{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zencir S"],"funding":["NIDDK NIH HHS"],"pagination":["792-7"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3157015"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["411(4)"],"pubmed_abstract":["The vast majority of physiological processes in living cells are mediated by protein-protein interactions often specified by particular protein sequence motifs. PDZ domains, composed of 80-100 amino acid residues, are an important class of interaction motif. Among the PDZ-containing proteins, glutaminase interacting protein (GIP), also known as Tax Interacting Protein TIP-1, is unique in being composed almost exclusively of a single PDZ domain. GIP has important roles in cellular signaling, protein scaffolding and modulation of tumor growth and interacts with a number of physiological partner proteins, including Glutaminase L, β-Catenin, FAS, HTLV-1 Tax, HPV16 E6, Rhotekin and Kir 2.3. To identify the network of proteins that interact with GIP, a human fetal brain cDNA library was screened"],"journal":["Biochemical and biophysical research communications"],"pubmed_title":["Identification of brain-specific angiogenesis inhibitor 2 as an interaction partner of glutaminase interacting protein."],"pmcid":["PMC3157015"],"funding_grant_id":["DK082397","R21 DK082397-01","R21 DK082397-02","R21 DK082397"],"pubmed_authors":["Mohanty S","Zencir S","Ovee M","Banerjee M","Dobson MJ","Topcu Z"],"additional_accession":[]},"is_claimable":false,"name":"Identification of brain-specific angiogenesis inhibitor 2 as an interaction partner of glutaminase interacting protein.","description":"The vast majority of physiological processes in living cells are mediated by protein-protein interactions often specified by particular protein sequence motifs. PDZ domains, composed of 80-100 amino acid residues, are an important class of interaction motif. Among the PDZ-containing proteins, glutaminase interacting protein (GIP), also known as Tax Interacting Protein TIP-1, is unique in being composed almost exclusively of a single PDZ domain. GIP has important roles in cellular signaling, protein scaffolding and modulation of tumor growth and interacts with a number of physiological partner proteins, including Glutaminase L, β-Catenin, FAS, HTLV-1 Tax, HPV16 E6, Rhotekin and Kir 2.3. To identify the network of proteins that interact with GIP, a human fetal brain cDNA library was screened","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Aug","modification":"2025-04-04T21:20:07.65Z","creation":"2019-03-27T03:08:01Z"},"accession":"S-EPMC3157015","cross_references":{"pubmed":["21787750"],"doi":["10.1016/j.bbrc.2011.07.029"]}}