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Gershagen, S, Fernlund, P and Lundwall, A (1987) A cDNA coding for human sex hormone binding globulin. Homology to vitamin K-dependent protein S. FEBS Lett. 220:129-35
Affinity purified antibodies to human sex hormone binding globulin (SHBG) were used in screening a human liver cDNA library, constructed in the expression vector lambda gt11. One clone, identified as producing recombinant SHBG, carried a cDNA insert of 1.1 kb. The nucleotide sequence of the insert had an open reading frame coding for 356 amino acid residues. The coding sequence was followed by a short 3'-region of 19 non-translated nucleotides and a poly(A) tail. Confirmation that the cDNA clone represented human SHBG was obtained by the finding of a complete agreement in amino acid sequence with several peptide fragments generated from purified SHBG by proteolytic cleavage. The primary structure of SHBG shows a considerable homology to that of protein S, a vitamin K-dependent protein with functions in the coagulation system.
Amino Acid Sequence; Animals; Base Sequence; Cattle; DNA/analysis; Glycoproteins/analysis; Glycoproteins/genetics; Humans; Liver/analysis; Peptide Fragments/analysis; Protein S; Sequence Homology, Nucleic Acid; Sex Hormone-Binding Globulin/analysis; Sex Hormone-Binding Globulin/genetics
|Gene product||Qualifier||GO Term||Evidence Code||with/from||Aspect||Extension||Notes||Status|
|GO:0007285: primary spermatocyte growth||
Analysis of Paper. See Figure 1(b). Shows the Amino acid sequences determined by peptides. Those generated from SHBG are underlined
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