Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8VO7

Cryo-EM structure of fascin crosslinked F-actin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001725	cellular_component	stress fiber
A	0001726	cellular_component	ruffle
A	0002102	cellular_component	podosome
A	0003723	molecular_function	RNA binding
A	0003779	molecular_function	actin binding
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005902	cellular_component	microvillus
A	0005911	cellular_component	cell-cell junction
A	0005938	cellular_component	cell cortex
A	0007015	biological_process	actin filament organization
A	0007043	biological_process	cell-cell junction assembly
A	0007163	biological_process	establishment or maintenance of cell polarity
A	0008144	molecular_function	obsolete drug binding
A	0010592	biological_process	positive regulation of lamellipodium assembly
A	0015629	cellular_component	actin cytoskeleton
A	0016477	biological_process	cell migration
A	0030027	cellular_component	lamellipodium
A	0030035	biological_process	microspike assembly
A	0030036	biological_process	actin cytoskeleton organization
A	0030046	biological_process	parallel actin filament bundle assembly
A	0030175	cellular_component	filopodium
A	0030426	cellular_component	growth cone
A	0030674	molecular_function	protein-macromolecule adaptor activity
A	0031252	cellular_component	cell leading edge
A	0031253	cellular_component	cell projection membrane
A	0032534	biological_process	regulation of microvillus assembly
A	0032956	biological_process	regulation of actin cytoskeleton organization
A	0035089	biological_process	establishment of apical/basal cell polarity
A	0042995	cellular_component	cell projection
A	0044393	cellular_component	microspike
A	0045296	molecular_function	cadherin binding
A	0048870	biological_process	cell motility
A	0051015	molecular_function	actin filament binding
A	0051017	biological_process	actin filament bundle assembly
A	0051491	biological_process	positive regulation of filopodium assembly
A	0070062	cellular_component	extracellular exosome
A	0070161	cellular_component	anchoring junction
A	0071803	biological_process	positive regulation of podosome assembly
A	0090091	biological_process	positive regulation of extracellular matrix disassembly
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
F	0000166	molecular_function	nucleotide binding
F	0001725	cellular_component	stress fiber
F	0005200	molecular_function	structural constituent of cytoskeleton
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP 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	0016787	molecular_function	hydrolase activity
F	0030240	biological_process	skeletal muscle thin filament assembly
F	0048741	biological_process	skeletal muscle fiber development
G	0000166	molecular_function	nucleotide binding
G	0001725	cellular_component	stress fiber
G	0005200	molecular_function	structural constituent of cytoskeleton
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP 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	0016787	molecular_function	hydrolase activity
G	0030240	biological_process	skeletal muscle thin filament assembly
G	0048741	biological_process	skeletal muscle fiber development

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
B	TYR53-GLY63

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

Chain	Residue	Details
B	TRP356-GLU364

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

Chain	Residue	Details
B	LEU104-ARG116

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"8999969","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22155786","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q61553","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
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":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P85845","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
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_FI9
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_FI10
Number of Residues	6
Details	Modified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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