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InterPro: IPR001202 WW/Rsp5/WWP

Protein matchesHelp
UniProtKB
Matches:
2606 proteins
AccessionHelp IPR001202 WW_Rsp5_WWP
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Children IPR002349 WW domain
Found in IPR016344 Dystrophin/utrophin
IPR017433 Dystrophin-related protein 2
GO Term annotationHelp
Function GO:0005515 protein binding
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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 [1, 2, 3, 4]. 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 [5, 6]. 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 organization; Rattus norvegicus (Rat) FE65, a transcription-factor activator expressed preferentially in liver; Nicotiana tabacum (Common tobacco) DB10 protein, amongst others.

Structural linksHelp
PDB - click here
CATH: 2.20.70.10
Database linksHelp
PDBe-motif: PS01159
PROSITE doc: PDOC50020
PANDIT: PF00397
Blocks: IPB001202
InteractionsHelp
This domain has been experimentally proven to be involved in Protein:Protein interactions.
Representative data is shown with the following example proteins:

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001202 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O00213 Amyloid beta A4 precursor protein-binding family B member 1

P33203 Pre-mRNA-processing protein PRP40

P34600 WW domain-containing protein ZK1098.1

Q6RHR9 Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1

Q9VVI3 E3 ubiquitin-protein ligase Nedd-4

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR011993 Pleckstrin homology-type
IPR020477 C2 region
IPR008145 Guanylate kinase/L-type calcium channel
IPR008144 Guanylate kinase
IPR018029 C2 membrane targeting protein
IPR006020 Phosphotyrosine interaction domain
IPR008973 C2 calcium/lipid-binding domain, CaLB
IPR000008 C2 calcium-dependent membrane targeting
IPR020590 Guanylate kinase, conserved site
IPR000569 HECT
IPR001478 PDZ/DHR/GLGF
IPR001202 WW/Rsp5/WWP
IPR002713 FF domain
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Bork P, Sudol M.
The WW domain: a signalling site in dystrophin?
Trends Biochem. Sci. 19 531-3 1994 [PubMed: 7846762]
http://dx.doi.org/10.1016/0968-0004(94)90053-1
2. Andre B, Springael JY.
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 1201-5 1994 [PubMed: 7802651]
http://dx.doi.org/10.1006/bbrc.1994.2793
3. Hofmann K, Bucher P.
The rsp5-domain is shared by proteins of diverse functions.
FEBS Lett. 358 153-7 1995 [PubMed: 7828727]
http://dx.doi.org/10.1016/0014-5793(94)01415-W
4. Sudol M, Chen HI, Bougeret C, Einbond A, Bork P.
Characterization of a novel protein-binding module--the WW domain.
FEBS Lett. 369 67-71 1995 [PubMed: 7641887]
http://dx.doi.org/10.1016/0014-5793(95)00550-S
5. Chen HI, Sudol M.
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 7819-23 1995 [PubMed: 7644498]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7644498&action=stream&blobtype=pdf
6. Macias MJ, Wiesner S, Sudol M.
WW and SH3 domains, two different scaffolds to recognize proline-rich ligands.
FEBS Lett. 513 30-7 2002 [PubMed: 11911877]
http://dx.doi.org/10.1016/S0014-5793(01)03290-2

Additional ReadingHelp
Ramirez-Espain X, Ruiz L, Martin-Malpartida P, Oschkinat H, Macias MJ.
Structural characterization of a new binding motif and a novel binding mode in group 2 WW domains.
J. Mol. Biol. 373 2007 1255-68 [PubMed: 17915251]
http://dx.doi.org/10.1016/j.jmb.2007.08.052
Shcherbik N, Kumar S, Haines DS.
Substrate proteolysis is inhibited by dominant-negative Nedd4 and Rsp5 mutants harboring alterations in WW domain 1.
J. Cell. Sci. 115 2002 1041-8 [PubMed: 11870222]
http://jcs.biologists.org/cgi/content/abstract/115/5/1041
Einbond A, Sudol M.
Towards prediction of cognate complexes between the WW domain and proline-rich ligands.
FEBS Lett. 384 1996 1-8 [PubMed: 8797792]
http://dx.doi.org/10.1016/0014-5793(96)00263-3
Macias MJ, Hyvonen M, Baraldi E, Schultz J, Sudol M, Saraste M, Oschkinat H.
Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide.
Nature 382 1996 646-9 [PubMed: 8757138]
http://dx.doi.org/10.1038/382646a0
Meiyappan M, Birrane G, Ladias JA.
Structural basis for polyproline recognition by the FE65 WW domain.
J. Mol. Biol. 372 2007 970-80 [PubMed: 17686488]
http://dx.doi.org/10.1016/j.jmb.2007.06.064
Zhang Y, Daum S, Wildemann D, Zhou XZ, Verdecia MA, Bowman ME, Lucke C, Hunter T, Lu KP, Fischer G, Noel JP.
Structural basis for high-affinity peptide inhibition of human Pin1.
ACS Chem. Biol. 2 2007 320-8 [PubMed: 17518432]
Bedford MT, Sarbassova D, Xu J, Leder P, Yaffe MB.
A novel pro-Arg motif recognized by WW domains.
J. Biol. Chem. 275 2000 10359-69 [PubMed: 10744724]
http://dx.doi.org/10.1074/jbc.275.14.10359
Zarrinpar A, Lim WA.
Converging on proline: the mechanism of WW domain peptide recognition.
Nat. Struct. Biol. 7 2000 611-3 [PubMed: 10932238]
http://dx.doi.org/10.1038/77891
Kanelis V, Rotin D, Forman-Kay JD.
Solution structure of a Nedd4 WW domain-ENaC peptide complex.
Nat. Struct. Biol. 8 2001 407-12 [PubMed: 11323714]
http://dx.doi.org/10.1038/87562
Sudol M, Bork P, Einbond A, Kastury K, Druck T, Negrini M, Huebner K, Lehman D.
Characterization of the mammalian YAP (Yes-associated protein) gene and its role in defining a novel protein module, the WW domain.
J. Biol. Chem. 270 1995 14733-41 [PubMed: 7782338]
http://dx.doi.org/10.1074/jbc.270.24.14733
Lu PJ, Zhou XZ, Shen M, Lu KP.
Function of WW domains as phosphoserine- or phosphothreonine-binding modules.
Science 283 1999 1325-8 [PubMed: 10037602]
http://dx.doi.org/10.1126/science.283.5406.1325
Pastorino L, Sun A, Lu PJ, Zhou XZ, Balastik M, Finn G, Wulf G, Lim J, Li SH, Li X, Xia W, Nicholson LK, Lu KP.
The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-beta production.
Nature 440 2006 528-34 [PubMed: 16554819]
http://dx.doi.org/10.1038/nature04543
Jennings MD, Blankley RT, Baron M, Golovanov AP, Avis JM.
Specificity and autoregulation of Notch binding by tandem WW domains in suppressor of Deltex.
J. Biol. Chem. 282 2007 29032-42 [PubMed: 17656366]
http://dx.doi.org/10.1074/jbc.M703453200
Jager M, Zhang Y, Bieschke J, Nguyen H, Dendle M, Bowman ME, Noel JP, Gruebele M, Kelly JW.
Structure-function-folding relationship in a WW domain.
Proc. Natl. Acad. Sci. U.S.A. 103 2006 10648-53 [PubMed: 16807295]
http://dx.doi.org/10.1073/pnas.0600511103
Narimatsu M, Bose R, Pye M, Zhang L, Miller B, Ching P, Sakuma R, Luga V, Roncari L, Attisano L, Wrana JL.
Regulation of planar cell polarity by Smurf ubiquitin ligases.
Cell 137 2009 295-307 [PubMed: 19379695]
http://dx.doi.org/10.1016/j.cell.2009.02.025
Lin CH, MacGurn JA, Chu T, Stefan CJ, Emr SD.
Arrestin-related ubiquitin-ligase adaptors regulate endocytosis and protein turnover at the cell surface.
Cell 135 2008 714-25 [PubMed: 18976803]
http://dx.doi.org/10.1016/j.cell.2008.09.025
Ermekova KS, Zambrano N, Linn H, Minopoli G, Gertler F, Russo T, Sudol M.
The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled.
J. Biol. Chem. 272 1997 32869-77 [PubMed: 9407065]
http://dx.doi.org/10.1074/jbc.272.52.32869
He J, Bellini M, Inuzuka H, Xu J, Xiong Y, Yang X, Castleberry AM, Hall RA.
Proteomic analysis of beta1-adrenergic receptor interactions with PDZ scaffold proteins.
J. Biol. Chem. 281 2006 2820-7 [PubMed: 16316992]
http://dx.doi.org/10.1074/jbc.M509503200
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InterPro 23.1