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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Transmembrane phosphoinositide 3-phosphatase and tensin homolog 2

TPIP, TPTE and PTEN homologous inositol lipid phosphatase
TPIP is a member of a large class of membrane-associated phosphatases with substrate specificity for the 3-position phosphate of inositol phospholipids.[supplied by OMIM, Jul 2002] (from NCBI)
Top mentioned proteins: PTEN, TNS, CAN, V1a, PrP
Papers on TPIP
TODRA, a lncRNA at the RAD51 Locus, Is Oppositely Regulated to RAD51, and Enhances RAD51-Dependent DSB (Double Strand Break) Repair.
Levy-Lahad et al., Jerusalem, Israel. In Plos One, 2014
TODRA overexpression in HeLa cells induced expression of TPIP, a member of the TPTE family which includes PTEN.
A human phospholipid phosphatase activated by a transmembrane control module.
Oliver et al., Marburg an der Lahn, Germany. In J Lipid Res, 2012
Here we demonstrate activation of a human VSP (hVSP1/TPIP) by an intramolecular switch.
Cell cycle arrest and apoptosis by expression of a novel TPIP (TPIP-C2) cDNA encoding a C2-domain in HEK-293 cells.
Rath et al., New Delhi, India. In Mol Biol Rep, 2012
findings suggest that C2-domain of TPIP-C2 may act as a dominant negative effector, which may bind to and arrest the cell proliferation signalling complex
3' Phosphatase activity toward phosphatidylinositol 3,4-bisphosphate [PI(3,4)P2] by voltage-sensing phosphatase (VSP).
Okamura et al., Suita, Japan. In Proc Natl Acad Sci U S A, 2012
To gain insights into this question, we performed in vitro assays of phosphatase activities of Ciona intestinalis VSP (Ci-VSP) and transmembrane phosphatase with tensin homology (TPTE) and PTEN homologous inositol lipid phosphatase (TPIP; one human ortholog of VSP) with radiolabeled PI(3,4,5)P(3).
A comprehensive functional analysis of PTEN mutations: implications in tumor- and autism-related syndromes.
Pulido et al., Madrid, Spain. In Hum Mol Genet, 2011
PTEN mutations that mimic the P-catalytic loop of mammalian PTEN-like proteins (TPTE, TPIP, tensins and auxilins) affected PTEN function variably, whereas tumor- or PHTS-associated mutations targeting the PTEN P-loop produced complete loss of function.
A novel human TPIP splice-variant (TPIP-C2) mRNA, expressed in human and mouse tissues, strongly inhibits cell growth in HeLa cells.
Rath et al., New Delhi, India. In Plos One, 2010
the TPIP splice-variant (TPIP-C2) mRNA is expressed in human and mouse tissues and strongly inhibits cell growth in HeLa cells
Thromboxane A2-induced signal transduction is negatively regulated by KIAA1005 that directly interacts with thromboxane A2 receptor.
Nakahata et al., Sendai, Japan. In Prostaglandins Other Lipid Mediat, 2009
We found KIAA1005 as a novel interacting protein of the TP alpha and TP beta C-terminal region (TP interacting protein, TPIP).
Acute regulation of the tumour suppressor phosphatase, PTEN, by anionic lipids and reactive oxygen species.
Leslie et al., Dundee, United Kingdom. In Biochem Soc Trans, 2004
TPIP [TPTE (transmembrane phosphatase with tensin homology) and PTEN homologous inositol lipid phosphatase] is a novel gene product which exists in multiply spliced forms.
The TPTE gene family: cellular expression, subcellular localization and alternative splicing.
Antonarakis et al., Genève, Switzerland. In Gene, 2004
Chromosomal mapping revealed multiple copies of the TPTE gene on chromosomes 13, 15, 21, 22 and Y. Human chromosomes 13 and 21 copies encode two functional proteins, TPIP (TPTE and PTEN homologous Inositol lipid Phosphatase) and TPTE, respectively, whereas only one copy of the gene exists in the mouse genome.
TPIP: a novel phosphoinositide 3-phosphatase.
Leslie et al., Dundee, United Kingdom. In Biochem J, 2002
TPIP (TPTE and PTEN homologous inositol lipid phosphatase) is a novel phosphatase that occurs in several differentially spliced forms of which two, TPIP alpha and TPIP beta, appear to be functionally distinct.
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