3CHW

Complex of Dictyostelium discoideum Actin with Profilin and the Last Poly-Pro of Human VASP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000281	biological_process	mitotic cytokinesis
A	0000902	biological_process	cell morphogenesis
A	0001778	biological_process	plasma membrane repair
A	0001891	cellular_component	phagocytic cup
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005515	molecular_function	protein binding
A	0005811	cellular_component	lipid droplet
A	0005856	cellular_component	cytoskeleton
A	0005884	cellular_component	actin filament
A	0005911	cellular_component	cell-cell junction
A	0005938	cellular_component	cell cortex
A	0006897	biological_process	endocytosis
A	0006909	biological_process	phagocytosis
A	0006935	biological_process	chemotaxis
A	0006972	biological_process	hyperosmotic response
A	0007010	biological_process	cytoskeleton organization
A	0015629	cellular_component	actin cytoskeleton
A	0016192	biological_process	vesicle-mediated transport
A	0017022	molecular_function	myosin binding
A	0030027	cellular_component	lamellipodium
A	0030139	cellular_component	endocytic vesicle
A	0030864	cellular_component	cortical actin cytoskeleton
A	0031143	cellular_component	pseudopodium
A	0031252	cellular_component	cell leading edge
A	0032009	cellular_component	early phagosome
A	0032010	cellular_component	phagolysosome
A	0042331	biological_process	phototaxis
A	0045335	cellular_component	phagocytic vesicle
A	0051591	biological_process	response to cAMP
A	0060187	cellular_component	cell pole
A	0061836	cellular_component	intranuclear rod
A	0061851	cellular_component	leading edge of lamellipodium
A	0070685	cellular_component	macropinocytic cup
P	0000774	molecular_function	adenyl-nucleotide exchange factor activity
P	0001784	molecular_function	phosphotyrosine residue binding
P	0003723	molecular_function	RNA binding
P	0003779	molecular_function	actin binding
P	0003785	molecular_function	actin monomer binding
P	0005515	molecular_function	protein binding
P	0005546	molecular_function	phosphatidylinositol-4,5-bisphosphate binding
P	0005634	cellular_component	nucleus
P	0005737	cellular_component	cytoplasm
P	0005829	cellular_component	cytosol
P	0005856	cellular_component	cytoskeleton
P	0005925	cellular_component	focal adhesion
P	0005938	cellular_component	cell cortex
P	0010634	biological_process	positive regulation of epithelial cell migration
P	0016020	cellular_component	membrane
P	0030036	biological_process	actin cytoskeleton organization
P	0030833	biological_process	regulation of actin filament polymerization
P	0030838	biological_process	positive regulation of actin filament polymerization
P	0031267	molecular_function	small GTPase binding
P	0032232	biological_process	negative regulation of actin filament bundle assembly
P	0032233	biological_process	positive regulation of actin filament bundle assembly
P	0045296	molecular_function	cadherin binding
P	0050804	biological_process	modulation of chemical synaptic transmission
P	0050821	biological_process	protein stabilization
P	0051497	biological_process	negative regulation of stress fiber assembly
P	0060074	biological_process	synapse maturation
P	0070062	cellular_component	extracellular exosome
P	0070064	molecular_function	proline-rich region binding
P	0072562	cellular_component	blood microparticle
P	0098885	biological_process	modification of postsynaptic actin cytoskeleton
P	0098978	cellular_component	glutamatergic synapse
P	0110053	biological_process	regulation of actin filament organization
P	1900029	biological_process	positive regulation of ruffle assembly

Functional Information from PDB Data

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP A 402

Chain	Residue
A	GLY13
A	ARG210
A	LYS213
A	GLU214
A	GLY301
A	GLY302
A	THR303
A	MET305
A	PHE306
A	LYS336
A	SER14
A	GLY15
A	MET16
A	LYS18
A	GLY156
A	ASP157
A	GLY158
A	GLY182

---

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	PS00414
Number of Residues	8
Details	PROFILIN Profilin signature. .AgWNaYiD

Chain	Residue	Details
P	ALA1-ASP8

---

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

Chain	Residue	Details
A	TRP356-GLU364

---

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	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"7498488","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"3342873","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62963","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by ROCK1","evidences":[{"source":"PubMed","id":"18573880","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}

Chain

Residue

Details

---