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Protein

Cofilin-1

Gene

CFL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation (PubMed:11812157, PubMed:15580268, PubMed:21834987, PubMed:23633677). Required for neural tube morphogenesis and neural crest cell migration (By similarity).By similarity4 Publications

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • signaling receptor binding Source: Ensembl

GO - Biological processi

  • actin cytoskeleton organization Source: ProtInc
  • actin filament depolymerization Source: UniProtKB
  • actin filament fragmentation Source: Ensembl
  • cytoskeleton organization Source: UniProtKB
  • establishment of cell polarity Source: Ensembl
  • interleukin-12-mediated signaling pathway Source: Reactome
  • mitotic cytokinesis Source: Ensembl
  • negative regulation of apoptotic process Source: UniProtKB
  • neural crest cell migration Source: Ensembl
  • neural fold formation Source: Ensembl
  • positive regulation by host of viral process Source: AgBase
  • positive regulation of actin filament depolymerization Source: Ensembl
  • protein phosphorylation Source: Ensembl
  • regulation of cell morphogenesis Source: UniProtKB
  • regulation of dendritic spine morphogenesis Source: ParkinsonsUK-UCL
  • response to amino acid Source: Ensembl
  • response to virus Source: UniProtKB
  • Rho protein signal transduction Source: ProtInc

Keywordsi

Molecular functionActin-binding

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-399954 Sema3A PAK dependent Axon repulsion
R-HSA-5627117 RHO GTPases Activate ROCKs
R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation
SignaLinkiP23528
SIGNORiP23528

Names & Taxonomyi

Protein namesi
Recommended name:
Cofilin-1
Alternative name(s):
18 kDa phosphoprotein
Short name:
p18
Cofilin, non-muscle isoform
Gene namesi
Name:CFL1
Synonyms:CFL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

EuPathDBiHostDB:ENSG00000172757.12
HGNCiHGNC:1874 CFL1
MIMi601442 gene
neXtProtiNX_P23528

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi1072
OpenTargetsiENSG00000172757
PharmGKBiPA26423

Chemistry databases

ChEMBLiCHEMBL1075129
DrugBankiDB04147 Lauryl Dimethylamine-N-Oxide

Polymorphism and mutation databases

BioMutaiCFL1
DMDMi116848

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources2 Publications
ChainiPRO_00002148982 – 166Cofilin-1Add BLAST165

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei3Phosphoserine; by NRKCombined sources1 Publication1
Modified residuei8PhosphoserineBy similarity1
Modified residuei13N6-acetyllysineCombined sources1
Modified residuei25PhosphothreonineCombined sources1
Modified residuei41PhosphoserineCombined sources1
Modified residuei68PhosphotyrosineCombined sources1
Modified residuei73N6-acetyllysineCombined sources1
Cross-linki132Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei140PhosphotyrosineCombined sources1
Modified residuei144N6-acetyllysineCombined sources1
Modified residuei156PhosphoserineCombined sources1

Post-translational modificationi

Inactivated by phosphorylation on Ser-3. Phosphorylated on Ser-3 in resting cells (By similarity). Dephosphorylated by PDXP/chronophin; this restores its activity in promoting actin filament depolymerization. The phosphorylation of Ser-24 may prevent recognition of the nuclear localization signal (By similarity). Phosphorylated via a ARRB1-RAC1-LIMK1-PAK1 cascade upon active ligand stimulation of atypical chemokine receptor ACKR2.By similarity2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP23528
PaxDbiP23528
PeptideAtlasiP23528
PRIDEiP23528
TopDownProteomicsiP23528

2D gel databases

DOSAC-COBS-2DPAGEiP23528
OGPiP23528
REPRODUCTION-2DPAGEiIPI00012011
SWISS-2DPAGEiP23528
UCD-2DPAGEiP23528

PTM databases

CarbonylDBiP23528
iPTMnetiP23528
PhosphoSitePlusiP23528
SwissPalmiP23528

Miscellaneous databases

PMAP-CutDBiP23528

Expressioni

Tissue specificityi

Widely distributed in various tissues.

Inductioni

Up-regulated in response to enterovirus 71 (EV71) infection (at protein level).1 Publication

Gene expression databases

BgeeiENSG00000172757
ExpressionAtlasiP23528 baseline and differential
GenevisibleiP23528 HS

Organism-specific databases

HPAiCAB033687
CAB037077
HPA053761

Interactioni

Subunit structurei

Can bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is a major component of intranuclear and cytoplasmic actin rods.By similarity

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • signaling receptor binding Source: Ensembl

Protein-protein interaction databases

BioGridi107499, 155 interactors
CORUMiP23528
DIPiDIP-33000N
IntActiP23528, 82 interactors
MINTiP23528
STRINGi9606.ENSP00000309629

Structurei

Secondary structure

1166
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 19Combined sources11
Helixi26 – 31Combined sources6
Beta strandi33 – 40Combined sources8
Beta strandi44 – 56Combined sources13
Helixi57 – 59Combined sources3
Turni61 – 63Combined sources3
Helixi67 – 74Combined sources8
Beta strandi77 – 79Combined sources3
Beta strandi81 – 90Combined sources10
Beta strandi95 – 104Combined sources10
Helixi111 – 127Combined sources17
Beta strandi134 – 139Combined sources6
Helixi140 – 144Combined sources5
Helixi147 – 154Combined sources8
Helixi155 – 157Combined sources3
Beta strandi160 – 165Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q8GNMR-A1-166[»]
1Q8XNMR-A1-166[»]
3J0Selectron microscopy9.00M/N/O/P/Q/R/S/T/U/V/W/X1-166[»]
4BEXX-ray2.8011-166[»]
5HVKX-ray3.50B/D2-166[»]
5L6WX-ray2.53C1-166[»]
ProteinModelPortaliP23528
SMRiP23528
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23528

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 153ADF-HPROSITE-ProRule annotationAdd BLAST150

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi30 – 34Nuclear localization signalSequence analysis5

Sequence similaritiesi

Belongs to the actin-binding proteins ADF family.Curated

Phylogenomic databases

eggNOGiKOG1735 Eukaryota
ENOG41122P5 LUCA
GeneTreeiENSGT00440000033289
HOGENOMiHOG000039697
HOVERGENiHBG000381
InParanoidiP23528
KOiK05765
PhylomeDBiP23528
TreeFamiTF328601

Family and domain databases

CDDicd11286 ADF_cofilin_like, 1 hit
Gene3Di3.40.20.10, 1 hit
InterProiView protein in InterPro
IPR002108 ADF-H
IPR029006 ADF-H/Gelsolin-like_dom_sf
IPR017904 ADF/Cofilin
IPR027234 Cofilin_1
PANTHERiPTHR11913 PTHR11913, 1 hit
PTHR11913:SF17 PTHR11913:SF17, 1 hit
PfamiView protein in Pfam
PF00241 Cofilin_ADF, 1 hit
PRINTSiPR00006 COFILIN
SMARTiView protein in SMART
SM00102 ADF, 1 hit
PROSITEiView protein in PROSITE
PS51263 ADF_H, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23528-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE
60 70 80 90 100
EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV
110 120 130 140 150
FIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA
160
EKLGGSAVIS LEGKPL
Length:166
Mass (Da):18,502
Last modified:January 23, 2007 - v3
Checksum:i589EF8FC1EC13719
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D00682 mRNA Translation: BAA00589.1
U21909 mRNA Translation: AAA64501.1
X95404 mRNA Translation: CAA64685.1
BT006846 mRNA Translation: AAP35492.1
AK097690 mRNA Translation: BAG53513.1
CH471076 Genomic DNA Translation: EAW74449.1
BC011005 mRNA Translation: AAH11005.1
BC012265 mRNA Translation: AAH12265.1
BC012318 mRNA Translation: AAH12318.1
BC018256 mRNA Translation: AAH18256.1
CCDSiCCDS8114.1
PIRiS12632
RefSeqiNP_005498.1, NM_005507.2
UniGeneiHs.170622

Genome annotation databases

EnsembliENST00000308162; ENSP00000309629; ENSG00000172757
ENST00000525451; ENSP00000432660; ENSG00000172757
GeneIDi1072
KEGGihsa:1072

Similar proteinsi

Entry informationi

Entry nameiCOF1_HUMAN
AccessioniPrimary (citable) accession number: P23528
Secondary accession number(s): B3KUQ1, Q53Y87, Q9UCA2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 208 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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