Determination of a cAMP-Dependent Protein Kinase Phosphorylation Site in the C-Terminal Region of Human Endothelial Actin-Binding Protein

2000 ◽  
Vol 377 (1) ◽  
pp. 80-84 ◽  
Author(s):  
David Jay ◽  
Elizabeth J. García ◽  
José Enrique Lara ◽  
Miguel Angel Medina ◽  
María de la Luz Ibarra
Keyword(s):  
Protein Kinase ◽  
Phosphorylation Site ◽  
Terminal Region ◽  
Actin Binding ◽  
Dependent Protein Kinase ◽  
Actin Binding Protein ◽  
Dependent Protein ◽  
Kinase Phosphorylation ◽  
Protein Kinase Phosphorylation Site

Bioinformatics Analysis of OmpA/MotB Protein Encoded by OmpA/MotB Gene(ORF 648bp) of Riemerella anatipestifer

2013 ◽  
Vol 647 ◽  
pp. 304-309
Author(s):  
Xu Pan ◽  
An Chun Cheng ◽  
Ming Shu Wang ◽  
De Kang Zhu ◽  
Xiao Jia Wang
Keyword(s):  
Protein Kinase ◽  
Phosphorylation Site ◽  
Evolutionary Relationship ◽  
Antigenic Determinants ◽  
Phosphorylation Sites ◽  
Dependent Protein ◽  
Relative Molecular Weight ◽  
Kinase Phosphorylation ◽  
Camp And Cgmp ◽  
Protein Kinase Phosphorylation Site

The OmpA/MotB gene from RA by our lab was sequenced. And the molecular characteristic of this gene was analyzed with bioinformatics software. The results indicated that this gene encodes an estimated 215 protein, contains the conserved domain of the OmpA-like protein. The relative molecular weight of the protein was 23.34525kDa, and there is no signal peptide and transmembrane region of the protein. One cAMP-and cGMP-dependent protein kinase phosphorylation site, six Protein kinase C phosphorylation sites, five Casein kinase II phosphorylation sites, five N-myristoylation sites and antigenic determinants were searched in the protein. Most of the total proteins were located in the Outer membrane and cytoplasmic. Phylogenetic tree of the amino acids sequences showed this gene has a close evolutionary relationship with Elizabethkingia anopheles Ag1 and Weeksella virosa DSM16922, indicating that the RA OmpA/MotB protein may have some similar functions with them. These results provided rational data to elucidate biological function and physiological features of the protein.

scholarly journals Alteration of a cyclic AMP-dependent protein kinase phosphorylation site in the c-Fos protein augments its transforming potential

1992 ◽  
Vol 12 (3) ◽  
pp. 998-1006
Author(s):  
I Tratner ◽  
R Ofir ◽  
I M Verma
Keyword(s):  
Protein Kinase ◽  
Cyclic Amp ◽  
Phosphorylation Site ◽  
Dependent Protein Kinase ◽  
Fos Protein ◽  
Dependent Protein ◽  
Cell Growth And Differentiation ◽  
Kinase Phosphorylation

We have studied the phosphorylation of the nuclear oncoprotein Fos by cyclic AMP-dependent protein kinase (PKA). We demonstrate that the human c-Fos protein, phosphorylated either in vitro with purified PKA or in vivo in JEG3 cells following treatment with forskolin, has similar phosphotryptic peptide maps. Serine 362, which constitutes part of a canonical PKA phosphorylation site (RKGSSS), is phosphorylated both in vivo and in vitro. A mutant of Fos protein in which serine residues 362 to 364 have been altered to alanine residues is not efficiently phosphorylated in vitro. Furthermore, Fos protein in which serines 362 to 364 have been altered to alanine shows increased transforming potential. We propose that phosphorylation of Fos by PKA is an important regulatory step in controlling its activity in normal cell growth and differentiation.

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