WBP11

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Wbp11
Identifiers
SymbolWbp11
PfamPF09429
InterProIPR019007
WBP11
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesWBP11, NPWBP, PPP1R165, SIPP1, WBP-11, WW domain binding protein 11
External IDsOMIM: 618083 MGI: 1891823 HomoloGene: 134037 GeneCards: WBP11
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for WBP11
Genomic location for WBP11
Band12p12.3Start14,784,582 bp[1]
End14,803,486 bp[1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_016312

NM_021714

RefSeq (protein)

NP_057396

NP_068360

Location (UCSC)Chr 12: 14.78 – 14.8 MbChr 6: 136.81 – 136.83 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Alternative names[edit]

  • 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)

Function[edit]

Studies suggest that Wbp11 plays a role in DNA/ RNA transcriptional or post-transcriptional events related to cell division.[5] Wbp11 is found in the nucleus but not the nucleoli of cells in interphase. However it is distributed throughout the cytoplasm in dividing cells.[6] 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.[7]

Protein interactions[edit]

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.[5] 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.[6]

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.[7]

A number of other interactions have been indicated such as:

  • Vimentin [6]
  • Growth factor receptor-bound protein 2 (GRB2) [8]
  • Genome polyprotein [9]
  • Tyrosine-protein kinase Fyn [8]
  • Pre-mRNA-processing factor 39 (PRP39) [10]
  • TNF receptor-associated factor 4 (TRAF4) [8]
  • Calcineurin B homologous protein 3 (TESC) [8]
  • Probable ATP-dependent RNA helicase DDX17 [11]
  • CD2 antigen cytoplasmic tail-binding protein 2 (CD2BP2) [12]
  • Poly(rC)-binding protein 1 (PCBP1) [13]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000084463 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030216 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ 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.
  6. ^ 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" (PDF). The Journal of Biological Chemistry. 276 (32): 30552–60. doi:10.1074/jbc.M103142200. PMID 11375989.
  7. ^ 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 1223944. PMID 14640981.
  8. ^ 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 4266588. PMID 25416956.
  9. ^ 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 4171131. PMID 24136289.
  10. ^ 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 4848758. PMID 27107014.
  11. ^ 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.
  12. ^ 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.
  13. ^ 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