WBP1

WW domain binding protein 1, also known as WBP1, is a human gene.cite web | title = Entrez Gene: WBP1 WW domain binding protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23559| accessdate = ]

PBB_Summary
section_title =
summary_text = 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 a conserved region: XPPXY motif. The function of this protein has not been determined.cite web | title = Entrez Gene: WBP1 WW domain binding protein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23559| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Ludes-Meyers JH, Kil H, Bednarek AK, "et al." |title=WWOX binds the specific proline-rich ligand PPXY: identification of candidate interacting proteins. |journal=Oncogene |volume=23 |issue= 29 |pages= 5049–55 |year= 2004 |pmid= 15064722 |doi= 10.1038/sj.onc.1207680
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Jolliffe CN, Harvey KF, Haines BP, "et al." |title=Identification of multiple proteins expressed in murine embryos as binding partners for the WW domains of the ubiquitin-protein ligase Nedd4. |journal=Biochem. J. |volume=351 Pt 3 |issue= |pages= 557–65 |year= 2001 |pmid= 11042109 |doi=
*cite journal | author=Chen HI, Einbond A, Kwak SJ, "et al." |title=Characterization of the WW domain of human yes-associated protein and its polyproline-containing ligands. |journal=J. Biol. Chem. |volume=272 |issue= 27 |pages= 17070–7 |year= 1997 |pmid= 9202023 |doi=
*cite journal | author=Pirozzi G, McConnell SJ, Uveges AJ, "et al." |title=Identification of novel human WW domain-containing proteins by cloning of ligand targets. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 14611–6 |year= 1997 |pmid= 9169421 |doi=
*cite journal | author=Chen HI, Sudol M |title=The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 17 |pages= 7819–23 |year= 1995 |pmid= 7644498 |doi=

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