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9EC0

Structure of the CARMIL dimer bound to Capping Protein

Functional Information from GO Data
ChainGOidnamespacecontents
C0003779molecular_functionactin binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0008290cellular_componentF-actin capping protein complex
C0015629cellular_componentactin cytoskeleton
C0030036biological_processactin cytoskeleton organization
C0030863cellular_componentcortical cytoskeleton
C0034329biological_processcell junction assembly
C0045296molecular_functioncadherin binding
C0051015molecular_functionactin filament binding
C0051016biological_processbarbed-end actin filament capping
C0065003biological_processprotein-containing complex assembly
C0070062cellular_componentextracellular exosome
C0071203cellular_componentWASH complex
D0003779molecular_functionactin binding
D0005515molecular_functionprotein binding
D0005829cellular_componentcytosol
D0005856cellular_componentcytoskeleton
D0005903cellular_componentbrush border
D0008290cellular_componentF-actin capping protein complex
D0014069cellular_componentpostsynaptic density
D0015629cellular_componentactin cytoskeleton
D0016020cellular_componentmembrane
D0030017cellular_componentsarcomere
D0030027cellular_componentlamellipodium
D0030863cellular_componentcortical cytoskeleton
D0045296molecular_functioncadherin binding
D0051016biological_processbarbed-end actin filament capping
D0070062cellular_componentextracellular exosome
D0071203cellular_componentWASH complex
D0098685cellular_componentSchaffer collateral - CA1 synapse
D0098686cellular_componenthippocampal mossy fiber to CA3 synapse
D0120212cellular_componentsperm head-tail coupling apparatus
E0003779molecular_functionactin binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005829cellular_componentcytosol
E0005856cellular_componentcytoskeleton
E0008290cellular_componentF-actin capping protein complex
E0015629cellular_componentactin cytoskeleton
E0030036biological_processactin cytoskeleton organization
E0030863cellular_componentcortical cytoskeleton
E0034329biological_processcell junction assembly
E0045296molecular_functioncadherin binding
E0051015molecular_functionactin filament binding
E0051016biological_processbarbed-end actin filament capping
E0065003biological_processprotein-containing complex assembly
E0070062cellular_componentextracellular exosome
E0071203cellular_componentWASH complex
F0003779molecular_functionactin binding
F0005515molecular_functionprotein binding
F0005829cellular_componentcytosol
F0005856cellular_componentcytoskeleton
F0005903cellular_componentbrush border
F0008290cellular_componentF-actin capping protein complex
F0014069cellular_componentpostsynaptic density
F0015629cellular_componentactin cytoskeleton
F0016020cellular_componentmembrane
F0030017cellular_componentsarcomere
F0030027cellular_componentlamellipodium
F0030863cellular_componentcortical cytoskeleton
F0045296molecular_functioncadherin binding
F0051016biological_processbarbed-end actin filament capping
F0070062cellular_componentextracellular exosome
F0071203cellular_componentWASH complex
F0098685cellular_componentSchaffer collateral - CA1 synapse
F0098686cellular_componenthippocampal mossy fiber to CA3 synapse
F0120212cellular_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
DCYS62-ASP67

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues48
DetailsRepeat: {"description":"LRR 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues46
DetailsRepeat: {"description":"LRR 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues46
DetailsRepeat: {"description":"LRR 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues54
DetailsRepeat: {"description":"LRR 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues54
DetailsRepeat: {"description":"LRR 5"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues48
DetailsRepeat: {"description":"LRR 6"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues50
DetailsRepeat: {"description":"LRR 7"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues46
DetailsRepeat: {"description":"LRR 8"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues46
DetailsRepeat: {"description":"LRR 9"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues48
DetailsRepeat: {"description":"LRR 10"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues48
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues18
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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