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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7CCC

The structure of the actin filament uncapping complex mediated by twinfilin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0001725cellular_componentstress fiber
A0003785molecular_functionactin monomer binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005523molecular_functiontropomyosin binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005865cellular_componentstriated muscle thin filament
A0005884cellular_componentactin filament
A0010628biological_processpositive regulation of gene expression
A0016787molecular_functionhydrolase activity
A0019904molecular_functionprotein domain specific binding
A0030027cellular_componentlamellipodium
A0030041biological_processactin filament polymerization
A0030175cellular_componentfilopodium
A0030240biological_processskeletal muscle thin filament assembly
A0031013molecular_functiontroponin I binding
A0031432molecular_functiontitin binding
A0031941cellular_componentfilamentous actin
A0032036molecular_functionmyosin heavy chain binding
A0032432cellular_componentactin filament bundle
A0042802molecular_functionidentical protein binding
A0044297cellular_componentcell body
A0048306molecular_functioncalcium-dependent protein binding
A0048741biological_processskeletal muscle fiber development
A0051017biological_processactin filament bundle assembly
A0090131biological_processmesenchyme migration
A0098723cellular_componentskeletal muscle myofibril
A0140660molecular_functioncytoskeletal motor activator activity
B0003779molecular_functionactin binding
B0003785molecular_functionactin monomer binding
B0004713molecular_functionprotein tyrosine kinase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005546molecular_functionphosphatidylinositol-4,5-bisphosphate binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005884cellular_componentactin filament
B0005911cellular_componentcell-cell junction
B0005925cellular_componentfocal adhesion
B0010591biological_processregulation of lamellipodium assembly
B0010613biological_processpositive regulation of cardiac muscle hypertrophy
B0010976biological_processpositive regulation of neuron projection development
B0015629cellular_componentactin cytoskeleton
B0030016cellular_componentmyofibril
B0030042biological_processactin filament depolymerization
B0030175cellular_componentfilopodium
B0030837biological_processnegative regulation of actin filament polymerization
B0032587cellular_componentruffle membrane
B0043168molecular_functionanion binding
B0044877molecular_functionprotein-containing complex binding
B0045296molecular_functioncadherin binding
B0048471cellular_componentperinuclear region of cytoplasm
B0051015molecular_functionactin filament binding
B0051016biological_processbarbed-end actin filament capping
C0003779molecular_functionactin binding
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0005903cellular_componentbrush border
C0005911cellular_componentcell-cell junction
C0008290cellular_componentF-actin capping protein complex
C0016020cellular_componentmembrane
C0030036biological_processactin cytoskeleton organization
C0030863cellular_componentcortical cytoskeleton
C0034329biological_processcell junction assembly
C0051015molecular_functionactin filament binding
C0051016biological_processbarbed-end actin filament capping
C0051693biological_processactin filament capping
C0071203cellular_componentWASH complex
D0003779molecular_functionactin binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0008290cellular_componentF-actin capping protein complex
D0030017cellular_componentsarcomere
D0030036biological_processactin cytoskeleton organization
D0051016biological_processbarbed-end actin filament capping
D0051693biological_processactin filament capping
E0000166molecular_functionnucleotide binding
E0000287molecular_functionmagnesium ion binding
E0001725cellular_componentstress fiber
E0003785molecular_functionactin monomer binding
E0005509molecular_functioncalcium ion binding
E0005515molecular_functionprotein binding
E0005523molecular_functiontropomyosin binding
E0005524molecular_functionATP binding
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005865cellular_componentstriated muscle thin filament
E0005884cellular_componentactin filament
E0010628biological_processpositive regulation of gene expression
E0016787molecular_functionhydrolase activity
E0019904molecular_functionprotein domain specific binding
E0030027cellular_componentlamellipodium
E0030041biological_processactin filament polymerization
E0030175cellular_componentfilopodium
E0030240biological_processskeletal muscle thin filament assembly
E0031013molecular_functiontroponin I binding
E0031432molecular_functiontitin binding
E0031941cellular_componentfilamentous actin
E0032036molecular_functionmyosin heavy chain binding
E0032432cellular_componentactin filament bundle
E0042802molecular_functionidentical protein binding
E0044297cellular_componentcell body
E0048306molecular_functioncalcium-dependent protein binding
E0048741biological_processskeletal muscle fiber development
E0051017biological_processactin filament bundle assembly
E0090131biological_processmesenchyme migration
E0098723cellular_componentskeletal muscle myofibril
E0140660molecular_functioncytoskeletal motor activator activity
Functional Information from PROSITE/UniProt
site_idPS00231
Number of Residues6
DetailsF_ACTIN_CAPPING_BETA F-actin capping protein beta subunit signature. CDYNRD
ChainResidueDetails
DCYS62-ASP67
site_idPS00406
Number of Residues11
DetailsACTINS_1 Actins signature 1. YVGDEAQs.KRG
ChainResidueDetails
ATYR53-GLY63
site_idPS00432
Number of Residues9
DetailsACTINS_2 Actins signature 2. WITKqEYDE
ChainResidueDetails
ATRP356-GLU364
site_idPS00748
Number of Residues9
DetailsF_ACTIN_CAPPING_A_1 F-actin capping protein alpha subunit signature 1. VHYYEDGNV
ChainResidueDetails
CVAL196-VAL204
site_idPS00749
Number of Residues11
DetailsF_ACTIN_CAPPING_A_2 F-actin capping protein alpha subunit signature 2. KaLRRqLPVTR
ChainResidueDetails
CLYS256-ARG266
site_idPS01132
Number of Residues13
DetailsACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApLNPkaNR
ChainResidueDetails
ALEU104-ARG116
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues26
DetailsRegion: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Tele-methylhistidine","evidences":[{"source":"PubMed","id":"1150665","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"213279","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2395459","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"499690","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ATN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NWK","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues137
DetailsDomain: {"description":"ADF-H 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00599","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues138
DetailsDomain: {"description":"ADF-H 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00599","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q5RJR2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P52907","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"23806337","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52907","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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