STY, a tyrosine-phosphorylating enzyme with sequence homology to serine/threonine kinases.
We have cloned a novel kinase (STY) from an embryonal carcinoma cell line. Sequence analysis of the STY cDNA reveals that it shares sequence homology with serine/threonine-type kinases and yet the bacterial expression product of the STY cDNA appears to have serine-, threonine-, and tyrosine-phosphorylating activities. The predicted STY protein is highly basic and contains a putative nuclear localization signal. During differentiation, two new mRNAs were detected in addition to the embryonic transcript.
Howell
B W
BW
Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
Afar
D E
DE
Lew
J
J
Douville
E M
EM
Icely
P L
PL
Gray
D A
DA
Bell
J C
JC
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D015139:Blotting, Southern; D002454:Cell Differentiation; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D015870:Gene Expression; D051379:Mice; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000235:genetics; D017346:Protein Serine-Threonine Kinases; D011505:Protein-Tyrosine Kinases / Q000235:genetics* / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D013379:Substrate Specificity; D014407:Tumor Cells, Cultured
D009687:Nuclear Proteins; D011993:Recombinant Fusion Proteins; D004247:DNA; C066780:Clk dual-specificity kinases; D011505:Protein-Tyrosine Kinases; D017346:Protein Serine-Threonine Kinases