PRIMARY STRUCTURE OF BMK1 - A NEW MAMMALIAN MAP KINASE
PRIMARY STRUCTURE OF BMK1 - A NEW MAMMALIAN MAP KINASE
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DOI：
10.1006/bbrc.1995.2189
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发表时间：
1995-08-15
影响因子：
3.1
通讯作者：
HAN, JH
中科院分区：
文献类型：
--
作者：
LEE, JD;ULEVITCH, RJ;HAN, JH
丝裂原活化蛋白(MAP)激酶是一类保守的真核生物酶，可调节对多种细胞外刺激的反应。我们发现了一个新的人类MAP激酶基因，命名为BMK1。BMK1编码816个氨基酸残基的蛋白质，至少有三种不同形式的信使核糖核酸。BMK1在心脏、胎盘和肾脏中含量丰富，但在肝脏中检测不到。虽然BMK1具有以ERK1和ERK2中发现的Tey序列为特征的MAP激酶的双重磷酸化位点，但与其他哺乳动物MAP激酶相比，它具有独特的C末端和环-12结构。这表明BMK1可能调节不同于ERK酶群控制的信号事件。(C)1995年学术出版社。
Mitogen-activated protein (MAP) kinases comprise a family of conserved, eukaryotic enzymes that mediate responses to a wide variety of extracellular stimuli. We have identified a new human MAP kinase gene here termed BMK1. BMK1 encodes a protein of 816 amino acid residues and has at least three different forms of mRNA. BMK1 messages are abundant in heart, placenta and kidney but not detectable in liver. Although BMK1 has the dual phosphorylation site of MAP kinases characterized by the TEY sequence found in ERK1 and ERK2, it has a distinct C-terminal and loop-12 structure when compared to other mammalian MAP kinases. This suggests BMK1 may regulate signaling events distinct from those controlled by the ERK group of enzymes. (C) 1995 Academic Press, Inc.