Publication Date:
1985-01-25
Description:
The transforming protein of Rous sarcoma virus, p60src, was shown to be acylated at its amino terminus with the long-chain fatty acid myristic acid by isolation of a tryptic peptide with the following structure: myristylglycylserylseryllysine. The occurrence of this unusual posttranslational modification in the cyclic adenosine monophosphate-dependent protein kinase and in several transforming protein kinases of mammalian retroviruses suggests that myristylation of the amino terminal glycyl residue may be critical for the function of certain proteins related to cell transformation and growth control.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schultz, A M -- Henderson, L E -- Oroszlan, S -- Garber, E A -- Hanafusa, H -- CA-14935/CA/NCI NIH HHS/ -- N01-CO-23909/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1985 Jan 25;227(4685):427-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3917576" target="_blank"〉PubMed〈/a〉
Keywords:
Acylation
;
Amino Acid Sequence
;
Cell Transformation, Neoplastic
;
Cell Transformation, Viral
;
Myristic Acid
;
Myristic Acids/*analysis/metabolism
;
Oncogene Protein pp60(v-src)
;
Protein Kinases/*analysis/metabolism
;
Protein Processing, Post-Translational
;
Viral Proteins/*analysis/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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