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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9Y9L

CP at the barbed end with one cofilin on second-to-last subunit

Functional Information from GO Data
ChainGOidnamespacecontents
a0005515molecular_functionprotein binding
a0005576cellular_componentextracellular region
a0005737cellular_componentcytoplasm
a0005856cellular_componentcytoskeleton
a0008154biological_processactin polymerization or depolymerization
a0015629cellular_componentactin cytoskeleton
a0016363cellular_componentnuclear matrix
a0030018cellular_componentZ disc
a0030042biological_processactin filament depolymerization
a0030043biological_processactin filament fragmentation
a0030836biological_processpositive regulation of actin filament depolymerization
a0031674cellular_componentI band
a0051014biological_processactin filament severing
a0051015molecular_functionactin filament binding
a0070062cellular_componentextracellular exosome
A0000287molecular_functionmagnesium ion binding
A0001725cellular_componentstress fiber
A0003785molecular_functionactin monomer binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005523molecular_functiontropomyosin binding
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005865cellular_componentstriated muscle thin filament
A0005884cellular_componentactin filament
A0010628biological_processpositive regulation of gene expression
A0016887molecular_functionATP hydrolysis 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
b0005515molecular_functionprotein binding
b0005576cellular_componentextracellular region
b0005737cellular_componentcytoplasm
b0005856cellular_componentcytoskeleton
b0008154biological_processactin polymerization or depolymerization
b0015629cellular_componentactin cytoskeleton
b0016363cellular_componentnuclear matrix
b0030018cellular_componentZ disc
b0030042biological_processactin filament depolymerization
b0030043biological_processactin filament fragmentation
b0030836biological_processpositive regulation of actin filament depolymerization
b0031674cellular_componentI band
b0051014biological_processactin filament severing
b0051015molecular_functionactin filament binding
b0070062cellular_componentextracellular exosome
B0000287molecular_functionmagnesium ion binding
B0001725cellular_componentstress fiber
B0003785molecular_functionactin monomer binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005523molecular_functiontropomyosin binding
B0005737cellular_componentcytoplasm
B0005856cellular_componentcytoskeleton
B0005865cellular_componentstriated muscle thin filament
B0005884cellular_componentactin filament
B0010628biological_processpositive regulation of gene expression
B0016887molecular_functionATP hydrolysis activity
B0019904molecular_functionprotein domain specific binding
B0030027cellular_componentlamellipodium
B0030041biological_processactin filament polymerization
B0030175cellular_componentfilopodium
B0030240biological_processskeletal muscle thin filament assembly
B0031013molecular_functiontroponin I binding
B0031432molecular_functiontitin binding
B0031941cellular_componentfilamentous actin
B0032036molecular_functionmyosin heavy chain binding
B0032432cellular_componentactin filament bundle
B0042802molecular_functionidentical protein binding
B0044297cellular_componentcell body
B0048306molecular_functioncalcium-dependent protein binding
B0048741biological_processskeletal muscle fiber development
B0051017biological_processactin filament bundle assembly
B0090131biological_processmesenchyme migration
B0098723cellular_componentskeletal muscle myofibril
B0140660molecular_functioncytoskeletal motor activator activity
c0005515molecular_functionprotein binding
c0005576cellular_componentextracellular region
c0005737cellular_componentcytoplasm
c0005856cellular_componentcytoskeleton
c0008154biological_processactin polymerization or depolymerization
c0015629cellular_componentactin cytoskeleton
c0016363cellular_componentnuclear matrix
c0030018cellular_componentZ disc
c0030042biological_processactin filament depolymerization
c0030043biological_processactin filament fragmentation
c0030836biological_processpositive regulation of actin filament depolymerization
c0031674cellular_componentI band
c0051014biological_processactin filament severing
c0051015molecular_functionactin filament binding
c0070062cellular_componentextracellular exosome
C0000287molecular_functionmagnesium ion binding
C0001725cellular_componentstress fiber
C0003785molecular_functionactin monomer binding
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005523molecular_functiontropomyosin binding
C0005737cellular_componentcytoplasm
C0005856cellular_componentcytoskeleton
C0005865cellular_componentstriated muscle thin filament
C0005884cellular_componentactin filament
C0010628biological_processpositive regulation of gene expression
C0016887molecular_functionATP hydrolysis activity
C0019904molecular_functionprotein domain specific binding
C0030027cellular_componentlamellipodium
C0030041biological_processactin filament polymerization
C0030175cellular_componentfilopodium
C0030240biological_processskeletal muscle thin filament assembly
C0031013molecular_functiontroponin I binding
C0031432molecular_functiontitin binding
C0031941cellular_componentfilamentous actin
C0032036molecular_functionmyosin heavy chain binding
C0032432cellular_componentactin filament bundle
C0042802molecular_functionidentical protein binding
C0044297cellular_componentcell body
C0048306molecular_functioncalcium-dependent protein binding
C0048741biological_processskeletal muscle fiber development
C0051017biological_processactin filament bundle assembly
C0090131biological_processmesenchyme migration
C0098723cellular_componentskeletal muscle myofibril
C0140660molecular_functioncytoskeletal motor activator activity
d0005515molecular_functionprotein binding
d0005576cellular_componentextracellular region
d0005737cellular_componentcytoplasm
d0005856cellular_componentcytoskeleton
d0008154biological_processactin polymerization or depolymerization
d0015629cellular_componentactin cytoskeleton
d0016363cellular_componentnuclear matrix
d0030018cellular_componentZ disc
d0030042biological_processactin filament depolymerization
d0030043biological_processactin filament fragmentation
d0030836biological_processpositive regulation of actin filament depolymerization
d0031674cellular_componentI band
d0051014biological_processactin filament severing
d0051015molecular_functionactin filament binding
d0070062cellular_componentextracellular exosome
D0000287molecular_functionmagnesium ion binding
D0001725cellular_componentstress fiber
D0003785molecular_functionactin monomer binding
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005523molecular_functiontropomyosin binding
D0005737cellular_componentcytoplasm
D0005856cellular_componentcytoskeleton
D0005865cellular_componentstriated muscle thin filament
D0005884cellular_componentactin filament
D0010628biological_processpositive regulation of gene expression
D0016887molecular_functionATP hydrolysis activity
D0019904molecular_functionprotein domain specific binding
D0030027cellular_componentlamellipodium
D0030041biological_processactin filament polymerization
D0030175cellular_componentfilopodium
D0030240biological_processskeletal muscle thin filament assembly
D0031013molecular_functiontroponin I binding
D0031432molecular_functiontitin binding
D0031941cellular_componentfilamentous actin
D0032036molecular_functionmyosin heavy chain binding
D0032432cellular_componentactin filament bundle
D0042802molecular_functionidentical protein binding
D0044297cellular_componentcell body
D0048306molecular_functioncalcium-dependent protein binding
D0048741biological_processskeletal muscle fiber development
D0051017biological_processactin filament bundle assembly
D0090131biological_processmesenchyme migration
D0098723cellular_componentskeletal muscle myofibril
D0140660molecular_functioncytoskeletal motor activator activity
E0000287molecular_functionmagnesium ion binding
E0001725cellular_componentstress fiber
E0003785molecular_functionactin monomer binding
E0005509molecular_functioncalcium ion binding
E0005515molecular_functionprotein binding
E0005523molecular_functiontropomyosin binding
E0005737cellular_componentcytoplasm
E0005856cellular_componentcytoskeleton
E0005865cellular_componentstriated muscle thin filament
E0005884cellular_componentactin filament
E0010628biological_processpositive regulation of gene expression
E0016887molecular_functionATP hydrolysis 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
Y0003779molecular_functionactin binding
Y0005515molecular_functionprotein binding
Y0005576cellular_componentextracellular region
Y0005829cellular_componentcytosol
Y0005856cellular_componentcytoskeleton
Y0008290cellular_componentF-actin capping protein complex
Y0015629cellular_componentactin cytoskeleton
Y0030036biological_processactin cytoskeleton organization
Y0030863cellular_componentcortical cytoskeleton
Y0034329biological_processcell junction assembly
Y0045296molecular_functioncadherin binding
Y0051015molecular_functionactin filament binding
Y0051016biological_processbarbed-end actin filament capping
Y0065003biological_processprotein-containing complex assembly
Y0070062cellular_componentextracellular exosome
Y0071203cellular_componentWASH complex
Z0003779molecular_functionactin binding
Z0005515molecular_functionprotein binding
Z0005829cellular_componentcytosol
Z0005856cellular_componentcytoskeleton
Z0005903cellular_componentbrush border
Z0008290cellular_componentF-actin capping protein complex
Z0014069cellular_componentpostsynaptic density
Z0015629cellular_componentactin cytoskeleton
Z0016020cellular_componentmembrane
Z0030017cellular_componentsarcomere
Z0030027cellular_componentlamellipodium
Z0030863cellular_componentcortical cytoskeleton
Z0045296molecular_functioncadherin binding
Z0051016biological_processbarbed-end actin filament capping
Z0070062cellular_componentextracellular exosome
Z0071203cellular_componentWASH complex
Z0098685cellular_componentSchaffer collateral - CA1 synapse
Z0098686cellular_componenthippocampal mossy fiber to CA3 synapse
Z0120212cellular_componentsperm head-tail coupling apparatus
Functional Information from PROSITE/UniProt
site_idPS00231
Number of Residues6
DetailsF_ACTIN_CAPPING_BETA F-actin capping protein beta subunit signature. CDYNRD
ChainResidueDetails
ZCYS62-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
YVAL196-VAL204
site_idPS00749
Number of Residues11
DetailsF_ACTIN_CAPPING_A_2 F-actin capping protein alpha subunit signature 2. KaLRRqLPVTR
ChainResidueDetails
YLYS256-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 Residues125
DetailsRegion: {"description":"Interaction with alpha-actinin","evidences":[{"source":"PubMed","id":"8449927","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues5
DetailsModified residue: {"description":"N6-malonyllysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues5
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 Residues5
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68133","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues5
DetailsModified residue: {"description":"ADP-ribosylarginine; by SpvB","evidences":[{"source":"PubMed","id":"16905096","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues3
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues596
DetailsDomain: {"description":"ADF-H","evidences":[{"source":"PROSITE-ProRule","id":"PRU00599","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues412
DetailsRegion: {"description":"Interaction with CSRP3","evidences":[{"source":"PubMed","id":"19752190","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues16
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"37316325","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Calvo F.","Kolch W."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P45591","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"37316325","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

253091

PDB entries from 2026-05-06

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