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Search results 1 to 3 out of 3 for Dab1

Category restricted to ProteinDomain (x)

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Category: ProteinDomain
Type Details Score
Protein Domain
Type: Family
Description: This entry represents the protein disabled (DAB) and related proteins. It includes DAB from Drosophila melanogaster and its mammlian homologues, DAB1 and DAB2 (also known as DOC1 and DOC2). This group of proteins are adapter proteins that play roles in development. In Drosophila melanogaster, DAB acts as an adapter protein for SH2-domain containing proteins in the sevenless (sev) signalling pathway []. Together with Abl, it is involved in embryonic neural development []. In mammals, DAB1 is implicated in neuronal development []. In humans, DAB2 is an adapter protein that functions as clathrin-associated sorting protein (CLASP) required for clathrin-mediated endocytosis of selected cargo proteins []. It is involved in several signalling pathways and plays an important part in cell growth and development [, , ].
Protein Domain
Type: Family
Description: DAB-2 interacting protein (Dab2IP) is a GTPase activating protein involved in the regulation of multiple signalling pathways. Dab2IP regulates PI3K-AKT signalling and functions as a tumour suppressor. It modulates the balance between phosphatidylinositol 3-kinase (PI3K) mediated cell survival and ASK1 mediated apoptosis [, ]. Besides its function as a tumour suppressor, Dab2IP is also highly expressed in the brain, where it interacts with Dab1 (Disabled homologue 1), a key mediator of the Reelin pathway that controls several aspects of brain development and function [, , ]. It also functions as an inhibitor in VEGFR2-mediated adaptative angiogenesis [].Dab2IP has been associated with metastatic prostate cancer [], abdominal aortic aneurysms []and coronary heart disease [].
Protein Domain
Type: Domain
Description: Proteins encoding phosphotyrosine binding (PTB) domains function as adaptors or scaffolds to organise the signaling complexes involved in wide-ranging physiological processes including neural development, immunity, tissue homeostasis and cell growth. Due to structural differences, PTB domains are divided into three groups represented by phosphotyrosine-dependent IRS-like, phosphotyrosine-dependent Shc-like, and phosphotyrosine-independent Dab-like PTBs. The last two PTBs have been named as phosphotyrosine interaction domain (PID or PI domain). PID domain has an average length of about 160 amino acids [].The Shc-like PID specifically binds to the Asn-Pro-Xaa-Tyr(P) motif found in many tyrosine-phosphorylated proteins including growth factor receptors. On the other hand the Dab-like PID domain binds to non-phosphorylated tyrosine residue or even a phenylalanine at the same position []. Most of the ligands for Shc-like PID domains are RTK or cytokine, whereas phosphotyrosine independent Dab-like PID domains seems to mediate other types of signaling pathways, like endocytosis/processing or exocytosis. This domain binds both peptides and headgroups of phosphatidylinositides, utilising two distinct binding motifs to mediate spatial organisation and localisation within cells [, , , ].The 3D structure of PID domain has been solved []. It shares a folding pattern, commonly referred to as the PH-domain "superfold". The core "superfold"consists of seven antiparallel beta strands forming two orthogonal beta sheets. This beta sandwich is capped at the C terminus by an alpha helix. It contains a peptide binding pocket (formed by the beta strand 5 and C-terminal alpha helix) and a highly basic phospholipid binding "crown"(largely composed of residues from loop regions near the N terminus). Both Shcand Dab1 have two additional alpha helices, one of which is located at the Nterminus and the other between beta 1 and beta 2 strands.