Glycine max (pS/pT)/FHA
※ FHA family introduction FHA domains are conserved sequences of 65-100 amino acid residues found principally within eukaryotic nuclear proteins and also exist in certain prokaryotes. Forkhead-associated (FHA) domains were first identified within a subset of forkhead transcriptional factors, located outside of the conserved DNA-binding forkhead domain.They were subsequently found in a number of other proteins by sequence homology analyses. The FHA domain is thought to possess phosphopeptide-binding specificity. The vast majority of FHA-containing proteins in eukaryotes reside within the nucleus, and many of these have been linked to the control of transcription, DNA repair, and/or cell cycle progression (1). Reference
1. Durocher, D. (1999) The FHA domain is a modular phosphopeptide recognition motif. Mol Cell, 4, 387-94. PMID: 10518219
There are 25 genes. Reviewed (0)
or Unreviewed (25) 
※ FHA family introduction FHA domains are conserved sequences of 65-100 amino acid residues found principally within eukaryotic nuclear proteins and also exist in certain prokaryotes. Forkhead-associated (FHA) domains were first identified within a subset of forkhead transcriptional factors, located outside of the conserved DNA-binding forkhead domain.They were subsequently found in a number of other proteins by sequence homology analyses. The FHA domain is thought to possess phosphopeptide-binding specificity. The vast majority of FHA-containing proteins in eukaryotes reside within the nucleus, and many of these have been linked to the control of transcription, DNA repair, and/or cell cycle progression (1). Reference
1. Durocher, D. (1999) The FHA domain is a modular phosphopeptide recognition motif. Mol Cell, 4, 387-94. PMID: 10518219
There are 25 genes. Reviewed (0)
or Unreviewed (25)