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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)
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).
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.
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.
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.
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.
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.
Nawaz et al., Miami, United States. In Mol Endocrinol, 2006
WW domain bindingprotein-2, an E6-associated protein interacting protein, acts together with YAP as coactivators of estrogen and progesterone receptors.
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).
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.