The ability of Nova-1 to activate exon selection in neurons is antagonized by a second RNA-binding protein, brPTB (brain-enriched polypyrimidine tract-binding protein), which interacts with Nova-1 and inhibits its function [ 24].
Finally, CALM1 encodes calmodulin, a calcium-binding protein, which interacts with titin and mediates smooth muscle contraction, making it a candidate for the BTA10 102 286 251–103 234 411-bp QTL.
The transcription factor Sp1, which was not determined on the Aroclor 1254 microarray, is a DNA-binding protein which interacts with a variety of gene promoters containing GC-box elements and is known to physically and functionally interact with AhR in promoters of several genes in which SP1 plays an important role in basal gene expression [ 24].
Four proteins putatively involved in vesicle transport were identified as interacting with LmjMCA: the Rab1 small GTP-binding protein, which interacted with the inactive catalytic domain (Table 2), the dynein heavy chain, the ADP-ribosylation factor (Arf) GTPase activating protein (GAP) and the transport sec-23-like protein, which interacted with the full-length LmjMCA.
We report the molecular characterization of the VARV- and MPXV-secreted type I interferon-binding proteins, which interact with the cell surface after secretion and prevent type I interferon responses.
L-Afadin, the longer version of two afadin isoforms with a F-actin-binding domain, is a scaffolding protein which interacts with both nectins and F-actin through independent domains suggesting that it directly links nectin-based adhesion sites to the actin cytoskeleton (Mandai et al. 1997) (Fig. 1).
The residue 292 might be also responsible for receptor binding, similar to K149 of VP2 protein which interacts with one of the receptors for PSGL-1 [ 24].
Gcn4p is a basic leucine zipper protein which interacts with DNA binding sites as a dimer [ 32], and is known to preferentially bind to several sequence motifs, including a 7-mer motif, TGACTCA [ 33, 34].
