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WW domain binding protein 2

WBP-2, WW domain binding protein-2
The globular WW domain is composed of 38 to 40 semiconserved amino acids shared by proteins of diverse functions including structural, regulatory, and signaling proteins. The domain is involved in mediating protein-protein interactions through the binding of polyproline ligands. This gene encodes a WW domain binding protein, which binds to the WW domain of Yes kinase-associated protein by its PY motifs. The function of this protein has not been determined. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: YAP, WWOX, Src, CAN, WBP-1
Papers on WBP-2
Sperm Factors and Oocyte Activation: Current Controversies and Considerations.
Review
New
Coward et al., Bandar Seri Begawan, Brunei. In Biol Reprod, Aug 2015
However, a series of recent publications has challenged the dominance of PLCzeta and proposed an alternative candidate protein, WBP2 N-terminal like (WBP2NL or PAWP).
The Evaluation of WBP2NL-Related Genes Expression in Breast Cancer.
New
Nouri et al., Tabrīz, Iran. In Pathol Oncol Res, Apr 2015
Recent studies have shown that WW Binding Protein 2 (WBP2) is an important protein for the oncogenic property of cancer.
Roles of the WWOX in pathogenesis and endocrine therapy of breast cancer.
Review
New
Liu et al., Xi'an, China. In Exp Biol Med (maywood), Mar 2015
At the molecular level, WWOX interacts with AP2γ, ErbB4, SMAD3, and WBP2 suppressing their transcription activities in breast cancer cell lines.
Elevated Expression of the Testis-specific Gene WBP2NL in Breast Cancer.
Modarressi et al., Tehrān, Iran. In Biomark Cancer, 2014
Recent studies have shown that WW domain-binding protein 2 (WBP2) is important for the oncogenic property of breast cancer.
Molecular mechanism of WW-domain binding protein-2 coactivation function in estrogen receptor signaling.
Nawaz et al., Miami, United States. In Iubmb Life, 2013
Our laboratory has previously identified the WW-domain binding protein-2 (WBP-2) as a bona fide coactivator of ER.
Biophysical basis of the binding of WWOX tumor suppressor to WBP1 and WBP2 adaptors.
Farooq et al., Miami, United States. In J Mol Biol, 2012
The WW-containing oxidoreductase (WWOX) tumor suppressor participates in a diverse array of cellular activities by virtue of its ability to recognize WW-binding protein 1 (WBP1) and WW-binding protein 2 (WBP2) signaling adaptors among a wide variety of other ligands.
Biophysical analysis of binding of WW domains of the YAP2 transcriptional regulator to PPXY motifs within WBP1 and WBP2 adaptors.
GeneRIF
Farooq et al., Miami, United States. In Biochemistry, 2011
The WW1 and WW2 domains of YAP2 recognize various PPXY motifs within WBP2 and WBP1 in a highly promiscuous and subtle manner.
Tyrosine phosphorylation of transcriptional coactivator WW-domain binding protein 2 regulates estrogen receptor α function in breast cancer via the Wnt pathway.
Lim et al., Singapore, Singapore. In Faseb J, 2011
WW-binding protein 2 (WBP2) has been demonstrated in different studies to be a tyrosine kinase substrate, to activate estrogen receptor α (ERα)/progesterone receptor (PR) transcription, and to play a role in breast cancer.
Wbp2 cooperates with Yorkie to drive tissue growth downstream of the Salvador-Warts-Hippo pathway.
Harvey et al., Melbourne, Australia. In Cell Death Differ, 2011
In this study, we define Wbp2 as a promoter of Yorkie-dependent growth of Drosophila melanogaster tissues.
Genome-wide association studies of cerebral white matter lesion burden: the CHARGE consortium.
Launer et al., Houston, United States. In Ann Neurol, 2011
RESULTS: We identified 6 novel risk-associated single nucleotide polymorphisms (SNPs) in 1 locus on chromosome 17q25 encompassing 6 known genes including WBP2, TRIM65, TRIM47, MRPL38, FBF1, and ACOX1.
WW domain-mediated interaction with Wbp2 is important for the oncogenic property of TAZ.
GeneRIF
Hong et al., Singapore, Singapore. In Oncogene, 2011
Data show that direct interaction of Wbp2 with TAZ depends on the WW domain of TAZ.
Newcomers to the WW Domain-Mediated Network of the Hippo Tumor Suppressor Pathway.
Sudol, United States. In Genes Cancer, 2010
We focus here on 2 families of such proteins, angiomotins and SMADs, plus 1 regulatory factor, WBP-2, which together shed new light on the rapidly expanding Hippo network.
Differential expression of novel tyrosine kinase substrates during breast cancer development.
Lim et al., Singapore, Singapore. In Mol Cell Proteomics, 2007
Seven of these proteins (SPAG9, Toll-interacting protein (TOLLIP), WBP2, NSFL1C, SLC4A7, CYFIP1, and RPS2) were validated to be novel tyrosine kinase substrates.
WW domain binding protein-2, an E6-associated protein interacting protein, acts as a coactivator of estrogen and progesterone receptors.
GeneRIF
Nawaz et al., Miami, United States. In Mol Endocrinol, 2006
WW domain binding protein-2, an E6-associated protein interacting protein, acts together with YAP as coactivators of estrogen and progesterone receptors.
WBP-2, a WW domain binding protein, interacts with the thyroid-specific transcription factor Pax8.
Zannini et al., Napoli, Italy. In Biochem J, 2004
In the present paper, we describe the identification by means of immunological screening of the WW domain binding protein WBP-2 as a biochemical interactor of Pax8 (a WW domain is a protein-interaction domain containing two conserved tryptophan residues).
Characterization of a novel protein-binding module--the WW domain.
Review
Bork et al., New York City, United States. In Febs Lett, 1995
Using a functional screen of a cDNA expression library, we have identified two putative ligands of the WW domain of YAP which we named WBP-1 and WBP-2.
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