Difference between revisions of "Cofilin-1"

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===Cys Function & Property===
 
===Cys Function & Property===
Both Cys234 and Cys179 are located within the first catalytic cysteine domain (FCCH) of E1, a subdomain conserved in human E1 that spans from residues 175–265 and forms one wall of a broad deep groove unique to eukaryotic E1. The rat Cys234 location is identical to that reported for human E1 in vitro whereas the modified Cys179 on rat E1 represents an additional modification.<br/>
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Molecules covalent bind with Cys139 would disrupt the interface between Cofilin1 and actin.<br/>
  
 
* Hydrophobic property:
 
* Hydrophobic property:
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# Gabrielsen M, Schuldt M, Munro J, et al. '''Cucurbitacin covalent bonding to cysteine thiols: the filamentous-actin severing protein Cofilin1 as an exemplary target[J].''' Cell Communication and Signaling, 2013, 11(1): 58. [https://www.ncbi.nlm.nih.gov/pubmed/?term=23945128 23945128]<br/>
 
# Gabrielsen M, Schuldt M, Munro J, et al. '''Cucurbitacin covalent bonding to cysteine thiols: the filamentous-actin severing protein Cofilin1 as an exemplary target[J].''' Cell Communication and Signaling, 2013, 11(1): 58. [https://www.ncbi.nlm.nih.gov/pubmed/?term=23945128 23945128]<br/>
  
[[Category:Targets|Targets]]
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[[Category:Targets]]
[[Category:Homo sapiens|Homo sapiens]]
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[[Category:Homo sapiens]]
[[Category:Structural protein|Structural protein]]
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[[Category:Structural protein]]
[[Category:Actin-binding proteins ADF family|Actin-binding proteins ADF family]]
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[[Category:Actin-binding proteins ADF family]]
[[Category:Fc gamma R-mediated phagocytosis|Fc gamma R-mediated phagocytosis]]
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[[Category:Fc gamma R-mediated phagocytosis]]
[[Category:Regulation of actin cytoskeleton|Regulation of actin cytoskeleton]]
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[[Category:Regulation of actin cytoskeleton]]
[[Category:Pertussis|Pertussis]]
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[[Category:Pertussis]]
[[Category:Human immunodeficiency virus 1 infection|Human immunodeficiency virus 1 infection]]
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[[Category:Human immunodeficiency virus 1 infection]]

Latest revision as of 22:06, 19 August 2019

Basic Information
Short Name Cofilin-1, p18
UNP ID P23528
Organism Homo sapiens
Cys Site Cys139
Family/Domain Cofilin/tropomyosin-type actin-binding protein,
Actin-binding proteins ADF family
Known Ligand Ligand list
Function Type Structural protein

Summary

Protein Function

Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus.
One group reports that reelin signaling leads to serine3-phosphorylation of cofilin-1, and this interaction may play a role in the reelin-related regulation of neuronal migration.

Cys Function & Property

Molecules covalent bind with Cys139 would disrupt the interface between Cofilin1 and actin.

  • Hydrophobic property:
540-hydro.png
  • SASA:
Cys139: 36.275 A^2

Protein Sequence

MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE
EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV
FIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA
EKLGGSAVIS LEGKPL

Structural Information

  • Known structures with covalent ligands:
Unknown
  • Protein structure:
540.png

Related Pathway

Experimental Evidence

Mass Spectrometry, Tryptic Digest

Reference

  1. Gabrielsen M, Schuldt M, Munro J, et al. Cucurbitacin covalent bonding to cysteine thiols: the filamentous-actin severing protein Cofilin1 as an exemplary target[J]. Cell Communication and Signaling, 2013, 11(1): 58. 23945128