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Protein

Cofilin-1

Gene

CFL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

GO - Biological processi

  • actin cytoskeleton organization Source: ProtInc
  • actin filament depolymerization Source: UniProtKB
  • cytoskeleton organization Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • positive regulation by host of viral process Source: AgBase
  • regulation of cell morphogenesis Source: UniProtKB
  • regulation of dendritic spine morphogenesis Source: ParkinsonsUK-UCL
  • response to virus Source: UniProtKB
  • Rho protein signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Actin-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.
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

HGNCiHGNC:1874. CFL1.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: InterPro
  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • extracellular space Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • lamellipodium membrane Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • nuclear matrix Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • ruffle membrane Source: UniProtKB-SubCell
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26423.

Chemistry

ChEMBLiCHEMBL1075129.

Polymorphism and mutation databases

BioMutaiCFL1.
DMDMi116848.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources2 Publications
Chaini2 – 166165Cofilin-1PRO_0000214898Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei3 – 31Phosphoserine; by NRKCombined sources1 Publication
Modified residuei8 – 81PhosphoserineBy similarity
Modified residuei13 – 131N6-acetyllysineCombined sources
Modified residuei25 – 251PhosphothreonineCombined sources
Modified residuei41 – 411PhosphoserineCombined sources
Modified residuei68 – 681PhosphotyrosineCombined sources
Modified residuei73 – 731N6-acetyllysineCombined sources
Modified residuei140 – 1401PhosphotyrosineCombined sources
Modified residuei144 – 1441N6-acetyllysineCombined sources
Modified residuei156 – 1561PhosphoserineCombined sources

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, Phosphoprotein

Proteomic databases

EPDiP23528.
PaxDbiP23528.
PeptideAtlasiP23528.
PRIDEiP23528.
TopDownProteomicsiP23528.

2D gel databases

DOSAC-COBS-2DPAGEP23528.
OGPiP23528.
REPRODUCTION-2DPAGEIPI00012011.
SWISS-2DPAGEP23528.
UCD-2DPAGEP23528.

PTM databases

iPTMnetiP23528.
PhosphoSiteiP23528.
SwissPalmiP23528.

Miscellaneous databases

PMAP-CutDBP23528.

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

WithEntry#Exp.IntActNotes
ACTBP607094EBI-352733,EBI-353944
ACTG1P632616EBI-352733,EBI-351292
ATXN1P542535EBI-352733,EBI-930964
CFL2Q549N03EBI-352733,EBI-10201319
LIMK1P536672EBI-352733,EBI-444403
MP034192EBI-352733,EBI-10042882From a different organism.
PLD1Q133934EBI-352733,EBI-2827556
PLD2O149392EBI-352733,EBI-1053996
PS1TP5BP1Q1KLZ03EBI-352733,EBI-9978131
SSH1Q8WYL52EBI-352733,EBI-1222387
YWHAZP631043EBI-352733,EBI-347088

GO - Molecular functioni

  • actin filament binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107499. 147 interactions.
DIPiDIP-33000N.
IntActiP23528. 76 interactions.
MINTiMINT-4999473.
STRINGi9606.ENSP00000309629.

Structurei

Secondary structure

1
166
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1810Combined sources
Turni28 – 303Combined sources
Beta strandi31 – 4010Combined sources
Beta strandi42 – 454Combined sources
Beta strandi46 – 5611Combined sources
Helixi57 – 593Combined sources
Helixi60 – 645Combined sources
Helixi67 – 748Combined sources
Beta strandi77 – 793Combined sources
Beta strandi81 – 9010Combined sources
Beta strandi95 – 10410Combined sources
Helixi111 – 1199Combined sources
Helixi121 – 1255Combined sources
Beta strandi133 – 1375Combined sources
Helixi140 – 1434Combined sources
Helixi146 – 1549Combined sources
Helixi155 – 1573Combined sources
Beta strandi161 – 1644Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-166.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23528.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 153150ADF-HPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi30 – 345Nuclear localization signalSequence analysis

Sequence similaritiesi

Belongs to the actin-binding proteins ADF family.Curated
Contains 1 ADF-H domain.PROSITE-ProRule annotation

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.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin.
IPR027234. Cofilin_1.
[Graphical view]
PANTHERiPTHR11913. PTHR11913. 1 hit.
PTHR11913:SF17. PTHR11913:SF17. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
PRINTSiPR00006. COFILIN.
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]

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.

Cross-referencesi

Web resourcesi

Wikipedia

Cofilin entry

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107499. 147 interactions.
DIPiDIP-33000N.
IntActiP23528. 76 interactions.
MINTiMINT-4999473.
STRINGi9606.ENSP00000309629.

Chemistry

ChEMBLiCHEMBL1075129.

PTM databases

iPTMnetiP23528.
PhosphoSiteiP23528.
SwissPalmiP23528.

Polymorphism and mutation databases

BioMutaiCFL1.
DMDMi116848.

2D gel databases

DOSAC-COBS-2DPAGEP23528.
OGPiP23528.
REPRODUCTION-2DPAGEIPI00012011.
SWISS-2DPAGEP23528.
UCD-2DPAGEP23528.

Proteomic databases

EPDiP23528.
PaxDbiP23528.
PeptideAtlasiP23528.
PRIDEiP23528.
TopDownProteomicsiP23528.

Protocols and materials databases

DNASUi1072.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1072.
GeneCardsiCFL1.
H-InvDBHIX0009009.
HGNCiHGNC:1874. CFL1.
HPAiCAB033687.
CAB037077.
HPA053761.
MIMi601442. gene.
neXtProtiNX_P23528.
PharmGKBiPA26423.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1735. Eukaryota.
ENOG41122P5. LUCA.
GeneTreeiENSGT00440000033289.
HOGENOMiHOG000039697.
HOVERGENiHBG000381.
InParanoidiP23528.
KOiK05765.
PhylomeDBiP23528.
TreeFamiTF328601.

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.
SignaLinkiP23528.
SIGNORiP23528.

Miscellaneous databases

ChiTaRSiCFL1. human.
EvolutionaryTraceiP23528.
GeneWikiiCofilin_1.
GenomeRNAii1072.
PMAP-CutDBP23528.
PROiP23528.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000172757.
ExpressionAtlasiP23528. baseline and differential.
GenevisibleiP23528. HS.

Family and domain databases

CDDicd11286. ADF_cofilin_like. 1 hit.
Gene3Di3.40.20.10. 1 hit.
InterProiIPR002108. ADF-H.
IPR029006. ADF-H/Gelsolin-like_dom.
IPR017904. ADF/Cofilin.
IPR027234. Cofilin_1.
[Graphical view]
PANTHERiPTHR11913. PTHR11913. 1 hit.
PTHR11913:SF17. PTHR11913:SF17. 1 hit.
PfamiPF00241. Cofilin_ADF. 1 hit.
[Graphical view]
PRINTSiPR00006. COFILIN.
SMARTiSM00102. ADF. 1 hit.
[Graphical view]
PROSITEiPS51263. ADF_H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCOF1_HUMAN
AccessioniPrimary (citable) accession number: P23528
Secondary accession number(s): B3KUQ1, Q53Y87, Q9UCA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 189 of the entry and version 3 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.