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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1Q8X

NMR structure of human cofilin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000281biological_processmitotic cytokinesis
A0001755biological_processneural crest cell migration
A0001842biological_processneural fold formation
A0003779molecular_functionactin binding
A0005102molecular_functionsignaling receptor binding
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005911cellular_componentcell-cell junction
A0005925cellular_componentfocal adhesion
A0006606biological_processprotein import into nucleus
A0007010biological_processcytoskeleton organization
A0007015biological_processactin filament organization
A0007162biological_processnegative regulation of cell adhesion
A0007266biological_processRho protein signal transduction
A0008154biological_processactin polymerization or depolymerization
A0009615biological_processresponse to virus
A0010592biological_processpositive regulation of lamellipodium assembly
A0010593biological_processnegative regulation of lamellipodium assembly
A0014823biological_processresponse to activity
A0015629cellular_componentactin cytoskeleton
A0016020cellular_componentmembrane
A0016363cellular_componentnuclear matrix
A0019903molecular_functionprotein phosphatase binding
A0021766biological_processhippocampus development
A0022604biological_processregulation of cell morphogenesis
A0030010biological_processestablishment of cell polarity
A0030027cellular_componentlamellipodium
A0030030biological_processcell projection organization
A0030036biological_processactin cytoskeleton organization
A0030042biological_processactin filament depolymerization
A0030043biological_processactin filament fragmentation
A0030175cellular_componentfilopodium
A0030307biological_processpositive regulation of cell growth
A0030424cellular_componentaxon
A0030426cellular_componentgrowth cone
A0030835biological_processnegative regulation of actin filament depolymerization
A0030836biological_processpositive regulation of actin filament depolymerization
A0030864cellular_componentcortical actin cytoskeleton
A0031252cellular_componentcell leading edge
A0031258cellular_componentlamellipodium membrane
A0031915biological_processpositive regulation of synaptic plasticity
A0031966cellular_componentmitochondrial membrane
A0031982cellular_componentvesicle
A0032232biological_processnegative regulation of actin filament bundle assembly
A0032587cellular_componentruffle membrane
A0040019biological_processpositive regulation of embryonic development
A0042995cellular_componentcell projection
A0043025cellular_componentneuronal cell body
A0043066biological_processnegative regulation of apoptotic process
A0043197cellular_componentdendritic spine
A0043200biological_processresponse to amino acid
A0044794biological_processhost-mediated activation of viral process
A0045792biological_processnegative regulation of cell size
A0045862biological_processpositive regulation of proteolysis
A0048870biological_processcell motility
A0050804biological_processmodulation of chemical synaptic transmission
A0051014biological_processactin filament severing
A0051015molecular_functionactin filament binding
A0051293biological_processestablishment of spindle localization
A0051511biological_processnegative regulation of unidimensional cell growth
A0051894biological_processpositive regulation of focal adhesion assembly
A0060999biological_processpositive regulation of dendritic spine development
A0061001biological_processregulation of dendritic spine morphogenesis
A0070062cellular_componentextracellular exosome
A0070301biological_processcellular response to hydrogen peroxide
A0071347biological_processcellular response to interleukin-1
A0071354biological_processcellular response to interleukin-6
A0071356biological_processcellular response to tumor necrosis factor
A0071362biological_processcellular response to ether
A0071364biological_processcellular response to epidermal growth factor stimulus
A0090732cellular_componentcofilin-actin rod
A0097060cellular_componentsynaptic membrane
A0098885biological_processmodification of postsynaptic actin cytoskeleton
A0098978cellular_componentglutamatergic synapse
A0099092cellular_componentpostsynaptic density, intracellular component
A1902936molecular_functionphosphatidylinositol bisphosphate binding
A1902951biological_processnegative regulation of dendritic spine maintenance
A1905873biological_processpositive regulation of protein localization to cell leading edge
A1905875biological_processnegative regulation of postsynaptic density organization
A1990314biological_processcellular response to insulin-like growth factor stimulus
A2000146biological_processnegative regulation of cell motility
A2000147biological_processpositive regulation of cell motility
A2000784biological_processpositive regulation of establishment of cell polarity regulating cell shape
A2000814biological_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

239803

PDB entries from 2025-08-06

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