| Gene |
CFL2
|
| Protein Name |
COF2_HUMAN |
| Organism |
Homo sapiens (Human) |
| Alternative name(s) |
Cofilin-2 (Cofilin, muscle isoform) |
| Protein Family |
Actin-binding proteins ADF family |
| NCBI Gene ID |
1073
|
| UniProt ID |
Q9Y281
|
| Enzyme Class |
- |
| Molecular Weight |
18737 |
| Protein Length |
166 |
| Protein Domain |
InterPro |
Pfam
|
| 3D Structure |
PDBe |
PDBj |
RCSB PDB |
DrugPort
ModBase |
SwissModel
|
| Gene Expression |
Gene Expression Atlas
|
| Function and Disease |
OMIM |
| Protein-protein Interaction Database |
STRING |
IntAct |
MINT
|
| Kinase Database |
Phospho.ELM
|
PhosphoSite
| NetworKIN
|
| Catalytic Activity (UniProt annotation) |
- |
| Localization |
Nucleus matrix |
| Function (UniProt annotation) |
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. Its F-actin depolymerization activity is regulated by association with CSPR3 (PubMed:19752190). It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods. Required for muscle maintenance. May play a role during the exchange of alpha-actin forms during the early postnatal remodeling of the sarcomere (By similarity). |
| Gene Ontology |
GO:0005615; GO:0007519; GO:0015629; GO:0016363; GO:0030018; GO:0030042; GO:0030043; GO:0030836; GO:0031674; GO:0045214; GO:0046716; GO:0051015; GO:0070062 |
