residues	11
Details	binding site for residue ADP D 401

Chain	Residue
D	GLY13
D	SER14
D	LEU16
D	LYS18
D	ASP157
D	LYS213
D	GLY301
D	GLY302
D	TYR306
D	LYS336
D	MG402

---

site_id	AC8
Number of Residues	2
Details	binding site for residue MG D 402

Chain	Residue
D	GLN137
D	ADP401

---

site_id	AC9
Number of Residues	12
Details	binding site for residue ADP E 401

Chain	Residue
E	GLY13
E	SER14
E	LEU16
E	LYS18
E	ASP157
E	LYS213
E	GLU214
E	GLY301
E	GLY302
E	TYR306
E	LYS336
E	MG402

---

site_id	AD1
Number of Residues	2
Details	binding site for residue MG E 402

Chain	Residue
E	GLN137
E	ADP401

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	TYR53-GLY63

---

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

Chain	Residue	Details
A	TRP356-GLU364

---

site_id	PS00663
Number of Residues	21
Details	VINCULIN_1 Vinculin family talin-binding region signature. KaLkpeVdkLnimaakRQQEL

Chain	Residue	Details
M	LYS178-LEU198

---

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

Chain	Residue	Details
A	LEU104-ARG116

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	10
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	5
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_FI5
Number of Residues	5
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---