Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation.
Analysis of the sequence of amino acids surrounding sites of tyrosine phosphorylation.
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DOI：
10.1073/pnas.79.4.973
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发表时间：
1982-02
影响因子：
11.1
通讯作者：
T. Patschinsky;T. Hunter;F. Esch;Jonathan A. Cooper;B. Sefton
中科院分区：
文献类型：
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作者：
T. Patschinsky;T. Hunter;F. Esch;Jonathan A. Cooper;B. Sefton
我们已经确定了单一的磷酸化酪氨酸在p60 src，劳斯肉瘤病毒的转化蛋白，作为序列的一部分。NH2-Arg-Leu-Ile-Glu-Asp-Asn-Glu-Tyr（P）-Thr-Ala-Arg-COOH。因此，这是在体内被酪氨酸蛋白激酶有效识别的序列。细胞蛋白质中酪氨酸的磷酸化似乎在四类遗传上不同的RNA肿瘤病毒的恶性转化中起作用。其他几种蛋白质中的磷酸化酪氨酸类似于p60 src中的酪氨酸，因为它们位于碱性氨基酸的COOH末端侧的7个残基和谷氨酸残基的COOH末端侧的4个残基或非常接近谷氨酸残基。因此，这些特征可能在某些酪氨酸蛋白激酶磷酸化位点的选择中发挥作用。然而，这一规则有几个明显的例外。
We have identified the single phosphorylated tyrosine in p60src, the transforming protein of Rous sarcoma virus, as part of the sequence. NH2-Arg-Leu-Ile-Glu-Asp-Asn-Glu-Tyr(P)-Thr-Ala-Arg-COOH. Therefore, this is a sequence that is recognized efficiently by a tyrosine protein kinase in vivo. Phosphorylation of tyrosine in cellular proteins appears to play a role in malignant transformation by four classes of genetically distinct RNA tumor viruses. Phosphorylated tyrosines in several other proteins resemble of the tyrosine in p60src in that they are located 7 residues to the COOH-terminal side of a basic amino acid and either 4 residues to the COOH-terminal side of, or in close proximity to, a glutamic acid residue. Therefore it is possible that these features play a role in the selection of sites of phosphorylation by some tyrosine protein kinases. However, several clear exceptions to this rule exist.