Summary: WW domain binding protein 11
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WBP11 Edit Wikipedia article
|WW domain binding protein 11|
|Symbols||; NPWBP; PPP1R165; SIPP1; WBP-11|
- WW domain binding protein 11 (WBP1)
- WWP domain
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.
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. 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. It is frequently associated with other domains typical for proteins in signal transduction processes.
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. WBP11 has also been shown to interact with PQBP1.
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.
- Komuro A, Saeki M, Kato S (January 2000). "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". J Biol Chem 274 (51): 36513–9. doi:10.1074/jbc.274.51.36513. PMID 10593949.
- "Entrez Gene: WBP11 WW domain binding protein 11".
- 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.
- AndrÃ© 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.
- 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.
- 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.
- 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.
- 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.
- Zhang, Y; Lindblom T; Chang A; Sudol M; Sluder A E; Golemis E A (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 (NETHERLANDS) 257 (1): 33–43. doi:10.1016/S0378-1119(00)00372-3. ISSN 0378-1119. PMID 11054566.
- Bedford MT, Sarbassova D, Xu J, et al. (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, et al. (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.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Llorian M, Beullens M, Andrés I, et al. (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.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
- Llorian M, Beullens M, Lesage B, et al. (2006). "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, et al. (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, et al. (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, et al. (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.
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WW domain binding protein 11 Provide feedback
The WW domain is a small protein module with a triple-stranded beta-sheet fold. This is a family of WW domain binding proteins.
Komuro A, Saeki M, Kato S;, J Biol Chem. 1999;274:36513-36519.: 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. PUBMED:10593949 EPMC:10593949
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR019007
Synonym(s): Rsp5 or WWP domain
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 [PUBMED:7846762, PUBMED:7802651, PUBMED:7828727, PUBMED:7641887]. 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 Pro. The WW domain binds to proteins with particular proline-motifs, [AP]-P-P-[AP]-Y, and/or phosphoserine- phosphothreonine-containing motifs [PUBMED:7644498, PUBMED:11911877]. It is frequently associated with other domains typical for proteins in signal transduction processes.
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.
This entry represents WW domain-binding protein 11, which may play a role in the regulation of pre-mRNA processing.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Biological process||RNA processing (GO:0006396)|
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|Seed source:||Pfam-B_13108 (release 21.0)|
|Author:||Mistry J, Wood V|
|Number in seed:||30|
|Number in full:||272|
|Average length of the domain:||77.90 aa|
|Average identity of full alignment:||41 %|
|Average coverage of the sequence by the domain:||17.48 %|
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build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
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