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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4BEX

Structure of human Cofilin1

Functional Information from GO Data
ChainGOidnamespacecontents
10000281biological_processmitotic cytokinesis
10003779molecular_functionactin binding
10005102molecular_functionsignaling receptor binding
10005515molecular_functionprotein binding
10005615cellular_componentextracellular space
10005634cellular_componentnucleus
10005737cellular_componentcytoplasm
10005829cellular_componentcytosol
10005856cellular_componentcytoskeleton
10005911cellular_componentcell-cell junction
10005925cellular_componentfocal adhesion
10006606biological_processprotein import into nucleus
10007162biological_processnegative regulation of cell adhesion
10007266biological_processRho protein signal transduction
10008154biological_processactin polymerization or depolymerization
10009615biological_processresponse to virus
10010592biological_processpositive regulation of lamellipodium assembly
10010593biological_processnegative regulation of lamellipodium assembly
10014823biological_processresponse to activity
10015629cellular_componentactin cytoskeleton
10016020cellular_componentmembrane
10016363cellular_componentnuclear matrix
10019903molecular_functionprotein phosphatase binding
10021766biological_processhippocampus development
10030027cellular_componentlamellipodium
10030036biological_processactin cytoskeleton organization
10030042biological_processactin filament depolymerization
10030043biological_processactin filament fragmentation
10030175cellular_componentfilopodium
10030307biological_processpositive regulation of cell growth
10030424cellular_componentaxon
10030426cellular_componentgrowth cone
10030835biological_processnegative regulation of actin filament depolymerization
10030836biological_processpositive regulation of actin filament depolymerization
10030864cellular_componentcortical actin cytoskeleton
10031252cellular_componentcell leading edge
10031258cellular_componentlamellipodium membrane
10031915biological_processpositive regulation of synaptic plasticity
10031966cellular_componentmitochondrial membrane
10031982cellular_componentvesicle
10032232biological_processnegative regulation of actin filament bundle assembly
10032587cellular_componentruffle membrane
10040019biological_processpositive regulation of embryonic development
10043025cellular_componentneuronal cell body
10043066biological_processnegative regulation of apoptotic process
10043197cellular_componentdendritic spine
10044794biological_processhost-mediated activation of viral process
10045862biological_processpositive regulation of proteolysis
10050804biological_processmodulation of chemical synaptic transmission
10051014biological_processactin filament severing
10051015molecular_functionactin filament binding
10051293biological_processestablishment of spindle localization
10051511biological_processnegative regulation of unidimensional cell growth
10051894biological_processpositive regulation of focal adhesion assembly
10060999biological_processpositive regulation of dendritic spine development
10061001biological_processregulation of dendritic spine morphogenesis
10070062cellular_componentextracellular exosome
10070301biological_processcellular response to hydrogen peroxide
10071347biological_processcellular response to interleukin-1
10071354biological_processcellular response to interleukin-6
10071356biological_processcellular response to tumor necrosis factor
10071362biological_processcellular response to ether
10071364biological_processcellular response to epidermal growth factor stimulus
10090732cellular_componentcofilin-actin rod
10097060cellular_componentsynaptic membrane
10098885biological_processmodification of postsynaptic actin cytoskeleton
10098978cellular_componentglutamatergic synapse
10099092cellular_componentpostsynaptic density, intracellular component
11902936molecular_functionphosphatidylinositol bisphosphate binding
11902951biological_processnegative regulation of dendritic spine maintenance
11905873biological_processpositive regulation of protein localization to cell leading edge
11905875biological_processnegative regulation of postsynaptic density organization
11990314biological_processcellular response to insulin-like growth factor stimulus
12000146biological_processnegative regulation of cell motility
12000147biological_processpositive regulation of cell motility
12000784biological_processpositive regulation of establishment of cell polarity regulating cell shape
12000814biological_processpositive regulation of barbed-end actin filament capping
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues149
DetailsDomain: {"description":"ADF-H","evidences":[{"source":"PROSITE-ProRule","id":"PRU00599","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"30550596","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2005","submissionDatabase":"UniProtKB","authors":["Quadroni M.","Bienvenut W.V."]}},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by NRK","evidences":[{"source":"PubMed","id":"12837278","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30550596","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P18760","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"30550596","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"30550596","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"30550596","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"30550596","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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