Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8VDP

Cryogenic electron microscopy model of full-length talin without FABD

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001726	cellular_component	ruffle
A	0001786	molecular_function	phosphatidylserine binding
A	0003779	molecular_function	actin binding
A	0005178	molecular_function	integrin binding
A	0005200	molecular_function	structural constituent of cytoskeleton
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005886	cellular_component	plasma membrane
A	0005912	cellular_component	adherens junction
A	0005925	cellular_component	focal adhesion
A	0006091	biological_process	generation of precursor metabolites and energy
A	0007044	biological_process	cell-substrate junction assembly
A	0007155	biological_process	cell adhesion
A	0007229	biological_process	integrin-mediated signaling pathway
A	0008218	biological_process	bioluminescence
A	0009986	cellular_component	cell surface
A	0017166	molecular_function	vinculin binding
A	0030036	biological_process	actin cytoskeleton organization
A	0030274	molecular_function	LIM domain binding
A	0030866	biological_process	cortical actin cytoskeleton organization
A	0032587	cellular_component	ruffle membrane
A	0033622	biological_process	integrin activation
A	0034329	biological_process	cell junction assembly
A	0034451	cellular_component	centriolar satellite
A	0035091	molecular_function	phosphatidylinositol binding
A	0043622	biological_process	cortical microtubule organization
A	0051015	molecular_function	actin filament binding
A	0070161	cellular_component	anchoring junction
A	0098609	biological_process	cell-cell adhesion

Functional Information from PROSITE/UniProt

site_id	PS00660
Number of Residues	29
Details	FERM_1 FERM domain signature 1. WLdhgRtLreQg.Veehetll.Lrrk..FFysD

Chain	Residue	Details
A	TRP173-ASP201

site_id	PS00661
Number of Residues	30
Details	FERM_2 FERM domain signature 2. HkncgqmseiEAkvrYVkl.ArsLktYGvSF

Chain	Residue	Details
A	HIS283-PHE312

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	130
Details	Region: {"description":"Helical bundle R2","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	124
Details	Region: {"description":"Helical bundle R3","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	131
Details	Region: {"description":"Helical bundle R4","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	160
Details	Region: {"description":"Helical bundle R5","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	150
Details	Region: {"description":"Helical bundle R6","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	621
Details	Region: {"description":"Interaction with SYNM","evidences":[{"source":"UniProtKB","id":"P54939","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	95
Details	Region: {"description":"Helical bundle R7A; Interaction with KANK1","evidences":[{"source":"PubMed","id":"27410476","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	300
Details	Region: {"description":"Interaction with VCL and F-actin","evidences":[{"source":"PubMed","id":"20610383","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	119
Details	Region: {"description":"Helical bundle R8","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	72
Details	Region: {"description":"Helical bundle R7B; Interaction with KANK1","evidences":[{"source":"PubMed","id":"27410476","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	167
Details	Region: {"description":"Helical bundle R9","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	150
Details	Region: {"description":"Helical bundle R10","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	166
Details	Region: {"description":"Helical bundle R11","evidences":[{"source":"PubMed","id":"23389036","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Y490","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	5
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21183079","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18034455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q9Y490","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9Y490","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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