<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Zencir S</submitter><funding>NIDDK NIH HHS</funding><pagination>792-7</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3157015</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>411(4)</volume><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</pubmed_abstract><journal>Biochemical and biophysical research communications</journal><pubmed_title>Identification of brain-specific angiogenesis inhibitor 2 as an interaction partner of glutaminase interacting protein.</pubmed_title><pmcid>PMC3157015</pmcid><funding_grant_id>DK082397</funding_grant_id><funding_grant_id>R21 DK082397-01</funding_grant_id><funding_grant_id>R21 DK082397-02</funding_grant_id><funding_grant_id>R21 DK082397</funding_grant_id><pubmed_authors>Mohanty S</pubmed_authors><pubmed_authors>Zencir S</pubmed_authors><pubmed_authors>Ovee M</pubmed_authors><pubmed_authors>Banerjee M</pubmed_authors><pubmed_authors>Dobson MJ</pubmed_authors><pubmed_authors>Topcu Z</pubmed_authors></additional><is_claimable>false</is_claimable><name>Identification of brain-specific angiogenesis inhibitor 2 as an interaction partner of glutaminase interacting protein.</name><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</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011 Aug</publication><modification>2025-04-04T21:20:07.65Z</modification><creation>2019-03-27T03:08:01Z</creation></dates><accession>S-EPMC3157015</accession><cross_references><pubmed>21787750</pubmed><doi>10.1016/j.bbrc.2011.07.029</doi></cross_references></HashMap>