Identification of the sites in myelin basic protein that are phosphorylated by meiosis-activated protein kinase p44mpk. 1990

J S Sanghera, and R Aebersold, and H D Morrison, and E J Bures, and S L Pelech
Biomedical Research Centre, University of British Columbia, Vancouver, Canada.

Myelin basic protein serves as a convenient substrate for detection of a 44 kDa protein-serine/threonine kinase (p44mpk) that is activated near the time of germinal vesicle breakdown in maturing echinoderm and amphibian oocytes. In vitro phosphorylation by purified p44mpk from sea star oocytes was primarily on threonine residues on a single tryptic peptide of bovine brain myelin basic protein. Amino acid composition analysis of the isolated posphopeptide revealed that it was rich in proline residues. Automated solid-phase sequencing by Edman degradation identified the major site as Thr-97 in the sequence NIVTPRTPPPSQGK, which corresponds to residues 91-104 in bovine brain myelin basic protein. Thr-94 was also phosphorylated by p44mpk to a very minor extent.

UI MeSH Term Description Entries
D008540 Meiosis A type of CELL NUCLEUS division, occurring during maturation of the GERM CELLS. Two successive cell nucleus divisions following a single chromosome duplication (S PHASE) result in daughter cells with half the number of CHROMOSOMES as the parent cells. M Phase, Meiotic,Meiotic M Phase,M Phases, Meiotic,Meioses,Meiotic M Phases,Phase, Meiotic M,Phases, Meiotic M
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
D008970 Molecular Weight The sum of the weight of all the atoms in a molecule. Molecular Weights,Weight, Molecular,Weights, Molecular
D010446 Peptide Fragments Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques. Peptide Fragment,Fragment, Peptide,Fragments, Peptide
D010748 Phosphopeptides PEPTIDES that incorporate a phosphate group via PHOSPHORYLATION. Phosphopeptide
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
D004676 Myelin Basic Protein An abundant cytosolic protein that plays a critical role in the structure of multilamellar myelin. Myelin basic protein binds to the cytosolic sides of myelin cell membranes and causes a tight adhesion between opposing cell membranes. Golli-MBP1 Protein,Golli-MBP2 Protein,HOG5 Protein,HOG7 Protein,MBP1 Protein,MBP2 Protein,MBP3 Protein,MBP4 Protein,Myelin Basic Protein, 17.2 kDa Isoform,Myelin Basic Protein, 18.5 kDa Isoform,Myelin Basic Protein, 20.2 kDa Isoform,Myelin Basic Protein, 21.5 kDa Isoform,Myelin Basic Protein, Isoform 1,Myelin Basic Protein, Isoform 2,Myelin Basic Protein, Isoform 3,Myelin Basic Protein, Isoform 4,Myelin Basic Protein, Isoform 5,Myelin Basic Protein, Isoform 6,Myelin Basic Protein, Isoform 7,Golli MBP1 Protein,Golli MBP2 Protein
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D000595 Amino Acid Sequence The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION. Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D000596 Amino Acids Organic compounds that generally contain an amino (-NH2) and a carboxyl (-COOH) group. Twenty alpha-amino acids are the subunits which are polymerized to form proteins. Amino Acid,Acid, Amino,Acids, Amino

Related Publications

J S Sanghera, and R Aebersold, and H D Morrison, and E J Bures, and S L Pelech
August 1991, The Journal of biological chemistry,
J S Sanghera, and R Aebersold, and H D Morrison, and E J Bures, and S L Pelech
January 1998, The Journal of biological chemistry,
J S Sanghera, and R Aebersold, and H D Morrison, and E J Bures, and S L Pelech
November 1990, Journal of neurochemistry,
J S Sanghera, and R Aebersold, and H D Morrison, and E J Bures, and S L Pelech
October 1991, Biochimica et biophysica acta,
J S Sanghera, and R Aebersold, and H D Morrison, and E J Bures, and S L Pelech
March 1996, Journal of neuroimmunology,
J S Sanghera, and R Aebersold, and H D Morrison, and E J Bures, and S L Pelech
November 1987, Journal of biochemistry,
J S Sanghera, and R Aebersold, and H D Morrison, and E J Bures, and S L Pelech
November 1982, Journal of neurochemistry,
J S Sanghera, and R Aebersold, and H D Morrison, and E J Bures, and S L Pelech
February 1985, Journal of neurochemistry,
J S Sanghera, and R Aebersold, and H D Morrison, and E J Bures, and S L Pelech
May 1987, Biochemical and biophysical research communications,
J S Sanghera, and R Aebersold, and H D Morrison, and E J Bures, and S L Pelech
January 2000, BMC biochemistry,
Copied contents to your clipboard!