Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2BTF

THE STRUCTURE OF CRYSTALLINE PROFILIN-BETA-ACTIN

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000786	cellular_component	nucleosome
A	0001738	biological_process	morphogenesis of a polarized epithelium
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005884	cellular_component	actin filament
A	0005886	cellular_component	plasma membrane
A	0005903	cellular_component	brush border
A	0005911	cellular_component	cell-cell junction
A	0005912	cellular_component	adherens junction
A	0005925	cellular_component	focal adhesion
A	0007163	biological_process	establishment or maintenance of cell polarity
A	0007409	biological_process	axonogenesis
A	0015629	cellular_component	actin cytoskeleton
A	0016020	cellular_component	membrane
A	0016787	molecular_function	hydrolase activity
A	0016887	molecular_function	ATP hydrolysis activity
A	0019894	molecular_function	kinesin binding
A	0019901	molecular_function	protein kinase binding
A	0030027	cellular_component	lamellipodium
A	0030235	molecular_function	nitric-oxide synthase regulator activity
A	0030424	cellular_component	axon
A	0030863	cellular_component	cortical cytoskeleton
A	0030957	molecular_function	Tat protein binding
A	0032991	cellular_component	protein-containing complex
A	0034333	biological_process	adherens junction assembly
A	0035267	cellular_component	NuA4 histone acetyltransferase complex
A	0036464	cellular_component	cytoplasmic ribonucleoprotein granule
A	0042802	molecular_function	identical protein binding
A	0043296	cellular_component	apical junction complex
A	0044305	cellular_component	calyx of Held
A	0045176	biological_process	apical protein localization
A	0045202	cellular_component	synapse
A	0048870	biological_process	cell motility
A	0050998	molecular_function	nitric-oxide synthase binding
A	0051621	biological_process	regulation of norepinephrine uptake
A	0051726	biological_process	regulation of cell cycle
A	0070160	cellular_component	tight junction
A	0071896	biological_process	protein localization to adherens junction
A	0072749	biological_process	cellular response to cytochalasin B
A	0097433	cellular_component	dense body
A	0098685	cellular_component	Schaffer collateral - CA1 synapse
A	0098871	cellular_component	postsynaptic actin cytoskeleton
A	0098973	molecular_function	structural constituent of postsynaptic actin cytoskeleton
A	0098974	biological_process	postsynaptic actin cytoskeleton organization
A	0098978	cellular_component	glutamatergic synapse
A	0141108	molecular_function	transporter regulator activity
A	0150111	biological_process	regulation of transepithelial transport
A	1900242	biological_process	regulation of synaptic vesicle endocytosis
A	1903076	biological_process	regulation of protein localization to plasma membrane
A	1905168	biological_process	positive regulation of double-strand break repair via homologous recombination
A	1990904	cellular_component	ribonucleoprotein complex
P	0003779	molecular_function	actin binding
P	0005737	cellular_component	cytoplasm
P	0005856	cellular_component	cytoskeleton
P	0030036	biological_process	actin cytoskeleton organization
P	0030833	biological_process	regulation of actin filament polymerization
P	0032233	biological_process	positive regulation of actin filament bundle assembly
P	0110053	biological_process	regulation of actin filament organization

Functional Information from PDB Data

site_id	1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SR A 1

Chain	Residue
A	GLN137
A	ATP377

site_id	2
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ATP A 377

Chain	Residue
A	GLY13
A	GLY182
A	LYS213
A	GLU214
A	GLY302
A	TYR306
A	LYS336
A	SR1
A	SER14
A	GLY15
A	MET16
A	LYS18
A	GLY156
A	ASP157
A	GLY158
A	VAL159

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SR A 1

Chain	Residue
A	GLN137
A	ATP377

site_id	AC2
Number of Residues	19
Details	BINDING SITE FOR RESIDUE ATP A 377

Chain	Residue
A	SR1
A	GLY13
A	SER14
A	GLY15
A	MET16
A	LYS18
A	GLY156
A	ASP157
A	GLY158
A	VAL159
A	GLY182
A	LYS213
A	GLU214
A	GLY301
A	GLY302
A	THR303
A	MET305
A	TYR306
A	LYS336

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	9
Details	PROFILIN Profilin signature. xAgWNaYiD

Chain	Residue	Details
P	ACE0-ASP8

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

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":"N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed","evidences":[{"source":"UniProtKB","id":"P60709","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Methionine (R)-sulfoxide","evidences":[{"source":"UniProtKB","id":"P60710","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"UniProtKB","id":"P60710","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P60709","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"3342873","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"446730","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P62963","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P07737","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07737","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P07737","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P07737","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)