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0  structures 854  species 0  interactions 963  sequences 16  architectures

Family: Wbp11 (PF09429)

Summary: WW domain binding protein 11

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This is the Wikipedia entry entitled "WBP11". More...

WBP11 Edit Wikipedia article

Symbol Wbp11
Pfam PF09429
InterPro IPR019007
Available structures
PDB Ortholog search: PDBe RCSB
Aliases WBP11, NPWBP, PPP1R165, SIPP1, WBP-11, WW domain binding protein 11
External IDs MGI: 1891823 HomoloGene: 134037 GeneCards: WBP11
Species Human Mouse
RefSeq (mRNA)



RefSeq (protein)



Location (UCSC) Chr 12: 14.78 – 14.8 Mb Chr 6: 136.81 – 136.83 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

Alternative names

  • WW domain binding protein 11 (WBP11)
  • Npw38-binding protein (NpwBP)
  • Splicing factor that Interacts with PQBP-1 and PP1 (SIPP1)
  • SH3 domain binding Protein, 70 kDa (SNP70)


Studies suggest that Wbp11 plays a role in DNA/ RNA transcriptional or post-transcriptional events related to cell division.[3] Wbp11 is found in the nucleus but not the nucleoli of cells in interphase. However it is distributed throughout the cytoplasm in dividing cells.[4] Immunoelectron-microscopy experiments suggest that relocation from a peri-nuclear to a cytoplasmic distribution, coinciding with the onset of mitosis in cell division. Other studies have shown that Wbp11 is a component of the spliceosome. Also, that Wbp11 fragments block pre-mRNA splicing catalysis.[5]

Protein interactions

Wbp11 is a polypeptide known to interact with other WW domain of proteins such as the nuclear protein Npw38 via two proline-rich regions. It associates with Npw38 (hence the name NpwBP) in the nuclei and with Poly(rG) and G-rich ssDNA.[3] The 70kDa protein has also been found to interact with SH3 (Src homology domain 3) domains. The C-terminal proline-rich sequences of SNP70/NpwBP/Wbp11, which binds to the WW domain of Npw38 also fits with both classic type I and type II SH3 binding sequences, hence the name (SNP70).

Wbp11 was found to bind strongly to the tandem SH3 domains of p47phox and to the N-terminal SH3 domain of p47phox, and more weakly to the SH3 domains from c-src and p85α. p47phox.[4]

Furthermore, it has been shown to interact with PP1(protein phosphotase 1), hence the name SIPP1. It has an inhibitory effect to PP1, with its inhibitory potency increasing upon phosphorylation with protein kinase CK1. The binding of Wbp11 with PP1 involves a RVXF (Arg-Val-Xaa-Phe) motif, which functions as a PP1- binding sequence in most interactors of PP1.[5]

A number of other interactions have been indicated such as:

  • Vimentin [4]
  • Growth factor receptor-bound protein 2 (GRB2) [6]
  • Genome polyprotein [7]
  • Tyrosine-protein kinase Fyn [6]
  • Pre-mRNA-processing factor 39 (PRP39) [8]
  • TNF receptor-associated factor 4 (TRAF4) [6]
  • Calcineurin B homologous protein 3 (TESC) [6]
  • Probable ATP-dependent RNA helicase DDX17 [9]
  • CD2 antigen cytoplasmic tail-binding protein 2 (CD2BP2) [10]
  • Poly(rC)-binding protein 1 (PCBP1) [11]


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ a b Komuro A, Saeki M, Kato S (December 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". The Journal of Biological Chemistry. 274 (51): 36513–9. doi:10.1074/jbc.274.51.36513. PMID 10593949. 
  4. ^ a b c Craggs G, Finan PM, Lawson D, Wingfield J, Perera T, Gadher S, Totty NF, Kellie S (August 2001). "A nuclear SH3 domain-binding protein that colocalizes with mRNA splicing factors and intermediate filament-containing perinuclear networks". The Journal of Biological Chemistry. 276 (32): 30552–60. doi:10.1074/jbc.M103142200. PMID 11375989. 
  5. ^ a b Llorian M, Beullens M, Andrés I, Ortiz JM, Bollen M (February 2004). "SIPP1, a novel pre-mRNA splicing factor and interactor of protein phosphatase-1". The Biochemical Journal. 378 (Pt 1): 229–38. doi:10.1042/BJ20030950. PMC 1223944Freely accessible. PMID 14640981. 
  6. ^ a b c d Rolland T, Taşan M, Charloteaux B, Pevzner SJ, Zhong Q, Sahni N, et al. (November 2014). "A proteome-scale map of the human interactome network". Cell. 159 (5): 1212–26. doi:10.1016/j.cell.2014.10.050. PMC 4266588Freely accessible. PMID 25416956. 
  7. ^ Dolan PT, Zhang C, Khadka S, Arumugaswami V, Vangeloff AD, Heaton NS, Sahasrabudhe S, Randall G, Sun R, LaCount DJ (December 2013). "Identification and comparative analysis of hepatitis C virus-host cell protein interactions". Molecular bioSystems. 9 (12): 3199–209. doi:10.1039/c3mb70343f. PMC 4171131Freely accessible. PMID 24136289. 
  8. ^ Zhong Q, Pevzner SJ, Hao T, Wang Y, Mosca R, Menche J, et al. (April 2016). "An inter-species protein-protein interaction network across vast evolutionary distance". Molecular Systems Biology. 12 (4): 865. doi:10.15252/msb.20156484. PMC 4848758Freely accessible. PMID 27107014. 
  9. ^ Hegele A, Kamburov A, Grossmann A, Sourlis C, Wowro S, Weimann M, Will CL, Pena V, Lührmann R, Stelzl U (February 2012). "Dynamic protein-protein interaction wiring of the human spliceosome". Molecular Cell. 45 (4): 567–80. doi:10.1016/j.molcel.2011.12.034. PMID 22365833. 
  10. ^ Kofler M, Motzny K, Beyermann M, Freund C (September 2005). "Novel interaction partners of the CD2BP2-GYF domain". The Journal of Biological Chemistry. 280 (39): 33397–402. doi:10.1074/jbc.M503989200. PMID 16000308. 
  11. ^ 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 (May 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. 

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

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

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.

Literature references

  1. 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

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.

Gene Ontology

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Seed source: Pfam-B_13108 (release 21.0)
Previous IDs: none
Type: Family
Sequence Ontology: SO:0100021
Author: Mistry J , Wood V
Number in seed: 96
Number in full: 963
Average length of the domain: 78.90 aa
Average identity of full alignment: 35 %
Average coverage of the sequence by the domain: 18.54 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 22.2 22.2
Trusted cut-off 22.2 22.2
Noise cut-off 22.1 22.1
Model length: 78
Family (HMM) version: 10
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