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PMID:9299544

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Citation

Aspbury, RA, Fisher, MJ, Rees, HH and Clegg, RA (1997) N-Myristoylation of the catalytic subunit of cAMP-dependent protein kinase in the free-living nematode Caenorhabditis elegans. Biochem. Biophys. Res. Commun. 238:523-7

Abstract

N-Myristoylation of the catalytic subunit (C-subunit) of cAMP-dependent protein kinase is widespread in animal cells. Some invertebrates express non-myristoylated isoforms of C-subunit but these co-exist with at least one myristoylated isoform. The generality of this observation implies an indispensable function for myristoylated C-subunit, but notwithstanding this, neither of the C-subunit isoforms hitherto described in C. elegans is apparently N-myristoylated. In light of this anomaly, the myristoylation status of the C-subunit has been examined in adult C. elegans. Evidence is presented for the presence of an N-myristoylated isoform.

Links

PubMed Online version:10.1006/bbrc.1997.7165

Keywords

Animals; Caenorhabditis elegans; Cyclic AMP-Dependent Protein Kinases/chemistry; Cyclic AMP-Dependent Protein Kinases/metabolism; Myristates

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

CAEEL:KAPC1

enables

GO:0004691: cAMP-dependent protein kinase activity

ECO:0000314: direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

CAEEL:KAPC1

involved_in

GO:0006468: protein phosphorylation

ECO:0000314: direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

CAEEL:KAPC1

part_of

GO:0005952: cAMP-dependent protein kinase complex

ECO:0000250: sequence similarity evidence used in manual assertion

UniProtKB:P06245

C

Seeded From UniProt

complete


See also

References

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