ISSN:
1573-4919
Keywords:
protein phosphorylation
;
human polypeptide
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
Summary A 1,820bp full-length clone encoding for a new human protein was isolated from a λgt11 placental cDNA library using anti-human hexokinase antibodies. The cDNA complete sequence includes a 12 by 5′ noncoding region, a single open reading frame encoding a protein of 55 KDa (HP-10) and a 177 by non-coding with two putative polyadenylation signals upstream of 3′poly(A)tail. The deduced amino acid sequence reveals a sequence of 492 amino acids that contains a stretch of 7 glutamic acid from position 169 and one potential glycosylation site at position 274. Although antibodies against hexokinase recognize the fusion protein and antibodies against the fusion protein recognize hexokinase, HP-10 is not human hexokinase, by a number of criteria including the alignment of determined amino acid sequences. In searching for a possible functional role of HP-10 its cDNA was inserted into a procaryotic vector which allows the expression of the non-fused protein. Bacteria expressing the HP-10 encoded protein were isolated and found to have a dramatic increase in endogenous phosphorylated proteins. Since HP-10 does not have a protein kinase activity per se it should be considered a new regulatory phosphorylation protein which is active in E. coli
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00225511
