BAIT
CASKIN1
CASK interacting protein 1
GO Process (1)
GO Function (2)
GO Component (1)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Rattus norvegicus
PREY
EPHA2
ARCC2, CTPA, CTPP1, CTRCT6, ECK
EPH receptor A2
GO Process (23)
GO Function (2)
GO Component (5)
Gene Ontology Biological Process
- activation of Rac GTPase activity [IMP]
- bone remodeling [ISS]
- branching involved in mammary gland duct morphogenesis [ISS]
- cell chemotaxis [IMP]
- cell migration [IMP]
- ephrin receptor signaling pathway [IDA]
- intrinsic apoptotic signaling pathway in response to DNA damage [IDA]
- keratinocyte differentiation [IMP]
- lens fiber cell morphogenesis [ISS]
- mammary gland epithelial cell proliferation [ISS]
- multicellular organismal development [TAS]
- negative regulation of protein kinase B signaling [IDA]
- osteoblast differentiation [ISS]
- osteoclast differentiation [ISS]
- peptidyl-tyrosine phosphorylation [IDA]
- positive regulation of establishment of protein localization to plasma membrane [IMP]
- protein kinase B signaling [IDA]
- regulation of ERK1 and ERK2 cascade [IMP]
- regulation of angiogenesis [ISS]
- regulation of blood vessel endothelial cell migration [ISS]
- regulation of cell adhesion mediated by integrin [IDA]
- regulation of lamellipodium assembly [IMP]
- response to growth factor [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Homo sapiens
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
High levels of structural disorder in scaffold proteins as exemplified by a novel neuronal protein, CASK-interactive protein1.
CASK-interactive protein1 is a newly recognized post-synaptic density protein in mammalian neurons. Although its N-terminal region contains several well-known functional domains, its entire C-terminal proline-rich region of 800 amino acids lacks detectable sequence homology to any previously characterized protein. We used multiple techniques for the structural characterization of this region and its three fragments. By bioinformatics predictions, CD spectroscopy, wide-line ... [more]
FEBS J. Jul. 01, 2009; 276(14);3744-56 [Pubmed: 19523119]
Throughput
- Low Throughput
Curated By
- BioGRID