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Q91YD9 (WASL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Neural Wiskott-Aldrich syndrome protein

Short name=N-WASP
Gene names
Name:Wasl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in mitosis and cytokinesis, via its role in the regulation of actin polymerization By similarity. Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. Ref.3

Subunit structure

Interacts with NOSTRIN, SNX9 and SNX33 By similarity. Binds to TNK2 By similarity. Binds actin and the Arp2/3 complex. Interacts with CDC42. Binds to SH3 domains of GRB2. Interacts with the C-terminal SH3 domain of DNMBP. Interacts with the WW domains of PRPF40A/FBP11. Interacts with PTK2/FAK1. Interacts with PACSIN1, PACSIN2 and PACSIN3. Ref.2 Ref.4 Ref.5 Ref.6

Subcellular location

Cytoplasmcytoskeleton. Nucleus. Note: Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated. Ref.3 Ref.6

Sequence similarities

Contains 1 CRIB domain.

Contains 1 WH1 domain.

Contains 2 WH2 domains.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Mitosis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   DomainRepeat
   LigandActin-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton organization

Inferred from mutant phenotype PubMed 21874009. Source: MGI

actin nucleation

Traceable author statement Ref.1. Source: MGI

cellular protein complex localization

Inferred from mutant phenotype PubMed 21874009. Source: MGI

membrane budding

Inferred from sequence or structural similarity. Source: BHF-UCL

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of Arp2/3 complex-mediated actin nucleation

Inferred from electronic annotation. Source: InterPro

positive regulation of clathrin-mediated endocytosis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of filopodium assembly

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of protein localization

Inferred from mutant phenotype PubMed 22966049. Source: MGI

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

response to bacterium

Inferred from mutant phenotype Ref.1. Source: MGI

spindle localization

Inferred from mutant phenotype PubMed 21874009. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

vesicle organization

Inferred from sequence or structural similarity. Source: BHF-UCL

vesicle transport along actin filament

Inferred from sequence or structural similarity. Source: BHF-UCL

   Cellular_componentactin cap

Inferred from direct assay PubMed 21874009. Source: MGI

cytoplasm

Inferred by curator Ref.1. Source: MGI

cytoplasmic membrane-bounded vesicle

Inferred from sequence or structural similarity. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

lamellipodium

Inferred from direct assay PubMed 15148305. Source: MGI

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 15169891PubMed 15585574PubMed 21427700. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 501500Neural Wiskott-Aldrich syndrome protein
PRO_0000189001

Regions

Domain31 – 138108WH1
Domain200 – 21314CRIB
Domain401 – 41818WH2 1
Domain429 – 44618WH2 2
Compositional bias274 – 385112Pro-rich
Compositional bias482 – 50120Asp-rich

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue2391Phosphoserine; by TNK2 By similarity
Modified residue2531Phosphotyrosine; by FAK1 and TNK2 Ref.6 Ref.7 Ref.8 Ref.9
Modified residue4801Phosphoserine By similarity
Modified residue4811Phosphoserine By similarity

Experimental info

Mutagenesis2531Y → E: No effect on phosphorylation. Protein preferentially localized in cytoplasm. Ref.3
Mutagenesis2531Y → F: Abolishes phosphorylation. Protein preferentially localized in nucleus. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q91YD9 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: F5ABF44DF9A9F716

FASTA50154,274
        10         20         30         40         50         60 
MSSGQQPPRR VTNVGSLLLT PQENESLFSF LGKKCVTMSS AVVQLYAADR NCMWAKKCSG 

        70         80         90        100        110        120 
VACLVKDNPQ RSYFLRIFDI KDGKLLWEQE LYNNFVYNSP RGYFHTFAGD TCQVALNFAN 

       130        140        150        160        170        180 
EEEAKKFRKA VTDLLGRRQR KSEKRRDAPN GPNLPMATVD IKNPEITTNR FYGSQVNNIS 

       190        200        210        220        230        240 
HTKEKKKGKA KKKRLTKADI GTPSNFQHIG HVGWDPNTGF DLNNLDPELK NLFDMCGISE 

       250        260        270        280        290        300 
AQLKDRETSK VIYDFIEKTG GVEAVKNELR RQAPPPPPPS RGGPPPPPPP PHSSGPPPPP 

       310        320        330        340        350        360 
ARGRGAPPPP PSRAPTAAPP PPPPSRPGVV VPPPPPNRMY PPPPPALPSS APSGPPPPPP 

       370        380        390        400        410        420 
PSMAGSTAPP PPPPPPPPPG PPPPPGLPSD GDHQVPAPSG NKAALLDQIR EGAQLKKVEQ 

       430        440        450        460        470        480 
NSRPVSCSGR DALLDQIRQG IQLKSVSDGQ ESTPPTPAPT SGIVGALMEV MQKRSKAIHS 

       490        500 
SDEDEDDDDE EDFEDDDEWE D 

« Hide

References

« Hide 'large scale' references
[1]"Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells."
Lommel S., Benesch S., Rottner K., Franz T., Wehland J., Kuehn R.
EMBO Rep. 2:850-857(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Brain.
[2]"All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis."
Modregger J., Ritter B., Witter B., Paulsson M., Plomann M.
J. Cell Sci. 113:4511-4521(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PACSIN1; PACSIN2 AND PACSIN3.
[3]"Translocation of N-WASP by nuclear localization and export signals into the nucleus modulates expression of HSP90."
Suetsugu S., Takenawa T.
J. Biol. Chem. 278:42515-42523(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-253.
[4]"Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton."
Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H., Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.
J. Biol. Chem. 278:49031-49043(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DNMBP.
[5]"FBP11 regulates nuclear localization of N-WASP and inhibits N-WASP-dependent microspike formation."
Mizutani K., Suetsugu S., Takenawa T.
Biochem. Biophys. Res. Commun. 313:468-474(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRPF40A.
[6]"Focal adhesion kinase regulation of N-WASP subcellular localization and function."
Wu X., Suetsugu S., Cooper L.A., Takenawa T., Guan J.L.
J. Biol. Chem. 279:9565-9576(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTK2/FAK1, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-253.
[7]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[8]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ318416 mRNA. Translation: CAC69994.1.
CCDSCCDS19945.1.
RefSeqNP_082735.2. NM_028459.2.
UniGeneMm.1574.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3M3NX-ray7.00W397-474[»]
ProteinModelPortalQ91YD9.
SMRQ91YD9. Positions 26-147, 204-267, 397-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid215819. 2 interactions.
DIPDIP-29788N.
IntActQ91YD9. 9 interactions.

PTM databases

PhosphoSiteQ91YD9.

Proteomic databases

MaxQBQ91YD9.
PaxDbQ91YD9.
PRIDEQ91YD9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031695; ENSMUSP00000031695; ENSMUSG00000029684.
GeneID73178.
KEGGmmu:73178.
UCSCuc009bbv.2. mouse.

Organism-specific databases

CTD8976.
MGIMGI:1920428. Wasl.

Phylogenomic databases

eggNOGNOG270974.
GeneTreeENSGT00730000110895.
HOVERGENHBG000222.
InParanoidQ91YD9.
KOK05747.
OMAPTPAGNK.
OrthoDBEOG7FJH20.
PhylomeDBQ91YD9.
TreeFamTF316736.

Gene expression databases

ArrayExpressQ91YD9.
BgeeQ91YD9.
CleanExMM_WASL.
GenevestigatorQ91YD9.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.90.810.10. 1 hit.
InterProIPR000095. CRIB_dom.
IPR011993. PH_like_dom.
IPR011026. WASP_C.
IPR000697. WH1/EVH1.
IPR003124. WH2_dom.
[Graphical view]
PfamPF00786. PBD. 1 hit.
PF00568. WH1. 1 hit.
PF02205. WH2. 2 hits.
[Graphical view]
SMARTSM00285. PBD. 1 hit.
SM00461. WH1. 1 hit.
SM00246. WH2. 2 hits.
[Graphical view]
SUPFAMSSF47912. SSF47912. 2 hits.
PROSITEPS50108. CRIB. 1 hit.
PS50229. WH1. 1 hit.
PS51082. WH2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWASL. mouse.
EvolutionaryTraceQ91YD9.
NextBio337617.
PROQ91YD9.
SOURCESearch...

Entry information

Entry nameWASL_MOUSE
AccessionPrimary (citable) accession number: Q91YD9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot