P23528 · COF1_HUMAN
- ProteinCofilin-1
- GeneCFL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids166 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity (PubMed:11812157).
In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (PubMed:15580268).
Required for the centralization of the mitotic spindle and symmetric division of zygotes (By similarity).
Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (PubMed:21834987).
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:23633677).
Required for neural tube morphogenesis and neural crest cell migration (By similarity).
In conjunction with the subcortical maternal complex (SCMC), plays an essential role for zygotes to progress beyond the first embryonic cell divisions via regulation of actin dynamics (PubMed:15580268).
Required for the centralization of the mitotic spindle and symmetric division of zygotes (By similarity).
Plays a role in the regulation of cell morphology and cytoskeletal organization in epithelial cells (PubMed:21834987).
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:23633677).
Required for neural tube morphogenesis and neural crest cell migration (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCofilin-1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP23528
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell projection, ruffle membrane ; Peripheral membrane protein
Cell projection, lamellipodium membrane ; Peripheral membrane protein
Note: Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Detected at the cleavage furrow and contractile ring during cytokinesis. Almost completely in nucleus in cells exposed to heat shock or 10% dimethyl sulfoxide.
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 104 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000214898 | 2-166 | UniProt | Cofilin-1 | |||
Sequence: ASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL | |||||||
Modified residue | 3 | UniProt | Phosphoserine; by NRK | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 3 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 8 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 8 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 13 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 24 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 25 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 25 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 41 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 41 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 63 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 68 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 68 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 70 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 73 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 82 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 82 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 88 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 89 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 91 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 108 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 113 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 129 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 132 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue | 140 | UniProt | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 140 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 144 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 156 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 156 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 160 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
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
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
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Widely distributed in various tissues.
Induction
Up-regulated in response to enterovirus 71 (EV71) infection (at protein level).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Can bind G- and F-actin in a 1:1 ratio of cofilin to actin (PubMed:11812157).
It is a major component of intranuclear and cytoplasmic actin rods (By similarity).
Interacts with the subcortical maternal complex (SCMC) via interaction with TLE6 isoform 1 and NLRP5 (By similarity).
Interacts with C9orf72 (By similarity).
It is a major component of intranuclear and cytoplasmic actin rods (By similarity).
Interacts with the subcortical maternal complex (SCMC) via interaction with TLE6 isoform 1 and NLRP5 (By similarity).
Interacts with C9orf72 (By similarity).
(Microbial infection) Interacts with human respiratory syncytial virus (HRSV) matrix protein; this interaction probably facilitates viral replication.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P23528 | ACTB P60709 | 11 | EBI-352733, EBI-353944 | |
BINARY | P23528 | ACTC1 P68032 | 2 | EBI-352733, EBI-352273 | |
BINARY | P23528 | ACTG1 P63261 | 10 | EBI-352733, EBI-351292 | |
BINARY | P23528 | ATXN1 P54253 | 11 | EBI-352733, EBI-930964 | |
BINARY | P23528 | CFL2 Q549N0 | 3 | EBI-352733, EBI-10201319 | |
BINARY | P23528 | CFL2 Q9Y281 | 3 | EBI-352733, EBI-351218 | |
BINARY | P23528 | EGFR P00533 | 3 | EBI-352733, EBI-297353 | |
BINARY | P23528 | HUNK P57058 | 2 | EBI-352733, EBI-3959804 | |
BINARY | P23528 | LIMK1 P53667 | 3 | EBI-352733, EBI-444403 | |
XENO | P23528 | M P0DOE7 | 2 | EBI-352733, EBI-10042882 | |
BINARY | P23528 | OPTN Q96CV9 | 3 | EBI-352733, EBI-748974 | |
BINARY | P23528 | PLD1 Q13393 | 4 | EBI-352733, EBI-2827556 | |
BINARY | P23528 | PLD2 O14939 | 2 | EBI-352733, EBI-1053996 | |
BINARY | P23528 | PS1TP5BP1 Q1KLZ0 | 3 | EBI-352733, EBI-9978131 | |
BINARY | P23528 | SSH1 Q8WYL5 | 2 | EBI-352733, EBI-1222387 | |
BINARY | P23528 | YWHAZ P63104 | 3 | EBI-352733, EBI-347088 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 4-153 | ADF-H | ||||
Sequence: GVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKL | ||||||
Motif | 30-34 | Nuclear localization signal | ||||
Sequence: KKRKK |
Sequence similarities
Belongs to the actin-binding proteins ADF family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length166
- Mass (Da)18,502
- Last updated2007-01-23 v3
- Checksum589EF8FC1EC13719
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D00682 EMBL· GenBank· DDBJ | BAA00589.1 EMBL· GenBank· DDBJ | mRNA | ||
U21909 EMBL· GenBank· DDBJ | AAA64501.1 EMBL· GenBank· DDBJ | mRNA | ||
X95404 EMBL· GenBank· DDBJ | CAA64685.1 EMBL· GenBank· DDBJ | mRNA | ||
BT006846 EMBL· GenBank· DDBJ | AAP35492.1 EMBL· GenBank· DDBJ | mRNA | ||
AK097690 EMBL· GenBank· DDBJ | BAG53513.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471076 EMBL· GenBank· DDBJ | EAW74449.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC011005 EMBL· GenBank· DDBJ | AAH11005.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012265 EMBL· GenBank· DDBJ | AAH12265.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012318 EMBL· GenBank· DDBJ | AAH12318.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018256 EMBL· GenBank· DDBJ | AAH18256.1 EMBL· GenBank· DDBJ | mRNA |