Abstract
The forkhead-associated (FHA) domain is a small protein module recently shown to recognize phosphothreonine epitopes on proteins. It is present in a diverse range of proteins in eukaryotic cells, such as kinases, phosphatases, kinesins, transcription factors, RNA-binding proteins, and metabolic enzymes. It is also found in a number of bacterial proteins. This suggests that FHA domain-mediated phospho-dependent assembly of protein complexes is an ancient and widespread regulatory mechanism.
Publication types
-
Research Support, Non-U.S. Gov't
-
Review
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Bacterial Proteins / chemistry
-
Bacterial Proteins / metabolism
-
Binding Sites
-
DNA Damage
-
DNA Repair
-
Enzymes / chemistry
-
Enzymes / metabolism
-
Epitopes / metabolism
-
Kinesins / chemistry
-
Kinesins / metabolism
-
Molecular Sequence Data
-
Phosphopeptides / chemistry*
-
Phosphopeptides / metabolism
-
Phosphoric Monoester Hydrolases / chemistry
-
Phosphoric Monoester Hydrolases / metabolism
-
Phosphothreonine / metabolism
-
Phosphotransferases / chemistry
-
Phosphotransferases / metabolism
-
Protein Conformation
-
RNA-Binding Proteins / chemistry
-
RNA-Binding Proteins / metabolism
-
Sequence Alignment
-
Sequence Homology, Amino Acid
-
Signal Transduction
-
Transcription Factors / chemistry
-
Transcription Factors / metabolism
Substances
-
Bacterial Proteins
-
Enzymes
-
Epitopes
-
Phosphopeptides
-
RNA-Binding Proteins
-
Transcription Factors
-
Phosphothreonine
-
Phosphotransferases
-
Phosphoric Monoester Hydrolases
-
Kinesins