Neural Wiskott-Aldrich syndrome protein

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Q91YD9 (WASL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Neural Wiskott-Aldrich syndrome protein
Short name=N-WASP

Gene names

Name:

Wasl

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Regulates actin polymerization by stimulating the actin-nucleating activity of the Arp2/3 complex. Binds to TNK2 By similarity. Binds to HSF1/HSTF1 and forms a complex on heat shock promoter elements (HSE) that negatively regulates HSP90 expression. Ref.2
Subunit structure	Interacts with NOSTRIN and SNX9 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. Ref.3 Ref.4 Ref.5
Subcellular location	Cytoplasm › cytoskeleton. Nucleus. Note: Preferentially localized in the cytoplasm when phosphorylated and in the nucleus when unphosphorylated. Ref.2 Ref.5
Sequence similarities	Contains 1 CRIB domain. Contains 1 WH1 domain. Contains 2 WH2 domains.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Domain	Repeat
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin nucleation Traceable author statement Ref.1. Source: MGI actin polymerization or depolymerization Inferred from electronic annotation. Source: InterPro cellular protein complex localization Inferred from mutant phenotype PubMed 21874009. Source: MGI membrane budding Inferred from sequence or structural similarity. Source: BHF-UCL 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 protein complex assembly Inferred from electronic annotation. Source: InterPro regulation of protein localization Inferred from mutant phenotype PubMed 22966049. Source: MGI regulation of transcription, DNA-dependent 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW vesicle transport along actin filament Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	actin cap Inferred from direct assay PubMed 21874009. Source: MGI cytoplasmic membrane-bounded vesicle Inferred from sequence or structural similarity. Source: BHF-UCL lamellipodium Inferred from direct assay PubMed 15148305. Source: MGI nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	small GTPase regulator activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cttn	Q60598	4	EBI-642417,EBI-397955

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 501

501

Neural Wiskott-Aldrich syndrome protein

PRO_0000189001

Regions

Domain

31 – 138

108

WH1

Domain

200 – 213

CRIB

Domain

401 – 418

WH2 1

Domain

429 – 446

WH2 2

Compositional bias

274 – 385

112

Pro-rich

Compositional bias

482 – 501

Asp-rich

Amino acid modifications

Modified residue

239

Phosphoserine; by TNK2 By similarity

Modified residue

253

Phosphotyrosine; by FAK1 and TNK2 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9

Modified residue

480

Phosphoserine By similarity

Modified residue

481

Phosphoserine By similarity

Experimental info

Mutagenesis

253

Y → E: No effect on phosphorylation. Protein preferentially localized in cytoplasm. Ref.2

Mutagenesis

253

Y → F: Abolishes phosphorylation. Protein preferentially localized in nucleus. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

Q91YD9 [UniParc].

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

501

54,274

        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' referencesShow '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]	"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.
[3]	"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.
[4]	"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.
[5]	"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.
[6]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-253, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Macrophage.
[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, MASS SPECTROMETRY. Tissue: Embryonic fibroblast.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ318416 mRNA. Translation: CAC69994.1.

IPI

IPI00468996.

RefSeq

NP_082735.2. NM_028459.2.

UniGene

Mm.1574.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3M3N	X-ray	7.00	W	399-444	[»]

ProteinModelPortal

Q91YD9.

SMR

Q91YD9. Positions 26-147, 204-267, 397-446.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29788N.

IntAct

Q91YD9. 6 interactions.

PTM databases

PhosphoSite

Q91YD9.

Proteomic databases

PaxDb

Q91YD9.

PRIDE

Q91YD9.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000031695; ENSMUSP00000031695; ENSMUSG00000029684.

GeneID

73178.

KEGG

mmu:73178.

Organism-specific databases

CTD

8976.

MGI

MGI:1920428. Wasl.

Phylogenomic databases

eggNOG

NOG270974.

GeneTree

ENSGT00550000074443.

HOVERGEN

HBG000222.

InParanoid

Q91YD9.

K05747.

OMA

SKKCCGV.

OrthoDB

EOG4JM7Q1.

Gene expression databases

ArrayExpress

Q91YD9.

Bgee

Q91YD9.

CleanEx

MM_WASL.

Genevestigator

Q91YD9.

GermOnline

ENSMUSG00000029684. Mus musculus.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR000697. EVH1.
IPR000095. PAK_box_Rho-bd.
IPR011993. PH_like_dom.
IPR011026. WASP_C.
IPR003124. WH2_dom.
[Graphical view]

Pfam

PF00786. PBD. 1 hit.
PF00568. WH1. 1 hit.
PF02205. WH2. 2 hits.
[Graphical view]

SMART

SM00285. PBD. 1 hit.
SM00461. WH1. 1 hit.
SM00246. WH2. 2 hits.
[Graphical view]

SUPFAM

SSF47912. WASP_C. 2 hits.

PROSITE

PS50108. CRIB. 1 hit.
PS50229. WH1. 1 hit.
PS51082. WH2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

WASL. mouse.

EvolutionaryTrace

Q91YD9.

NextBio

337617.

SOURCE

Search...

Entry information

Entry name

WASL_MOUSE

Accession

Primary (citable) accession number: Q91YD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents