BIOMAT Database Logo BIOMAT Database Logo

Phosphorylation of cAMP response element-binding protein, CRE-BP1, by cAMP-dependent protein kinase and protein kinase C. 1991

A Sakurai, and T Maekawa, and T Sudo, and S Ishii, and A Kishimoto
Department of Biochemistry, Kobe University School of Medicine, Japan.

The human recombinant CRE-BP1 was phosphorylated by cAMP-dependent protein kinase and protein kinase C, in vitro. These two protein kinases modified distinct serine residues of CRE-BP1. Ser-62 downstream of a putative metal finger structure of CRE-BP1 was the phosphorylation site by cAMP-dependent protein kinase, whereas two serine residues, Ser-340 and Ser-367, located in the basic region of this protein were the major protein kinase C phosphorylation sites. It seems possible that transcriptional and DNA-binding activities of CRE-BP1 are regulated by phosphorylation with these protein kinases.

UI MeSH Term Description Entries
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D010449 Peptide Mapping Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases. Fingerprints, Peptide,Peptide Fingerprinting,Protein Fingerprinting,Fingerprints, Protein,Fingerprint, Peptide,Fingerprint, Protein,Fingerprinting, Peptide,Fingerprinting, Protein,Mapping, Peptide,Peptide Fingerprint,Peptide Fingerprints,Protein Fingerprint,Protein Fingerprints
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D010768 Phosphoserine The phosphoric acid ester of serine. Serine Phosphate,Phosphorylserine,Seryl Phosphate,Phosphate, Serine,Phosphate, Seryl
D011493 Protein Kinase C An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters. Calcium Phospholipid-Dependent Protein Kinase,Calcium-Activated Phospholipid-Dependent Kinase,PKC Serine-Threonine Kinase,Phospholipid-Sensitive Calcium-Dependent Protein Kinase,Protein Kinase M,Calcium Activated Phospholipid Dependent Kinase,Calcium Phospholipid Dependent Protein Kinase,PKC Serine Threonine Kinase,Phospholipid Sensitive Calcium Dependent Protein Kinase,Phospholipid-Dependent Kinase, Calcium-Activated,Serine-Threonine Kinase, PKC
D011494 Protein Kinases A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein. Protein Kinase,Kinase, Protein,Kinases, Protein
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D004268 DNA-Binding Proteins Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases. DNA Helix Destabilizing Proteins,DNA-Binding Protein,Single-Stranded DNA Binding Proteins,DNA Binding Protein,DNA Single-Stranded Binding Protein,SS DNA BP,Single-Stranded DNA-Binding Protein,Binding Protein, DNA,DNA Binding Proteins,DNA Single Stranded Binding Protein,DNA-Binding Protein, Single-Stranded,Protein, DNA-Binding,Single Stranded DNA Binding Protein,Single Stranded DNA Binding Proteins
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000242 Cyclic AMP An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH. Adenosine Cyclic 3',5'-Monophosphate,Adenosine Cyclic 3,5 Monophosphate,Adenosine Cyclic Monophosphate,Adenosine Cyclic-3',5'-Monophosphate,Cyclic AMP, (R)-Isomer,Cyclic AMP, Disodium Salt,Cyclic AMP, Monoammonium Salt,Cyclic AMP, Monopotassium Salt,Cyclic AMP, Monosodium Salt,Cyclic AMP, Sodium Salt,3',5'-Monophosphate, Adenosine Cyclic,AMP, Cyclic,Adenosine Cyclic 3',5' Monophosphate,Cyclic 3',5'-Monophosphate, Adenosine,Cyclic Monophosphate, Adenosine,Cyclic-3',5'-Monophosphate, Adenosine,Monophosphate, Adenosine Cyclic

Related Publications

A Sakurai, and T Maekawa, and T Sudo, and S Ishii, and A Kishimoto
Phosphorylation of CRE-BP1, a cyclic AMP response element binding protein, by protein kinase C and cyclic AMP-dependent protein kinase.
June 1992, The Kobe journal of medical sciences,
A Sakurai, and T Maekawa, and T Sudo, and S Ishii, and A Kishimoto
Ethanol stimulates cAMP-responsive element (CRE)-mediated transcription via CRE-binding protein and cAMP-dependent protein kinase.
April 2002, The Journal of pharmacology and experimental therapeutics,
A Sakurai, and T Maekawa, and T Sudo, and S Ishii, and A Kishimoto
Phosphorylation of cyclic adenosine 3',5'-monophosphate (cAMP) response element-binding protein isoforms by the cAMP-dependent protein kinase.
November 1992, Molecular endocrinology (Baltimore, Md.),
A Sakurai, and T Maekawa, and T Sudo, and S Ishii, and A Kishimoto
Cyclin-dependent kinase 1-dependent phosphorylation of cAMP response element-binding protein decreases chromatin occupancy.
August 2013, The Journal of biological chemistry,
A Sakurai, and T Maekawa, and T Sudo, and S Ishii, and A Kishimoto
Protein kinase C-regulated cAMP response element-binding protein phosphorylation in cultured rat striatal neurons.
May 2007, Brain research bulletin,
A Sakurai, and T Maekawa, and T Sudo, and S Ishii, and A Kishimoto
cAMP-dependent regulation of gene transcription by cAMP response element-binding protein and cAMP response element modulator.
January 1995, Vitamins and hormones,
A Sakurai, and T Maekawa, and T Sudo, and S Ishii, and A Kishimoto
Isolation and characterization of a novel member of the gene family encoding the cAMP response element-binding protein CRE-BP1.
February 1993, The Journal of biological chemistry,
A Sakurai, and T Maekawa, and T Sudo, and S Ishii, and A Kishimoto
cAMP-dependent protein kinase induces cAMP-response element-binding protein phosphorylation via an intracellular calcium release/ERK-dependent pathway in striatal neurons.
April 2001, The Journal of biological chemistry,
A Sakurai, and T Maekawa, and T Sudo, and S Ishii, and A Kishimoto
cAMP response element-binding protein is activated by Ca2+/calmodulin- as well as cAMP-dependent protein kinase.
June 1991, Proceedings of the National Academy of Sciences of the United States of America,
A Sakurai, and T Maekawa, and T Sudo, and S Ishii, and A Kishimoto
Phosphorylation of the cAMP response element binding protein CREB by cAMP-dependent protein kinase A and glycogen synthase kinase-3 alters DNA-binding affinity, conformation, and increases net charge.
March 1998, Biochemistry,
Copied contents to your clipboard!