Dysbindin protein family domains

More members of the dysbindin protein family are known in humans than in any other species at present. In articular, there are eight human proteins with dysbindin domains listed by the National Center for Biotechnology Information (NCBI http //www.ncbi.nlm.nih.gov/) and/or by the Universal Protein Resource (UniProt http //www.pir.uniprot.org/index.shtml). They are schematically shown in Figure 2.2-1, which... 

Dysbindin family paralogs and isoforms known in humans. See textQ Section 2.2.3 for explanation of segmentation of the proteins into an amino terminal region (NTR), coiled-coil domain (CCD) divided into two helices (HI and H2), and a carboxy terminal region (CTR) consisting of the dysbindin domain (DD), PEST domain (PD), and uncharacterized areas X1-X3. Dysbindin-1 B is not found in the mouse... 

Further discussion of the dysbindin family is limited to dysbindin-1 since little is known about other family members apart from the fact that dysbindin-2B is a casein kinase 1 binding partner and a stem cell factor apoptosis response protein. In contrast, much has been learned about dysbindin-1 since its discovery was reported by Benson et al. (2001). It is the only member of the dysbindin family known to exist in invertebrates, specifically the fruit fly, and may thus date back 600 million years. Unlike all other dysbindin paralogs, it contains a coiled coil domain (CCD) allowing extensive interactions with other proteins. A leucine zipper motif in the CCD changed in the course of evolution in a manner permitting more durable interactions with binding partners. 

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