Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4BEX

Structure of human Cofilin1

Functional Information from GO Data
ChainGOidnamespacecontents
10000281biological_processmitotic cytokinesis
10001755biological_processneural crest cell migration
10001842biological_processneural fold formation
10003779molecular_functionactin binding
10005102molecular_functionsignaling receptor binding
10005515molecular_functionprotein binding
10005615cellular_componentextracellular space
10005634cellular_componentnucleus
10005737cellular_componentcytoplasm
10005829cellular_componentcytosol
10005856cellular_componentcytoskeleton
10005886cellular_componentplasma membrane
10005911cellular_componentcell-cell junction
10005925cellular_componentfocal adhesion
10006606biological_processprotein import into nucleus
10007010biological_processcytoskeleton organization
10007015biological_processactin filament organization
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
10022604biological_processregulation of cell morphogenesis
10030010biological_processestablishment of cell polarity
10030027cellular_componentlamellipodium
10030030biological_processcell projection organization
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
10042995cellular_componentcell projection
10043025cellular_componentneuronal cell body
10043066biological_processnegative regulation of apoptotic process
10043197cellular_componentdendritic spine
10043200biological_processresponse to amino acid
10044794biological_processpositive regulation by host of viral process
10045792biological_processnegative regulation of cell size
10045862biological_processpositive regulation of proteolysis
10048870biological_processcell motility
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 Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:30550596, ECO:0000269|Ref.9, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
1ALA2

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine; by NRK => ECO:0000269|PubMed:12837278, ECO:0000269|PubMed:30550596, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
1SER3

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P18760
ChainResidueDetails
1SER8

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
1LYS13
1LYS73
1LYS144

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
1THR25

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
1SER41

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:30550596
ChainResidueDetails
1THR63

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
1TYR68

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:30550596
ChainResidueDetails
1TYR82

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:30550596
ChainResidueDetails
1SER108

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
1TYR140

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:30550596, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
1SER156

site_idSWS_FT_FI13
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
1LYS132

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon