WBP11

Wbp11
Identifiers
Symbol	Wbp11
Pfam	PF09429
InterPro	IPR019007
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

WW domain binding protein 11
Identifiers
Symbols	WBP11 ; NPWBP; PPP1R165; SIPP1; WBP-11
External IDs	MGI: 1891823 HomoloGene: 134037 GeneCards: WBP11 Gene
Gene ontology Molecular function • single-stranded DNA binding • protein binding • protein phosphatase type 1 regulator activity • poly(A) RNA binding • WW domain binding Cellular component • nucleus • nucleoplasm • cytoplasm • nuclear speck Biological process • rRNA processing • mRNA processing • RNA splicing • regulation of catalytic activity • regulation of mitophagy • positive regulation of protein targeting to mitochondrion Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	51729	60321
Ensembl	ENSG00000084463	ENSMUSG00000030216
UniProt	Q9Y2W2	Q923D5
RefSeq (mRNA)	NM_016312	NM_021714
RefSeq (protein)	NP_057396	NP_068360
Location (UCSC)	Chr 12: 14.78 – 14.8 Mb	Chr 6: 136.81 – 136.83 Mb
PubMed search

Alternative names

• WW domain binding protein 11 (WBP1)
• Rsp5
• WWP domain

Function

WW domain-binding protein 11 is a protein that in humans, is encoded by the WBP11 gene. The function of WBP11 is to play a role in the regulation of pre-mRNA processing. More specifically, this nuclear protein, colocalizes with mRNA splicing factors and intermediate filament-containing perinuclear networks.^[1][2]

Structure

The WW domain is a short conserved region in a number of unrelated proteins, which folds as a stable, triple stranded beta-sheet. This short domain of approximately 40 amino acids, may be repeated up to four times in some proteins.^[3][4][5][6] The name WW or WWP derives from the presence of two signature tryptophan residues that are spaced 20-23 amino acids apart and are present in most WW domains known to date, as well as that of a conserved Proline. The WW domain binds to proteins with particular proline-motifs, [AP]-P-P-[AP]-Y, and/or phosphoserine- phosphothreonine-containing motifs.^[7][8] It is frequently associated with other domains typical for proteins in signal transduction processes.

Protein interactions

Wbp11 contains two proline-rich regions that bind to the WW domain of the nuclear protein, Npw38, hence leading to its alternative name, Npw38-binding protein, NpwBP. The Npw38-NpwBP complex functions as a component of an mRNA factory in the nucleus.^[2] WBP11 has also been shown to interact with PQBP1.^[1][9]

Proteins containing Wbp11 domain

A large variety of proteins containing the WW domain are known. These include:

• dystrophin, a multidomain cytoskeletal protein;
• utrophin, a dystrophin-like protein of unknown function;
• vertebrate YAP protein, substrate of an unknown serine kinase;
• Mus musculus (Mouse) NEDD-4, involved in the embryonic development and differentiation of the central nervous system;
• Saccharomyces cerevisiae (Baker's yeast) RSP5, similar to NEDD-4 in its molecular organisation;
• Rattus norvegicus (Rat) FE65, a transcription factor activator expressed preferentially in liver;
• Nicotiana tabacum (Common tobacco) DB10 protein, amongst others.

References

1. Komuro, A.; Saeki, M.; Kato, S. (1999). "Association of Two Nuclear Proteins, Npw38 and NpwBP, via the Interaction between the WW Domain and a Novel Proline-rich Motif Containing Glycine and Arginine". Journal of Biological Chemistry 274 (51): 36513–36519. doi:10.1074/jbc.274.51.36513. ISSN 0021-9258. PMID 10593949.
2. "Entrez Gene: WBP11 WW domain binding protein 11".
3. Bork P, Sudol M (December 1994). "The WW domain: a signalling site in dystrophin?". Trends Biochem. Sci. 19 (12): 531–3. doi:10.1016/0968-0004(94)90053-1. PMID 7846762.
4. André B, Springael JY (December 1994). "WWP, a new amino acid motif present in single or multiple copies in various proteins including dystrophin and the SH3-binding Yes-associated protein YAP65". Biochem. Biophys. Res. Commun. 205 (2): 1201–5. doi:10.1006/bbrc.1994.2793. PMID 7802651.
5. Hofmann K, Bucher P (January 1995). "The rsp5-domain is shared by proteins of diverse functions". FEBS Lett. 358 (2): 153–7. doi:10.1016/0014-5793(94)01415-W. PMID 7828727.
6. Sudol M, Chen HI, Bougeret C, Einbond A, Bork P (August 1995). "Characterization of a novel protein-binding module--the WW domain". FEBS Lett. 369 (1): 67–71. doi:10.1016/0014-5793(95)00550-S. PMID 7641887.
7. Chen HI, Sudol M (August 1995). "The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules". Proc. Natl. Acad. Sci. U.S.A. 92 (17): 7819–23. doi:10.1073/pnas.92.17.7819. PMC 41237. PMID 7644498.
8. Macias MJ, Wiesner S, Sudol M (February 2002). "WW and SH3 domains, two different scaffolds to recognize proline-rich ligands". FEBS Lett. 513 (1): 30–7. doi:10.1016/S0014-5793(01)03290-2. PMID 11911877.
9. Zhang Y, Lindblom T, Chang A, Sudol M, Sluder AE, Golemis EA (October 2000). "Evidence that dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for dim1 interactions with hnRNP F and Npw38/PQBP-1". Gene 257 (1): 33–43. doi:10.1016/S0378-1119(00)00372-3. PMID 11054566.

This article incorporates text from the public domain Pfam and InterPro IPR019007

Further reading

• Bedford MT, Sarbassova D, Xu J, Leder P, Yaffe MB (2000). "A novel pro-Arg motif recognized by WW domains". J. Biol. Chem. 275 (14): 10359–69. doi:10.1074/jbc.275.14.10359. PMID 10744724.
• Craggs G, Finan PM, Lawson D, Wingfield J, Perera T, Gadher S, Totty NF, Kellie S (2001). "A nuclear SH3 domain-binding protein that colocalizes with mRNA splicing factors and intermediate filament-containing perinuclear networks". J. Biol. Chem. 276 (32): 30552–60. doi:10.1074/jbc.M103142200. PMID 11375989.
• Llorian M, Beullens M, Andrés I, Ortiz JM, Bollen M (2004). "SIPP1, a novel pre-mRNA splicing factor and interactor of protein phosphatase-1". Biochem. J. 378 (Pt 1): 229–38. doi:10.1042/BJ20030950. PMC 1223944. PMID 14640981.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
• Llorian M, Beullens M, Lesage B, Nicolaescu E, Beke L, Landuyt W, Ortiz JM, Bollen M (2005). "Nucleocytoplasmic shuttling of the splicing factor SIPP1". J. Biol. Chem. 280 (46): 38862–9. doi:10.1074/jbc.M509185200. PMID 16162498.
• Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
• Lim J, Hao T, Shaw C, Patel AJ, Szabó G, Rual JF, Fisk CJ, Li N, Smolyar A, Hill DE, Barabási AL, Vidal M, Zoghbi HY (2006). "A protein-protein interaction network for human inherited ataxias and disorders of Purkinje cell degeneration". Cell 125 (4): 801–14. doi:10.1016/j.cell.2006.03.032. PMID 16713569.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.