Xref: utzoo bionet.molbio.proteins:101 bionet.software:414 bionet.molbio.swiss-prot:11 bionet.molbio.bio-matrix:199 bionet.molbio.evolution:115 Path: utzoo!telly!attcan!uunet!bionet!revel From: revel@genbank.bio.net (Jean-Paul Revel) Newsgroups: bionet.molbio.proteins,bionet.software,bionet.molbio.swiss-prot,bionet.molbio.pir,bionet.molbio.bio-matrix,bionet.molbio.evolution Subject: protein alignment Keywords: connexin phophorylation modification Message-ID: Date: 4 Sep 90 21:00:59 GMT Followup-To: bionet.molbio.proteins Distribution: bionet Organization: GenBank Online Service Lines: 21 I recently isolated a new member of the connexin gene family. These molecules have a conserved 200 amino acid 'core' (that contains 4 transmembrane segments) but the C-termini are highly diverged and vary in length from 20 to 150 amino acids. To improve the alignment of our new connexin with other members of the gene family, particularly over the C-terminal domain, we ran all the connexins through the PC-Gene program PROSITE which detects consensus protein modification sites, and conserved modification sites were used to force the alignment. Doing this we discovered what appears to be a significant conservation of three phophorylation sites that none of the other alignment programs we have tried revealed. Does anyone know of any papers that use this approach and/or discuss the significance of the conservation of putative modification sites? Any comments related to this problem would be appreciated. Jan Hoh jhoh@romeo.bitnet